Author: "Philippe Pierre" / Topic: humans - Searchworks@Jio Institute Digital Library Search Results

66 results on '"Philippe Pierre"'

1. Distinct metabolic states guide maturation of inflammatory and tolerogenic dendritic cells

Author: Juraj Adamik, Paul V. Munson, Felix J. Hartmann, Alexis J. Combes, Philippe Pierre, Matthew F. Krummel, Sean C. Bendall, Rafael J. Argüello, Lisa H. Butterfield, Parker Institute for Cancer Immunotherapy [San Francisco, CA] (PICI), German Cancer Research Center - Deutsches Krebsforschungszentrum [Heidelberg] (DKFZ), University of California [San Francisco] (UC San Francisco), University of California (UC), Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Stanford University, and DUMENIL, Anita
Subjects: Cell biology, Multidisciplinary, 1.1 Normal biological development and functioning, Inflammatory and immune system, [SDV]Life Sciences [q-bio], Translational immunology, General Physics and Astronomy, Cell Differentiation, Dendritic Cells, General Chemistry, Monocytes, Oxidative Phosphorylation, General Biochemistry, Genetics and Molecular Biology, [SDV] Life Sciences [q-bio], Vaccine Related, Underpinning research, 2.1 Biological and endogenous factors, Humans, Aetiology, Glycolysis, Metabolic and endocrine
Abstract: Cellular metabolism underpins immune cell functionality, yet our understanding of metabolic influences in human dendritic cell biology and their ability to orchestrate immune responses is poorly developed. Here, we map single-cell metabolic states and immune profiles of inflammatory and tolerogenic monocytic dendritic cells using recently developed multiparametric approaches. Single-cell metabolic pathway activation scores reveal simultaneous engagement of multiple metabolic pathways in distinct monocytic dendritic cell differentiation stages. GM-CSF/IL4-induce rapid reprogramming of glycolytic monocytes and transient co-activation of mitochondrial pathways followed by TLR4-dependent maturation of dendritic cells. Skewing of the mTOR:AMPK phosphorylation balance and upregulation of OXPHOS, glycolytic and fatty acid oxidation metabolism underpin metabolic hyperactivity and an immunosuppressive phenotype of tolerogenic dendritic cells, which exhibit maturation-resistance and a de-differentiated immune phenotype marked by unique immunoregulatory receptor signatures. This single-cell dataset provides important insights into metabolic pathways impacting the immune profiles of human dendritic cells.
Published: 2022
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2. Pathogenic variants carrier screening in New Brunswick: Acadians reveal high carrier frequency for multiple genetic disorders

Author: Philippe Pierre, Robichaud, Eric P, Allain, Sarah, Belbraouet, Claude, Bhérer, Jean, Mamelona, Jason, Harquail, Stéphanie, Crapoulet, Nicolas, Crapoulet, Mathieu, Bélanger, and Mouna, Ben Amor
Subjects: Canada, Exome Sequencing, Ethnicity, Infant, Newborn, Genetics, Humans, New Brunswick, Pilot Projects, Genetics (clinical)
Abstract: Background Founder populations that have recently undergone important genetic bottlenecks such as French-Canadians and Ashkenazi Jews can harbor some pathogenic variants at a higher carrier rate than the general population, putting them at a higher risk for certain genetic diseases. In these populations, there can be considerable benefit to performing ethnic-based or expanded preconception carrier screening, which can help in the prevention or early diagnosis and management of some genetic diseases. Acadians are descendants of French immigrants who settled in the Atlantic Coast of Canada in the seventeenth century. Yet, the Acadian population has never been investigated for the prevalence/frequency of disease-causing genetic variants. Methods An exome sequencing panel for 312 autosomal recessive and 30 X-linked diseases was designed and specimens from 60 healthy participants were sequenced to assess carrier frequency for the targeted diseases. Results In this study, we show that a sample population of Acadians in South-East New Brunswick harbor variants for 28 autosomal recessive and 1 X-linked diseases, some of which are significantly more frequent in comparison to reference populations. Conclusion Results from this pilot study suggests a need for further investigation of genomic variation in this population and possibly implementation of targeted carrier and neonatal screening programs.
Published: 2022
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3. Loss of detection of fatty acid-metabolizing proteins in Western blot analyses - Impact of sample heating

Author: Roody S. Biam, Philippe-Pierre Robichaud, Maroua Mbarik, Paskale Pineau, and Marc E. Surette
Subjects: Heating, HEK293 Cells, Blotting, Western, Fatty Acids, Biophysics, Humans, Proteins, Electrophoresis, Polyacrylamide Gel, Cell Biology, Molecular Biology, Biochemistry
Abstract: When performing western blots for protein detection using the classical Laemmli method, experimenters often encounter difficulties with the detection of transmembrane proteins involved in lipid or fatty acid metabolism. A crucial phase in sample preparation is heating the samples to 100 °C in a Laemmli sample buffer containing SDS before separation by polyacrylamide gel electrophoresis (PAGE). In the current study, the analysis of several proteins was performed following modifications of the heating step during sample preparation. Multiple samples of the human Jurkat cell line were prepared using commercial or homemade Laemmli sample buffer. Samples were subjected to incubation at different temperatures for varying periods of time prior to separation by SDS-PAGE, transfer onto PVDF membranes and detection with specific antibodies. In samples incubated at temperatures of 25 °C, 40 °C, 70 °C and 100 °C, detection of the transmembrane protein elongase of long chain fatty acids 5 (ELOVL5) significantly decreased with temperature to a near total absence of signal at 100 °C. Heating (100 °C) the samples even for 1 min resulted in significant loss of ELOVL5 band intensity that was associated with the appearance of higher molecular weight immunoreactive materials. Loss of ELOVL5 band intensity was also observed with heating of samples at 100 °C prepared from HepG2, HEK293, MCF-7 and SKRB cells. The robust induction of ELOVL5 in stimulated primary T cells was not detected when sample were heated. The detection of fatty acid-metabolizing enzymes stearoyl-CoA desaturase-1 and long-chain-fatty-acid-CoA ligases 3 and 4 showed bands with significantly less intensity after heating at 100 °C compared to samples prepared at room temperature. Heating samples at 100 °C did not affect the detection of transmembrane proteins ERBB2 and five-lipoxygenase activating protein, or the soluble 5-lipoxygenase protein. Overall, the number of transmembrane passes of a protein was not predictive of loss of band intensity after heating, however this study indicates that sample heating can drastically affect the ability to detect proteins following separation by SDS-PAGE. This has implications for any detection methods that follow SDS-PAGE.
Published: 2022

4. The Reproductive Role of the Human Breast [and Comments and Reply]

Author: Anderson, Peter, Frisch, Rose E., Graham, Charles E., Manderson, Lenore, Orubuloye, I. O., Philippe, Pierre, Raphael, Dana, Stini, William A., and Van Esterik, Penny
Published: 1983

5. Experimental Efficacy of the Face Shield and the Mask against Emitted and Potentially Received Particles

Author: Jean Michel Wendling, Philippe Pierre Pébaÿ, Thibaut Fabacher, Isabelle Cosperec, Michaël Rochoy, Laboratoire des sciences de l'ingénieur, de l'informatique et de l'imagerie (ICube), École Nationale du Génie de l'Eau et de l'Environnement de Strasbourg (ENGEES)-Université de Strasbourg (UNISTRA)-Institut National des Sciences Appliquées - Strasbourg (INSA Strasbourg), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de Recherche en Informatique et en Automatique (Inria)-Les Hôpitaux Universitaires de Strasbourg (HUS)-Centre National de la Recherche Scientifique (CNRS)-Matériaux et Nanosciences Grand-Est (MNGE), Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Réseau nanophotonique et optique, and Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)
Subjects: Face shield, business.product_category, Materials science, masks, experimental setup, Particle number, receiver, Health, Toxicology and Mutagenesis, Airflow, lcsh:Medicine, pandemics, Article, covid19, 03 medical and health sciences, coronavirus infections, 0302 clinical medicine, Optics, Aerosol generator, Humans, pneumonia, prevention and control, 030212 general & internal medicine, face shields, aerosolization, Personal Protective Equipment, Reduction factor, Common emitter, Aerosols, emitter, particles, Inhalation Exposure, protective devices, business.industry, coronavirus infections, aerosols, lcsh:R, Public Health, Environmental and Occupational Health, COVID-19, covid, Short distance, Face masks, [INFO.INFO-TI]Computer Science [cs]/Image Processing [eess.IV], Communicable Disease Control, 030221 ophthalmology & optometry, Barrier effect, Community setting, Particle, business, Particle counter
Abstract: There is currently not sufficient evidence to support the effectiveness of face shields for source control. In order to evaluate the comparative barrier performance effect of face masks and face shields, we used an aerosol generator and a particle counter to evaluate the performance of the various devices in comparable situations. We tested different configurations in an experimental setup with manikin heads wearing masks (surgical type I), face shields (22.5 cm high with overhang under the chin of 7 cm and circumference of 35 cm) on an emitter or a receiver manikin head, or both. The manikins were face to face, 25 cm apart, with an intense particle emission (52.5 L/min) for 30 s. The particle counter calculated the total cumulative particles aspirated on a volume of 1.416 L In our experimental conditions, when the receiver alone wore a protection, the face shield was more effective (reduction factor = 54.8%), while reduction was lower with a mask (reduction factor = 21.8%) (p = 0.002). The wearing of a protective device by the emitter alone reduced the level of received particles by 96.8% for both the mask and face shield (p = NS). When both the emitter and receiver manikin heads wore a face shield, the protection allowed for better results in our experimental conditions: 98% reduction for the face shields versus 97.3% for the masks (p = 0.01). Face shields offered an even better barrier effect than the mask against small inhaled particles (&lt, 0.3 µm–0.3 to 0.5 µm–0.5 to 1 µm) in all configurations. Therefore, it would be interesting to include face shields as used in our experimental study as part of strategies to reduce transmission within the community setting.
Published: 2021
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6. EBF1 drives hallmark B cell gene expression by enabling the interaction of PAX5 with the MLL H3K4 methyltransferase complex

Author: Andrew P. Joy, Rodney J. Ouellette, David Barnett, Charles E. Bullerwell, Philippe Pierre Robichaud, Pierre M. L. Deprez, Gabriel Wajnberg, Darwin D’Souza, Simi Chacko, Stephen M. Lewis, Stéphanie Fournier, and Nicolas Crapoulet
Subjects: 0301 basic medicine, Lymphoma, B-Cell, Molecular biology, Science, Antigens, CD19, Gene Expression, Diseases, Lymphocyte Activation, Article, CD19, 03 medical and health sciences, 0302 clinical medicine, immune system diseases, Transcription (biology), Cell Line, Tumor, hemic and lymphatic diseases, Gene expression, Transcriptional regulation, medicine, Humans, Gene silencing, Cell Lineage, B cell, Cancer, B-Lymphocytes, Multidisciplinary, biology, Methyltransferase complex, Chemistry, PAX5 Transcription Factor, Cell Differentiation, Methyltransferases, Cell biology, 030104 developmental biology, Histone, medicine.anatomical_structure, Oncology, Gene Expression Regulation, 030220 oncology & carcinogenesis, Trans-Activators, biology.protein, Medicine
Abstract: PAX5 and EBF1 work synergistically to regulate genes that are involved in B lymphocyte differentiation. We used the KIS-1 diffuse large B cell lymphoma cell line, which is reported to have elevated levels of PAX5 expression, to investigate the mechanism of EBF1- and PAX5-regulated gene expression. We demonstrate the lack of expression of hallmark B cell genes, including CD19, CD79b, and EBF1, in the KIS-1 cell line. Upon restoration of EBF1 expression we observed activation of CD19, CD79b and other genes with critical roles in B cell differentiation. Mass spectrometry analyses of proteins co-immunoprecipitated with PAX5 in KIS-1 identified components of the MLL H3K4 methylation complex, which drives histone modifications associated with transcription activation. Immunoblotting showed a stronger association of this complex with PAX5 in the presence of EBF1. Silencing of KMT2A, the catalytic component of MLL, repressed the ability of exogenous EBF1 to activate transcription of both CD19 and CD79b in KIS-1 cells. We also find association of PAX5 with the MLL complex and decreased CD19 expression following silencing of KMT2A in other human B cell lines. These data support an important role for the MLL complex in PAX5-mediated transcription regulation.
Published: 2021
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7. Zdhhc2 Is Essential for Plasmacytoid Dendritic Cells Mediated Inflammatory Response in Psoriasis

Author: Binhui Zhou, Wenyi Yang, Wushan Li, Le He, Liaoxun Lu, Lichen Zhang, Zhuangzhuang Liu, Ying Wang, Tianzhu Chao, Rong Huang, Yanrong Gu, Tingting Jia, Qiaoli Liu, Shuanghua Tian, Philippe Pierre, Takahiro Maeda, Yinming Liang, Eryan Kong, Centre d'Immunologie de Marseille - Luminy (CIML), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU), Laboratory of Mouse Genetics, Institute of Psychiatry and Neuroscience, Xinxiang Medical University, Henan, China, Xinxiang Medical University, Henan - Laboratory of Genetic Regulators in the Immune System, Institute for Research in Biomedicine ( iBiMED), Universidade de Aveiro, E-institute of Shanghai University Immunology Division, Shanghai University, Graduate School of Biomedical Sciences [Nagasaki University, Japan], Nagasaki University, National Natural ScienceFoundation of China (Grant No. 31770824 and 32000491), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), and DUMENIL, Anita
Subjects: Male, 0301 basic medicine, T-Lymphocytes, medicine.medical_treatment, [SDV]Life Sciences [q-bio], Plasmacytoid dendritic cell, Lymphocyte Activation, 030207 dermatology & venereal diseases, 0302 clinical medicine, Immunology and Allergy, ComputingMilieux_MISCELLANEOUS, Skin, Original Research, Zdhhc2, Mice, Knockout, Imiquimod, Chemistry, autoimmunity, psoriasis, inflammatory response, Up-Regulation, 3. Good health, [SDV] Life Sciences [q-bio], Cytokine, plasmacytoid dendritic cells, medicine.symptom, Signal Transduction, lcsh:Immunologic diseases. Allergy, Immunology, Inflammation, Cell Line, 03 medical and health sciences, Immune system, Psoriasis, medicine, Animals, Humans, Tumor Suppressor Proteins, Interferon-alpha, Dendritic Cells, medicine.disease, Mice, Inbred C57BL, Disease Models, Animal, 030104 developmental biology, Cancer research, IRF7, lcsh:RC581-607, Acyltransferases, CD80, Interferon regulatory factors
Abstract: Zdhhc family genes are composed of 24 members that regulate palmitoylation, a post-translational modification process for proteins. Mutations in genes that alter palmitoylation or de-palmitoylation could result in neurodegenerative diseases and inflammatory disorders. In this study, we found that Zdhhc2 was robustly induced in psoriatic skin and loss of Zdhhc2 in mice by CRISPR/Cas9 dramatically inhibited pathology of the ear skin following imiquimod treatment. As psoriasis is an inflammatory disorder, we analyzed tissue infiltrating immune cells and cytokine production. Strikingly we found that a master psoriatic cytokine interferon-α (IFN-α) in the lesioned skin of wildtype (WT) mice was 23-fold higher than that in Zdhhc2 deficient counterparts. In addition, we found that CD45+ white blood cells (WBC) infiltrating in the skin of Zdhhc2 deficient mice were also significantly reduced. Amelioration in psoriasis and dramatically reduced inflammation of Zdhhc2 deficient mice led us to analyze the cellular components that were affected by loss of Zdhhc2. We found that imiquimod induced plasmacytoid dendritic cell (pDC) accumulation in psoriatic skin, spleen, and draining lymph nodes (DLN) were drastically decreased in Zdhhc2 deficient mice, and the expression of pDC activation marker CD80 also exhibited significantly inhibited in psoriatic skin. In further experiments, we confirmed the cell intrinsic effect of Zdhhc2 on pDCs as we found that loss of zDHHC2 in human CAL-1 pDC dampened both interferon regulatory factor 7 (IRF7) phosphorylation and IFN-α production. Therefore, we identified novel function of Zdhhc2 in controlling inflammatory response in psoriasis in mice and we also confirmed that crucial role of Zdhhc2 in pDCs by regulating IRF7 activity and production of the critical cytokine. Our results finding the dependence of IFN-α production on Zdhhc2 in inflamed murine skin and in human pDCs provide rationale for targeting this new molecule in treatment of inflammation.
Published: 2021
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8. LAMP-5 is an essential inflammatory-signaling regulator and novel immunotherapy target for Mixed Lineage Leukemia-Rearranged acute leukemia

Author: Mark Wunderlich, Brenay Greenslade, Matthew Burwinkel, Lynn Lee, Gabriel Gracia-Maldonado, Philippe Pierre, Jason Clark, Ashish R Kumar, Evelina Gatti, Dario Leone, Nathan Salomonis, Cincinnati Children's Hospital Medical Center, Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), DUMENIL, Anita, and Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)
Subjects: medicine.medical_treatment, [SDV]Life Sciences [q-bio], Interleukin-1 receptor, Biology, 03 medical and health sciences, 0302 clinical medicine, Downregulation and upregulation, Interferon, hemic and lymphatic diseases, medicine, Humans, neoplasms, 030304 developmental biology, 0303 health sciences, Acute leukemia, Leukemia, Cell growth, Hematology, Immunotherapy, Histone-Lysine N-Methyltransferase, medicine.disease, 3. Good health, Leukemia, Biphenotypic, Acute, [SDV] Life Sciences [q-bio], 030220 oncology & carcinogenesis, Cancer research, IRF7, Myeloid-Lymphoid Leukemia Protein, medicine.drug
Abstract: Although great advances have been made in understanding the pathobiology of mixed lineage leukemia-rearranged (MLL-r) leukemias, therapies for this leukemia have remained limited, and clinical outcomes remain bleak. In order to identify novel targets for immunotherapy treatments, we compiled a lineage-independent MLL-r leukemia gene signature using publicly available data sets. Data from large leukemia repositories were filtered through the in silico human surfaceome, providing a list of highly predicted cell surface proteins overexpressed in MLL-r leukemias. LAMP5, a lysosomal associated membrane protein, is expressed highly and specifically in MLL-r leukemia. We found that LAMP5 is a direct target of the oncogenic MLL-fusion protein. LAMP5 depletion significantly inhibited leukemia cell growth in vitro and in vivo. Functional studies showed that LAMP-5 is a novel modulator of innate-immune pathways in MLL-r leukemias. Downregulation of LAMP5 led to inhibition of NF-kB signaling and increased activation of type-1 interferon signaling downstream of Toll-like receptor/interleukin 1 receptor activation. These effects were attributable to the critical role of LAMP-5 in transferring the signal flux from interferon signaling endosomes to pro-inflammatory signaling endosomes. Depletion of IRF7 was able to partially rescue the cell growth inhibition upon LAMP5 downregulation. Lastly, LAMP-5 was readily detected on the surface of MLL-r leukemia cells. Targeting surface LAMP-5 using an antibody-drug conjugate leads to significant cell viability decrease specifically in MLL-r leukemias. Overall, based on the limited expression throughout human tissues, we postulate that LAMP-5 could potentially serve as an immunotherapeutic target with a wide therapeutic window to treat MLL-r leukemias.
Published: 2020
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9. COVID-19: beta-thalassemia subjects immunised?

Author: Jean Laurent Picard, Edouard Lansiaux, Philippe Pierre Pébaÿ, and Joachim Son-Forget
Subjects: 0301 basic medicine, Male, thalassemia, Disease, medicine.disease_cause, Hemoglobins, 0302 clinical medicine, Prevalence, heme, Coronavirus, education.field_of_study, biology, immunisation, Beta thalassemia, General Medicine, Middle Aged, Regression, Treatment Outcome, Italy, statistics, Regression Analysis, Female, Coronavirus Infections, Heterozygote, Pneumonia, Viral, Population, Sardinia, Article, 03 medical and health sciences, Betacoronavirus, Favipiravir, Novel Coronavirus, respiratory distress, medicine, Humans, education, Pandemics, SARS-CoV-2, business.industry, beta-Thalassemia, other, COVID-19, Heterozygote advantage, biology.organism_classification, medicine.disease, 030104 developmental biology, Infectious disease (medical specialty), correlation, Immune System, Novel virus, Immunology, beta, Immunization, Hemoglobin, business, 030217 neurology & neurosurgery
Abstract: The novel coronavirus pneumonia (COVID-19) is a contagious acute respiratory infectious disease whose causative agent has been demonstrated to be a novel virus of the coronavirus family, SARSCoV-2. A recent pre-print study has showed a heme attack on the 1-beta chain of hemoglobin by COVID19. Beta-thalassemia results of a default in the hemoglobin beta- chain synthesis. 1,5% global population are heterozygotes for this disease. In this study, by a multiple linear regression, we have analyzed the evolution of COVID-19 infection in three Italian regions (Puglia, Sardinia, Sicilia) with different beta-thalassemic prevalences, in order to search a link. The results have showed that betathalassemic heterozygote population prevalence is correlated to immunity against COVID-19, by a regression. This paper is only for academic discussion, the hypotheses and conclusions needs to be confirmed by further research .
Published: 2020
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10. Distinct metabolic programs established in the thymus control effector functions of γδ T cell subsets in tumor microenvironments

Author: Ayano C. Kohlgruber, Claire McIntyre, Bruno Silva-Santos, Mathilde Raverdeau, Lydia Dyck, Noëlla Lopes, Róisín M. Loftus, Leandro Z. Agudelo, Rafael J. Argüello, Nital Sumaria, Aaron Douglas, Philippe Pierre, Manolis Kellis, Hannah Prendeville, Harry Kane, Stefania Martin, Stephen Cunningham, Daniel J. Pennington, Michael B. Brenner, Gina J. Fiala, Colleen Carmody, Lydia Lynch, Trinity College Dublin, Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Computer Science and Artificial Intelligence Laboratory [Cambridge] (CSAIL), Massachusetts Institute of Technology (MIT), Harvard Medical School [Boston] (HMS), Queen Mary University of London (QMUL), Repositório da Universidade de Lisboa, Universidade de Lisboa - Instituto de Medicina Molecular João Lobo Antunes, Brigham & Women’s Hospital [Boston] (BWH), Blizard Institute, Universidade de Lisboa - Instituto de Medicina Molecular João Lobo Antune, and Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)
Subjects: 0301 basic medicine, Adoptive cell transfer, medicine.medical_treatment, Melanoma, Experimental, Immunotherapy, Adoptive, 0302 clinical medicine, Cancer immunotherapy, Interferon, T-Lymphocyte Subsets, Tumor Microenvironment, Immunology and Allergy, Interleukin-17, Receptors, Antigen, T-Cell, gamma-delta, 3. Good health, Cell biology, Mitochondria, Tumor Burden, medicine.anatomical_structure, Phenotype, [SDV.IMM.IA]Life Sciences [q-bio]/Immunology/Adaptive immunology, Colonic Neoplasms, Female, Glycolysis, medicine.drug, Signal Transduction, T cell, Immunology, [SDV.CAN]Life Sciences [q-bio]/Cancer, Breast Neoplasms, Mice, Transgenic, Thymus Gland, Biology, Article, 03 medical and health sciences, Interferon-gamma, Immune system, Lymphocytes, Tumor-Infiltrating, Organ Culture Techniques, Antigen, Cell Line, Tumor, medicine, Animals, Humans, Cell Lineage, Obesity, Tumor microenvironment, Immunotherapy, Lipid Metabolism, Mice, Inbred C57BL, 030104 developmental biology, Glucose, Energy Metabolism, 030215 immunology
Abstract: © The Author(s), under exclusive licence to Springer Nature America, Inc. 2021, Metabolic programming controls immune cell lineages and functions, but little is known about γδ T cell metabolism. Here, we found that γδ T cell subsets making either interferon-γ (IFN-γ) or interleukin (IL)-17 have intrinsically distinct metabolic requirements. Whereas IFN-γ+ γδ T cells were almost exclusively dependent on glycolysis, IL-17+ γδ T cells strongly engaged oxidative metabolism, with increased mitochondrial mass and activity. These distinct metabolic signatures were surprisingly imprinted early during thymic development and were stably maintained in the periphery and within tumors. Moreover, pro-tumoral IL-17+ γδ T cells selectively showed high lipid uptake and intracellular lipid storage and were expanded in obesity and in tumors of obese mice. Conversely, glucose supplementation enhanced the antitumor functions of IFN-γ+ γδ T cells and reduced tumor growth upon adoptive transfer. These findings have important implications for the differentiation of effector γδ T cells and their manipulation in cancer immunotherapy., This work was supported by the Wellcome Trust (092973/Z/10/Z to D.J.P.), Biotechnology and Biological Sciences Research Council (BBSRC) UK (BB/R017808/1 to D.J.P.), European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation programme (grant agreement no. 646701 to B.S.-S.; StG_679173 to L.L.), Science Foundation Ireland (SFI) (16/FRL/3865 to L.L.), NIH (NS115064, HG008155, AG062377 to M.K.), NIH (R01 AI134861 and metabolic core grant S10 OD020100 to L.L.), Fundação Astrazeneca (Prémio FAZ Ciência 2019 to B.S.-S. and N.L.) and PAC-PRECISE LISBOA-01-0145-FEDER-016394, co-funded by FEDER (POR Lisboa 2020 (Programa Operacional Regional de Lisboa, do Portugal 2020)) and Fundação para a Ciência e a Tecnologia (Portugal). N.L. is supported by a postdoctoral fellowship from EMBO (ALTF 752-2018); S.M. was supported by a studentship from the Medical Research Council (MRC) UK; G.F. is supported by the European Union’s Horizon 2020 research and innovation programme under the Marie Skłodowska-Curie grant agreement no. 752932; and A.D., S.C., L.D. and H.P. are supported by Irish Research Council fellowships.
Published: 2020
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11. Polyunsaturated fatty acid elongation and desaturation in activated human T-cells: ELOVL5 is the key elongase

Author: Philippe-Pierre Robichaud, Jean Eric Munganyiki, Eric Boilard, and Marc E. Surette
Subjects: Male, 0301 basic medicine, Fatty Acid Elongases, T-Lymphocytes, FADS2, Blotting, Western, Apoptosis, elongation of very long chain fatty acids protein 5, QD415-436, Biochemistry, Jurkat cells, lipids, Jurkat Cells, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Endocrinology, Acetyltransferases, arachidonic acid, Humans, desaturases, Cells, Cultured, Research Articles, Cell Proliferation, chemistry.chemical_classification, Gene knockdown, biology, Chemistry, food and beverages, Cell Biology, Metabolism, Cell cycle, eye diseases, Cell biology, 030104 developmental biology, Fatty acid desaturase, 030220 oncology & carcinogenesis, Fatty Acids, Unsaturated, ω-3, biology.protein, Female, lipids (amino acids, peptides, and proteins), Arachidonic acid, sense organs, metabolism, Polyunsaturated fatty acid
Abstract: PUFAs are important constituents of membrane glycerophospholipids. However, changes in the capacities to incorporate and metabolize PUFAs when cells enter the cell cycle have not been thoroughly studied. In this study, differences in the incorporation and metabolism of exogenous PUFAs in resting and proliferating primary human T-cells and in the Jurkat cell line were measured. Overall, proliferating T-cells and Jurkat cells had a greater capacity to incorporate and elongate exogenous 18- and 20-carbon PUFAs compared with resting T-cells. Proliferating T-cells and Jurkat cells also showed a greater capacity to desaturate 18-carbon PUFA substrates. Consistent with these observations, a significant increase in the expression of fatty acid desaturase (FADS) 1, FADS2, and elongation of very long chain fatty acids protein (ELOVL) 5 was measured in proliferating T-cells compared with resting T-cells. No quantifiable ELOVL2 was measured. Knockdown of ELOVL5 in T-cells and Jurkat cells significantly affected cellular monounsaturated and PUFA profiles and strongly impaired the elongation of 18- and 20-carbon PUFAs. In conclusion, the induction of proliferation in human T-cells is associated with a significant increase in the capacity to take up and metabolize exogenous PUFAs, and ELOVL5 is responsible for the elongation of 18- and 20-carbon PUFAs in these cells.
Published: 2018
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12. Circulating cell-free DNA as potential diagnostic tools for amyotrophic lateral sclerosis

Author: Pier Jr Morin, Philippe-Pierre Robichaud, Colleen O’Connell, Rodney J. Ouellette, and Michael Arseneault
Subjects: 0301 basic medicine, business.industry, General Neuroscience, Amyotrophic Lateral Sclerosis, Cancer, Methylation, DNA Methylation, Bioinformatics, medicine.disease, Circulating Cell-Free DNA, 03 medical and health sciences, 030104 developmental biology, 0302 clinical medicine, Cell-free fetal DNA, DNA methylation, medicine, Animals, Humans, Clinical significance, Liquid biopsy, Amyotrophic lateral sclerosis, business, Cell-Free Nucleic Acids, Biomarkers, 030217 neurology & neurosurgery
Abstract: DNA methylation has garnered much attention in recent years for its diagnostic potential in multiple conditions including cancer and neurodegenerative diseases. Conversely, advances regarding the potential diagnostic relevance of DNA methylation status have been sparse in the field of amyotrophic lateral sclerosis (ALS) even though patients diagnosed with this condition would significantly benefit from improved molecular assays aimed at furthering the current diagnostic and therapeutic options available. This review will provide an overview of the current diagnostic approaches available for ALS diagnosis and discuss the potential clinical usefulness of DNA methylation. We will also present examples of DNA methylation as a diagnostic tool in various types of cancer and neurodegenerative conditions and expand on how circulating cfDNA methylation may be leveraged for the early detection of ALS. In general, this article will reinforce the importance of cfDNA methylation as diagnostic tools and will further highlight its clinical relevance for persons diagnosed with ALS.
Published: 2021
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13. SCENITH: A Flow Cytometry-Based Method to Functionally Profile Energy Metabolism with Single-Cell Resolution

Author: Evelina Gatti, Julien-Paul Gigan, Sébastien Boissonneau, Alexis J. Combes, Peter Yan, Jessica Tsui, Rafael J. Argüello, Ania I. Baaziz, Remy Char, Matthew F. Krummel, Voahirana Camosseto, Evens Bousiquot, Bushra Samad, Emeline Tabouret, Dominique Figarella-Branger, Philippe Pierre, Institut de neurophysiopathologie (INP), Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU), Service d'Anatomie Pathologique et de Neuropathologie [Hôpital de la Timone - CHU - APHM], Hôpital de la Timone [CHU - APHM] (TIMONE)-Assistance Publique - Hôpitaux de Marseille (APHM), Neuro-Oncologie [Hôpital de la Timone - APHM], Aix Marseille Université (AMU)-Assistance Publique - Hôpitaux de Marseille (APHM)- Hôpital de la Timone [CHU - APHM] (TIMONE), Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM), University of California [San Francisco] (UC San Francisco), University of California (UC), Department of Pathology, University of California, San Francisco, Aix-Marseille Université - Faculté de médecine (AMU MED), Aix Marseille Université (AMU), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Laboratoire d'Anatomie Pathologique-Neuropathologique [AP-HM Hôpital La Timone], Hôpital de la Timone [CHU - APHM] (TIMONE), Institute for Research in Biomedicine ( iBiMED), Universidade de Aveiro, Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU), University of California [San Francisco] (UCSF), University of California, and ARGUELLO, Rafael
Subjects: Male, protein synthesis and metabolism, 0301 basic medicine, Physiology, [SDV]Life Sciences [q-bio], Cell, metabolism analysis in samples from patients, Medical Biochemistry and Metabolomics, Inbred C57BL, Mice, 0302 clinical medicine, Neoplasms, 2.1 Biological and endogenous factors, Aetiology, Cells, Cultured, Cancer, Whole blood, Cultured, medicine.diagnostic_test, Hematology, Middle Aged, Phenotype, medicine.anatomical_structure, Metabolome, [SDV.IMM]Life Sciences [q-bio]/Immunology, Female, Single-Cell Analysis, Reprogramming, Adult, Pediatric Research Initiative, Cell type, [SDV.IMM] Life Sciences [q-bio]/Immunology, metabolic profiling of blood samples, Cells, metabolic function by flow cytometry, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Computational biology, Biology, Article, Flow cytometry, Endocrinology & Metabolism, 03 medical and health sciences, Immune system, Clinical Research, Genetics, medicine, Animals, Humans, [SDV.BC] Life Sciences [q-bio]/Cellular Biology, Molecular Biology, tumor immunometabolism, Inflammatory and immune system, translation and metabolism, Cell Biology, Fibroblasts, Mice, Inbred C57BL, 030104 developmental biology, Biochemistry and Cell Biology, cell culture media and metabolism, metabolic gene signatures, Energy Metabolism, functional assay metabolism single cells, 030217 neurology & neurosurgery, Ex vivo
Abstract: International audience; Energetic metabolism reprogramming is critical for cancer and immune responses. Current methods to functionally profile the global metabolic capacities and dependencies of cells are performed in bulk. We designed a simple method for complex metabolic profiling called SCENITH, for single-cell energetic metabolism by profiling translation inhibition. SCENITH allows for the study of metabolic responses in multiple cell types in parallel by flow cytometry. SCENITH is designed to perform metabolic studies ex vivo, particularly for rare cells in whole blood samples, avoiding metabolic biases introduced by culture media. We analyzed myeloid cells in solid tumors from patients and identified variable metabolic profiles, in ways that are not linked to their lineage or their activation phenotype. SCENITH's ability to reveal global metabolic functions and determine complex and linked immune-phenotypes in rare cell subpopulations will contribute to the information needed for evaluating therapeutic responses or patient stratification.
Published: 2020
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14. At the crossway of ER-stress and proinflammatory responses

Author: Philippe Pierre, Marisa Reverendo, Rafael J. Argüello, Andreia Mendes, Evelina Gatti, ARGUELLO, Rafael, Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), and Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)
Subjects: 0301 basic medicine, [SDV.IMM] Life Sciences [q-bio]/Immunology, medicine.medical_treatment, Inflammation, Biology, Endoplasmic Reticulum, Dendritic cells, Biochemistry, Proinflammatory cytokine, Unfolded protein response, 03 medical and health sciences, 0302 clinical medicine, Immune system, medicine, Animals, Humans, Molecular Biology, ComputingMilieux_MISCELLANEOUS, Innate immunity, Innate immune system, Cell Biology, Endoplasmic Reticulum Stress, Immunity, Innate, Cell biology, 030104 developmental biology, Proteostasis, Cytokine, 030220 oncology & carcinogenesis, Unfolded Protein Response, [SDV.IMM]Life Sciences [q-bio]/Immunology, Signal transduction, medicine.symptom, Endoplasmic reticulum, Signal Transduction
Abstract: Immune cells detect specific microbes or damage to tissue integrity in order to initiate efficient immune responses. Abnormal accumulation of proteins in the endoplasmic reticulum (ER) can be seen as a sign of cellular malfunction and stress that triggers a collection of conserved emergency rescue programs. These different signaling cascades, which favor ER proteostasis and promote cell survival, are collectively known as the unfolded protein response (UPR). In recent years, a synergy between the UPR and inflammatory cytokine production has been unraveled, with different branches of the UPR entering in a cross-talk with specialized microbe sensing pathways, which turns on or amplify inflammatory cytokines production. Complementary to this synergetic activity, UPR induction alone, can itself be seen as a danger signal, and triggers directly or indirectly inflammation in different cellular and pathological models, this independently of the presence of pathogens. Here, we discuss recent advances on the nature of these cross-talks and how innate immunity, metabolism dysregulation, and ER-signaling pathways intersect in specialized immune cells, such as dendritic cells (DCs), and contribute to the pathogenesis of inflammatory diseases.
Published: 2019
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15. The impact of PUFA on cell responses: Caution should be exercised when selecting PUFA concentrations in cell culture

Author: Marc E. Surette, Maroua Mbarik, Philippe-Pierre Robichaud, and Roody S Biam
Subjects: 0301 basic medicine, medicine.medical_specialty, Pyridines, THP-1 Cells, Clinical Biochemistry, Cell, Cell Culture Techniques, Apoptosis, 030209 endocrinology & metabolism, Protective Agents, Jurkat cells, Jurkat Cells, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, In vivo, Internal medicine, medicine, Humans, Diacylglycerol O-Acyltransferase, Phospholipids, Triglycerides, Cell Proliferation, chemistry.chemical_classification, Arachidonic Acid, 030109 nutrition & dietetics, Cell growth, Cell Membrane, Imidazoles, food and beverages, Hep G2 Cells, Cell Biology, eye diseases, Endocrinology, medicine.anatomical_structure, Eicosapentaenoic Acid, chemistry, Cell culture, MCF-7 Cells, lipids (amino acids, peptides, and proteins), Arachidonic acid, sense organs, human activities, Polyunsaturated fatty acid
Abstract: Polyunsaturated fatty acids (PUFA) are important components of cellular membranes, serving both structural and signaling functions. Investigation of the functional responses of cells to various PUFA often involves cell culture experiments, which can then inform or guide subsequent in vivo and clinical investigations. In this study, human carcinoma and leukemia cell lines (MCF-7, HepG2, THP-1, Jurkat) were incubated for 3 days in the presence of up to 150 μM of exogenous arachidonic or eicosapentaenoic acids. At concentrations up to 20 μM these PUFA were enriched in cellular phospholipids, but at concentrations of 20 μM or higher cells accumulated large quantities of these PUFA and their elongation products into triglycerides. This coincided with decreased cell proliferation and enhanced apoptosis. Inhibition of DGAT1 but not DGAT2 enhanced the cytotoxic effect of exogenous PUFA suggesting a protective role of PUFA sequestration into TGs. Lower (10 μM) and higher (50 μM) exogenous PUFA concentrations also had different impacts on the expression of PUFA metabolizing enzymes. Overall, these results indicate that caution must be exercised when planning in vitro experiments since elevated concentrations of PUFA can lead to dysfunctional cellular responses that are not predictive of in vivo responses to dietary PUFA.
Published: 2020
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16. 20-Hydroxy- and 20-carboxy-leukotriene (LT) B

Author: Anne-Sophie, Archambault, Samuel, Poirier, Julie-S, Lefebvre, Philippe-Pierre, Robichaud, Marie-Chantal, Larose, Caroline, Turcotte, Cyril, Martin, Véronique, Provost, Luc H, Boudreau, Patrick P, McDonald, Michel, Laviolette, Marc E, Surette, and Nicolas, Flamand
Subjects: Eosinophils, Eicosapentaenoic Acid, Neutrophils, Carboxylic Acids, Receptors, Leukotriene B4, Humans, Benzopyrans, Arachidonic Acids, Leukotriene B4
Abstract: Leukotriene B
Published: 2018

17. Autophagy and MHC-restricted antigen presentation

Author: Philippe Pierre, Bing Su, Catarina R. Almeida, Evelina Gatti, and Jan Valečka
Subjects: 0301 basic medicine, Immunology, Antigen presentation, chemical and pharmacologic phenomena, Major histocompatibility complex, Major Histocompatibility Complex, 03 medical and health sciences, 0302 clinical medicine, Cross-Priming, Antigen, MHC class I, Autophagy, Animals, Humans, Antigen-presenting cell, Molecular Biology, MHC class II, Antigen Presentation, biology, Antigen processing, Histocompatibility Antigens Class II, Dendritic cell, Cell biology, 030104 developmental biology, 030220 oncology & carcinogenesis, biology.protein, Lysosomes
Abstract: Major histocompatibility complex (MHC) molecules present peptide antigens to T lymphocytes and initiate immune responses. The peptides loaded onto MHC class I or MHC class II molecules can be derived from cytosolic proteins, both self and foreign. A variety of cellular processes, including endocytosis, vesicle trafficking, and autophagy, play critical roles in presentation of these antigens. We discuss the role of autophagy, a major intracellular degradation system that delivers cytoplasmic constituents to lysosomes in both MHC class I and II-restricted antigen presentation. We propose the new term "Type 2 cross-presentation" (CP2) to define the autophagy-dependent processes leading to MHC II-restricted presentation of intracellular antigens by professional antigen presenting cells. A better understanding of Type 2 cross-presentation may guide future efforts to control the immune system through autophagy manipulation.
Published: 2018

18. Protein synthesis regulation, a pillar of strength for innate immunity?

Author: Rafael J. Argüello, Evelina Gatti, Christian Rodriguez Rodrigues, and Philippe Pierre
Subjects: Immunology, Biology, Infections, Immune system, Immunity, Gene expression, Animals, Humans, Immunology and Allergy, Peptide Chain Initiation, Translational, Receptor, Cell Nucleus, Regulation of gene expression, Antigen Presentation, Innate immune system, TOR Serine-Threonine Kinases, Pattern recognition receptor, Immunity, Innate, Cell biology, Gene Expression Regulation, Protein Biosynthesis, Receptors, Pattern Recognition, Host-Pathogen Interactions, Signal transduction, Signal Transduction
Abstract: Recognition of pathogen derived molecules by Pattern Recognition Receptors (PRR) induces the production of cytokines (i.e. type I interferons) that stimulate the surrounding cells to transcribe and translate hundreds of genes, in order to prevent further infection and organize the immune response. Here, we report on the rising matter that metabolism sensing and gene expression control at the level of mRNA translation, allow swift responses that mobilize host defenses and coordinate innate responses to infection.
Published: 2015
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19. Guanabenz inhibits TLR9 signaling through a pathway that is independent of eIF2α dephosphorylation by the GADD34/PP1c complex

Author: Alexandre Dalet, Manuel A. S. Santos, Jessica Perego, Thien-Phong Vu Manh, Evelina Gatti, Alexis J. Combes, Lionel Spinelli, Nathalie Bardin, Clarisse Bourbon, Laurent Chiche, Andreia Mendes, Lionel Chasson, Philippe Pierre, Voahirana Camosseto, Hong Liu, Centre d'Immunologie de Marseille - Luminy (CIML), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU), Vascular research center of Marseille (VRCM), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire d'Immunologie [Hôpital de la Conception - APHM], Assistance Publique - Hôpitaux de Marseille (APHM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Hôpital de la Conception [CHU - APHM] (LA CONCEPTION )-Centre National de la Recherche Scientifique (CNRS), Centre recherche en CardioVasculaire et Nutrition (C2VN), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Hôpital Européen [Fondation Ambroise Paré - Marseille], Institute for Research in Biomedicine ( iBiMED), Universidade de Aveiro, Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Assistance Publique - Hôpitaux de Marseille (APHM)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Hôpital de la Conception [CHU - APHM] (LA CONCEPTION)-Centre National de la Recherche Scientifique (CNRS), Centre recherche en CardioVasculaire et Nutrition = Center for CardioVascular and Nutrition research (C2VN), and Institut National de la Santé et de la Recherche Médicale (INSERM)-Aix Marseille Université (AMU)
Subjects: Male, 0301 basic medicine, CpG Oligodeoxynucleotide, medicine.medical_treatment, [SDV]Life Sciences [q-bio], Eukaryotic Initiation Factor-2, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Biochemistry, Proinflammatory cytokine, Mice, 03 medical and health sciences, 0302 clinical medicine, Immune system, Protein Phosphatase 1, medicine, Animals, Humans, Lupus Erythematosus, Systemic, Phosphorylation, Molecular Biology, Antihypertensive Agents, Cells, Cultured, ComputingMilieux_MISCELLANEOUS, Guanabenz, Chemistry, Liver Diseases, Endoplasmic reticulum, TLR9, Dendritic Cells, Cell Biology, Endoplasmic Reticulum Stress, 3. Good health, Cell biology, Mice, Inbred C57BL, 030104 developmental biology, Cytokine, Gene Expression Regulation, Toll-Like Receptor 9, 030220 oncology & carcinogenesis, Unfolded protein response, [SDV.IMM]Life Sciences [q-bio]/Immunology, medicine.drug
Abstract: Endoplasmic reticulum (ER) stress triggers or amplifies inflammatory signals and cytokine production in immune cells. Upon the resolution of ER stress, the inducible phosphatase 1 cofactor GADD34 promotes the dephosphorylation of the initiation factor eIF2α, thereby enabling protein translation to resume. Several aminoguanidine compounds, such as guanabenz, perturb the eIF2α phosphorylation-dephosphorylation cycle and protect different cell or tissue types from protein misfolding and degeneration. We investigated how pharmacological interference with the eIF2α pathway could be beneficial to treat autoinflammatory diseases dependent on proinflammatory cytokines and type I interferons (IFNs), the production of which is regulated by GADD34 in dendritic cells (DCs). In mouse and human DCs and B cells, guanabenz prevented the activation of Toll-like receptor 9 (TLR9) by CpG oligodeoxynucleotides or DNA-immunoglobulin complexes in endosomes. In vivo, guanabenz protected mice from CpG oligonucleotide-dependent cytokine shock and decreased autoimmune symptom severity in a chemically induced model of systemic lupus erythematosus. However, we found that guanabenz exerted its inhibitory effect independently of GADD34 activity on eIF2α and instead decreased the abundance of CH25H, a cholesterol hydroxylase linked to antiviral immunity. Our results therefore suggest that guanabenz and similar compounds could be used to treat type I IFN-dependent pathologies and that CH25H could be a therapeutic target to control these diseases. published
Published: 2018
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20. Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Author: Daniel J. Klionsky, Kotb Abdelmohsen, Akihisa Abe, Md Joynal Abedin, Hagai Abeliovich, Abraham Acevedo Arozena, Hiroaki Adachi, Christopher M. Adams, Peter D. Adams, Khosrow Adeli, Peter J. Adhihetty, Sharon G. Adler, Galila Agam, Rajesh Agarwal, Manish K. Aghi, Maria Agnello, Patrizia Agostinis, Patricia V. Aguilar, Julio Aguirre Ghiso, Edoardo M. Airoldi, Slimane Ait Si Ali, Takahiko Akematsu, Emmanuel T. Akporiaye, Mohamed Al Rubeai, Guillermo M. Albaiceta, Chris Albanese, Diego Albani, Matthew L. Albert, Jesus Aldudo, Hana Algül, Mehrdad Alirezaei, Iraide Alloza, Alexandru Almasan, Maylin Almonte Beceril, Emad S. Alnemri, Covadonga Alonso, Nihal Altan Bonnet, Dario C. Altieri, Silvia Alvarez, Lydia Alvarez Erviti, Sandro Alves, Giuseppina Amadoro, Atsuo Amano, Consuelo Amantini, Santiago Ambrosio, Ivano Amelio, Amal O. Amer, Mohamed Amessou, Angelika Amon, Zhenyi An, Frank A. Anania, Stig U. Andersen, Usha P. Andley, Catherine K. Andreadi, Nathalie Andrieu Abadie, Alberto Anel, David K. Ann, Shailendra Anoopkumar Dukie, Manuela Antonioli, Hiroshi Aoki, Nadezda Apostolova, Saveria Aquila, Katia Aquilano, Koichi Araki, Eli Arama, Agustin Aranda, Jun Araya, Alexandre Arcaro, Esperanza Arias, Hirokazu Arimoto, Aileen R. Ariosa, Jane L. Armstrong, Thierry Arnould, Ivica Arsov, Katsuhiko Asanuma, Valerie Askanas, Eric Asselin, Ryuichiro Atarashi, Sally S. Atherton, Julie D. Atkin, Laura D. Attardi, Patrick Auberger, Georg Auburger, Laure Aurelian, Riccardo Autelli, Laura Avagliano, Maria Laura Avantaggiati, Limor Avrahami, Suresh Awale, Neelam Azad, Tiziana Bachetti, Jonathan M. Backer, Dong Hun Bae, Jae sung Bae, Ok Nam Bae, Soo Han Bae, Eric H. Baehrecke, Seung Hoon Baek, Stephen Baghdiguian, Agnieszka Bagniewska Zadworna, Hua Bai, Jie Bai, Xue Yuan Bai, Yannick Bailly, Kithiganahalli Narayanaswamy Balaji, Walter Balduini, Andrea Ballabio, Rena Balzan, Rajkumar Banerjee, Gábor Bánhegyi, Haijun Bao, Benoit Barbeau, Maria D. Barrachina, Esther Barreiro, Bonnie Bartel, Alberto Bartolomé, Diane C. Bassham, Maria Teresa Bassi, Robert C. Bast Jr, Alakananda Basu, Maria Teresa Batista, Henri Batoko, Maurizio Battino, Kyle Bauckman, Bradley L. Baumgarner, K. Ulrich Bayer, Rupert Beale, Jean François Beaulieu, George R. Beck Jr, Christoph Becker, J. David Beckham, Pierre André Bédard, Patrick J. Bednarski, Thomas J. Begley, Christian Behl, Christian Behrends, Georg MN Behrens, Kevin E. Behrns, Eloy Bejarano, Amine Belaid, Francesca Belleudi, Giovanni Bénard, Guy Berchem, Daniele Bergamaschi, Matteo Bergami, Ben Berkhout, Laura Berliocchi, Amélie Bernard, Monique Bernard, Francesca Bernassola, Anne Bertolotti, Amanda S. Bess, Sébastien Besteiro, Saverio Bettuzzi, Savita Bhalla, Shalmoli Bhattacharyya, Sujit K. Bhutia, Caroline Biagosch, Michele Wolfe Bianchi, Martine Biard Piechaczyk, Viktor Billes, Claudia Bincoletto, Baris Bingol, Sara W. Bird, Marc Bitoun, Ivana Bjedov, Craig Blackstone, Lionel Blanc, Guillermo A. Blanco, Heidi Kiil Blomhoff, Emilio Boada Romero, Stefan Böckler, Marianne Boes, Kathleen Boesze Battaglia, Lawrence H. Boise, Alessandra Bolino, Andrea Boman, Paolo Bonaldo, Matteo Bordi, Jürgen Bosch, Luis M. Botana, Joelle Botti, German Bou, Marina Bouché, Marion Bouchecareilh, Marie Josée Boucher, Michael E. Boulton, Sebastien G. Bouret, Patricia Boya, Michaël Boyer Guittaut, Peter V. Bozhkov, Nathan Brady, Vania MM Braga, Claudio Brancolini, Gerhard H. Braus, José M. Bravo San Pedro, Lisa A. Brennan, Emery H. Bresnick, Patrick Brest, Dave Bridges, MarieAgnès Bringer, Marisa Brini, Glauber C. Brito, Bertha Brodin, Paul S. Brookes, Eric J. Brown, Karen Brown, Hal E. Broxmeyer, Alain Bruhat, Patricia Chakur Brum, John H. Brumell, Nicola Brunetti Pierri, Robert J. Bryson Richardson, Shilpa Buch, Alastair M. Buchan, Hikmet Budak, Dmitry V. Bulavin, Scott J. Bultman, Geert Bultynck, Vladimir Bumbasirevic, Yan Burelle, Robert E. Burke, Margit Burmeister, Peter Bütikofer, Laura Caberlotto, Ken Cadwell, Monika Cahova, Dongsheng Cai, Jingjing Cai, Qian Cai, Sara Calatayud, Nadine Camougrand, Michelangelo Campanella, Grant R. Campbell, Matthew Campbell, Silvia Campello, Robin Candau, Isabella Caniggia, Lavinia Cantoni, Lizhi Cao, Allan B. Caplan, Michele Caraglia, Claudio Cardinali, Sandra Morais Cardoso, Jennifer S. Carew, Laura A. Carleton, Cathleen R. Carlin, Silvia Carloni, Sven R. Carlsson, Didac Carmona Gutierrez, Leticia AM Carneiro, Oliana Carnevali, Serena Carra, Alice Carrier, Bernadette Carroll, Caty Casas, Josefina Casas, Giuliana Cassinelli, Perrine Castets, Susana Castro Obregon, Gabriella Cavallini, Isabella Ceccherini, Francesco Cecconi, Arthur I. Cederbaum, Valentín Ceña, Simone Cenci, Claudia Cerella, Davide Cervia, CETRULLO, SILVIA, Hassan Chaachouay, Han Jung Chae, Andrei S. Chagin, Chee Yin Chai, Gopal Chakrabarti, Georgios Chamilos, Edmond YW Chan, Matthew TV Chan, Dhyan Chandra, Pallavi Chandra, Chih Peng Chang, Raymond Chuen Chung Chang, Ta Yuan Chang, John C. Chatham, Saurabh Chatterjee, Santosh Chauhan, Yongsheng Che, Michael E. Cheetham, Rajkumar Cheluvappa, Chun Jung Chen, Gang Chen, Guang Chao Chen, Guoqiang Chen, Hongzhuan Chen, Jeff W. Chen, Jian Kang Chen, Min Chen, Mingzhou Chen, Peiwen Chen, Qi Chen, Quan Chen, Shang Der Chen, Si Chen, Steve S. L. Chen, Wei Chen, Wei Jung Chen, Wen Qiang Chen, Wenli Chen, Xiangmei Chen, Yau Hung Chen, Ye Guang Chen, Yin Chen, Yingyu Chen, Yongshun Chen, Yu Jen Chen, Yue Qin Chen, Yujie Chen, Zhen Chen, Zhong Chen, Alan Cheng, Christopher HK Cheng, Hua Cheng, Heesun Cheong, Sara Cherry, Jason Chesney, Chun Hei Antonio Cheung, Eric Chevet, Hsiang Cheng Chi, Sung Gil Chi, Fulvio Chiacchiera, Hui Ling Chiang, Roberto Chiarelli, Mario Chiariello, Marcello Chieppa, Lih Shen Chin, Mario Chiong, Gigi NC Chiu, Dong Hyung Cho, Ssang Goo Cho, William C. Cho, Yong Yeon Cho, Young Seok Cho, Augustine MK Choi, Eui Ju Choi, Eun Kyoung Choi, Jayoung Choi, Mary E. Choi, Seung Il Choi, Tsui Fen Chou, Salem Chouaib, Divaker Choubey, Vinay Choubey, Kuan Chih Chow, Kamal Chowdhury, Charleen T. Chu, Tsung Hsien Chuang, Taehoon Chun, Hyewon Chung, Taijoon Chung, Yuen Li Chung, Yong Joon Chwae, Valentina Cianfanelli, Roberto Ciarcia, Iwona A. Ciechomska, Maria Rosa Ciriolo, Mara Cirone, Sofie Claerhout, Michael J. Clague, Joan Clària, Peter GH Clarke, Robert Clarke, Emilio Clementi, Cédric Cleyrat, Miriam Cnop, Eliana M. Coccia, Tiziana Cocco, Patrice Codogno, Jörn Coers, Ezra EW Cohen, David Colecchia, Luisa Coletto, Núria S. Coll, Emma Colucci Guyon, Sergio Comincini, Maria Condello, Katherine L. Cook, Graham H. Coombs, Cynthia D. Cooper, J. Mark Cooper, Isabelle Coppens, Maria Tiziana Corasaniti, Marco Corazzari, Ramon Corbalan, Elisabeth Corcelle Termeau, Mario D. Cordero, Cristina Corral Ramos, Olga Corti, Andrea Cossarizza, Paola Costelli, Safia Costes, Susan L. Cotman, Ana Coto Montes, Sandra Cottet, Eduardo Couve, Lori R. Covey, L. Ashley Cowart, Jeffery S. Cox, Fraser P. Coxon, Carolyn B. Coyne, Mark S. Cragg, Rolf J. Craven, Tiziana Crepaldi, Jose L. Crespo, Alfredo Criollo, Valeria Crippa, Maria Teresa Cruz, Ana Maria Cuervo, Jose M. Cuezva, Taixing Cui, Pedro R. Cutillas, Mark J. Czaja, Maria F. Czyzyk Krzeska, Ruben K. Dagda, Uta Dahmen, Chunsun Dai, Wenjie Dai, Yun Dai, Kevin N. Dalby, Luisa Dalla Valle, Guillaume Dalmasso, Marcello D'Amelio, Markus Damme, Arlette Darfeuille Michaud, Catherine Dargemont, Victor M. Darley Usmar, Srinivasan Dasarathy, Biplab Dasgupta, Srikanta Dash, Crispin R. Dass, Hazel Marie Davey, Lester M. Davids, David Dávila, Roger J. Davis, Ted M. Dawson, Valina L. Dawson, Paula Daza, Jackie de Belleroche, Paul de Figueiredo, Regina Celia Bressan Queiroz de Figueiredo, José de la Fuente, Luisa De Martino, Antonella De Matteis, Guido RY De Meyer, Angelo De Milito, Mauro De Santi, Wanderley de Souza, Vincenzo De Tata, Daniela De Zio, Jayanta Debnath, Reinhard Dechant, Jean Paul Decuypere, Shane Deegan, Benjamin Dehay, Barbara Del Bello, Dominic P. Del Re, Régis Delage Mourroux, Lea MD Delbridge, Louise Deldicque, Elizabeth Delorme Axford, Yizhen Deng, Joern Dengjel, Melanie Denizot, Paul Dent, Channing J. Der, Vojo Deretic, Benoît Derrien, Eric Deutsch, Timothy P. Devarenne, Rodney J. Devenish, Sabrina Di Bartolomeo, Nicola Di Daniele, Fabio Di Domenico, Alessia Di Nardo, Simone Di Paola, Antonio Di Pietro, Livia Di Renzo, Aaron DiAntonio, Guillermo Díaz Araya, Ines Díaz Laviada, Maria T. Diaz Meco, Javier Diaz Nido, Chad A. Dickey, Robert C. Dickson, Marc Diederich, Paul Digard, Ivan Dikic, Savithrama P. Dinesh Kumar, Chan Ding, Wen Xing Ding, Zufeng Ding, Luciana Dini, Jörg HW Distler, Abhinav Diwan, Mojgan Djavaheri Mergny, Kostyantyn Dmytruk, Renwick CJ Dobson, Volker Doetsch, Karol Dokladny, Svetlana Dokudovskaya, Massimo Donadelli, X. Charlie Dong, Xiaonan Dong, Zheng Dong, Terrence M. Donohue Jr, Kelly S. Doran, Gabriella D'Orazi, Gerald W. Dorn II, Victor Dosenko, Sami Dridi, Liat Drucker, Jie Du, Li Lin Du, Lihuan Du, André du Toit, Priyamvada Dua, Lei Duan, Pu Duann, Vikash Kumar Dubey, Michael R. Duchen, Michel A. Duchosal, Helene Duez, Isabelle Dugail, Verónica I. Dumit, Mara C. Duncan, Elaine A. Dunlop, William A. Dunn Jr, Nicolas Dupont, Luc Dupuis, Raúl V. Durán, Thomas M. Durcan, Stéphane Duvezin Caubet, Umamaheswar Duvvuri, Vinay Eapen, Darius Ebrahimi Fakhari, Arnaud Echard, Leopold Eckhart, Charles L. Edelstein, Aimee L. Edinger, Ludwig Eichinger, Tobias Eisenberg, Avital Eisenberg Lerner, N. Tony Eissa, Wafik S. El Deiry, Victoria El Khoury, Zvulun Elazar, Hagit Eldar Finkelman, Chris JH Elliott, Enzo Emanuele, Urban Emmenegger, Nikolai Engedal, Anna Mart Engelbrecht, Simone Engelender, Jorrit M. Enserink, Ralf Erdmann, Jekaterina Erenpreisa, Rajaraman Eri, Jason L. Eriksen, Andreja Erman, Ricardo Escalante, Eeva Liisa Eskelinen, Lucile Espert, Lorena Esteban Martínez, Thomas J. Evans, Mario Fabri, Gemma Fabrias, Cinzia Fabrizi, Antonio Facchiano, Nils J. Færgeman, Alberto Faggioni, W. Douglas Fairlie, Chunhai Fan, Daping Fan, Jie Fan, Shengyun Fang, Manolis Fanto, Alessandro Fanzani, Thomas Farkas, Mathias Faure, Francois B. Favier, Howard Fearnhead, Massimo Federici, Erkang Fei, Tania C. Felizardo, Hua Feng, Yibin Feng, Yuchen Feng, Thomas A. Ferguson, Álvaro F. Fernández, Maite G. Fernandez Barrena, Jose C. Fernandez Checa, Arsenio Fernández López, Martin E. Fernandez Zapico, Olivier Feron, Elisabetta Ferraro, Carmen Veríssima Ferreira Halder, Laszlo Fesus, Ralph Feuer, Fabienne C. Fiesel, Eduardo C. Filippi Chiela, Giuseppe Filomeni, Gian Maria Fimia, John H. Fingert, Steven Finkbeiner, Toren Finkel, Filomena Fiorito, Paul B. Fisher, Marc Flajolet, FLAMIGNI, FLAVIO, Oliver Florey, Salvatore Florio, R. Andres Floto, Marco Folini, Carlo Follo, Edward A. Fon, Francesco Fornai, Franco Fortunato, Alessandro Fraldi, Rodrigo Franco, Arnaud Francois, Aurélie François, Lisa B. Frankel, Iain DC Fraser, Norbert Frey, Damien G. Freyssenet, Christian Frezza, Scott L. Friedman, Daniel E. Frigo, Dongxu Fu, José M. Fuentes, Juan Fueyo, Yoshio Fujitani, Yuuki Fujiwara, Mikihiro Fujiya, Mitsunori Fukuda, Simone Fulda, Carmela Fusco, Bozena Gabryel, Matthias Gaestel, Philippe Gailly, Malgorzata Gajewska, Sehamuddin Galadari, Gad Galili, Inmaculada Galindo, Maria F. Galindo, Giovanna Galliciotti, Lorenzo Galluzzi, Luca Galluzzi, Vincent Galy, Noor Gammoh, Sam Gandy, Anand K. Ganesan, Swamynathan Ganesan, Ian G. Ganley, Monique Gannagé, Fen Biao Gao, Feng Gao, Jian Xin Gao, Lorena García Nannig, Eleonora García Véscovi, Marina Garcia Macía, Carmen Garcia Ruiz, Abhishek D. Garg, Pramod Kumar Garg, Ricardo Gargini, Nils Christian Gassen, Damián Gatica, Evelina Gatti, Julie Gavard, Evripidis Gavathiotis, Liang Ge, Pengfei Ge, Shengfang Ge, Po Wu Gean, Vania Gelmetti, Armando A. Genazzani, Jiefei Geng, Pascal Genschik, Lisa Gerner, Jason E. Gestwicki, David A. Gewirtz, Saeid Ghavami, Eric Ghigo, Debabrata Ghosh, Anna Maria Giammarioli, Francesca Giampieri, Claudia Giampietri, Alexandra Giatromanolaki, Derrick J. Gibbings, Lara Gibellini, Spencer B. Gibson, Vanessa Ginet, Antonio Giordano, Flaviano Giorgini, Elisa Giovannetti, Stephen E. Girardin, Suzana Gispert, Sandy Giuliano, Candece L. Gladson, Alvaro Glavic, Martin Gleave, Nelly Godefroy, Robert M. Gogal Jr, Kuppan Gokulan, Gustavo H. Goldman, Delia Goletti, Michael S. Goligorsky, Aldrin V. Gomes, Ligia C. Gomes, Hernando Gomez, Candelaria Gomez Manzano, Rubén Gómez Sánchez, Dawit AP Gonçalves, Ebru Goncu, Qingqiu Gong, Céline Gongora, Carlos B. Gonzalez, Pedro Gonzalez Alegre, Pilar Gonzalez Cabo, Rosa Ana González Polo, Ing Swie Goping, Carlos Gorbea, Nikolai V. Gorbunov, Daphne R. Goring, Adrienne M. Gorman, Sharon M. Gorski, Sandro Goruppi, Shino Goto Yamada, Cecilia Gotor, Roberta A. Gottlieb, Illana Gozes, Devrim Gozuacik, Yacine Graba, Martin Graef, Giovanna E. Granato, Gary Dean Grant, Steven Grant, Giovanni Luca Gravina, Douglas R. Green, Alexander Greenhough, Michael T. Greenwood, Benedetto Grimaldi, Frédéric Gros, Charles Grose, Jean Francois Groulx, Florian Gruber, Paolo Grumati, Tilman Grune, Jun Lin Guan, Kun Liang Guan, Barbara Guerra, Carlos Guillen, Kailash Gulshan, Jan Gunst, Chuanyong Guo, Lei Guo, Ming Guo, Wenjie Guo, Xu Guang Guo, Andrea A. Gust, Åsa B. Gustafsson, Elaine Gutierrez, Maximiliano G. Gutierrez, Ho Shin Gwak, Albert Haas, James E. Haber, Shinji Hadano, Monica Hagedorn, David R. Hahn, Andrew J. Halayko, Anne Hamacher Brady, Kozo Hamada, Ahmed Hamai, Andrea Hamann, Maho Hamasaki, Isabelle Hamer, Qutayba Hamid, Ester M. Hammond, Feng Han, Weidong Han, James T. Handa, John A. Hanover, Malene Hansen, Masaru Harada, Ljubica Harhaji Trajkovic, J. Wade Harper, Abdel Halim Harrath, Adrian L. Harris, James Harris, Udo Hasler, Peter Hasselblatt, Kazuhisa Hasui, Robert G. Hawley, Teresa S. Hawley, Congcong He, Cynthia Y. He, Fengtian He, Gu He, Rong Rong He, Xian Hui He, You Wen He, Yu Ying He, Joan K. Heath, Marie Josée Hébert, Robert A. Heinzen, Gudmundur Vignir Helgason, Michael Hensel, Elizabeth P. Henske, Chengtao Her, Paul K. Herman, Agustín Hernández, Carlos Hernandez, Sonia Hernández Tiedra, Claudio Hetz, P. Robin Hiesinger, Katsumi Higaki, Sabine Hilfiker, Bradford G. Hill, Joseph A. Hill, William D. Hill, Keisuke Hino, Daniel Hofius, Paul Hofman, Günter U. Höglinger, Jörg Höhfeld, Marina K. Holz, Yonggeun Hong, David A. Hood, Jeroen JM Hoozemans, Thorsten Hoppe, Chin Hsu, Chin Yuan Hsu, Li Chung Hsu, Dong Hu, Guochang Hu, Hong Ming Hu, Hongbo Hu, Ming Chang Hu, Yu Chen Hu, Zhuo Wei Hu, Fang Hua, Ya Hua, Canhua Huang, Huey Lan Huang, Kuo How Huang, Kuo Yang Huang, Shile Huang, Shiqian Huang, Wei Pang Huang, Yi Ran Huang, Yong Huang, Yunfei Huang, Tobias B. Huber, Patricia Huebbe, Won Ki Huh, Juha J. Hulmi, Gang Min Hur, James H. Hurley, Zvenyslava Husak, Sabah NA Hussain, Salik Hussain, Jung Jin Hwang, Seungmin Hwang, Thomas IS Hwang, Atsuhiro Ichihara, Yuzuru Imai, Carol Imbriano, Megumi Inomata, Takeshi Into, Valentina Iovane, Juan L. Iovanna, Renato V. Iozzo, Nancy Y. Ip, Javier E. Irazoqui, Pablo Iribarren, Yoshitaka Isaka, Aleksandra J. Isakovic, Harry Ischiropoulos, Jeffrey S. Isenberg, Mohammad Ishaq, Hiroyuki Ishida, Isao Ishii, Jane E. Ishmael, Ciro Isidoro, Ken ichi Isobe, Erika Isono, Shohreh Issazadeh Navikas, Koji Itahana, Eisuke Itakura, Andrei I. Ivanov, Anand Krishnan V. Iyer, José M. Izquierdo, Yotaro Izumi, Valentina Izzo, Marja Jäättelä, Nadia Jaber, Daniel John Jackson, William T. Jackson, Tony George Jacob, Thomas S. Jacques, Chinnaswamy Jagannath, Ashish Jain, Nihar Ranjan Jana, Byoung Kuk Jang, Alkesh Jani, Bassam Janji, Paulo Roberto Jannig, Patric J. Jansson, Steve Jean, Marina Jendrach, Ju Hong Jeon, Niels Jessen, Eui Bae Jeung, Kailiang Jia, Lijun Jia, Hong Jiang, Hongchi Jiang, Liwen Jiang, Teng Jiang, Xiaoyan Jiang, Xuejun Jiang, Ying Jiang, Yongjun Jiang, Alberto Jiménez, Cheng Jin, Hongchuan Jin, Lei Jin, Meiyan Jin, Shengkan Jin, Umesh Kumar Jinwal, Eun Kyeong Jo, Terje Johansen, Daniel E. Johnson, Gail VW Johnson, James D. Johnson, Eric Jonasch, Chris Jones, Leo AB Joosten, Joaquin Jordan, Anna Maria Joseph, Bertrand Joseph, Annie M. Joubert, Dianwen Ju, Jingfang Ju, Hsueh Fen Juan, Katrin Juenemann, Gábor Juhász, Hye Seung Jung, Jae U. Jung, Yong Keun Jung, Heinz Jungbluth, Matthew J. Justice, Barry Jutten, Nadeem O. Kaakoush, Kai Kaarniranta, Allen Kaasik, Tomohiro Kabuta, Bertrand Kaeffer, Katarina Kågedal, Alon Kahana, Shingo Kajimura, Or Kakhlon, Manjula Kalia, Dhan V. Kalvakolanu, Yoshiaki Kamada, Konstantinos Kambas, Vitaliy O. Kaminskyy, Harm H. Kampinga, Mustapha Kandouz, Chanhee Kang, Rui Kang, Tae Cheon Kang, Tomotake Kanki, Thirumala Devi Kanneganti, Haruo Kanno, Anumantha G. Kanthasamy, Marc Kantorow, Maria Kaparakis Liaskos, Orsolya Kapuy, Vassiliki Karantza, Md Razaul Karim, Parimal Karmakar, Arthur Kaser, Susmita Kaushik, Thomas Kawula, A. Murat Kaynar, Po Yuan Ke, Zun Ji Ke, John H. Kehrl, Kate E. Keller, Jongsook Kim Kemper, Anne K. Kenworthy, Oliver Kepp, Andreas Kern, Santosh Kesari, David Kessel, Robin Ketteler, Isis do Carmo Kettelhut, Bilon Khambu, Muzamil Majid Khan, Vinoth KM Khandelwal, Sangeeta Khare, Juliann G. Kiang, Amy A. Kiger, Akio Kihara, Arianna L. Kim, Cheol Hyeon Kim, Deok Ryong Kim, Do Hyung Kim, Eung Kweon Kim, Hye Young Kim, Hyung Ryong Kim, Jae Sung Kim, Jeong Hun Kim, Jin Cheon Kim, Jin Hyoung Kim, Kwang Woon Kim, Michael D. Kim, Moon Moo Kim, Peter K. Kim, Seong Who Kim, Soo Youl Kim, Yong Sun Kim, Yonghyun Kim, Adi Kimchi, Alec C. Kimmelman, Tomonori Kimura, Jason S. King, Karla Kirkegaard, Vladimir Kirkin, Lorrie A. Kirshenbaum, Shuji Kishi, Yasuo Kitajima, Katsuhiko Kitamoto, Yasushi Kitaoka, Kaio Kitazato, Rudolf A. Kley, Walter T. Klimecki, Michael Klinkenberg, Jochen Klucken, Helene Knævelsrud, Erwin Knecht, Laura Knuppertz, Jiunn Liang Ko, Satoru Kobayashi, Jan C. Koch, Christelle Koechlin Ramonatxo, Ulrich Koenig, Young Ho Koh, Katja Köhler, Sepp D. Kohlwein, Masato Koike, Masaaki Komatsu, Eiki Kominami, Dexin Kong, Hee Jeong Kong, Eumorphia G. Konstantakou, Benjamin T. Kopp, Tamas Korcsmaros, Laura Korhonen, Viktor I. Korolchuk, Nadya V. Koshkina, Yanjun Kou, Michael I. Koukourakis, Constantinos Koumenis, Attila L. Kovács, Tibor Kovács, Werner J. Kovacs, Daisuke Koya, Claudine Kraft, Dimitri Krainc, Helmut Kramer, Tamara Kravic Stevovic, Wilhelm Krek, Carole Kretz Remy, Roswitha Krick, Malathi Krishnamurthy, Janos Kriston Vizi, Guido Kroemer, Michael C. Kruer, Rejko Kruger, Nicholas T. Ktistakis, Kazuyuki Kuchitsu, Christian Kuhn, Addanki Pratap Kumar, Anuj Kumar, Ashok Kumar, Deepak Kumar, Dhiraj Kumar, Rakesh Kumar, Sharad Kumar, Mondira Kundu, Hsing Jien Kung, Atsushi Kuno, Sheng Han Kuo, Jeff Kuret, Tino Kurz, Terry Kwok, Taeg Kyu Kwon, Yong Tae Kwon, Irene Kyrmizi, Albert R. La Spada, Frank Lafont, Tim Lahm, Aparna Lakkaraju, Truong Lam, Trond Lamark, Steve Lancel, Terry H. Landowski, Darius JR Lane, Jon D. Lane, Cinzia Lanzi, Pierre Lapaquette, Louis R. Lapierre, Jocelyn Laporte, Johanna Laukkarinen, Gordon W. Laurie, Sergio Lavandero, Lena Lavie, Matthew J. LaVoie, Betty Yuen Kwan Law, Helen Ka wai Law, Kelsey B. Law, Robert Layfield, Pedro A. Lazo, Laurent Le Cam, Karine G. Le Roch, Hervé Le Stunff, Vijittra Leardkamolkarn, Marc Lecuit, Byung Hoon Lee, Che Hsin Lee, Erinna F. Lee, Gyun Min Lee, He Jin Lee, Hsinyu Lee, Jae Keun Lee, Jongdae Lee, Juhyun Lee, Jun Hee Lee, Michael Lee, Myung Shik Lee, Patty J. Lee, Sam W. Lee, Seung Jae Lee, Shiow Ju Lee, Stella Y. Lee, Sug Hyung Lee, Sung Sik Lee, Sung Joon Lee, Sunhee Lee, Ying Ray Lee, Yong J. Lee, Young H. Lee, Christiaan Leeuwenburgh, Sylvain Lefort, Renaud Legouis, Jinzhi Lei, Qun Ying Lei, David A. Leib, Gil Leibowitz, Istvan Lekli, Stéphane D. Lemaire, John J. Lemasters, Marius K. Lemberg, Antoinette Lemoine, Shuilong Leng, Guido Lenz, Paola Lenzi, Lilach O. Lerman, Daniele Lettieri Barbato, Julia I. Ju Leu, Hing Y. Leung, Beth Levine, Patrick A. Lewis, Frank Lezoualc'h, Chi Li, Faqiang Li, Feng Jun Li, Jun Li, Ke Li, Lian Li, Min Li, Qiang Li, Rui Li, Sheng Li, Wei Li, Xiaotao Li, Yumin Li, Jiqin Lian, Chengyu Liang, Qiangrong Liang, Yulin Liao, Joana Liberal, Pawel P. Liberski, Pearl Lie, Andrew P. Lieberman, Hyunjung Jade Lim, Kah Leong Lim, Kyu Lim, Raquel T. Lima, Chang Shen Lin, Chiou Feng Lin, Fang Lin, Fangming Lin, Fu Cheng Lin, Kui Lin, Kwang Huei Lin, Pei Hui Lin, Tianwei Lin, Wan Wan Lin, Yee Shin Lin, Yong Lin, Rafael Linden, Dan Lindholm, Lisa M. Lindqvist, Paul Lingor, Andreas Linkermann, Lance A. Liotta, Marta M. Lipinski, Vitor A. Lira, Michael P. Lisanti, Paloma B. Liton, Bo Liu, Chong Liu, Chun Feng Liu, Fei Liu, Hung Jen Liu, Jianxun Liu, Jing Jing Liu, Jing Lan Liu, Ke Liu, Leyuan Liu, Liang Liu, Quentin Liu, Rong Yu Liu, Shiming Liu, Shuwen Liu, Wei Liu, Xian De Liu, Xiangguo Liu, Xiao Hong Liu, Xinfeng Liu, Xu Liu, Xueqin Liu, Yang Liu, Yule Liu, Zexian Liu, Zhe Liu, Juan P. Liuzzi, Gérard Lizard, Mila Ljujic, Irfan J. Lodhi, Susan E. Logue, Bal L. Lokeshwar, Yun Chau Long, Sagar Lonial, Benjamin Loos, Carlos López Otín, Cristina López Vicario, Mar Lorente, Philip L. Lorenzi, Péter Lõrincz, Marek Los, Michael T. Lotze, Penny E. Lovat, Binfeng Lu, Bo Lu, Jiahong Lu, Qing Lu, She Min Lu, Shuyan Lu, Yingying Lu, Frédéric Luciano, Shirley Luckhart, John Milton Lucocq, Paula Ludovico, Aurelia Lugea, Nicholas W. Lukacs, Julian J. Lum, Anders H. Lund, Honglin Luo, Jia Luo, Shouqing Luo, Claudio Luparello, Timothy Lyons, Jianjie Ma, Yi Ma, Yong Ma, Zhenyi Ma, Juliano Machado, Glaucia M. Machado Santelli, Fernando Macian, Gustavo C. MacIntosh, Jeffrey P. MacKeigan, Kay F. Macleod, John D. MacMicking, Lee Ann MacMillan Crow, Frank Madeo, Muniswamy Madesh, Julio Madrigal Matute, Akiko Maeda, Tatsuya Maeda, Gustavo Maegawa, Emilia Maellaro, Hannelore Maes, Marta Magariños, Kenneth Maiese, Tapas K. Maiti, Luigi Maiuri, Maria Chiara Maiuri, Carl G. Maki, Roland Malli, Walter Malorni, Alina Maloyan, Fathia Mami Chouaib, Na Man, Joseph D. Mancias, Eva Maria Mandelkow, Michael A. Mandell, Angelo A. Manfredi, Serge N. Manié, Claudia Manzoni, Kai Mao, Zixu Mao, Zong Wan Mao, Philippe Marambaud, Anna Maria Marconi, Zvonimir Marelja, Gabriella Marfe, Marta Margeta, Eva Margittai, Muriel Mari, Francesca V. Mariani, Concepcio Marin, Sara Marinelli, Guillermo Mariño, Ivanka Markovic, Rebecca Marquez, MARTELLI, ALBERTO MARIA, Sascha Martens, Katie R. Martin, Seamus J. Martin, Shaun Martin, Miguel A. Martin Acebes, Paloma Martín Sanz, Camille Martinand Mari, Wim Martinet, Jennifer Martinez, Nuria Martinez Lopez, Ubaldo Martinez Outschoorn, Moisés Martínez Velázquez, Marta Martinez Vicente, Waleska Kerllen Martins, Hirosato Mashima, James A. Mastrianni, Giuseppe Matarese, Paola Matarrese, Roberto Mateo, Satoaki Matoba, Naomichi Matsumoto, Takehiko Matsushita, Akira Matsuura, Takeshi Matsuzawa, Mark P. Mattson, Soledad Matus, Norma Maugeri, Caroline Mauvezin, Andreas Mayer, Dusica Maysinger, Guillermo D. Mazzolini, Mary Kate McBrayer, Kimberly McCall, Craig McCormick, Gerald M. McInerney, Skye C. McIver, Sharon McKenna, John J. McMahon, Iain A. McNeish, Fatima Mechta Grigoriou, Jan Paul Medema, Diego L. Medina, Klara Megyeri, Maryam Mehrpour, Jawahar L. Mehta, Yide Mei, Ute Christiane Meier, Alfred J. Meijer, Alicia Meléndez, Gerry Melino, Sonia Melino, Edesio Jose Tenorio de Melo, Maria A. Mena, Marc D. Meneghini, Javier A. Menendez, Regina Menezes, Liesu Meng, Ling hua Meng, Songshu Meng, Rossella Menghini, A. Sue Menko, Rubem FS Menna Barreto, Manoj B. Menon, Marco A. Meraz Ríos, Giuseppe Merla, Luciano Merlini, Angelica M. Merlot, Andreas Meryk, Stefania Meschini, Joel N. Meyer, Man tian Mi, Chao Yu Miao, Lucia Micale, Simon Michaeli, Carine Michiels, FRANCO MIGLIACCIO, ANNA RITA, Anastasia Susie Mihailidou, Dalibor Mijaljica, Katsuhiko Mikoshiba, Enrico Milan, Leonor Miller Fleming, Gordon B. Mills, Ian G. Mills, Georgia Minakaki, Berge A. Minassian, Xiu Fen Ming, Farida Minibayeva, Elena A. Minina, Justine D. Mintern, Saverio Minucci, Antonio Miranda Vizuete, Claire H. Mitchell, Shigeki Miyamoto, Keisuke Miyazawa, Noboru Mizushima, Katarzyna Mnich, Baharia Mograbi, Simin Mohseni, Luis Ferreira Moita, Marco Molinari, Maurizio Molinari, Andreas Buch Møller, Bertrand Mollereau, Faustino Mollinedo, Marco Mongillo, Martha M. Monick, Serena Montagnaro, Craig Montell, Darren J. Moore, Michael N. Moore, Rodrigo Mora Rodriguez, Paula I. Moreira, Etienne Morel, Maria Beatrice Morelli, Sandra Moreno, Michael J. Morgan, Arnaud Moris, Yuji Moriyasu, Janna L. Morrison, Lynda A. Morrison, Eugenia Morselli, Jorge Moscat, Pope L. Moseley, Serge Mostowy, Elisa Motori, Denis Mottet, Jeremy C. Mottram, Charbel E. H. Moussa, Vassiliki E. Mpakou, Hasan Mukhtar, Jean M. Mulcahy Levy, Sylviane Muller, Raquel Muñoz Moreno, Cristina Muñoz Pinedo, Christian Münz, Maureen E. Murphy, James T. Murray, Aditya Murthy, Indira U. Mysorekar, Ivan R. Nabi, Massimo Nabissi, Gustavo A. Nader, Yukitoshi Nagahara, Yoshitaka Nagai, Kazuhiro Nagata, Anika Nagelkerke, Péter Nagy, Samisubbu R. Naidu, Sreejayan Nair, Hiroyasu Nakano, Hitoshi Nakatogawa, Meera Nanjundan, Gennaro Napolitano, Naweed I. Naqvi, Roberta Nardacci, Derek P. Narendra, Masashi Narita, Anna Chiara Nascimbeni, Ramesh Natarajan, Luiz C. Navegantes, Steffan T. Nawrocki, Taras Y. Nazarko, Volodymyr Y. Nazarko, Thomas Neill, Luca M. Neri, Mihai G. Netea, Romana T. Netea Maier, Bruno M. Neves, Paul A. Ney, Ioannis P. Nezis, Hang TT Nguyen, Huu Phuc Nguyen, Anne Sophie Nicot, Hilde Nilsen, Per Nilsson, Mikio Nishimura, Ichizo Nishino, Mireia Niso Santano, Hua Niu, Ralph A. Nixon, Vincent CO Njar, Takeshi Noda, Angelika A. Noegel, Elsie Magdalena Nolte, Erik Norberg, Koenraad K. Norga, Sakineh Kazemi Noureini, Shoji Notomi, Lucia Notterpek, Karin Nowikovsky, Nobuyuki Nukina, Thorsten Nürnberger, Valerie B. O'Donnell, Tracey O'Donovan, Peter J. O'Dwyer, Ina Oehme, Clara L. Oeste, Michinaga Ogawa, Besim Ogretmen, Yuji Ogura, Young J. Oh, Masaki Ohmuraya, Takayuki Ohshima, Rani Ojha, Koji Okamoto, Toshiro Okazaki, F. Javier Oliver, Karin Ollinger, Stefan Olsson, Daniel P. Orban, Paulina Ordonez, Idil Orhon, Laszlo Orosz, Eyleen J. O'Rourke, Helena Orozco, Angel L. Ortega, Elena Ortona, Laura D. Osellame, Junko Oshima, Shigeru Oshima, Heinz D. Osiewacz, Takanobu Otomo, Kinya Otsu, Jing hsiung James Ou, Tiago F. Outeiro, Dong yun Ouyang, Hongjiao Ouyang, Michael Overholtzer, Michelle A. Ozbun, P. Hande Ozdinler, Bulent Ozpolat, Consiglia Pacelli, Paolo Paganetti, Guylène Page, Gilles Pages, Ugo Pagnini, Beata Pajak, Stephen C. Pak, Karolina Pakos Zebrucka, Nazzy Pakpour, Zdena Palková, Francesca Palladino, Kathrin Pallauf, Nicolas Pallet, Marta Palmieri, Søren R. Paludan, Camilla Palumbo, Silvia Palumbo, Olatz Pampliega, Hongming Pan, Wei Pan, Theocharis Panaretakis, Aseem Pandey, Areti Pantazopoulou, Zuzana Papackova, Daniela L. Papademetrio, Issidora Papassideri, Alessio Papini, Nirmala Parajuli, Julian Pardo, Vrajesh V. Parekh, Giancarlo Parenti, Jong In Park, Junsoo Park, Ohkmae K. Park, Roy Parker, Rosanna Parlato, Jan B. Parys, Katherine R. Parzych, Jean Max Pasquet, Benoit Pasquier, Kishore BS Pasumarthi, Daniel Patschan, Cam Patterson, Sophie Pattingre, Scott Pattison, Arnim Pause, Hermann Pavenstädt, Flaminia Pavone, Zully Pedrozo, Fernando J. Peña, Miguel A. Peñalva, Mario Pende, Jianxin Peng, Fabio Penna, Josef M. Penninger, Anna Pensalfini, Salvatore Pepe, Gustavo JS Pereira, Paulo C. Pereira, Verónica Pérez de la Cruz, María Esther Pérez Pérez, Diego Pérez Rodríguez, Dolores Pérez Sala, Celine Perier, Andras Perl, David H. Perlmutter, Ida Perrotta, Shazib Pervaiz, Maija Pesonen, Jeffrey E. Pessin, Godefridus J. Peters, Morten Petersen, Irina Petrache, Basil J. Petrof, Goran Petrovski, James M. Phang, Mauro Piacentini, Marina Pierdominici, Philippe Pierre, Valérie Pierrefite Carle, Federico Pietrocola, Felipe X. Pimentel Muiños, Mario Pinar, Benjamin Pineda, Ronit Pinkas Kramarski, Marcello Pinti, Paolo Pinton, Bilal Piperdi, James M. Piret, Leonidas C. Platanias, Harald W. Platta, Edward D. Plowey, Stefanie Pöggeler, Marc Poirot, Peter Polčic, Angelo Poletti, Audrey H. Poon, Hana Popelka, Blagovesta Popova, Izabela Poprawa, Shibu M. Poulose, Joanna Poulton, Scott K. Powers, Ted Powers, Mercedes Pozuelo Rubio, Krisna Prak, Reinhild Prange, Mark Prescott, Muriel Priault, Sharon Prince, Richard L. Proia, Tassula Proikas Cezanne, Holger Prokisch, Vasilis J. Promponas, Karin Przyklenk, Rosa Puertollano, Subbiah Pugazhenthi, Luigi Puglielli, Aurora Pujol, Julien Puyal, Dohun Pyeon, Xin Qi, Wen bin Qian, Zheng Hong Qin, Yu Qiu, Ziwei Qu, Joe Quadrilatero, Frederick Quinn, Nina Raben, Hannah Rabinowich, Flavia Radogna, Michael J. Ragusa, Mohamed Rahmani, Komal Raina, Sasanka Ramanadham, Rajagopal Ramesh, Abdelhaq Rami, Sarron Randall Demllo, Felix Randow, Hai Rao, V. Ashutosh Rao, Blake B. Rasmussen, Tobias M. Rasse, Edward A. Ratovitski, Pierre Emmanuel Rautou, Swapan K. Ray, Babak Razani, Bruce H. Reed, Fulvio Reggiori, Markus Rehm, Andreas S. Reichert, Theo Rein, David J. Reiner, Eric Reits, Jun Ren, Xingcong Ren, Maurizio Renna, Jane EB Reusch, Jose L. Revuelta, Leticia Reyes, Alireza R. Rezaie, Robert I. Richards, Des R. Richardson, Clémence Richetta, Michael A. Riehle, Bertrand H. Rihn, Yasuko Rikihisa, Brigit E. Riley, Gerald Rimbach, Maria Rita Rippo, Konstantinos Ritis, Federica Rizzi, Elizete Rizzo, Peter J. Roach, Jeffrey Robbins, Michel Roberge, Gabriela Roca, Maria Carmela Roccheri, Sonia Rocha, Cecilia MP Rodrigues, Clara I. Rodríguez, Santiago Rodriguez de Cordoba, Natalia Rodriguez Muela, Jeroen Roelofs, Vladimir V. Rogov, Troy T. Rohn, Bärbel Rohrer, Davide Romanelli, Luigina Romani, Patricia Silvia Romano, M. Isabel G. Roncero, Jose Luis Rosa, Alicia Rosello, Kirill V. Rosen, Philip Rosenstiel, Magdalena Rost Roszkowska, Kevin A. Roth, Gael Roué, Mustapha Rouis, Kasper M. Rouschop, Daniel T. Ruan, Diego Ruano, David C. Rubinsztein, Edmund B. Rucker III, Assaf Rudich, Emil Rudolf, Ruediger Rudolf, Markus A. Ruegg, Carmen Ruiz Roldan, Avnika Ashok Ruparelia, Paola Rusmini, David W. Russ, Gian Luigi Russo, Giuseppe Russo, Rossella Russo, Tor Erik Rusten, Victoria Ryabovol, Kevin M. Ryan, Stefan W. Ryter, David M. Sabatini, Michael Sacher, Carsten Sachse, Michael N. Sack, Junichi Sadoshima, Paul Saftig, Ronit Sagi Eisenberg, Sumit Sahni, Pothana Saikumar, Tsunenori Saito, Tatsuya Saitoh, Koichi Sakakura, Machiko Sakoh Nakatogawa, Yasuhito Sakuraba, María Salazar Roa, Paolo Salomoni, Ashok K. Saluja, Paul M. Salvaterra, Rosa Salvioli, Afshin Samali, Anthony MJ Sanchez, José A. Sánchez Alcázar, Ricardo Sanchez Prieto, Marco Sandri, Miguel A. Sanjuan, Stefano Santaguida, Laura Santambrogio, Giorgio Santoni, Claudia Nunes dos Santos, Shweta Saran, Marco Sardiello, Graeme Sargent, Pallabi Sarkar, Sovan Sarkar, Maria Rosa Sarrias, Minnie M. Sarwal, Chihiro Sasakawa, Motoko Sasaki, Miklos Sass, Ken Sato, Miyuki Sato, Joseph Satriano, Niramol Savaraj, Svetlana Saveljeva, Liliana Schaefer, Ulrich E. Schaible, Michael Scharl, Hermann M. Schatzl, Randy Schekman, Wiep Scheper, Alfonso Schiavi, Hyman M. Schipper, Hana Schmeisser, Jens Schmidt, Ingo Schmitz, Bianca E. Schneider, E. Marion Schneider, Jaime L. Schneider, Eric A. Schon, Miriam J. Schönenberger, Axel H. Schönthal, Daniel F. Schorderet, Bernd Schröder, Sebastian Schuck, Ryan J. Schulze, Melanie Schwarten, Thomas L. Schwarz, Sebastiano Sciarretta, Kathleen Scotto, A. Ivana Scovassi, Robert A. Screaton, Mark Screen, Hugo Seca, Simon Sedej, Laura Segatori, Nava Segev, Per O. Seglen, Jose M. Seguí Simarro, Juan Segura Aguilar, Ekihiro Seki, Iban Seiliez, Christian Sell, Clay F. Semenkovich, Gregg L. Semenza, Utpal Sen, Andreas L. Serra, Ana Serrano Puebla, Hiromi Sesaki, Takao Setoguchi, Carmine Settembre, John J. Shacka, Ayesha N. Shajahan Haq, Irving M. Shapiro, Shweta Sharma, Hua She, C. K. James Shen, Chiung Chyi Shen, Han Ming Shen, Sanbing Shen, Weili Shen, Rui Sheng, Xianyong Sheng, Zu Hang Sheng, Trevor G. Shepherd, Junyan Shi, Qiang Shi, Qinghua Shi, Yuguang Shi, Shusaku Shibutani, Kenichi Shibuya, Yoshihiro Shidoji, Jeng Jer Shieh, Chwen Ming Shih, Yohta Shimada, Shigeomi Shimizu, Dong Wook Shin, Mari L. Shinohara, Michiko Shintani, Takahiro Shintani, Tetsuo Shioi, Ken Shirabe, Ronit Shiri Sverdlov, Orian Shirihai, Gordon C. Shore, Chih Wen Shu, Deepak Shukla, Andriy A. Sibirny, Valentina Sica, Christina J. Sigurdson, Einar M. Sigurdsson, Puran Singh Sijwali, Beata Sikorska, Wilian A. Silveira, Sandrine Silvente Poirot, Gary A. Silverman, Jan Simak, Thomas Simmet, Anna Katharina Simon, Hans Uwe Simon, Cristiano Simone, Matias Simons, Anne Simonsen, Rajat Singh, Shivendra V. Singh, Shrawan K. Singh, Debasish Sinha, Sangita Sinha, Frank A. Sinicrope, Agnieszka Sirko, Kapil Sirohi, Balindiwe JN Sishi, Annie Sittler, Parco M. Siu, Efthimios Sivridis, Anna Skwarska, Ruth Slack, Iva Slaninová, Nikolai Slavov, Soraya S. Smaili, Keiran SM Smalley, Duncan R. Smith, Stefaan J. Soenen, Scott A. Soleimanpour, Anita Solhaug, Kumaravel Somasundaram, Jin H. Son, Avinash Sonawane, Chunjuan Song, Fuyong Song, Hyun Kyu Song, Ju Xian Song, Wei Song, Kai Y. Soo, Anil K. Sood, Tuck Wah Soong, Virawudh Soontornniyomkij, Maurizio Sorice, Federica Sotgia, David R. Soto Pantoja, Areechun Sotthibundhu, Maria João Sousa, Herman P. Spaink, Paul N. Span, Anne Spang, Janet D. Sparks, Peter G. Speck, Stephen A. Spector, Claudia D. Spies, Wolfdieter Springer, Daret St Clair, Alessandra Stacchiotti, Bart Staels, Michael T. Stang, Daniel T. Starczynowski, Petro Starokadomskyy, Clemens Steegborn, John W. Steele, Leonidas Stefanis, Joan Steffan, Christine M. Stellrecht, Harald Stenmark, Tomasz M. Stepkowski, Stęphan T. Stern, Craig Stevens, Brent R. Stockwell, Veronika Stoka, Zuzana Storchova, Björn Stork, Vassilis Stratoulias, Dimitrios J. Stravopodis, Pavel Strnad, Anne Marie Strohecker, Anna Lena Ström, Per Stromhaug, Jiri Stulik, Yu Xiong Su, Zhaoliang Su, Carlos S. Subauste, Srinivasa Subramaniam, Carolyn M. Sue, Sang Won Suh, Xinbing Sui, Supawadee Sukseree, David Sulzer, Fang Lin Sun, Jiaren Sun, Jun Sun, Shi Yong Sun, Yang Sun, Yi Sun, Yingjie Sun, Vinod Sundaramoorthy, Joseph Sung, Hidekazu Suzuki, Kuninori Suzuki, Naoki Suzuki, Tadashi Suzuki, Yuichiro J. Suzuki, Michele S. Swanson, Charles Swanton, Karl Swärd, Ghanshyam Swarup, Sean T. Sweeney, Paul W. Sylvester, Zsuzsanna Szatmari, Eva Szegezdi, Peter W. Szlosarek, Heinrich Taegtmeyer, Marco Tafani, Emmanuel Taillebourg, Stephen WG Tait, Krisztina Takacs Vellai, Yoshinori Takahashi, Szabolcs Takáts, Genzou Takemura, Nagio Takigawa, Nicholas J. Talbot, Elena Tamagno, Jerome Tamburini, Cai Ping Tan, Lan Tan, Mei Lan Tan, Ming Tan, Yee Joo Tan, Keiji Tanaka, Masaki Tanaka, Daolin Tang, Dingzhong Tang, Guomei Tang, Isei Tanida, Kunikazu Tanji, Bakhos A. Tannous, Jose A. Tapia, Inmaculada Tasset Cuevas, Marc Tatar, Iman Tavassoly, Nektarios Tavernarakis, Allen Taylor, Graham S. Taylor, Gregory A. Taylor, J. Paul Taylor, Mark J. Taylor, Elena V. Tchetina, Andrew R. Tee, Fatima Teixeira Clerc, Sucheta Telang, Tewin Tencomnao, Ba Bie Teng, Ru Jeng Teng, Faraj Terro, Gianluca Tettamanti, Arianne L. Theiss, Anne E. Theron, Kelly Jean Thomas, Marcos P. Thomé, Paul G. Thomes, Andrew Thorburn, Jeremy Thorner, Thomas Thum, Michael Thumm, Teresa LM Thurston, Ling Tian, Andreas Till, Jenny Pan yun Ting, Vladimir I. Titorenko, Lilach Toker, Stefano Toldo, Sharon A. Tooze, Ivan Topisirovic, Maria Lyngaas Torgersen, Liliana Torosantucci, Alicia Torriglia, Maria Rosaria Torrisi, Cathy Tournier, Roberto Towns, Vladimir Trajkovic, Leonardo H. Travassos, Gemma Triola, Durga Nand Tripathi, Daniela Trisciuoglio, Rodrigo Troncoso, Ioannis P. Trougakos, Anita C. Truttmann, Kuen Jer Tsai, Mario P. Tschan, Yi Hsin Tseng, Takayuki Tsukuba, Allan Tsung, Andrey S. Tsvetkov, Shuiping Tu, Hsing Yu Tuan, Marco Tucci, David A. Tumbarello, Boris Turk, Vito Turk, Robin FB Turner, Anders A. Tveita, Suresh C. Tyagi, Makoto Ubukata, Yasuo Uchiyama, Andrej Udelnow, Takashi Ueno, Midori Umekawa, Rika Umemiya Shirafuji, Benjamin R. Underwood, Christian Ungermann, Rodrigo P. Ureshino, Ryo Ushioda, Vladimir N. Uversky, Néstor L. Uzcátegui, Thomas Vaccari, Maria I. Vaccaro, Libuše Váchová, Helin Vakifahmetoglu Norberg, Rut Valdor, Enza Maria Valente, Francois Vallette, Angela M. Valverde, Greet Van den Berghe, Ludo Van Den Bosch, Gijs R. van den Brink, F. Gisou van der Goot, Ida J. van der Klei, Luc JW van der Laan, Wouter G. van Doorn, Marjolein van Egmond, Kenneth L. van Golen, Luc Van Kaer, Menno van Lookeren Campagne, Peter Vandenabeele, Wim Vandenberghe, Ilse Vanhorebeek, Isabel Varela Nieto, M. Helena Vasconcelos, Radovan Vasko, Demetrios G. Vavvas, Ignacio Vega Naredo, Guillermo Velasco, Athanassios D. Velentzas, Panagiotis D. Velentzas, Tibor Vellai, Edo Vellenga, Mikkel Holm Vendelbo, Kartik Venkatachalam, Natascia Ventura, Salvador Ventura, Patrícia ST Veras, Mireille Verdier, Beata G. Vertessy, Andrea Viale, Michel Vidal, Helena LA Vieira, Richard D. Vierstra, Nadarajah Vigneswaran, Neeraj Vij, Miquel Vila, Margarita Villar, Victor H. Villar, Joan Villarroya, Cécile Vindis, Giampietro Viola, Maria Teresa Viscomi, Giovanni Vitale, Dan T. Vogl, Olga V. Voitsekhovskaja, Clarissa von Haefen, Karin von Schwarzenberg, Daniel E. Voth, Valérie Vouret Craviari, Kristina Vuori, Jatin M. Vyas, Christian Waeber, Cheryl Lyn Walker, Mark J. Walker, Jochen Walter, Lei Wan, Xiangbo Wan, Bo Wang, Caihong Wang, Chao Yung Wang, Chengshu Wang, Chenran Wang, Chuangui Wang, Dong Wang, Fen Wang, Fuxin Wang, Guanghui Wang, Hai jie Wang, Haichao Wang, Hong Gang Wang, Hongmin Wang, Horng Dar Wang, Jing Wang, Junjun Wang, Mei Wang, Mei Qing Wang, Pei Yu Wang, Peng Wang, Richard C. Wang, Shuo Wang, Ting Fang Wang, Xian Wang, Xiao jia Wang, Xiao Wei Wang, Xin Wang, Xuejun Wang, Yan Wang, Yanming Wang, Ying Wang, Ying Jan Wang, Yipeng Wang, Yu Wang, Yu Tian Wang, Yuqing Wang, Zhi Nong Wang, Pablo Wappner, Carl Ward, Diane McVey Ward, Gary Warnes, Hirotaka Watada, Yoshihisa Watanabe, Kei Watase, Timothy E. Full Terms, Conditions of access, use can be found at h.t.t.p.:././.w.w.w. t.a.n.d.f.o.n.l.i.n.e. com/action/journalInformation?journalCode=kaup20 Download by: [Alma Mater Studiorum Università di Bologna] Date: 23 September 2016, At: 06:43 Weaver, Colin D. Weekes, Jiwu Wei, Thomas Weide, Conrad C. Weihl, Günther Weindl, Simone Nardin Weis, Longping Wen, Xin Wen, Yunfei Wen, Benedikt Westermann, Cornelia M. Weyand, Anthony R. White, Eileen White, J. Lindsay Whitton, Alexander J. Whitworth, Joëlle Wiels, Franziska Wild, Manon E. Wildenberg, Tom Wileman, Deepti Srinivas Wilkinson, Simon Wilkinson, Dieter Willbold, Chris Williams, Katherine Williams, Peter R. Williamson, Konstanze F. Winklhofer, Steven S. Witkin, Stephanie E. Wohlgemuth, Thomas Wollert, Ernst J. Wolvetang, Esther Wong, G. William Wong, Richard W. Wong, Vincent Kam Wai Wong, Elizabeth A. Woodcock, Karen L. Wright, Chunlai Wu, Defeng Wu, Gen Sheng Wu, Jian Wu, Junfang Wu, Mian Wu, Min Wu, Shengzhou Wu, William KK Wu, Yaohua Wu, Zhenlong Wu, Cristina PR Xavier, Ramnik J. Xavier, Gui Xian Xia, Tian Xia, Weiliang Xia, Yong Xia, Hengyi Xiao, Jian Xiao, Shi Xiao, Wuhan Xiao, Chuan Ming Xie, Zhiping Xie, Zhonglin Xie, Maria Xilouri, Yuyan Xiong, Chuanshan Xu, Congfeng Xu, Feng Xu, Haoxing Xu, Hongwei Xu, Jian Xu, Jianzhen Xu, Jinxian Xu, Liang Xu, Xiaolei Xu, Yangqing Xu, Ye Xu, Zhi Xiang Xu, Ziheng Xu, Yu Xue, Takahiro Yamada, Ai Yamamoto, Koji Yamanaka, Shunhei Yamashina, Shigeko Yamashiro, Bing Yan, Bo Yan, Xianghua Yan, Zhen Yan, Yasuo Yanagi, Dun Sheng Yang, Jin Ming Yang, Liu Yang, Minghua Yang, Pei Ming Yang, Peixin Yang, Qian Yang, Wannian Yang, Wei Yuan Yang, Xuesong Yang, Yi Yang, Ying Yang, Zhifen Yang, Zhihong Yang, Meng Chao Yao, Pamela J. Yao, Xiaofeng Yao, Zhenyu Yao, Zhiyuan Yao, Linda S. Yasui, Mingxiang Ye, Barry Yedvobnick, Behzad Yeganeh, Elizabeth S. Yeh, Patricia L. Yeyati, Fan Yi, Long Yi, Xiao Ming Yin, Calvin K. Yip, Yeong Min Yoo, Young Hyun Yoo, Seung Yong Yoon, Ken Ichi Yoshida, Tamotsu Yoshimori, Ken H. Young, Huixin Yu, Jane J. Yu, Jin Tai Yu, Jun Yu, Li Yu, W. Haung Yu, Xiao Fang Yu, Zhengping Yu, Junying Yuan, Zhi Min Yuan, Beatrice YJT Yue, Jianbo Yue, Zhenyu Yue, David N. Zacks, Eldad Zacksenhaus, Nadia Zaffaroni, Tania Zaglia, Zahra Zakeri, Vincent Zecchini, Jinsheng Zeng, Min Zeng, Qi Zeng, Antonis S. Zervos, Donna D. Zhang, Fan Zhang, Guo Zhang, Guo Chang Zhang, Hao Zhang, Hong Zhang, Hongbing Zhang, Jian Zhang, Jiangwei Zhang, Jianhua Zhang, Jing pu Zhang, Li Zhang, Lin Zhang, Long Zhang, Ming Yong Zhang, Xiangnan Zhang, Xu Dong Zhang, Yan Zhang, Yang Zhang, Yanjin Zhang, Yingmei Zhang, Yunjiao Zhang, Mei Zhao, Wei Li Zhao, Xiaonan Zhao, Yan G. Zhao, Ying Zhao, Yongchao Zhao, Yu xia Zhao, Zhendong Zhao, Zhizhuang J. Zhao, Dexian Zheng, Xi Long Zheng, Xiaoxiang Zheng, Boris Zhivotovsky, Qing Zhong, Guang Zhou Zhou, Guofei Zhou, Huiping Zhou, Shu Feng Zhou, Xu jie Zhou, Hongxin Zhu, Hua Zhu, Wei Guo Zhu, Wenhua Zhu, Xiao Feng Zhu, Yuhua Zhu, Shi Mei Zhuang, Xiaohong Zhuang, Elio Ziparo, Christos E. Zois, Teresa Zoladek, Wei Xing Zong, Antonio Zorzano, Susu M. Zughaier, Life Sciences Institute and Department of Molecular, Cellular, and Developmental Biology and Biological Chemistry, University of Michigan [Ann Arbor], University of Michigan System-University of Michigan System, Tokyo Medical University, The Hebrew University of Jerusalem (HUJ), Mammalian Genetics Unit, Medical Research Council Harwell, University of Occupational and Environmental Health School of Medicine, Partenaires INRAE, University of Toronto, Ben-Gurion University of the Negev (BGU), University of Colorado [Boulder], Cell Death Research & Therapy (CDRT) Lab, Université Catholique de Louvain = Catholic University of Louvain (UCL), University of Vienna [Vienna], Conway Institute of Biomolecular and Biomedical Research and School of Chemical and Bioprocess Engineering, University College Dublin [Dublin] (UCD), Georgetown University, Candiolo Cancer Institute (IRCCS), Centro de Investigacion Biomédica en Red sobre Enfermedades Neurodegenerativas (CIBERNED), Instituto de Salud Carlos III [Madrid] (ISC), Ikerbasque - Basque Foundation for Science, Cleveland Clinic, Sidney Kimmel Cancer Center, Jefferson (Philadelphia University + Thomas Jefferson University), Universidad de Buenos Aires (UBA), Department of Clinical Neurosciences, University College of London [London] (UCL)-Institute of Neurology, Thérapie génique, Génomique et Epigénomique (U 1169), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Saclay, Consiglio Nazionale delle Ricerche (CNR), Osaka University, Department of Experimental Medicine and Public Health, University of Camerino, University of Barcelona, Institut Universitaire d'Hématologie (IUH), Université Paris Diderot - Paris 7 (UPD7), Génomique Fonctionnelle des Tumeurs Solides (U1162), Université Paris 13 (UP13)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Université Paris Descartes - Paris 5 (UPD5), Institut National de la Santé et de la Recherche Médicale (INSERM), Department of Physics, Technical University of Denmark [Lyngby] (DTU), University of Zaragoza - Universidad de Zaragoza [Zaragoza], Department of Pharmaco-Biology, Università della Calabria [Arcavacata di Rende] (Unical), Fondation Universitaire Notre Dame de la Paix (FUNDP), Facultés Universitaires Notre Dame de la Paix (FUNDP), USC Neuromuscular Center, Department of Neurology, University of Southern California (USC), Physiopathologie de la survie et de la mort cellulaire et infection virale, Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-IFR50-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Côte d'Azur (UCA), Giannina Gaslini Institute, Institut des Sciences de l'Evolution de Montpellier (UMR ISEM), École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université de Montpellier (UM)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre National de la Recherche Scientifique (CNRS)-Institut de recherche pour le développement [IRD] : UR226, Inner Mongolia Agricultural University (IMAU), Politecnico di Milano [Milan] (POLIMI), Department of Civil, Geological, and Mining Engineering, École Polytechnique de Montréal (EPM)-NSERC Industrial Chair on Drinking Water, Institut de Recherche sur le Cancer et le Vieillissement (IRCAN), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA), Department of Molecular Medicine, Institut Pasteur, Fondation Cenci Bolognetti - Istituto Pasteur Italia, Fondazione Cenci Bolognetti, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome], Physiopathologie du système nerveux central - Institut François Magendie, Université Bordeaux Segalen - Bordeaux 2-IFR8-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratory of Experimental Virology - Department of Medical Microbiology [Amsterdam, The Netherlands], Academic Medical Center - Academisch Medisch Centrum [Amsterdam] (AMC), University of Amsterdam [Amsterdam] (UvA)-University of Amsterdam [Amsterdam] (UvA)-Center for Infection and Immunity Amsterdam - CINIMA [Amsterdam, The Netherlands], Centre de résonance magnétique biologique et médicale (CRMBM), Aix Marseille Université (AMU)-Assistance Publique - Hôpitaux de Marseille (APHM)-Centre National de la Recherche Scientifique (CNRS), Dynamique des interactions membranaires normales et pathologiques (DIMNP), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université Montpellier 1 (UM1), Department of Internal Medicine, Hospital Universitario Infanta Sofía, Celullar and Molecular Medicine, Infection bactérienne, inflammation, et carcinogenèse digestive, University of Edinburgh, Unité de Nutrition Humaine (UNH), Institut National de la Recherche Agronomique (INRA)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université, Faculty of Engineering and Natural Sciences, Sabanci University [Istanbul], University of Science and Technology Beijing [Beijing] (USTB), Centre for Computational and Systems Biology (COSBI), Sun Yat-Sen University [Guangzhou] (SYSU), Dynamique Musculaire et Métabolisme (DMEM), Université de Montpellier (UM)-Institut National de la Recherche Agronomique (INRA), CAS Institute of Oceanology (IOCAS), Chinese Academy of Sciences [Beijing] (CAS), Polytechnic University of Marche, Centre de Recherche en Cancérologie de Marseille (CRCM), Aix Marseille Université (AMU)-Institut Paoli-Calmettes, Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Cell Biology, Physiology and Immunology, Department of Experimental Oncology and Molecular Medicine, Fondazione IRCCS Istituto Nazionale dei Tumori, University of Pisa - Università di Pisa, Dulbecco Telethon Institute/Department of Biology, Fondation de Recherche Cancer et Sang - Hôpital Kirchberg, China University of Petroleum, Unilever R&D, University of Queensland [Brisbane], University of Minnesota [Twin Cities] (UMN), University of Minnesota System, Laboratoire de Génie des Procédés et Matériaux - EA 4038 (LGPM), CentraleSupélec, Institute for Advanced Study [Tsinghua], Tsinghua University [Beijing] (THU), Nanayang Technological University (NTU), Nanayang Technological University, Institute of Microelectronics [Beijing] (IMETU), Laboratoire de photonique et de nanostructures (LPN), Centre National de la Recherche Scientifique (CNRS), Institut de biologie moléculaire des plantes (IBMP), Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA), Northwestern Polytechnical University [Xi'an] (NPU), University of Pennsylvania [Philadelphia], City University of Hong Kong (CityU), Department of Mathematics [Berkeley], University of California [Berkeley], University of California-University of California, ZJU-ENS Joint Laboratory of Medicinal Chemistry, Zhejiang University, University of Cincinnati (UC), Réponses immunes : régulation et développement, Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM), The University of New Mexico [Albuquerque], Centre de Recherche de l'Institut du Cerveau et de la Moelle épinière (CRICM), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Dipartimento di Scienze Biomediche, Università degli Studi di Modena e Reggio Emilia (UNIMORE), Department of Experimental Medicine and Oncology, University of Turin, Institut de Génomique Fonctionnelle (IGF), Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS), CNV, University of Valparaiso, Université Paris 1 Panthéon-Sorbonne - UFR d'Arts plastiques et sciences de l'art (UP1 UFR04), Université Paris 1 Panthéon-Sorbonne (UP1), Department of General, Visceral and Vascular Surgery [Jena], Friedrich-Schiller-Universität Jena, Récepteurs nucléaires, maladies cardiovasculaires et diabète - U 1011 (RNMCD), Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Institut National de la Santé et de la Recherche Médicale (INSERM), Réseau International des Instituts Pasteur (RIIP), Macrophages et Développement de l’Immunité, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Immunobiologie des Cellules Dendritiques, Institut Pasteur [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre d'infectiologie Necker-Pasteur [CHU Necker], Institut Pasteur [Paris]-CHU Necker - Enfants Malades [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Institut Pasteur [Paris], Trafic membranaire et Division cellulaire - Membrane Traffic and Cell Division, Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur [Paris], Cibles thérapeutiques, formulation et expertise pré-clinique du médicament (CITHEFOR), Université de Lorraine (UL), This work was supported in part by the National Institutes of Health, including Public Health Service grant GM053396 to D.J.K. Due to space and other limitations, it is not possible to include all other sources of financial support., In a rapidly expanding and highly dynamic field such as autophagy, it is possible that some authors who should have been included on this article have been missed. D.J.K. extends his apologies to researchers in the field of autophagy who, due to oversight or any other reason, could not be included on this article. I also note that two of our colleagues on this manuscript have passed away: Arlette Darfeuille-Michaud and Wouter van Doorn., Life Sciences Institute [Ann Arbor, MI, USA], Laboratoire de Biogenèse Membranaire, CNRS UMR 5200, Université de Bordeaux, INRA Bordeaux Aquitaine, Villenave d'Ornon, France., Amelio, Ivano [0000-0002-9126-5391], Beale, Rupert [0000-0002-6705-8560], Floto, Andres [0000-0002-2188-5659], Frezza, Christian [0000-0002-3293-7397], Ktistakis, Nicholas [0000-0001-9397-2914], Melino, Gerry [0000-0001-9428-5972], Narita, Masashi [0000-0001-7764-577X], Rubinsztein, David [0000-0001-5002-5263], Underwood, Benjamin [0000-0003-3427-9487], Whitworth, Alex [0000-0002-1154-6629], Apollo - University of Cambridge Repository, Université Catholique de Louvain, Facultés Universitaires Notre-Dame de la Paix, Institut National de la Santé et de la Recherche Médicale (INSERM)-IFR50-Université Nice Sophia Antipolis (... - 2019) (UNS), Université Côte d'Azur (UCA)-Université Côte d'Azur (UCA), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-École pratique des hautes études (EPHE)-Université de Montpellier (UM)-Institut de recherche pour le développement [IRD] : UR226-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Nice Sophia Antipolis (... - 2019) (UNS), Department of Clinical and Molecular Medicine, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' [Rome], Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Université Côte d'Azur (UCA)-Université Côte d'Azur (UCA)-IFR50-Institut National de la Santé et de la Recherche Médicale (INSERM), Unité de Nutrition Humaine - Clermont Auvergne (UNH), Institut National de la Recherche Agronomique (INRA)-Université Clermont Auvergne (UCA), Sun Yat-Sen University (SYSU), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Paoli-Calmettes, Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Aix Marseille Université (AMU), University of Minnesota [Twin Cities], Tsinghua University [Beijing], Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), Université Panthéon-Sorbonne - UFR d'Arts plastiques et sciences de l'art (UP1 UFR04), Université Panthéon-Sorbonne (UP1), Récepteurs nucléaires, maladies cardiovasculaires et diabète (EGID), Université de Lille, Droit et Santé-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), CHU Necker - Enfants Malades [AP-HP], Trafic membranaire et Division cellulaire, Institut de Biologie du Développement de Marseille (IBDM), Aix Marseille Université (AMU)-Collège de France (CdF)-Centre National de la Recherche Scientifique (CNRS), Klionsky, D., Abdelmohsen, K., Abe, A., Abedin, M., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C., Adams, P., Adeli, K., Adhihetty, P., Adler, S., Agam, G., Agarwal, R., Aghi, M., Agnello, M., Agostinis, P., Aguilar, P., Aguirre-Ghiso, J., Airoldi, E., Ait-Si-Ali, S., Akematsu, T., Akporiaye, E., Al-Rubeai, M., Albaiceta, G., Albanese, C., Albani, D., Albert, M., Aldudo, J., Algül, H., Alirezaei, M., Alloza, I., Almasan, A., Almonte-Beceril, M., Alnemri, E., Alonso, C., Altan-Bonnet, N., Altieri, D., Alvarez, S., Alvarez-Erviti, L., Alves, S., Amadoro, G., Amano, A., Amantini, C., Ambrosio, S., Amelio, I., Amer, A., Amessou, M., Amon, A., 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L, Chen, Wei, Chen, Wei Jung, Chen, Wen Qiang, Chen, Wenli, Chen, Xiangmei, Chen, Yau Hung, Chen, Ye Guang, Chen, Yin, Chen, Yingyu, Chen, Yongshun, Chen, Yu Jen, Chen, Yue Qin, Chen, Yujie, Chen, Zhen, Chen, Zhong, Cheng, Alan, Cheng, Christopher Hk, Cheng, Hua, Cheong, Heesun, Cherry, Sara, Chesney, Jason, Cheung, Chun Hei Antonio, Chevet, Eric, Chi, Hsiang Cheng, Chi, Sung Gil, Chiacchiera, Fulvio, Chiang, Hui Ling, Chiarelli, Roberto, Chiariello, Mario, Chieppa, Marcello, Chin, Lih Shen, Chiong, Mario, Chiu, Gigi Nc, Cho, Dong Hyung, Cho, Ssang Goo, Cho, William C, Cho, Yong Yeon, Cho, Young Seok, Choi, Augustine Mk, Choi, Eui Ju, Choi, Eun Kyoung, Choi, Jayoung, Choi, Mary E, Choi, Seung Il, Chou, Tsui Fen, Chouaib, Salem, Choubey, Divaker, Choubey, Vinay, Chow, Kuan Chih, Chowdhury, Kamal, Chu, Charleen T, Chuang, Tsung Hsien, Chun, Taehoon, Chung, Hyewon, Chung, Taijoon, Chung, Yuen Li, Chwae, Yong Joon, Cianfanelli, Valentina, Ciarcia, Roberto, Ciechomska, Iwona A, Ciriolo, Maria Rosa, Cirone, Mara, Claerhout, Sofie, Clague, Michael J, Clària, Joan, Clarke, Peter Gh, Clarke, Robert, Clementi, Emilio, Cleyrat, Cédric, Cnop, Miriam, Coccia, Eliana M, Cocco, Tiziana, Codogno, Patrice, Coers, Jörn, Cohen, Ezra Ew, Colecchia, David, Coletto, Luisa, Coll, Núria S, Colucci Guyon, Emma, Comincini, Sergio, Condello, Maria, Cook, Katherine L, Coombs, Graham H, Cooper, Cynthia D, Cooper, J. Mark, Coppens, Isabelle, Corasaniti, Maria Tiziana, Corazzari, Marco, Corbalan, Ramon, Corcelle Termeau, Elisabeth, Cordero, Mario D, Corral Ramos, Cristina, Corti, Olga, Cossarizza, Andrea, Costelli, Paola, Costes, Safia, Cotman, Susan L, Coto Montes, Ana, Cottet, Sandra, Couve, Eduardo, Covey, Lori R, Cowart, L. 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Tony, El Deiry, Wafik S, El Khoury, Victoria, Elazar, Zvulun, Eldar Finkelman, Hagit, Elliott, Chris Jh, Emanuele, Enzo, Emmenegger, Urban, Engedal, Nikolai, Engelbrecht, Anna Mart, Engelender, Simone, Enserink, Jorrit M, Erdmann, Ralf, Erenpreisa, Jekaterina, Eri, Rajaraman, Eriksen, Jason L, Erman, Andreja, Escalante, Ricardo, Eskelinen, Eeva Liisa, Espert, Lucile, Esteban Martínez, Lorena, Evans, Thomas J, Fabri, Mario, Fabrias, Gemma, Fabrizi, Cinzia, Facchiano, Antonio, Færgeman, Nils J, Faggioni, Alberto, Fairlie, W. 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Berghe, G, Van Den Bosch, L, van den Brink, Gr, van der Goot, Fg, van der Klei, Ij, van der Laan, Lj, van Doorn, Wg, van Egmond, M, van Golen, Kl, Van Kaer, L, van Lookeren Campagne, M, Vandenabeele, P, Vandenberghe, W, Vanhorebeek, I, Varela Nieto, I, Vasconcelos, Mh, Vasko, R, Vavvas, Dg, Vega Naredo, I, Velasco, G, Velentzas, Ad, Velentzas, Pd, Vellai, T, Vellenga, E, Vendelbo, Mh, Venkatachalam, K, Ventura, N, Ventura, S, Veras, P, Verdier, M, Vertessy, Bg, Viale, A, Vidal, M, Vieira, H, Vierstra, Rd, Vigneswaran, N, Vij, N, Vila, M, Villar, M, Villar, Vh, Villarroya, J, Vindis, C, Viola, G, Viscomi, Mt, Vitale, G, Vogl, Dt, Voitsekhovskaja, Ov, von Haefen, C, von Schwarzenberg, K, Voth, De, Vouret Craviari, V, Vuori, K, Vyas, Jm, Waeber, C, Walker, Cl, Walker, Mj, Walter, J, Wan, L, Wan, X, Wang, B, Wang, C, Wang, Cy, Wang, D, Wang, F, Wang, G, Wang, Hj, Wang, H, Wang, Hg, Wang, Hd, Wang, J, Wang, M, Wang, Mq, Wang, Py, Wang, P, Wang, Rc, Wang, S, Wang, Tf, Wang, X, Wang, Xj, 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Yang, W, Yang, Wy, Yang, X, Yang, Y, Yang, Z, Yao, Mc, Yao, Pj, Yao, X, Yao, Z, Yasui, L, Ye, M, Yedvobnick, B, Yeganeh, B, Yeh, E, Yeyati, Pl, Yi, F, Yi, L, Yin, Xm, Yip, Ck, Yoo, Ym, Yoo, Yh, Yoon, Sy, Yoshida, Ki, Yoshimori, T, Young, Kh, Yu, H, Yu, Jj, Yu, Jt, Yu, J, Yu, L, Yu, Wh, Yu, Xf, Yu, Z, Yuan, J, Yuan, Zm, Yue, By, Yue, J, Yue, Z, Zacks, Dn, Zacksenhaus, E, Zaffaroni, N, Zaglia, T, Zakeri, Z, Zecchini, V, Zeng, J, Zeng, M, Zeng, Q, Zervos, A, Zhang, Dd, Zhang, F, Zhang, G, Zhang, Gc, Zhang, H, Zhang, J, Zhang, Jp, Zhang, L, Zhang, My, Zhang, X, Zhang, Xd, Zhang, Y, Zhao, M, Zhao, Wl, Zhao, X, Zhao, Yg, Zhao, Y, Zhao, Yx, Zhao, Z, Zhao, Zj, Zheng, D, Zheng, Xl, Zheng, X, Zhivotovsky, B, Zhong, Q, Zhou, Gz, Zhou, G, Zhou, H, Zhou, Sf, Zhou, Xj, Zhu, H, Zhu, Wg, Zhu, W, Zhu, Xf, Zhu, Y, Zhuang, Sm, Zhuang, X, Ziparo, E, Zois, Ce, Zoladek, T, Zong, Wx, Zorzano, A, Zughaier, Sm, AII - Amsterdam institute for Infection and Immunity, Medical Microbiology and Infection Prevention, Other departments, CCA -Cancer Center Amsterdam, Center of Experimental and Molecular Medicine, Radiotherapy, AGEM - Amsterdam Gastroenterology Endocrinology Metabolism, Medical Biochemistry, ANS - Cellular & Molecular Mechanisms, Cell Biology and Histology, Gastroenterology and Hepatology, Tytgat Institute for Liver and Intestinal Research, Daniel J Klionsky, Kotb Abdelmohsen, Akihisa Abe, Md Joynal Abedin, Hagai Abeliovich, Abraham Acevedo Arozena, Hiroaki Adachi, Christopher M Adam, Peter D Adam, Khosrow Adeli, Peter J Adhihetty, Sharon G Adler, Galila Agam, Rajesh Agarwal, Manish K Aghi, Maria Agnello, Patrizia Agostini, Patricia V Aguilar, Julio Aguirre-Ghiso, Edoardo M Airoldi, Slimane Ait-Si-Ali, Takahiko Akematsu, Emmanuel T Akporiaye, Mohamed Al-Rubeai, Guillermo M Albaiceta, Chris Albanese, Diego Albani, Matthew L Albert, Jesus Aldudo, Hana Algül, Mehrdad Alirezaei, Iraide Alloza, Alexandru Almasan, Maylin Almonte-Beceril, Emad S Alnemri, Covadonga Alonso, Nihal Altan-Bonnet, Dario C Altieri, Silvia Alvarez, Lydia Alvarez- Erviti, Sandro Alve, Giuseppina Amadoro, Atsuo Amano, Consuelo Amantini, Santiago Ambrosio, Ivano Amelio, Amal O Amer, Mohamed Amessou, Angelika Amon, Zhenyi An, Frank A Anania, Stig U Andersen, Usha P Andley, Catherine K Andreadi, Nathalie Andrieu- Abadie, Alberto Anel, David K Ann, Shailendra Anoopkumar-Dukie, Manuela Antonioli, Hiroshi Aoki, Nadezda Apostolova, Saveria Aquila, Katia Aquilano, Koichi Araki, Eli Arama, Agustin Aranda, Jun Araya, Alexandre Arcaro, Esperanza Aria, Hirokazu Arimoto, Aileen R Ariosa, Jane L Armstrong, Thierry Arnould, Ivica Arsov, Katsuhiko Asanuma, Valerie Askana, Eric Asselin, Ryuichiro Atarashi, Sally S Atherton, Julie D Atkin, Laura D Attardi, Patrick Auberger, Georg Auburger, Laure Aurelian, Riccardo Autelli, Laura Avagliano, Maria Laura Avantaggiati, Limor Avrahami, Suresh Awale, Neelam Azad, Tiziana Bachetti, Jonathan M Backer, Dong- Hun Bae, Jae-sung Bae, Ok-Nam Bae, Soo Han Bae, Eric H Baehrecke, Seung-Hoon Baek, Stephen Baghdiguian, Agnieszka Bagniewska-Zadworna, Hua Bai, Jie Bai, Xue-Yuan Bai, Yannick Bailly, Kithiganahalli Narayanaswamy Balaji, Walter Balduini, Andrea Ballabio, Rena Balzan, Rajkumar Banerjee, Gábor Bánhegyi, Haijun Bao, Benoit Barbeau, Maria D Barrachina, Esther Barreiro, Bonnie Bartel, Alberto Bartolomé, Diane C Bassham, Maria Teresa Bassi, Robert C Bast Jr, Alakananda Basu, Maria Teresa Batista, Henri Batoko, Maurizio Battino, Kyle Bauckman, Bradley L Baumgarner, K Ulrich Bayer, Rupert Beale, Jean-François Beaulieu, George R. Beck Jr, Christoph Becker, J David Beckham, Pierre-André Bédard, Patrick J Bednarski, Thomas J Begley, Christian Behl, Christian Behrend, Georg MN Behren, Kevin E Behrn, Eloy Bejarano, Amine Belaid, Francesca Belleudi, Giovanni Bénard, Guy Berchem, Daniele Bergamaschi, Matteo Bergami, Ben Berkhout, Laura Berliocchi, Amélie Bernard, Monique Bernard, Francesca Bernassola, Anne Bertolotti, Amanda S Be, Sébastien Besteiro, Saverio Bettuzzi, Savita Bhalla, Shalmoli Bhattacharyya, Sujit K Bhutia, Caroline Biagosch, Michele Wolfe Bianchi, Martine Biard-Piechaczyk, Viktor Bille, Claudia Bincoletto, Baris Bingol, Sara W Bird, Marc Bitoun, Ivana Bjedov, Craig Blackstone, Lionel Blanc, Guillermo A Blanco, Heidi Kiil Blomhoff, Emilio Boada-Romero, Stefan Böckler, Marianne Boe, Kathleen Boesze-Battaglia, Lawrence H Boise, Alessandra Bolino, Andrea Boman, Paolo Bonaldo, Matteo Bordi, Jürgen Bosch, Luis M Botana, Joelle Botti, German Bou, Marina Bouché, Marion Bouchecareilh, Marie- Josée Boucher, Michael E Boulton, Sebastien G Bouret, Patricia Boya, Michaël Boyer-Guittaut, Peter V Bozhkov, Nathan Brady, Vania MM Braga, Claudio Brancolini, Gerhard H Brau, José M Bravo-San Pedro, Lisa A Brennan, Emery H Bresnick, Patrick Brest, Dave Bridge, MarieAgnès Bringer, Marisa Brini, Glauber C Brito, Bertha Brodin, Paul S Brooke, Eric J Brown, Karen Brown, Hal E Broxmeyer, Alain Bruhat, Patricia Chakur Brum, John H Brumell, Nicola Brunetti-Pierri, Robert J Bryson-Richardson, Shilpa Buch, Alastair M Buchan, Hikmet Budak, Dmitry V Bulavin, Scott J Bultman, Geert Bultynck, Vladimir Bumbasirevic, Yan Burelle, Robert E Burke, Margit Burmeister, Peter Bütikofer, Laura Caberlotto, Ken Cadwell, Monika Cahova, Dongsheng Cai, Jingjing Cai, Qian Cai, Sara Calatayud, Nadine Camougrand, Michelangelo Campanella, Grant R Campbell, Matthew Campbell, Silvia Campello, Robin Candau, Isabella Caniggia, Lavinia Cantoni, Lizhi Cao, Allan B Caplan, Michele Caraglia, Claudio Cardinali, Sandra Morais Cardoso, Jennifer S Carew, Laura A Carleton, Cathleen R Carlin, Silvia Carloni, Sven R Carlsson, Didac Carmona-Gutierrez, Leticia AM Carneiro, Oliana Carnevali, Serena Carra, Alice Carrier, Bernadette Carroll, Caty Casa, Josefina Casa, Giuliana Cassinelli, Perrine Castet, Susana Castro-Obregon, Gabriella Cavallini, Isabella Ceccherini, Francesco Cecconi, Arthur I Cederbaum, Valentín Ceña, Simone Cenci, Claudia Cerella, Davide Cervia, Silvia Cetrullo, Hassan Chaachouay, Han-Jung Chae, Andrei S Chagin, Chee-Yin Chai, Gopal Chakrabarti, Georgios Chamilo, Edmond YW Chan, Matthew TV Chan, Dhyan Chandra, Pallavi Chandra, Chih-Peng Chang, Raymond Chuen-Chung Chang, Ta Yuan Chang, John C Chatham, Saurabh Chatterjee, Santosh Chauhan, Yongsheng Che, Michael E Cheetham, Rajkumar Cheluvappa, Chun-Jung Chen, Gang Chen, Guang-Chao Chen, Guoqiang Chen, Hongzhuan Chen, Jeff W Chen, Jian-Kang Chen, Min Chen, Mingzhou Chen, Peiwen Chen, Qi Chen, Quan Chen, Shang- Der Chen, Si Chen, Steve S-L Chen, Wei Chen, Wei-Jung Chen, Wen Qiang Chen, Wenli Chen, Xiangmei Chen, Yau-Hung Chen, Ye-Guang Chen, Yin Chen, Yingyu Chen, Yongshun Chen, Yu- Jen Chen, Yue-Qin Chen, Yujie Chen, Zhen Chen, Zhong Chen, Alan Cheng, Christopher HK Cheng, Hua Cheng, Heesun Cheong, Sara Cherry, Jason Chesney, Chun Hei Antonio Cheung, Eric Chevet, Hsiang Cheng Chi, Sung-Gil Chi, Fulvio Chiacchiera, Hui-Ling Chiang, Roberto Chiarelli, Mario Chiariello, Marcello Chieppa, Lih-Shen Chin, Mario Chiong, Gigi NC Chiu, Dong-Hyung Cho, Ssang-Goo Cho, William C Cho, Yong-Yeon Cho, Young-Seok Cho, Augustine MK Choi, Eui-Ju Choi, Eun-Kyoung Choi, Jayoung Choi, Mary E Choi, Seung-Il Choi, Tsui-Fen Chou, Salem Chouaib, Divaker Choubey, Vinay Choubey, Kuan-Chih Chow, Kamal Chowdhury, Charleen T Chu, Tsung-Hsien Chuang, Taehoon Chun, Hyewon Chung, Taijoon Chung, Yuen-Li Chung, Yong-Joon Chwae, Valentina Cianfanelli, Roberto Ciarcia, Iwona A Ciechomska, Maria Rosa Ciriolo, Mara Cirone, Sofie Claerhout, Michael J Clague, Joan Clària, Peter GH Clarke, Robert Clarke, Emilio Clementi, Cédric Cleyrat, Miriam Cnop, Eliana M Coccia, Tiziana Cocco, Patrice Codogno, Jörn Coer, Ezra EW Cohen, David Colecchia, Luisa Coletto, Núria S Coll, Emma Colucci-Guyon, Sergio Comincini, Maria Condello, Katherine L Cook, Graham H Coomb, Cynthia D Cooper, J Mark Cooper, Isabelle Coppen, Maria Tiziana Corasaniti, Marco Corazzari, Ramon Corbalan, Elisabeth Corcelle-Termeau, Mario D Cordero, Cristina Corral-Ramo, Olga Corti, Andrea Cossarizza, Paola Costelli, Safia Coste, Susan L Cotman, Ana Coto-Monte, Sandra Cottet, Eduardo Couve, Lori R Covey, L Ashley Cowart, Jeffery S Cox, Fraser P Coxon, Carolyn B Coyne, Mark S Cragg, Rolf J Craven, Tiziana Crepaldi, Jose L Crespo, Alfredo Criollo, Valeria Crippa, Maria Teresa Cruz, Ana Maria Cuervo, Jose M Cuezva, Taixing Cui, Pedro R Cutilla, Mark J Czaja, Maria F Czyzyk-Krzeska, Ruben K Dagda, Uta Dahmen, Chunsun Dai, Wenjie Dai, Yun Dai, Kevin N Dalby, Luisa Dalla Valle, Guillaume Dalmasso, Marcello D'Amelio, Markus Damme, Arlette Darfeuille-Michaud, Catherine Dargemont, Victor M Darley-Usmar, Srinivasan Dasarathy, Biplab Dasgupta, Srikanta Dash, Crispin R Da, Hazel Marie Davey, Lester M David, David Dávila, Roger J Davi, Ted M Dawson, Valina L Dawson, Paula Daza, Jackie de Belleroche, Paul de Figueiredo, Regina Celia Bressan Queiroz de Figueiredo, José de la Fuente, Luisa De Martino, Antonella De Mattei, Guido RY De Meyer, Angelo De Milito, Mauro De Santi, Wanderley de Souza, Vincenzo De Tata, Daniela De Zio, Jayanta Debnath, Reinhard Dechant, Jean-Paul Decuypere, Shane Deegan, Benjamin Dehay, Barbara Del Bello, Dominic P Del Re, Régis Delage-Mourroux, Lea MD Delbridge, Louise Deldicque, Elizabeth Delorme-Axford, Yizhen Deng, Joern Dengjel, Melanie Denizot, Paul Dent, Channing J Der, Vojo Deretic, Benoît Derrien, Eric Deutsch, Timothy P Devarenne, Rodney J Devenish, Sabrina Di Bartolomeo, Nicola Di Daniele, Fabio Di Domenico, Alessia Di Nardo, Simone Di Paola, Antonio Di Pietro, Livia Di Renzo, Aaron DiAntonio, Guillermo Díaz-Araya, Ines Díaz-Laviada, Maria T Diaz-Meco, Javier Diaz-Nido, Chad A Dickey, Robert C Dickson, Marc Diederich, Paul Digard, Ivan Dikic, Savithrama P Dinesh-Kumar, Chan Ding, Wen-Xing Ding, Zufeng Ding, Luciana Dini, Jörg HW Distler, Abhinav Diwan, Mojgan Djavaheri-Mergny, Kostyantyn Dmytruk, Renwick CJ Dobson, Volker Doetsch, Karol Dokladny, Svetlana Dokudovskaya, Massimo Donadelli, X Charlie Dong, Xiaonan Dong, Zheng Dong, Terrence M Donohue Jr, Kelly S Doran, Gabriella D'Orazi, Gerald W Dorn II, Victor Dosenko, Sami Dridi, Liat Drucker, Jie Du, Li-Lin Du, Lihuan Du, André du Toit, Priyamvada Dua, Lei Duan, Pu Duann, Vikash Kumar Dubey, Michael R Duchen, Michel A Duchosal, Helene Duez, Isabelle Dugail, Verónica I Dumit, Mara C Duncan, Elaine A Dunlop, William A Dunn Jr, Nicolas Dupont, Luc Dupui, Raúl V Durán, Thomas M Durcan, Stéphane Duvezin-Caubet, Umamaheswar Duvvuri, Vinay Eapen, Darius Ebrahimi-Fakhari, Arnaud Echard, Leopold Eckhart, Charles L Edelstein, Aimee L Edinger, Ludwig Eichinger, Tobias Eisenberg, Avital Eisenberg-Lerner, N Tony Eissa, Wafik S El-Deiry, Victoria El-Khoury, Zvulun Elazar, Hagit Eldar-Finkelman, Chris JH Elliott, Enzo Emanuele, Urban Emmenegger, Nikolai Engedal, Anna-Mart Engelbrecht, Simone Engelender, Jorrit M Enserink, Ralf Erdmann, Jekaterina Erenpreisa, Rajaraman Eri, Jason L Eriksen, Andreja Erman, Ricardo Escalante, Eeva- Liisa Eskelinen, Lucile Espert, Lorena Esteban-Martínez, Thomas J Evan, Mario Fabri, Gemma Fabria, Cinzia Fabrizi, Antonio Facchiano, Nils J Færgeman, Alberto Faggioni, W Douglas Fairlie, Chunhai Fan, Daping Fan, Jie Fan, Shengyun Fang, Manolis Fanto, Alessandro Fanzani, Thomas Farka, Mathias Faure, Francois B Favier, Howard Fearnhead, Massimo Federici, Erkang Fei, Tania C Felizardo, Hua Feng, Yibin Feng, Yuchen Feng, Thomas A Ferguson, Álvaro F Fernández, Maite G Fernandez-Barrena, Jose C Fernandez-Checa, Arsenio Fernández-López, Martin E Fernandez-Zapico, Olivier Feron, Elisabetta Ferraro, Carmen Veríssima Ferreira-Halder, Laszlo Fesu, Ralph Feuer, Fabienne C Fiesel, Eduardo C Filippi-Chiela, Giuseppe Filomeni, Gian Maria Fimia, John H Fingert, Steven Finkbeiner, Toren Finkel, Filomena Fiorito, Paul B Fisher, Marc Flajolet, Flavio Flamigni, Oliver Florey, Salvatore Florio, R Andres Floto, Marco Folini, Carlo Follo, Edward A Fon, Francesco Fornai, Franco Fortunato, Alessandro Fraldi, Rodrigo Franco, Arnaud Francoi, Aurélie Françoi, Lisa B Frankel, Iain DC Fraser, Norbert Frey, Damien G Freyssenet, Christian Frezza, Scott L Friedman, Daniel E Frigo, Dongxu Fu, José M Fuente, Juan Fueyo, Yoshio Fujitani, Yuuki Fujiwara, Mikihiro Fujiya, Mitsunori Fukuda, Simone Fulda, Carmela Fusco, Bozena Gabryel, Matthias Gaestel, Philippe Gailly, Malgorzata Gajewska, Sehamuddin Galadari, Gad Galili, Inmaculada Galindo, Maria F Galindo, Giovanna Galliciotti, Lorenzo Galluzzi, Luca Galluzzi, Vincent Galy, Noor Gammoh, Sam Gandy, Anand K Ganesan, Swamynathan Ganesan, Ian G Ganley, Monique Gannagé, Fen-Biao Gao, Feng Gao, Jian-Xin Gao, Lorena García Nannig, Eleonora García Véscovi, Marina Garcia-Macía, Carmen Garcia- Ruiz, Abhishek D Garg, Pramod Kumar Garg, Ricardo Gargini, Nils Christian Gassen, Damián Gatica, Evelina Gatti, Julie Gavard, Evripidis Gavathioti, Liang Ge, Pengfei Ge, Shengfang Ge, Po-Wu Gean, Vania Gelmetti, Armando A Genazzani, Jiefei Geng, Pascal Genschik, Lisa Gerner, Jason E Gestwicki, David A Gewirtz, Saeid Ghavami, Eric Ghigo, Debabrata Ghosh, Anna Maria Giammarioli, Francesca Giampieri, Claudia Giampietri, Alexandra Giatromanolaki, Derrick J Gibbing, Lara Gibellini, Spencer B Gibson, Vanessa Ginet, Antonio Giordano, Flaviano Giorgini, Elisa Giovannetti, Stephen E Girardin, Suzana Gispert, Sandy Giuliano, Candece L Gladson, Alvaro Glavic, Martin Gleave, Nelly Godefroy, Robert M Gogal Jr, Kuppan Gokulan, Gustavo H Goldman, Delia Goletti, Michael S Goligorsky, Aldrin V Gome, Ligia C Gome, Hernando Gomez, Candelaria Gomez-Manzano, Rubén Gómez-Sánchez, Dawit AP Gonçalve, Ebru Goncu, Qingqiu Gong, Céline Gongora, Carlos B Gonzalez, Pedro Gonzalez-Alegre, Pilar Gonzalez-Cabo, Rosa Ana González-Polo, Ing Swie Goping, Carlos Gorbea, Nikolai V Gorbunov, Daphne R Goring, Adrienne M Gorman, Sharon M Gorski, Sandro Goruppi, Shino Goto- Yamada, Cecilia Gotor, Roberta A Gottlieb, Illana Goze, Devrim Gozuacik, Yacine Graba, Martin Graef, Giovanna E Granato, Gary Dean Grant, Steven Grant, Giovanni Luca Gravina, Douglas R Green, Alexander Greenhough, Michael T Greenwood, Benedetto Grimaldi, Frédéric Gro, Charles Grose, Jean-Francois Groulx, Florian Gruber, Paolo Grumati, Tilman Grune, Jun-Lin Guan, Kun-Liang Guan, Barbara Guerra, Carlos Guillen, Kailash Gulshan, Jan Gunst, Chuanyong Guo, Lei Guo, Ming Guo, Wenjie Guo, Xu-Guang Guo, Andrea A Gust, Åsa B Gustafsson, Elaine Gutierrez, Maximiliano G Gutierrez, Ho-Shin Gwak, Albert Haa, James E Haber, Shinji Hadano, Monica Hagedorn, David R Hahn, 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L Semenza, Utpal Sen, Andreas L Serra, Ana Serrano-Puebla, Hiromi Sesaki, Takao Setoguchi, Carmine Settembre, John J Shacka, Ayesha N Shajahan-Haq, Irving M Shapiro, Shweta Sharma, Hua She, C-K James Shen, Chiung-Chyi Shen, Han-Ming Shen, Sanbing Shen, Weili Shen, Rui Sheng, Xianyong Sheng, Zu-Hang Sheng, Trevor G Shepherd, Junyan Shi, Qiang Shi, Qinghua Shi, Yuguang Shi, Shusaku Shibutani, Kenichi Shibuya, Yoshihiro Shidoji, Jeng- Jer Shieh, Chwen-Ming Shih, Yohta Shimada, Shigeomi Shimizu, Dong Wook Shin, Mari L Shinohara, Michiko Shintani, Takahiro Shintani, Tetsuo Shioi, Ken Shirabe, Ronit Shiri-Sverdlov, Orian Shirihai, Gordon C Shore, Chih-Wen Shu, Deepak Shukla, Andriy A Sibirny, Valentina Sica, Christina J Sigurdson, Einar M Sigurdsson, Puran Singh Sijwali, Beata Sikorska, Wilian A Silveira, Sandrine Silvente-Poirot, Gary A Silverman, Jan Simak, Thomas Simmet, Anna Katharina Simon, Hans-Uwe Simon, Cristiano Simone, Matias Simon, Anne Simonsen, Rajat Singh, Shivendra V Singh, Shrawan K Singh, Debasish Sinha, Sangita Sinha, Frank A Sinicrope, Agnieszka Sirko, Kapil Sirohi, Balindiwe JN Sishi, Annie Sittler, Parco M Siu, Efthimios Sivridi, Anna Skwarska, Ruth Slack, Iva Slaninová, Nikolai Slavov, Soraya S Smaili, Keiran SM Smalley, Duncan R Smith, Stefaan J Soenen, Scott A Soleimanpour, Anita Solhaug, Kumaravel Somasundaram, Jin H Son, Avinash Sonawane, Chunjuan Song, Fuyong Song, Hyun Kyu Song, Ju-Xian Song, Wei Song, Kai Y Soo, Anil K Sood, Tuck Wah Soong, Virawudh Soontornniyomkij, Maurizio Sorice, Federica Sotgia, David R Soto-Pantoja, Areechun Sotthibundhu, Maria João Sousa, Herman P Spaink, Paul N Span, Anne Spang, Janet D Spark, Peter G Speck, Stephen A Spector, Claudia D Spie, Wolfdieter Springer, Daret St Clair, Alessandra Stacchiotti, Bart Stael, Michael T Stang, Daniel T Starczynowski, Petro Starokadomskyy, Clemens Steegborn, John W Steele, Leonidas Stefani, Joan Steffan, Christine M Stellrecht, Harald Stenmark, Tomasz M Stepkowski, Stęphan T Stern, Craig Steven, Brent R Stockwell, Veronika Stoka, Zuzana Storchova, Björn Stork, Vassilis Stratoulia, Dimitrios J Stravopodi, Pavel Strnad, Anne Marie Strohecker, Anna- Lena Ström, Per Stromhaug, Jiri Stulik, Yu-Xiong Su, Zhaoliang Su, Carlos S Subauste, Srinivasa Subramaniam, Carolyn M Sue, Sang Won Suh, Xinbing Sui, Supawadee Sukseree, David Sulzer, Fang-Lin Sun, Jiaren Sun, Jun Sun, Shi-Yong Sun, Yang Sun, Yi Sun, Yingjie Sun, Vinod Sundaramoorthy, Joseph Sung, Hidekazu Suzuki, Kuninori Suzuki, Naoki Suzuki, Tadashi Suzuki, Yuichiro J Suzuki, Michele S Swanson, Charles Swanton, Karl Swärd, Ghanshyam Swarup, Sean T Sweeney, Paul W Sylvester, Zsuzsanna Szatmari, Eva Szegezdi, Peter W Szlosarek, Heinrich Taegtmeyer, Marco Tafani, Emmanuel Taillebourg, Stephen WG Tait, Krisztina Takacs-Vellai, Yoshinori Takahashi, Szabolcs Takát, Genzou Takemura, Nagio Takigawa, Nicholas J Talbot, Elena Tamagno, Jerome Tamburini, Cai-Ping Tan, Lan Tan, Mei Lan Tan, Ming Tan, Yee-Joo Tan, Keiji Tanaka, Masaki Tanaka, Daolin Tang, Dingzhong Tang, Guomei Tang, Isei Tanida, Kunikazu Tanji, Bakhos A Tannou, Jose A Tapia, Inmaculada Tasset-Cueva, Marc Tatar, Iman Tavassoly, Nektarios Tavernaraki, Allen Taylor, Graham S Taylor, Gregory A Taylor, J Paul Taylor, Mark J Taylor, Elena V Tchetina, Andrew R Tee, Fatima Teixeira-Clerc, Sucheta Telang, Tewin Tencomnao, Ba-Bie Teng, Ru-Jeng Teng, Faraj Terro, Gianluca Tettamanti, Arianne L Thei, Anne E Theron, Kelly Jean Thoma, Marcos P Thomé, Paul G Thome, Andrew Thorburn, Jeremy Thorner, Thomas Thum, Michael Thumm, Teresa LM Thurston, Ling Tian, Andreas Till, Jenny Pan-yun Ting, Vladimir I Titorenko, Lilach Toker, Stefano Toldo, Sharon A Tooze, Ivan Topisirovic, Maria Lyngaas Torgersen, Liliana Torosantucci, Alicia Torriglia, Maria Rosaria Torrisi, Cathy Tournier, Roberto Town, Vladimir Trajkovic, Leonardo H Travasso, Gemma Triola, Durga Nand Tripathi, Daniela Trisciuoglio, Rodrigo Troncoso, Ioannis P Trougako, Anita C Truttmann, Kuen-Jer Tsai, Mario P Tschan, Yi-Hsin Tseng, Takayuki Tsukuba, Allan Tsung, Andrey S Tsvetkov, Shuiping Tu, Hsing-Yu Tuan, Marco Tucci, David A Tumbarello, Boris Turk, Vito Turk, Robin FB Turner, Anders A Tveita, Suresh C Tyagi, Makoto Ubukata, Yasuo Uchiyama, Andrej Udelnow, Takashi Ueno, Midori Umekawa, Rika Umemiya-Shirafuji, Benjamin R Underwood, Christian Ungermann, Rodrigo P. Ureshino, Ryo Ushioda, Vladimir N Uversky, Néstor L Uzcátegui, Thomas Vaccari, Maria I Vaccaro, Libuše Váchová, Helin Vakifahmetoglu-Norberg, Rut Valdor, Enza Maria Valente, Francois Vallette, Angela M Valverde, Greet Van den Berghe, Ludo Van Den Bosch, Gijs R van den Brink, F Gisou van der Goot, Ida J van der Klei, Luc JW van der Laan, Wouter G van Doorn, Marjolein van Egmond, Kenneth L van Golen, Luc Van Kaer, Menno van Lookeren Campagne, Peter Vandenabeele, Wim Vandenberghe, Ilse Vanhorebeek, Isabel Varela-Nieto, M Helena Vasconcelo, Radovan Vasko, Demetrios G Vavva, Ignacio Vega- Naredo, Guillermo Velasco, Athanassios D Velentza, Panagiotis D Velentza, Tibor Vellai, Edo Vellenga, Mikkel Holm Vendelbo, Kartik Venkatachalam, Natascia Ventura, Salvador Ventura, Patrícia ST Vera, Mireille Verdier, Beata G Vertessy, Andrea Viale, Michel Vidal, Helena LA Vieira, Richard D Vierstra, Nadarajah Vigneswaran, Neeraj Vij, Miquel Vila, Margarita Villar, Victor H Villar, Joan Villarroya, Cécile Vindi, Giampietro Viola, Maria Teresa Viscomi, Giovanni Vitale, Dan T Vogl, Olga V Voitsekhovskaja, Clarissa von Haefen, Karin von Schwarzenberg, Daniel E Voth, Valérie Vouret-Craviari, Kristina Vuori, Jatin M Vya, Christian Waeber, Cheryl Lyn Walker, Mark J Walker, Jochen Walter, Lei Wan, Xiangbo Wan, Bo Wang, Caihong Wang, Chao-Yung Wang, Chengshu Wang, Chenran Wang, Chuangui Wang, Dong Wang, Fen Wang, Fuxin Wang, Guanghui Wang, Hai-jie Wang, Haichao Wang, Hong-Gang Wang, Hongmin Wang, Horng-Dar Wang, Jing Wang, Junjun Wang, Mei Wang, Mei-Qing Wang, Pei-Yu Wang, Peng Wang, Richard C Wang, Shuo Wang, Ting-Fang Wang, Xian Wang, Xiao-jia Wang, Xiao-Wei Wang, Xin Wang, Xuejun Wang, Yan Wang, Yanming Wang, Ying Wang, Ying-Jan Wang, Yipeng Wang, Yu Wang, Yu Tian Wang, Yuqing Wang, Zhi-Nong Wang, Pablo Wappner, Carl Ward, Diane McVey Ward, Gary Warne, Hirotaka Watada, Yoshihisa Watanabe, Kei Watase, Timothy E Full Terms & Conditions of access and use can be found at http://www.tandfonline.com/action/journalInformation?journalCode=kaup20 Download by: [Alma Mater Studiorum - Università di Bologna] Date: 23 September 2016, At: 06:43 Weaver, Colin D Weeke, Jiwu Wei, Thomas Weide, Conrad C Weihl, Günther Weindl, Simone Nardin Wei, Longping Wen, Xin Wen, Yunfei Wen, Benedikt Westermann, Cornelia M Weyand, Anthony R White, Eileen White, J Lindsay Whitton, Alexander J Whitworth, Joëlle Wiel, Franziska Wild, Manon E Wildenberg, Tom Wileman, Deepti Srinivas Wilkinson, Simon Wilkinson, Dieter Willbold, Chris William, Katherine William, Peter R Williamson, Konstanze F Winklhofer, Steven S Witkin, Stephanie E Wohlgemuth, Thomas Wollert, Ernst J Wolvetang, Esther Wong, G William Wong, Richard W Wong, Vincent Kam Wai Wong, Elizabeth A Woodcock, Karen L Wright, Chunlai Wu, Defeng Wu, Gen Sheng Wu, Jian Wu, Junfang Wu, Mian Wu, Min Wu, Shengzhou Wu, William KK Wu, Yaohua Wu, Zhenlong Wu, Cristina PR Xavier, Ramnik J Xavier, Gui-Xian Xia, Tian Xia, Weiliang Xia, Yong Xia, Hengyi Xiao, Jian Xiao, Shi Xiao, Wuhan Xiao, Chuan-Ming Xie, Zhiping Xie, Zhonglin Xie, Maria Xilouri, Yuyan Xiong, Chuanshan Xu, Congfeng Xu, Feng Xu, Haoxing Xu, Hongwei Xu, Jian Xu, Jianzhen Xu, Jinxian Xu, Liang Xu, Xiaolei Xu, Yangqing Xu, Ye Xu, Zhi-Xiang Xu, Ziheng Xu, Yu Xue, Takahiro Yamada, Ai Yamamoto, Koji Yamanaka, Shunhei Yamashina, Shigeko Yamashiro, Bing Yan, Bo Yan, Xianghua Yan, Zhen Yan, Yasuo Yanagi, Dun-Sheng Yang, Jin-Ming Yang, Liu Yang, Minghua Yang, Pei-Ming Yang, Peixin Yang, Qian Yang, Wannian Yang, Wei Yuan Yang, Xuesong Yang, Yi Yang, Ying Yang, Zhifen Yang, Zhihong Yang, Meng-Chao Yao, Pamela J Yao, Xiaofeng Yao, Zhenyu Yao, Zhiyuan Yao, Linda S Yasui, Mingxiang Ye, Barry Yedvobnick, Behzad Yeganeh, Elizabeth S Yeh, Patricia L Yeyati, Fan Yi, Long Yi, Xiao-Ming Yin, Calvin K Yip, Yeong-Min Yoo, Young Hyun Yoo, Seung-Yong Yoon, Ken-Ichi Yoshida, Tamotsu Yoshimori, Ken H Young, Huixin Yu, Jane J Yu, Jin-Tai Yu, Jun Yu, Li Yu, W Haung Yu, Xiao-Fang Yu, Zhengping Yu, Junying Yuan, Zhi-Min Yuan, Beatrice YJT Yue, Jianbo Yue, Zhenyu Yue, David N Zack, Eldad Zacksenhau, Nadia Zaffaroni, Tania Zaglia, Zahra Zakeri, Vincent Zecchini, Jinsheng Zeng, Min Zeng, Qi Zeng, Antonis S Zervo, Donna D Zhang, Fan Zhang, Guo Zhang, Guo-Chang Zhang, Hao Zhang, Hong Zhang, Hongbing Zhang, Jian Zhang, Jiangwei Zhang, Jianhua Zhang, Jing-pu Zhang, Li Zhang, Lin Zhang, Long Zhang, Ming-Yong Zhang, Xiangnan Zhang, Xu Dong Zhang, Yan Zhang, Yang Zhang, Yanjin Zhang, Yingmei Zhang, Yunjiao Zhang, Mei Zhao, Wei-Li Zhao, Xiaonan Zhao, Yan G Zhao, Ying Zhao, Yongchao Zhao, Yu-xia Zhao, Zhendong Zhao, Zhizhuang J Zhao, Dexian Zheng, Xi-Long Zheng, Xiaoxiang Zheng, Boris Zhivotovsky, Qing Zhong, Guang-Zhou Zhou, Guofei Zhou, Huiping Zhou, Shu-Feng Zhou, Xu-jie Zhou, Hongxin Zhu, Hua Zhu, Wei- Guo Zhu, Wenhua Zhu, Xiao-Feng Zhu, Yuhua Zhu, Shi-Mei Zhuang, Xiaohong Zhuang, Elio Ziparo, Christos E Zoi, Teresa Zoladek, Wei-Xing Zong, and Antonio Zorzano & Susu M Zughaier
Subjects: [SDV]Life Sciences [q-bio], autophagosome, Review Article, ddc:616.07, stress, stre, LC3, MESH: Animals, Settore MED/49 - Scienze Tecniche Dietetiche Applicate, Settore BIO/06 - Anatomia Comparata E Citologia, chaperone-mediated autophagy, ComputingMilieux_MISCELLANEOUS, Settore BIO/11, Pharmacology. Therapy, Settore BIO/13, standards [Biological Assay], autolysosome, MESH: Autophagy*/physiology, lysosome, methods [Biological Assay], Biological Assay, Settore BIO/17 - ISTOLOGIA, Erratum, Human, Biochemistry & Molecular Biology, Settore BIO/06, physiology [Autophagy], Chaperonemediated autophagy, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, NO, autophagy, guidelines, molecular biology, ultrastructure, flux, macroautophagy, phagophore, vacuole, MESH: Biological Assay/methods, MESH: Computer Simulation, ddc:570, Autolysosome, Autophagosome, Chaperonemediated autophagy, Flux, LC3, Lysosome, Macroautophagy, Phagophore, Stress, Vacuole, Autophagy, Animals, Humans, Computer Simulation, Settore BIO/10, ddc:612, Biology, MESH: Humans, Animal, 0601 Biochemistry And Cell Biology, MESH: Biological Assay/standards, Human medicine
Abstract: Seuls les 100 premiers auteurs dont les auteurs INRA ont été entrés dans la notice. La liste complète des auteurs et de leurs affiliations est accessible sur la publication.; International audience; In 2008 we published the first set of guidelines for standardizing research in autophagy. Since then, research on this topic has continued to accelerate, and many new scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Accordingly, it is important to update these guidelines for monitoring autophagy in different organisms. Various reviews have described the range of assays that have been used for this purpose. Nevertheless, there continues to be confusion regarding acceptable methods to measure autophagy, especially in multicellular eukaryotes.For example, a key point that needs to be emphasized is that there is a difference between measurements that monitor the numbers or volume of autophagic elements (e.g., autophagosomes or autolysosomes) at any stage of the autophagic process versus those that measure flux through the autophagy pathway (i.e., the complete process including the amount and rate of cargo sequestered and degraded). In particular, a block in macroautophagy that results in autophagosome accumulation must be differentiated from stimuli that increase autophagic activity, defined as increased autophagy induction coupled with increased delivery to, and degradation within, lysosomes (in most higher eukaryotes and some protists such as Dictyostelium) or the vacuole (in plants and fungi). In other words, it is especially important that investigators new to the field understand that the appearance of more autophagosomes does not necessarily equate with more autophagy. In fact, in many cases, autophagosomes accumulate because of a block in trafficking to lysosomes without a concomitant change in autophagosome biogenesis, whereas an increase in autolysosomes may reflect a reduction in degradative activity. It is worth emphasizing here that lysosomal digestion is a stage of autophagy and evaluating its competence is a crucial part of the evaluation of autophagic flux, or complete autophagy.Here, we present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macroautophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes. These guidelines are not meant to be a formulaic set of rules, because the appropriate assays depend in part on the question being asked and the system being used. In addition, we emphasize that no individual assay is guaranteed to be the most appropriate one in every situation, and we strongly recommend the use of multiple assays to monitor autophagy. Along these lines, because of the potential for pleiotropic effects due to blocking autophagy through genetic manipulation, it is imperative to target by gene knockout or RNA interference more than one autophagy-related protein. In addition, some individual Atg proteins, or groups of proteins, are involved in other cellular pathways implying that not all Atg proteins can be used as a specific marker for an autophagic process. In these guidelines, we consider these various methods of assessing autophagy and what information can, or cannot, be obtained from them. Finally, by discussing the merits and limits of particular assays, we hope to encourage technical innovation in the field.
Published: 2016
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21. Suppression of eIF2α kinases alleviates AD-related synaptic plasticity and spatial memory deficits

Author: Douglas R. Cavener, Eric Klann, Alyse J Wexler, Tao Ma, Clarisse Bourbon, Mimi A. Trinh, Evelina Gatti, and Philippe Pierre
Subjects: Male, Hippocampus, Mice, Transgenic, In Vitro Techniques, Biology, Presenilin, Article, Amyloid beta-Protein Precursor, Mice, eIF-2 Kinase, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Alzheimer Disease, Neuroplasticity, Presenilin-1, medicine, PSEN1, Animals, Humans, Maze Learning, Anisomycin, Aged, 030304 developmental biology, Aged, 80 and over, Protein Synthesis Inhibitors, Memory Disorders, 0303 health sciences, Neuronal Plasticity, General Neuroscience, Recognition, Psychology, Long-term potentiation, medicine.disease, Mice, Inbred C57BL, Disease Models, Animal, chemistry, Mutation, Synaptic plasticity, Female, Alzheimer's disease, Neuroscience, 030217 neurology & neurosurgery
Abstract: Expression of long-lasting synaptic plasticity and long-term memory requires protein synthesis, which can be repressed by phosphorylation of eukaryotic initiation factor 2 α-subunit (eIF2α). Elevated phosphorylation of eIF2α has been observed in the brains of Alzheimer's disease patients and Alzheimer's disease model mice. Therefore, we tested whether suppressing eIF2α kinases could alleviate synaptic plasticity and memory deficits in Alzheimer's disease model mice. Genetic deletion of eIF2α kinase PERK prevented enhanced phosphorylation of eIF2α and deficits in protein synthesis, synaptic plasticity and spatial memory in mice that express familial Alzheimer's disease-related mutations in APP and PSEN1. Similarly, deletion of another eIF2α kinase, GCN2, prevented impairments of synaptic plasticity and defects in spatial memory exhibited by the Alzheimer's disease model mice. Our findings implicate aberrant eIF2α phosphorylation as a previously unidentified molecular mechanism underlying Alzheimer's disease-related synaptic pathophysioloy and memory dysfunction and suggest that PERK and GCN2 are potential therapeutic targets for treatment of individuals with Alzheimer's disease.
Published: 2013

22. Mapping the crossroads of immune activation and cellular stress response pathways

Author: Nuno Cláudio, Alexandre Dalet, Philippe Pierre, and Evelina Gatti
Subjects: Inflammation, Review Article, Biology, Models, Biological, General Biochemistry, Genetics and Molecular Biology, Proinflammatory cytokine, Immune system, Stress, Physiological, Cellular stress response, medicine, Animals, Humans, Molecular Biology, Innate immune system, General Immunology and Microbiology, Endoplasmic reticulum, General Neuroscience, Chromosome Mapping, Receptor Cross-Talk, Endoplasmic Reticulum Stress, Cell biology, Immunity, Active, Unfolded protein response, Signal transduction, medicine.symptom, Signal Transduction
Abstract: The innate immune cell network detects specific microbes and damages to cell integrity in order to coordinate and polarize the immune response against invading pathogens. In recent years, a cross-talk between microbial-sensing pathways and endoplasmic reticulum (ER) homeostasis has been discovered and have attracted the attention of many researchers from the inflammation field. Abnormal accumulation of proteins in the ER can be seen as a sign of cellular malfunction and triggers a collection of conserved emergency rescue pathways. These signalling cascades, which increase ER homeostasis and favour cell survival, are collectively known as the unfolded protein response (UPR). The induction or activation by microbial stimuli of several molecules linked to the ER stress response pathway have led to the conclusion that microbe sensing by immunocytes is generally associated with an UPR, which serves as a signal amplification cascade favouring inflammatory cytokines production. Induction of the UPR alone was shown to promote inflammation in different cellular and pathological models. Here we discuss how the innate immune and ER-signalling pathways intersect. Moreover, we propose that the induction of UPR-related molecules by microbial products does not necessarily reflect ER stress, but instead is an integral part of a specific transcription programme controlled by innate immunity receptors.
Published: 2013
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23. Time trend of clinical cases of Lyme disease in two hospitals in Belgium, 2000–2013

Author: Mathilde de Keukeleire, Annie Robert, Victor Luyasu, Benoit Kabamba, Sophie O. Vanwambeke, Philippe Pierre, Leila Belkhir, UCL - SST/ELI/ELIC - Earth & Climate, UCL - SSS/IREC/EPID - Pôle d'épidémiologie et biostatistique, UCL - SSS/IREC/MBLG - Pôle de Microbiologie médicale, UCL - (SLuc) Service de microbiologie, and UCL - (SLuc) Service de médecine interne générale
Subjects: Adult, Male, 0301 basic medicine, medicine.medical_specialty, Pediatrics, Adolescent, Databases, Factual, 030231 tropical medicine, Lyme Borreliosis, Annual incidence, lcsh:Infectious and parasitic diseases, Young Adult, 03 medical and health sciences, 0302 clinical medicine, Lyme disease, Belgium, Clinical cases, medicine, Retrospective analysis, Humans, lcsh:RC109-216, Child, Aged, Retrospective Studies, Aged, 80 and over, Lyme Disease, business.industry, Lyme borreliosis, Incidence, Infant, Newborn, Infant, Middle Aged, Recording system, medicine.disease, Hospitals, Hospitalization, 030104 developmental biology, Infectious Diseases, Child, Preschool, Hospital admission, Tropical medicine, Female, business, Research Article
Abstract: Background As several studies indicated an increase in Lyme disease (LD), notably in neighbouring countries, concerns have arisen regarding the evolution of Lyme disease in Belgium. In order to confirm or infirm the increase of LD in Belgium, we focused on hospital admissions of patients diagnosed with LD between 2000 and 2013 based on hospital admission databases from two hospitals in Belgium. Methods Hospital databases are a stable recording system. We did a retrospective analysis of the medical files of patients hospitalized with Lyme disease in two Belgian hospitals between 2000 and 2013. Results The annual number of cases of LD for the two studied Belgian hospitals remained stable between 2000 and 2013, ranging from 1 for the Cliniques universitaires Saint-Luc to 15 for the the Clinique Saint-Pierre. No increasing trend were noted in the estimated annual incidence rate but the average estimated annual incidence rate was higher for the hospital Saint-Pierre (8.1 ± 3.7 per 100,000 inhabitants) than Saint-Luc (2.2 ± 1.5 per 100,000 inhabitants). The number of hospital cases of LD peaked between June and November. Conclusions Based on hospital admissions with LD, no increasing trend was observed for the period 2000–2013 in the two studied Belgian hospitals. This is in line with other studies carried out in Belgium.
Published: 2017

24. Inhibition of protein translation as a mechanism of acidotic pH protection against ischaemic injury through inhibition of CREB mediated tRNA synthetase expression

Author: Martin O. Leonard, Luca Felice, Daniel Crean, Philippe Pierre, and Paul Jennings
Subjects: Programmed cell death, Cycloheximide, CREB, Brain Ischemia, Amino Acyl-tRNA Synthetases, 03 medical and health sciences, chemistry.chemical_compound, Mice, 0302 clinical medicine, Gene expression, Cyclic AMP Response Element-Binding Protein, Protein biosynthesis, Animals, Humans, Transcription factor, Cells, Cultured, 030304 developmental biology, 0303 health sciences, biology, Gene Expression Profiling, Cell Biology, Hydrogen-Ion Concentration, Molecular biology, Mice, Inbred C57BL, Oxygen, Glucose, chemistry, 030220 oncology & carcinogenesis, Brain Injuries, Protein Biosynthesis, Unfolded protein response, biology.protein, Acidosis
Abstract: Ischaemia associated reduction in local tissue pH is well documented but the mechanisms through which it influences cell survival remain poorly understood. Using renal epithelial HK-2 cells we demonstrate acidotic pH6.4 protects against oxygen glucose deprivation (OGD) induced cell death. Initial exploration of the mechanisms responsible using microarray analysis revealed acidotic inhibition of OGD induced aminoacyl-tRNA synthetase (ARS) gene expression. These genes are key components of protein translation, which was markedly attenuated by reduced pH. Inhibition of protein synthesis using the ARS inhibitor halofuginone or cycloheximide protected against OGD induced injury. To explore further we focussed on the transcription factor CREB, identified by pathway analysis of microarray data and observed a pH dependent decrease in OGD induced activation. Inhibition of CREB/CBP interaction prevented OGD induced isoleucyl-ARS (IARS) expression, reduced protein synthesis and protected against OGD induced cellular injury. In addition we also observed that acidotic pH attenuated the OGD induced pro-apoptotic unfolded protein response (UPR) activated gene DDIT3. We suggest that maladaptive activation of CREB and ARS gene expression, through the maintenance of protein synthesis contributes to ER stress and UPR activation and that acidotic pH through inhibition of CREB activation inhibits protein synthesis and ultimately UPR activated apoptotic signals.
Published: 2013
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25. On the cellular metabolism of the click chemistry probe 19-alkyne arachidonic acid[S]

Author: Eric Boilard, Luc H. Boudreau, David Barnett, Philippe Pierre Robichaud, Marc E. Surette, Samuel J. Poirier, and Jérémie A. Doiron
Subjects: 0301 basic medicine, Leukotriene B4, Neutrophils, Phospholipid, QD415-436, Arachidonic Acids, Arachidonate 12-Lipoxygenase, Biochemistry, phospholipid remodeling, 03 medical and health sciences, chemistry.chemical_compound, Jurkat Cells, Endocrinology, hemic and lymphatic diseases, Humans, Research Articles, Phospholipids, Leukotriene, Arachidonate 5-Lipoxygenase, leukotriene, Biological activity, Leukotriene B4 Receptor 1, Cell Biology, Metabolism, lipoxygenase, cyclooxygenase, 030104 developmental biology, chemistry, Eicosanoid, eicosanoid, Arachidonic acid, Click Chemistry
Abstract: Alkyne and azide analogs of natural compounds that can be coupled to sensitive tags by click chemistry are powerful tools to study biological processes. Arachidonic acid (AA) is a FA precursor to biologically active compounds. 19-Alkyne-AA (AA-alk) is a sensitive clickable AA analog; however, its use as a surrogate to study AA metabolism requires further evaluation. In this study, AA-alk metabolism was compared with that of AA in human cells. Jurkat cell uptake of AA was 2-fold greater than that of AA-alk, but significantly more AA-Alk was elongated to 22:4. AA and AA-alk incorporation into and remodeling between phospholipid (PL) classes was identical indicating equivalent CoA-independent AA-PL remodeling. Platelets stimulated in the presence of AA-alk synthesized significantly less 12-lipoxygenase (12-LOX) and cyclooxygenase products than in the presence of AA. Ionophore-stimulated neutrophils produced significantly more 5-LOX products in the presence of AA-alk than AA. Neutrophils stimulated with only exogenous AA-alk produced significantly less 5-LOX products compared with AA, and leukotriene B4 (LTB4)-alk was 12-fold less potent at stimulating neutrophil migration than LTB4, collectively indicative of weaker leukotriene B4 receptor 1 agonist activity of LTB4-alk. Overall, these results suggest that the use of AA-alk as a surrogate for the study of AA metabolism should be carried out with caution.
Published: 2016

26. Sleep deprivation impairs memory by attenuating mTORC1-dependent protein synthesis

Author: Ted Abel, Caroline W. Chung, Emily J. Davis, Shane G. Poplawski, Erik van Tilborg, Mathieu E. Wimmer, Jennifer C. Tudor, Lucia Peixoto, Evelina Gatti, Alan J. Park, Philippe Pierre, Jiayan Huang, Robbert Havekes, Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), and Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)
Subjects: 0301 basic medicine, Male, mTORC1, Hippocampal formation, Biochemistry, Hippocampus, chemistry.chemical_compound, Mice, 0302 clinical medicine, Cognition, Neurobiology, Eukaryotic Initiation Factors, Phosphorylation, Endoplasmic Reticulum Chaperone BiP, Heat-Shock Proteins, Neurons, EIF4G, EIF4E, Brain, Sleep in non-human animals, Immunohistochemistry, 3. Good health, [SDV.IMM]Life Sciences [q-bio]/Immunology, Puromycin, medicine.symptom, medicine.medical_specialty, Blotting, Western, Enzyme-Linked Immunosorbent Assay, Nerve Tissue Proteins, Biology, Mechanistic Target of Rapamycin Complex 1, Real-Time Polymerase Chain Reaction, Article, Statistics, Nonparametric, 03 medical and health sciences, Memory, Internal medicine, medicine, Initiation factor, Humans, Animals, Molecular Biology, Memory Disorders, Cell Biology, Mice, Inbred C57BL, Sleep deprivation, Cytoskeletal Proteins, 030104 developmental biology, Endocrinology, Eukaryotic Initiation Factor-4E, chemistry, Protein Biosynthesis, Sleep Deprivation, Eukaryotic Initiation Factor-4G, 030217 neurology & neurosurgery
Abstract: Sleep deprivation is a public health epidemic that causes wide-ranging deleterious consequences, including impaired memory and cognition. Protein synthesis in hippocampal neurons promotes memory and cognition. The kinase complex mammalian target of rapamycin complex 1 (mTORC1) stimulates protein synthesis by phosphorylating and inhibiting the eukaryotic translation initiation factor 4E binding protein 2 (4EBP2). We investigated the involvement of the mTORC1-4EBP2 axis in the molecular mechanisms mediating the cognitive deficits caused by sleep deprivation in mice. Using an in vivo protein translation assay, we found that loss of sleep impaired protein synthesis in the hippocampus. Five hours of sleep loss attenuated both mTORC1-mediated phosphorylation of 4EBP2 and the interaction between eukaryotic initiation factor 4E (eIF4E) and eukaryotic initiation factor 4G (eIF4G) in the hippocampi of sleep-deprived mice. Increasing the abundance of 4EBP2 in hippocampal excitatory neurons prior to sleep deprivation increased the abundance of phosphorylated 4EBP2, restored the amount of eIF4E-eIF4G interaction and hippocampal protein synthesis to that seen in mice that were not sleep-deprived, and prevented the hippocampus-dependent memory deficits associated with sleep loss. These findings collectively demonstrate that 4EBP2-regulated protein synthesis is a critical mediator of the memory deficits caused by sleep deprivation.
Published: 2016
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27. Unfolded protein response gene GADD34 is overexpressed in rheumatoid arthritis and related to the presence of circulating anti-citrullinated protein antibodies

Author: Laurent Grange, Maxime Chevreau, Philippe Pierre, Candice Trocme, Marine Clay, Souad Adriouach, Evelina Gatti, Jean-Louis Quesada, Jean-Yves Cesbron, Chantal Dumestre-Pérard, Philippe Gaudin, Giovanna Clavarino, Barrière Naturelle et Infectiosité (TIMC-IMAG-BNI), Techniques de l'Ingénierie Médicale et de la Complexité - Informatique, Mathématiques et Applications, Grenoble - UMR 5525 (TIMC-IMAG), Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Laboratoire d'immunologie, CHU Grenoble, Direction de la Recherche Clinique et de l'Innovation, Pole Recherche, Clinique Universitaire de Rhumatologie, hôpital Sud, CHU de Grenoble, Université Grenoble Alpes - UFR Médecine (UGA UFRM), Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Laboratoire de Biochemie des enzymes et des protéines, Centre Hospitalier Universitaire [Grenoble] (CHU), Centre d'Immunologie de Marseille - Luminy (CIML), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU), and Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)
Subjects: 0301 basic medicine, Male, Immunology, Gene Expression, Peripheral blood mononuclear cell, Proinflammatory cytokine, Arthritis, Rheumatoid, 03 medical and health sciences, Protein Phosphatase 1, Gene expression, Odds Ratio, Immunology and Allergy, Medicine, Humans, ComputingMilieux_MISCELLANEOUS, Autoantibodies, biology, business.industry, Anti–citrullinated protein antibody, 3. Good health, 030104 developmental biology, Real-time polymerase chain reaction, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, Case-Control Studies, Unfolded protein response, biology.protein, Leukocytes, Mononuclear, Biomarker (medicine), Female, Antibody, business, Biomarkers
Abstract: Growth arrest and DNA damage-inducible gene 34 (GADD34) is an inducible cofactor of protein phosphatase 1, which has an important role in the unfolded protein response. GADD34 has been shown to be necessary for type I interferon and proinflammatory cytokine production in response to viral infection in murine models. We investigate the expression of GADD34 in rheumatoid arthritis (RA), in which proinflammatory cytokines have an important pathogenic role. The objective of this study was to evaluate the potential of GADD34 expression as a biomarker in RA patients. We report a case-control study on GADD34 gene expression in peripheral blood mononuclear cells of patients (n = 75) with RA and age- and sex-matched healthy controls (n = 25). The study was approved by the relevant local ethics committees. GADD34 gene expression level in peripheral blood mononuclear cells was measured by quantitative PCR and analyzed with Mann-Whitney test. The relation between GADD34 gene overexpression and clinical or biological characteristics was analyzed with univariate and multivariate analysis. GADD34 gene expression was significantly higher in RA patients compared with healthy controls (p ≤ 0.001). Interestingly, GADD34 overexpression in PBMC of patients was related to the presence of circulating anti-citrullinated protein antibodies (p = 0.030). Data of this study strengthen the evidence of an unfolded protein response during the course of RA and provide an insight of the potential interest in GADD34 as a relevant marker for RA.
Published: 2016

28. Large G3BP-induced granules trigger eIF2α phosphorylation

Author: Lucas C. Reineke, Philippe Pierre, Richard E. Lloyd, and Jonathan D. Dougherty
Subjects: Biosynthesis and Biodegradation, Blotting, Western, Eukaryotic Initiation Factor-2, Green Fluorescent Proteins, Biology, Cytoplasmic Granules, Transfection, 03 medical and health sciences, Mice, eIF-2 Kinase, Stress granule, Eukaryotic translation, Eukaryotic initiation factor, Animals, Humans, Phosphorylation, Poly-ADP-Ribose Binding Proteins, Molecular Biology, Cells, Cultured, 030304 developmental biology, Mice, Knockout, 0303 health sciences, EIF-2 kinase, Microscopy, Confocal, Stress granule disassembly, 030302 biochemistry & molecular biology, Granule (cell biology), DNA Helicases, Cell Biology, Articles, Fibroblasts, Embryo, Mammalian, Protein kinase R, Cell biology, RNA Recognition Motif Proteins, Ribonucleoproteins, Protein Biosynthesis, Mutation, biology.protein, Carrier Proteins, RNA Helicases, HeLa Cells
Abstract: Increasing size of G3BP-induced stress granules is associated with a threshold or switch that must be triggered for eIF2α phosphorylation and subsequent translational repression to occur. Stress granules are active in signaling to the translational machinery and may be important regulators of the innate immune response., Stress granules are large messenger ribonucleoprotein (mRNP) aggregates composed of translation initiation factors and mRNAs that appear when the cell encounters various stressors. Current dogma indicates that stress granules function as inert storage depots for translationally silenced mRNPs until the cell signals for renewed translation and stress granule disassembly. We used RasGAP SH3-binding protein (G3BP) overexpression to induce stress granules and study their assembly process and signaling to the translation apparatus. We found that assembly of large G3BP-induced stress granules, but not small granules, precedes phosphorylation of eIF2α. Using mouse embryonic fibroblasts depleted for individual eukaryotic initiation factor 2α (eIF2α) kinases, we identified protein kinase R as the principal kinase that mediates eIF2α phosphorylation by large G3BP-induced granules. These data indicate that increasing stress granule size is associated with a threshold or switch that must be triggered in order for eIF2α phosphorylation and subsequent translational repression to occur. Furthermore, these data suggest that stress granules are active in signaling to the translational machinery and may be important regulators of the innate immune response.
Published: 2012

29. RNA Binding Targets Aminoacyl-tRNA Synthetases to Translating Ribosomes

Author: Nir Netzer, Jack R. Bennink, Michael Brad Strader, Philippe Pierre, Alexandre David, Cai Yun Chen, Suman R. Das, Jonathan W. Yewdell, James S. Gibbs, National Institutes of Health [Bethesda] (NIH), Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), and Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)
Subjects: RNA-binding protein, Alphavirus, Poxviridae Infections, Biology, Biochemistry, Ribosome, Amino Acyl-tRNA Synthetases, 03 medical and health sciences, chemistry.chemical_compound, Stress granule, Protein biosynthesis, Humans, RNA, Messenger, Molecular Biology, 030304 developmental biology, 0303 health sciences, Messenger RNA, Alphavirus Infections, Aminoacyl tRNA synthetase, Poxviridae, 030302 biochemistry & molecular biology, RNA, Translation (biology), Cell Biology, HEK293 Cells, chemistry, Protein Synthesis and Degradation, Protein Biosynthesis, [SDV.IMM]Life Sciences [q-bio]/Immunology, Ribosomes, HeLa Cells
Abstract: International audience; Here, we examine tRNA-aminoacyl synthetase (ARS) localization in protein synthesis. Proteomics reveals that ten of the twenty cytosolic ARSs associate with ribosomes in sucrose gradients: phenylalanyl-RS (FRS), and the 9 ARSs that form the multi-ARS complex (MSC). Using the ribopuromycylation method (RPM) for localizing intracellular translation, we show that FRS and the MSC, and to a lesser extent other ARSs, localize to translating ribosomes, most strikingly when translation is restricted to poxvirus or alphavirus factories in infected cells. Immunoproximity fluorescence indicates close proximity between MSC and the ribosome. Stress induced-translational shutdown recruits the MSC to stress-granules, a depot for mRNA and translation components. MSC binding to mRNA provides a facile explanation for its delivery to translating ribosomes and stress granules. These findings, along with the abundance of the MSC (9 × 10(6) copies per cell, roughly equimolar with ribosomes), is consistent with the idea that MSC specificity, recently reported to vary with cellular stress (Netzer, N., Goodenbour, J. M., David, A., Dittmar, K. A., Jones, R. B., Schneider, J. R., Boone, D., Eves, E. M., Rosner, M. R., Gibbs, J. S., Embry, A., Dolan, B., Das, S., Hickman, H. D., Berglund, P., Bennink, J. R., Yewdell, J. W., and Pan, T. (2009) Nature 462, 522-526) can be modulated at the level of individual mRNAs to modify decoding of specific gene products.
Published: 2011
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30. Chikungunya Virus Induces IPS-1-Dependent Innate Immune Activation and Protein Kinase R-Independent Translational Shutoff

Author: Victor R. DeFilippis, David Alvarado, Daniel N. Streblow, Tina M. Sali, Philippe Pierre, Evelina Gatti, and Laura White
Subjects: viruses, Immunology, Biology, Microbiology, Cell Line, eIF-2 Kinase, Interferon, Cricetinae, Virology, Eukaryotic initiation factor, medicine, Animals, Humans, Transcription factor, Cells, Cultured, Adaptor Proteins, Signal Transducing, Immune Evasion, EIF-2 kinase, Innate immune system, Proteins, virus diseases, Interferon-beta, Fibroblasts, Protein kinase R, Immunity, Innate, Virus-Cell Interactions, Gene Expression Regulation, Protein Biosynthesis, Insect Science, biology.protein, IRF3, Chikungunya virus, Interferon regulatory factors, medicine.drug
Abstract: Chikungunya virus (CHIKV) is an arthritogenic mosquito-transmitted alphavirus that is undergoing reemergence in areas around the Indian Ocean. Despite the current and potential danger posed by this virus, we know surprisingly little about the induction and evasion of CHIKV-associated antiviral immune responses. With this in mind we investigated innate immune reactions to CHIKV in human fibroblasts, a demonstrable in vivo target of virus replication and spread. We show that CHIKV infection leads to activation of the transcription factor interferon regulatory factor 3 (IRF3) and subsequent transcription of IRF3-dependent antiviral genes, including beta interferon (IFN-β). IRF3 activation occurs by way of a virus-induced innate immune signaling pathway that includes the adaptor molecule interferon promoter stimulator 1 (IPS-1). Despite strong transcriptional upregulation of these genes, however, translation of the corresponding proteins is not observed. We further demonstrate that translation of cellular (but not viral) genes is blocked during infection and that although CHIKV is found to trigger inactivation of the translational molecule eukaryotic initiation factor subunit 2α by way of the double-stranded RNA sensor protein kinase R, this response is not required for the block to protein synthesis. Furthermore, overall diminution of cellular RNA synthesis is also observed in the presence of CHIKV and transcription of IRF3-dependent antiviral genes appears specifically blocked late in infection. We hypothesize that the observed absence of IFN-β and antiviral proteins during infection results from an evasion mechanism exhibited by CHIKV that is dependent on widespread shutoff of cellular protein synthesis and a targeted block to late synthesis of antiviral mRNA transcripts.
Published: 2011
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31. Novel 5‐lipoxygenase isoforms affect the biosynthesis of 5‐lipoxygenase products

Author: Mark Laflamme, Luc H. Boudreau, Rodney J. Ouellette, Nicolas Flamand, Philippe Pierre Robichaud, Jonathan O Bertin, and Marc E. Surette
Subjects: Gene isoform, Leukotrienes, Neutrophils, Biochemistry, Isozyme, Gene Expression Regulation, Enzymologic, 03 medical and health sciences, Exon, Enzyme activator, 0302 clinical medicine, Genetics, Humans, RNA, Messenger, Molecular Biology, Cell Line, Transformed, 030304 developmental biology, Inflammation, B-Lymphocytes, 0303 health sciences, Arachidonate 5-Lipoxygenase, biology, Chemistry, Alternative splicing, Intron, Exons, Burkitt Lymphoma, Enzyme Activation, Isoenzymes, Alternative Splicing, HEK293 Cells, 030220 oncology & carcinogenesis, Leukemia, Monocytic, Acute, Arachidonate 5-lipoxygenase, RNA splicing, biology.protein, Eicosanoids, Biotechnology
Abstract: 5-Lipoxygenase (5-LO) is the essential enzyme for the biosynthesis of leukotrienes, important mediators of inflammation. This study investigated whether variants of 5-LO exist in human leukocytes. 5-LO mRNA isoforms that are consistent with alternative splicing were identified by RT-PCR in a cell line or cell type-specific pattern. All evaluated cells expressed mRNA containing all 14 exons of 5-LO with the expected splicing sites. Individual isoforms that retained intron 10 (α-10), lacked exon 13 (Δ-13), and lacked exons 10 and 13 (Δ-10,13) or that lacked the first 96 base pairs of exon 10 (Δ-p10) were identified. Immunoreactive bands coeluting with the cloned α-10 and Δ-13 isoforms were measured in primary neutrophils and in Raji cells. When expressed in HEK293 cells, alternative proteins were without catalytic activity. However, when coexpressed with the active full-length 5-LO, alternative isoforms significantly decreased the biosynthesis of 5-LO products by up to 44%, as assessed by reverse-phase HPLC analysis. Additionally, in stimulated neutrophils the full-length active 5-LO was detected by immunoblot in both nuclear and non-nuclear compartments, while the Δ-13 isoform was only detected in the nuclear fraction. These alternative 5-LO isoforms may represent a new mechanism for the regulation of the 5-LO pathway and lipid mediator biosynthesis.
Published: 2010
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32. Venous thromboembolism risk and prophylaxis in hospitalised medically ill patients

Author: Kaynar, Leylagül, Yildirim, Cuma, PANTOJA, Joao, Rocha, Ana, SCHRAMM, Edgar, TIMI, Jorge, STAIKOV, Ivan, BENOV, Haralambi, MIRAZCHIJSKI, Boyko, STATELOV, Evgenii, STOYKOVA, Antoaneta, TODOROV, Radostin, DENNIS, Rodolfo, DURA, Freddy Rafael Mendez, RESTREPO, Hector, ROA, Jairo H., VILLADIEGO, Juan, MALY, Jaroslav, BRABEC, Tomas, GUMULEC, Jaromir, JOCHYMEK, Roman, KELLNEROVA, Ivana, SKARKOVA, Jindra, SLEZAK, Premysl, VIT, Patrik, GOBRAN, Hadi, EL HADDAD, Alaa, RIZK-ALLAH, Mounir, BERGMANN, Jean Francois, ABINADER, Marid, KHOUDIR, Falah Abou, BOYER, Jean-Francois, BRUN, Natacha, CANET, Bernard, COLLARD, Catherine, CORDIER, Christophe, DURROUX, Claire, EMMERICH, Joseph, FRIOCOURT, Patrick, ANDERSON, Frederick A., CHERFI, Lyes, AMMOUR, Dehbia, BOURENANE, Razika, GRAINAT, Nadia, MAAROUF, Abderahmane, SISSAOUI, Abdelhak, GALLUS, Alexander, AYYAR, Venkatraman, CRIMMINS, Denis, GAN, Eng, MCRAE, Simon, SELDON, Michael, SINGH, Bhuwan, MOULA, Kaniz, NAWAZ, Taimor, NAZIMUDDIN, Khwaja, RAHMAN, Saiyeedur, SARKER, Shyamal, BRANDAO, Carlos, COSTA, Jose, MACEDO, Alex, MARINO, Roberto, MENEZES, Paulo, Bergmann, Jean-Francois, Cohen, Alexander T., Tapson, Victor F., Goldhaber, Samuel Z., Kakkar, Ajay K., Deslandes, Bruno, MOUMEN, Abdelrhani, PHILIPPE, Pierre, PROTIN, Yves, QUERE, Isabelle, RIZCALLAH, Marie-Jeanne, BENSCH, Kristina, BENSMANN, Klaus, Dropmann, Axl, Gerold, Dieter, Gussmann, Andreas, Kube, Lutz, Kuster, Stefan, Leupolz, Werner, Neuhaus, Thomas, Nobel, Wolfgang, Pfiel, Sascha, Pleger, Eberhard, Trautmann, Harald, Voigt, Ingo, Liapis, Christos, Antoniadis, Pavlos, Arvanitis, Dimitrios, Bakatsglos, Spyridon, Christakis, Christos, Gerassimidis, Thomas, Kostakis, Alkiviadis, Losonczy, Hajna, Hajna, Bela, Gyani, Eva, Jojart, Istvan, Kecskes, Gabor, Lakatos, Jozsef, Ledniczki, Istvan, Mayer, Klara, Nyuzo, Balint, Zeher, Margit, Agnihotri, Vinod, Balraj, A., Chakraborty, Amiya, Desai, Sanjay, Elangovan, Antony, Goswami, Partha, Rupert, Emmanuel, Toraskar, Kedar, Venkatesh, Kakollu, Gaine, Sean, Costello, Richard, Liston, Richard, Zubieta, Ricardo Martinez, Fematt, Flor Mario Avila, Esponda, Juan Alejandro Baeza, Benitez Maldonado, Daniel R., Serrano, Maricela Escarela, Montalvo, Carlos Lavalle, Marquez, Santa Lopez, Sanchez, Alejandro Quesada, Diaz, Santiago Ramirez, Serrano, Alejandro Tovar, de la Vega, Maria Isabel Villa, Faridi, Salman, Javaid, Mansur, Khan, Farrukh, Malik, Asif Zafar, Sadiq, Muzafaruddin, Musial, Jacek, Biedziuk, Bartlomiej, Gellert, Ryszard, Kosiniau-Kamysz, Andrzey, Kuta, Marcin, Prajs, Zozislav, Sell, Marek, Tadeusz, Kalbarczyk, Witkiewicz, Wojciech, Wysota, Janusz, Franca, Ana, Abreu, Rui, Cartucho, Daniel, Lohmann, Corinna, Moreira, Pedro, Paulino, Aida, Reis, Abilio, Rojao de Morais, Maria Luisa, Tribolet de Abreu, Tiago, Tulbure, Dan, Andrei, Muresan, Christian, Pricop, Ciurea, Mircea, Enachescu, Mihaela, Gostian, Ovidiu, Grintescu, Ioana Marina, Mimor, Ovidiu, Natalia, Hagau, Puiac, Claudiu, Valerica, Stan, Sulimov, Vitalyi Andreevich, Belentsov, Sergey, Eliseeva, Ekaterina, Fridman, Irina, Kazantchian, Perch, Mashtacov, Boris, Redkin, Alexander, Rodoman, Grigory, Shershnev, Vladislav, Zhidkov, Konstantin, Gaspar, Ludovit, Benova, Katarina, Duris, Tibor, Fecik, Juraj, Hajas, Jan, Herman, Oto, Lehotsky, Jan, Macek, Vladimir, Pradova, Viera, Carrascosa, Miguel, Luque, Rafael Cuenca, del Val Gil, Jose, Diaz de Souza, Pedro, Enfedaque, Muriel Alvaro, Gonzalo, Francesc Epelde, Sanchez, Florentino Garcia, Garcia, Guil, Lopez, Luciano, Rodriguez, Jose Antonio Nieto, Mateo Paredes, Ramon, Ramos Rodriguez, Jose Luis, Cantero, Alberto Ruiz, Lorenzo, Pedro Ruiz, Legarre, Angel Luis Samperiz, Clavo Sanchez, Antonio, Bernad, Reina Valle, Vela Moreno, Jeronimo Ramon, Doerffler, Janine, Beer, Jurg, Brunner, Brigitte, Chopard, Pierre, Fischer, Joseph, Ludwig, Christian, Rime, Francis, Salomon, Franco, Ulrich, Munch, Angchaisuksiri, Pantep, Chetanachan, Mariam, Chuamuangphan, Nonlawan, Insiripong, Somchai, Nawarawong, Weerasak, Ben Salah, Afif, Houman, Mohamed Habib, Mohamed, Mnif, Samir, Kammoun, Smiti-Khanfir, Monia, Zouheir, Jerbi, Ongen, Gul, Altintas, Faik, Cirak, Ali Kadri, Demirtas, Nazmi, Erden, Faruk, Guven, Hulya, Halezeroglu, Semih, Karaoglan, Halim, Tereci, Hikmet, Wilmott, Rosalind, Cohen, Alexander, Calvey, Thomas, Cohen, Angela, Gallegos, Nick, Gaminara, Elizabeth, James, Anthony, Jeffreys, Mike, Jowett, Nigel, Keaney, Niall, Kesteven, Patrick, Khan, Zafar, Mallick, Abhiram, Marval, Paul, Parapia, L., Picozzi, Natalie, Praveen, Bandipalyam, Satchi, Gnanam, Valerio, David, Tapson, Victor, Anderson, Fred, Baker, Gennfer, Beaver, Richard, Becker, William, Beckett, Cynthia, Borchardt, Carla, Briggs, Michael, Bruckman, Joseph, Buck, Lisa, Chausow, Alan, Christopulos, Danielle, Cica, Paula, Cody, Jean, Condit, Bruce, Cronin, Sherill, Huang, Wei, BENTAKOUK, Cherif, SIDDIQUI, F. M., OIGMAN, Wille, PAIVA, Marcelo, TANDEITNIK, Liane, BORISOV, Stefan Dimitrov, LALOV, Anton, POSTADZIYAN, Arman, Cysyk, Barbara, Driggers, Steven, Ellis, Paula, Elvenia, Jaeda, Feinbloom, David, Feldman, Mark, Fischer, Marian, Froehlich, James, Frost, Christopher, Galster, Ruth, Geldmeier, Richard, George, Joyce, Glielmi, Vincent, Goodwin, James, Gottlieb, Anita, Gray, Bruce, Harrington, Darrell, Henry, Edwina, Hill, David, Hutchinson, Melissa, Johnson, Juanita, Johnson, Roberta, Kapre, Sheela, Kedzie, Robyn, Kowaloff, Harvey, Krodel, John, Lehman, James, Marshall, Ingeborg, McDaniels, Mary, Middleton, Robert, Mitchell, Phillip, Nelson, Carrie, Netherland, Susan, Ogden, Maureen, Packard, Keith, Poole, Lorie, Radford, Martha, Rathbun, Suman, Roberts, Cathy, Robinson, Margaret, Rollins, David, Rubinate, Donna, Schmidt, Cheryl, Scott, Julia, Slone, Betty, Spyropoulos, Alex, Subramanian, Seshan, Sullivan, Jacqueline, Timmerman, Carman, Vizzard, Carolyn, Wheeler, Connie, White, Diane, White, Nancy, Wright, Joyce, Young, Dereck, SOKOLOV, Krassimir, STEFANOV, Chavdar, TADZHER, Sheri, POSADA, Jose Alfredo, KVASNICKA, Jan, PENKA, Miroslav, VOJTISEK, Petr, EL RAHMAN, Alaa Mahmaud Aba, GORGY, George Sobhy, SHOLKAMY, Sherif, GENAY, Patrick, IBOUANGA, Florent, PLANCHON, Pierre, ZOTZ, Rainer, Kortmann, Bernd, Wolf, Stefan, Domjan, Gyula, Pinjala, Ramakrishna, Connaughton, John, Perez, Fernando Elias Garcia, Yusaf-Shah, Muhammad, Klonowski, Wlodzimierz, Campello, Maria da Gloria Cabral, Constantin, Palivan, Dubrovnaya, Nina, Barta, Peter, Arcelus, Juan, Lobo-Beristain, Jose Luis, Cardenas, Maria Jose Soto, Peter, Jurg, Ghedira, Habib, Dokucu, Ali, Mackie, Peter, Antonacci, Anthony, Caushaj, Philip, Diefendorf, Anne, Gaffey, Joseph, Hernandez, Cecilia, Marney, Terri, Pieske, Marlys, Shutt, Sandra, and Whitehead, Alva
Subjects: Adult, medicine.medical_specialty, Cross-sectional study, Population, Hemorrhage, Risk Assessment, Fibrinolytic Agents, Residence Characteristics, Risk Factors, Intensive care, Odds Ratio, medicine, Humans, Registries, cardiovascular diseases, Healthcare Disparities, Risk factor, education, Intensive care medicine, Aged, Cardiopulmonary disease, Aged, 80 and over, Inpatients, education.field_of_study, business.industry, Contraindications, Age Factors, Venous Thromboembolism, Hematology, Odds ratio, Middle Aged, medicine.disease, Hospitalization, Venous thrombosis, Cross-Sectional Studies, Logistic Models, Treatment Outcome, Health Care Surveys, Practice Guidelines as Topic, Guideline Adherence, Risk assessment, business
Abstract: SummaryLimited data are available regarding the risk for venous thromboembolism (VTE) and VTE prophylaxis use in hospitalised medically ill patients. We analysed data from the global ENDORSE survey to evaluate VTE risk and prophylaxis use in this population according to diagnosis, baseline characteristics, and country. Data on patient characteristics, VTE risk, and prophylaxis use were abstracted from hospital charts. VTE risk and prophylaxis use were evaluated according to the 2004 American College of Chest Physicians (ACCP) guidelines. Multivariable analysis was performed to identify factors associated with use of ACCP-recommended prophylaxis. Data were evaluated for 37,356 hospitalised medical patients across 32 countries. VTE risk varied according to medical diagnosis, from 31.2% of patients with gastrointestinal/hepatobiliary diseases to 100% of patients with acute heart failure, active non-infectious respiratory disease, or pulmonary infection (global rate, 41.5%). Among those at risk for VTE, ACCP-recommended prophylaxis was used in 24.4% haemorrhagic stroke patients and 40–45% of cardiopulmonary disease patients (global rate, 39.5%). Large differences in prophylaxis use were observed among countries. Markers of disease severity, including central venous catheters, mechanical ventilation, and admission to intensive care units, were strongly associated with use of ACCP-recommended prophylaxis. In conclusion, VTE risk varies according to medical diagnosis. Less than 40% of at-risk hospitalised medical patients receive ACCP-recommended prophylaxis. Prophylaxis use appears to be associated with disease severity rather than medical diagnosis. These data support the necessity to improve implementation of available guidelines for evaluating VTE risk and providing prophylaxis to hospitalised medical patients.
Published: 2010
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33. RUFY4: Immunity piggybacking on autophagy?

Author: Seigo Terawaki, Philippe Pierre, Evelina Gatti, Voahirana Camosseto, Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), and Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)
Subjects: 0301 basic medicine, Cell type, Autophagy, Endocytic cycle, Immunity, Proteins, Cell Biology, Biology, Autophagic Puncta, Cell biology, 03 medical and health sciences, 030104 developmental biology, Immune system, Mitophagy, FYVE domain, Xenophagy, [SDV.IMM]Life Sciences [q-bio]/Immunology, Humans, Lysosomes, Molecular Biology, Interleukin 4, HeLa Cells
Abstract: International audience; Although autophagy is a highly conserved mechanism among species and cell types, few are the molecules involved with the autophagic process that display cell-or tissue-specific expression. We have unraveled the positive regulatory role on autophagy of RUFY4 (RUN and FYVE domain containing 4), which is expressed in subsets of immune cells, including dendritic cells (DCs). DCs orchestrate the eradication of pathogens by coordinating the action of the different cell types involved in microbe recognition and destruction during the immune response. To fulfill this function, DC display particular regulation of their endocytic and autophagy pathways in response to the immune environment. Autophagy flux is downmodulated in DCs upon microbe sensing, but is remarkably augmented, when cells are differentiated in the presence of the pleiotropic cytokine IL4 (interleukin 4). From gene expression studies aimed at comparing the impact of IL4 on DC differentiation, we identified RUFY4, as a novel regulator that augments autophagy flux and, when overexpressed, induces drastic membrane redistribution and strongly tethers lysosomes. RUFY4 is therefore one of the few known positive regulators of autophagy that is expressed in a cell-specific manner or under specific immunological conditions associated with IL4 expression such as allergic asthma.
Published: 2016
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34. MRF4 negatively regulates adult skeletal muscle growth by repressing MEF2 activity

Author: Takayuki Akimoto, N. Henriette Uhlenhaut, Philippe Pierre, Elisa Calabria, Reimar Abraham, Stefano Ciciliot, Lisa Agatea, Peter W. J. Rigby, Silvio Bicciato, Marta Murgia, Mattia Forcato, Stefano Schiaffino, Kenneth A. Dyar, Jaime J. Carvajal, Irene Moretti, Bert Blaauw, Association Française contre les Myopathies, European Commission, Venetian Institute Molecular Medicine (VIMM), Helmholtz-Zentrum München (HZM), University of Padova [Padova, Italy], University - Hospital of Modena and Reggio Emilia [Modena, Italy], Centre d'Immunologie de Marseille - Luminy (CIML), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU), Chester Beatty Laboratories, Centro Andaluz de Biologia del Desarrollo, Association Francaise pour les Myopathies, European Project: 0223576(2002), Helmholtz Zentrum München = German Research Center for Environmental Health, Università degli Studi di Padova = University of Padua (Unipd), and Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)
Subjects: Genetics and Molecular Biology (all), 0301 basic medicine, Male, Aging, Transcription, Genetic, Muscle Fibers, Skeletal, Skeletal muscle, General Physics and Astronomy, Biochemistry, Muscle hypertrophy, Cell growth, Myosin, RNA, Small Interfering, Gene knockdown, Multidisciplinary, MEF2 Transcription Factors, Chemistry (all), musculoskeletal system, Cell biology, Up-Regulation, medicine.anatomical_structure, Myogenic Regulatory Factors, Organ Specificity, Gene Knockdown Techniques, embryonic structures, [SDV.IMM]Life Sciences [q-bio]/Immunology, RNA Interference, tissues, Protein Binding, Mef2, animal structures, Science, Active Transport, Cell Nucleus, Repressor, Biology, General Biochemistry, Genetics and Molecular Biology, Histone Deacetylases, Article, Physics and Astronomy (all), 03 medical and health sciences, medicine, Animals, Humans, Rats, Wistar, Muscle, Skeletal, Cell Nucleus, Gene Expression Profiling, General Chemistry, Hypertrophy, medicine.disease, Molecular biology, Repressor Proteins, 030104 developmental biology, HEK293 Cells, Sarcopenia, Protein Biosynthesis, Biochemistry, Genetics and Molecular Biology (all), Corepressor
Abstract: et al., The myogenic regulatory factor MRF4 is highly expressed in adult skeletal muscle but its function is unknown. Here we show that Mrf4 knockdown in adult muscle induces hypertrophy and prevents denervation-induced atrophy. This effect is accompanied by increased protein synthesis and widespread activation of muscle-specific genes, many of which are targets of MEF2 transcription factors. MEF2-dependent genes represent the top-ranking gene set enriched after Mrf4 RNAi and a MEF2 reporter is inhibited by co-transfected MRF4 and activated by Mrf4 RNAi. The Mrf4 RNAi-dependent increase in fibre size is prevented by dominant negative MEF2, while constitutively active MEF2 is able to induce myofibre hypertrophy. The nuclear localization of the MEF2 corepressor HDAC4 is impaired by Mrf4 knockdown, suggesting that MRF4 acts by stabilizing a repressor complex that controls MEF2 activity. These findings open new perspectives in the search for therapeutic targets to prevent muscle wasting, in particular sarcopenia and cachexia., This work is supported by grants from the European Commission (Integrated Project MYOAGE no. 223576 to SS) and Association Francaise pour les Myopathies (AFMTelethon grant to SS).
Published: 2016
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35. Polyunsaturated fatty acid-phospholipid remodeling and inflammation

Author: Marc E. Surette and Philippe Pierre Robichaud
Subjects: Cell signaling, Endocrinology, Diabetes and Metabolism, Phospholipid, Inflammation, chemistry.chemical_compound, Endocrinology, Phospholipase A2, Biosynthesis, Coenzyme A Ligases, Internal Medicine, medicine, Animals, Humans, Phospholipids, chemistry.chemical_classification, Nutrition and Dietetics, biology, Cell Membrane, 1-Acylglycerophosphocholine O-Acyltransferase, Lipid signaling, Phospholipases A2, Enzyme, chemistry, Biochemistry, biology.protein, Fatty Acids, Unsaturated, lipids (amino acids, peptides, and proteins), medicine.symptom, Polyunsaturated fatty acid
Abstract: Purpose of review To highlight some of the recent advances related to the control of polyunsaturated fatty acid (PUFA) incorporation and remodeling in membrane glycerophospholipids in inflammatory cells. Recent findings Several enzymes have recently been identified that are associated with the control of PUFA incorporation and remodeling into membrane phospholipids and their release. The functional roles of the different enzyme isotypes in the control of PUFA availability for lipid mediator biosynthesis and cell signaling are only now being established. The expression of specific acyl-CoA synthetase, lysophospholipid acyltransferase and phospholipase A2 isotypes has recently been shown to have an impact on membrane PUFA content, on the production of lipid mediators and on inflammation. Summary A better understanding of the complex processes associated with the control PUFA remodeling in membrane phospholipids may lead to the discovery of new therapeutic targets for the treatment of inflammatory diseases.
Published: 2015

36. Cystatin F is secreted, but artificial modification of its C-terminus can induce its endocytic targeting

Author: Philippe Pierre, Alexandre David, Hugues Lelouard, Fanny Cappello, Evelina Gatti, and Voahirana Camossetto
Subjects: Glycosylation, Endosome, Recombinant Fusion Proteins, Green Fluorescent Proteins, Molecular Sequence Data, Endocytic cycle, Biology, Endoplasmic Reticulum, urologic and male genital diseases, Mice, Biomarkers, Tumor, medicine, Animals, Humans, Amino Acid Sequence, Disulfides, Amino Acids, reproductive and urinary physiology, Microscopy, Confocal, U937 Cells, Cell Biology, Transfection, Cystatins, Cysteine protease, Endocytosis, female genital diseases and pregnancy complications, Protease inhibitor (biology), Cell biology, Molecular Weight, Luminescent Proteins, Cystatin B, Biochemistry, Langerhans Cells, Cystatin A, Cystatin, Dimerization, HeLa Cells, medicine.drug
Abstract: Cystatins constitute a superfamily of cysteine protease inhibitors. A member of the type II secreted cystatin family, cystatin F, has been identified through different gene array experiments to be specifically expressed in hematopoietic cells as well as to be associated with several malignant tumors, suggesting a role in immunity or cancer progression. Cystatin F specificity as a protease inhibitor is still elusive, and understanding the cellular traffic of this molecule is therefore a major step in its characterization. Although the mannosylation-6 phosphate of cystatin F has been suggested, no conclusive evidences of its endosomal targeting have been reported. Here we show using U937 cells that cystatin F is secreted as a disulfide bridge-linked dimer and is not associated with endosomes intracellularly. Interestingly, although cystatin F targeting to endosomes or lysosomes is not observed in U937, modification of its C-terminal end by the addition of several amino acids promotes its accumulation in the lysosomes of transfected HeLa cells. This observation suggests that cystatin F can be targeted to the endocytic pathway under specific conditions and its C-terminal domain might contribute to this event.
Published: 2004
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37. Human cathepsin S, but not cathepsin L, degrades efficiently MHC class II-associated invariant chain in nonprofessional APCs

Author: Hugues Lelouard, Ekkehard Weber, Jacek Bania, Fanny Cappello, Philippe Pierre, Alexandre David, Voahirana Camosseto, and Evelina Gatti
Subjects: MHC class II, Multidisciplinary, Base Sequence, biology, CD74, Reverse Transcriptase Polymerase Chain Reaction, Antigen processing, Cathepsin L, Antigen presentation, Histocompatibility Antigens Class II, Antigen-Presenting Cells, Biological Sciences, MHC restriction, Cathepsins, Molecular biology, Cell Line, Cell biology, Cysteine Endopeptidases, MHC class I, biology.protein, Humans, RNA, Messenger, DNA Primers, Cathepsin S
Abstract: MHC class II-restricted antigen presentation plays a central role in the immune response against exogenous antigens. The association of invariant (Ii) chain with MHC class II dimers is required for proper antigen presentation to CD4 + T cells by antigen-presenting cells. MHC class II complexes first traffic through the endocytic pathway to allow Ii chain degradation and antigenic peptide loading before their arrival at the cell surface. In recent years, a considerable effort has been directed toward the identification of proteases responsible for Ii chain degradation. Targeted gene deletion in mice has allowed a precise description of the cysteine proteases involved in the last step of Ii chain degradation. By using nonspecialized cellular models expressing MHC II molecules, we are now exploring the contribution of known cysteine proteases to human Ii chain processing. Surprisingly and contrary to the situation in mouse, cathepsin S was found to be the only human cysteine protease able to efficiently degrade the Ii-p10 fragment in epithelial cells. This selectivity has implications for thymic selection and indicates that differences between man and mice are probably more profound at this level than expected.
Published: 2003
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38. PLEKHM1 regulates autophagosome-lysosome fusion through HOPS complex and LC3/GABARAP proteins

Author: Hironori Suzuki, Sagar Bhogaraju, Philippe Pierre, Anja Kirchof, Karthik Maddi, David G. McEwan, Diana Miranda de Stegmann, Fraser P. Coxon, Soichi Wakatsuki, Ivan Dikic, Seigo Terawaki, Miep H. Helfrich, Doris Popovic, Evelina Gatti, Andrea Gubas, Christian Behrends, and Daniela Stadel
Subjects: Models, Molecular, Endosome, GABARAP, Endocytic cycle, Molecular Sequence Data, Autophagy-Related Proteins, Mice, Transgenic, Endosomes, Biology, Membrane Fusion, Mice, Lysosome, Phagosomes, medicine, Autophagy, Animals, Humans, Protein Interaction Domains and Motifs, Amino Acid Sequence, RNA, Small Interfering, Molecular Biology, Adaptor Proteins, Signal Transducing, Membrane Glycoproteins, Signal transducing adaptor protein, rab7 GTP-Binding Proteins, Cell Biology, Cell biology, Transport protein, Pleckstrin homology domain, Protein Transport, medicine.anatomical_structure, Gene Expression Regulation, rab GTP-Binding Proteins, Apoptosis Regulatory Proteins, Lysosomes, Microtubule-Associated Proteins, Sequence Alignment, HeLa Cells, Protein Binding, Signal Transduction
Abstract: The lysosome is the final destination for degradation of endocytic cargo, plasma membrane constituents, and intracellular components sequestered by macroautophagy. Fusion of endosomes and autophagosomes with the lysosome depends on the GTPase Rab7 and the homotypic fusion and protein sorting (HOPS) complex, but adaptor proteins that link endocytic and autophagy pathways with lysosomes are poorly characterized. Herein, we show that Pleckstrin homology domain containing protein family member 1 (PLEKHM1) directly interacts with HOPS complex and contains a LC3-interacting region (LIR) that mediates its binding to autophagosomal membranes. Depletion of PLEKHM1 blocks lysosomal degradation of endocytic (EGFR) cargo and enhances presentation of MHC class I molecules. Moreover, genetic loss of PLEKHM1 impedes autophagy flux upon mTOR inhibition and PLEKHM1 regulates clearance of protein aggregates in an autophagy- and LIR-dependent manner. PLEKHM1 is thus a multivalent endocytic adaptor involved in the lysosome fusion events controlling selective and nonselective autophagy pathways.
Published: 2014

39. Most human proteins made in both nucleus and cytoplasm turn over within minutes

Author: Sabyasachi Baboo, Philippe Pierre, Haibo Jiang, Peter R. Cook, Benjamin G. Davis, Chris R. M. Grovenor, and Bhaskar Bhushan
Subjects: Signal peptide, Cytoplasm, Time Factors, Proteomes, Materials Science, lcsh:Medicine, Gene Expression, Protein Synthesis, Biology, Ribosome, Biochemistry, Cell Line, chemistry.chemical_compound, Transcription (biology), Chemical Biology, Molecular Cell Biology, Protein biosynthesis, Genetics, Animals, Humans, RNA, Messenger, Amino Acids, lcsh:Science, Cell Nucleus, Multidisciplinary, lcsh:R, RNA, Proteins, Biology and Life Sciences, Cell Biology, Stop codon, Nonsense Mediated mRNA Decay, Protein Transport, Chemistry, chemistry, Puromycin, Protein Biosynthesis, Physical Sciences, lcsh:Q, Protein Translation, Materials Characterization, Peptides, Ribosomes, Research Article
Abstract: In bacteria, protein synthesis can be coupled to transcription, but in eukaryotes it is believed to occur solely in the cytoplasm. Using pulses as short as 5 s, we find that three analogues – L-azidohomoalanine, puromycin (detected after attaching fluors using ‘click’ chemistry or immuno-labeling), and amino acids tagged with ‘heavy’ 15N and 13C (detected using secondary ion mass spectrometry) – are incorporated into the nucleus and cytoplasm in a process sensitive to translational inhibitors. The nuclear incorporation represents a significant fraction of the total, and labels in both compartments have half-lives of less than a minute; results are consistent with most newly-made peptides being destroyed soon after they are made. As nascent RNA bearing a premature termination codon (detected by fluorescence in situ hybridization) is also eliminated by a mechanism sensitive to a translational inhibitor, the nuclear turnover of peptides is probably a by-product of proof-reading the RNA for stop codons (a process known as nonsense-mediated decay). We speculate that the apparently-wasteful turnover of this previously-hidden (‘dark-matter’) world of peptide is involved in regulating protein production.
Published: 2014

40. Fatty acid remodeling in cellular glycerophospholipids following the activation of human T cells

Author: Marc E. Surette, Philippe Pierre Robichaud, Jean Eric Munganyiki, and Katherine Boulay
Subjects: T cell, T-Lymphocytes, stearoyl-CoA desaturase 1, lysophospholipid acyltransferase, Gene Expression, QD415-436, Arachidonic Acids, Glycerophospholipids, Biology, Lymphocyte Activation, Jurkat cells, Biochemistry, chemistry.chemical_compound, acyl-CoA synthetase, Endocrinology, Phospholipase A2, medicine, arachidonic acid, Humans, Cells, Cultured, Research Articles, fatty acid synthase, Fatty Acids, Cell Biology, Cell cycle, Cell biology, Fatty Acid Synthase, Type I, Fatty acid synthase, medicine.anatomical_structure, chemistry, Glycerophospholipid, biology.protein, Arachidonic acid, phospholipase A2, Stearoyl-CoA desaturase-1, Stearoyl-CoA Desaturase
Abstract: Changes in fatty acid (FA) and glycerophospholipid (GPL) metabolism associated with cell cycle entry are not fully understood. In this study FA-GPL remodeling was investigated in resting and proliferating primary human T cells. Significant changes were measured in the composition and distribution of FAs in GPLs following receptor activation of human T cells. The FA distribution of proliferating T cells was very similar to that of the human Jurkat T cell line and when the stimulus was removed from proliferating T cells, they stopped proliferating and the FA distribution largely reverted back to that of resting T cells. The cellular content of saturated and monounsaturated FAs was significantly increased in proliferating cells, which was associated with an induction of FA synthase and stearoyl-CoA desaturase-1 gene expression. Additionally, cellular arachidonate was redistributed in GPLs in a distinct pattern that was unlike any other FAs. This redistribution was associated with an induction of CoA-dependent and CoA-independent remodeling. Accordingly, significant changes in the expression of several acyl-CoA synthetases, lysophospholipid acyltransferases, and phospholipase A2 were measured. Overall, these results suggest that metabolic pathways are activated in proliferating T cells that may represent fundamental changes associated with human cell proliferation.
Published: 2013

41. Species-specific impact of the autophagy machinery on Chikungunya virus infection

Author: Nicolas Gangneux, Mickaël Lelek, Marie-Christine Prévost, Mehdi Bouraï, Yves Jacob, Pierre-Olivier Vidalain, Thérèse Couderc, Marc Lecuit, Marianne Lucas-Hourani, Serge Mostowy, Christophe Zimmer, Delphine Judith, Philippe Pierre, Nadège Cayet, Frédéric Tangy, Biologie des Infections - Biology of Infection, Institut Pasteur [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Interactions Bactéries-Cellules (UIBC), Institut National de la Recherche Agronomique (INRA)-Institut Pasteur [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Génomique Virale et Vaccination, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Imagerie et Modélisation, Microscopie Ultrastructurale (Plate-forme), Génétique, Papillomavirus et Cancer Humain, Institut Pasteur [Paris], Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université Paris Descartes - Paris 5 (UPD5), Institut Necker Enfants-Malades (INEM - UM 111 (UMR 8253 / U1151)), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), This work was supported by Institut Pasteur, FRM, Ville de Paris, Fondation BNP‐Paribas, ICRES FP7, LabEx IBEID and the Programme Interdisciplinaire CNRS Maladies Infectieuses Emergentes. D.J. was supported by a doctoral fellowship from the Axa Research Fund and M.B. by a doctoral fellowship from Région Ile‐de‐France., We are grateful to S. Higgs for providing CHIKV cDNA clones and to N. Mizushima for providing Atg5−/− and Atg5+/+ MEFs. We thank V. Sancho‐Shimizu, C. Prehault, M. Hamon, L. Radoshevich, P. Desprès, A. Merits, V. Meas‐Yedid Hardy, E. Meurs and A. Dufour for their generous gift of reagents or technical advices. We also thank members of the Biology of Infection Unit, F. Rey, P. Cossart and P. Codogno, for their helpful discussions and critical reading of the manuscript., Institut Pasteur [Paris] (IP)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut National de la Recherche Agronomique (INRA)-Institut Pasteur [Paris] (IP)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Institut Pasteur [Paris] (IP), Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Pasteur [Paris]-Institut National de la Recherche Agronomique (INRA), and Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)
Subjects: MESH: Virus Replication, viruses, MESH: Adaptor Proteins, Signal Transducing/metabolism, MESH: Chikungunya Fever, Viral Nonstructural Proteins, MESH: Chikungunya virus/physiology, medicine.disease_cause, Virus Replication, Biochemistry, Upfront, Mice, Ubiquitin, Phagosomes, Sequestosome-1 Protein, MESH: Sequestosome-1 Protein, NDP52, MESH: Animals, Chikungunya, Nuclear protein, 0303 health sciences, MESH: Viral Nonstructural Proteins/metabolism, biology, MESH: Phagosomes/virology, p62, Nuclear Proteins, virus diseases, 3. Good health, Cell biology, Protein Transport, MESH: Phagosomes/metabolism, Capsid, Host-Pathogen Interactions, MESH: Immunity, Innate, MESH: Capsid/metabolism, Microtubule-Associated Proteins, Chikungunya virus, Protein Binding, autophagy, MESH: Protein Transport, MESH: Alphavirus Infections/virology, Virus, 03 medical and health sciences, parasitic diseases, Genetics, medicine, Animals, Humans, MESH: Species Specificity, MESH: Protein Binding, MESH: Autophagy, MESH: Nuclear Proteins/metabolism, Molecular Biology, MESH: Mice, 030304 developmental biology, Adaptor Proteins, Signal Transducing, Sirolimus, MESH: Humans, 030306 microbiology, Alphavirus Infections, Autophagy, Scientific Reports, MESH: Host-Pathogen Interactions, Virology, Immunity, Innate, MESH: Sirolimus/pharmacology, species specificity, Viral replication, MESH: HeLa Cells, MESH: Microtubule-Associated Proteins/metabolism, biology.protein, Chikungunya Fever, [SDV.SPEE]Life Sciences [q-bio]/Santé publique et épidémiologie, HeLa Cells
Abstract: Comment in : Macroautophagy--friend or foe of viral replication? [EMBO Rep. 2013]; International audience; Chikungunya virus (CHIKV) is a recently re-emerged arbovirus that triggers autophagy. Here, we show that CHIKV interacts with components of the autophagy machinery during its replication cycle, inducing a cytoprotective effect. The autophagy receptor p62 protects cells from death by binding ubiquitinated capsid and targeting it to autophagolysosomes. By contrast, the human autophagy receptor NDP52-but not its mouse orthologue-interacts with the non-structural protein nsP2, thereby promoting viral replication. These results highlight the distinct roles of p62 and NDP52 in viral infection, and identify NDP52 as a cellular factor that accounts for CHIKV species specificity.
Published: 2013
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42. Lonely MHC molecules seeking immunogenic peptides for meaningful relationships

Author: Ira Mellman, Sebastian Amigorena, and Philippe Pierre
Subjects: HLA-D Antigens, MHC class II, biology, Antigen processing, Endosome, Histocompatibility Antigens Class II, Biological Transport, Cell Biology, Transporter associated with antigen processing, MHC restriction, Major histocompatibility complex, Endocytosis, Cell biology, Antigen, Antibody Formation, MHC class I, biology.protein, Animals, Humans, Peptides
Abstract: The association between antigenic peptides and MHC class II molecules represents a critical event in the initiation of the immune response to extracellular antigens. Understanding the molecular basis of antigen processing requires the characterization of the intracellular compartments, or ‘single bars’, in which immunogenic peptides are generated and loaded onto class II molecules. In the past year, something of a breakthrough occurred with the identification of specialized compartments that host antigen processing and/or peptide loading, designated ‘MHC class II compartment’ and ‘class II vesicles’. It is becoming increasingly clear, however, that these compartments are themselves heterogeneous and not always distinct from conventional endosomes and lysosomes.
Published: 1995
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43. Nuclear translation visualized by ribosome-bound nascent chain puromycylation

Author: Brian P. Dolan, Jonathan J. Knowlton, Heather D. Hickman, Philippe Pierre, Alexandre David, Jack R. Bennink, Jonathan W. Yewdell, Giovanna Clavarino, Center for Indlejrede Software Systemer (CISS), Aalborg University [Denmark] (AAU), National Institute of Allergy and Infectious Diseases [Bethesda] (NIAID-NIH), National Institutes of Health [Bethesda] (NIH), Centre d'Immunologie de Marseille - Luminy (CIML), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU), Laboratoire Adaptation et pathogénie des micro-organismes [Grenoble] (LAPM), Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), and Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)
Subjects: MESH: Cell Nucleus, genetic structures, Nucleolus, cells, MESH: Puromycin, Cell, genetic processes, MESH: Microscopy, Fluorescence, Biology, Ribosome, environment and public health, Article, MESH: Antibodies, Monoclonal, 03 medical and health sciences, chemistry.chemical_compound, medicine, Protein biosynthesis, Humans, Research Articles, 030304 developmental biology, Cell Nucleus, 0303 health sciences, Nucleoplasm, MESH: Humans, 030302 biochemistry & molecular biology, Translation (biology), Cell Biology, equipment and supplies, MESH: Catalysis, 3. Good health, Cell biology, Cell nucleus, stomatognathic diseases, medicine.anatomical_structure, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, chemistry, Puromycin, Protein Biosynthesis, MESH: Protein Biosynthesis, MESH: HeLa Cells, MESH: Cell Nucleolus, Ribosomes, MESH: Ribosomes
Abstract: A new method for visualizing translation in cells via standard immunofluorescence microscopy provides evidence for translation in the nucleoplasm and nucleolus., Whether protein translation occurs in the nucleus is contentious. To address this question, we developed the ribopuromycylation method (RPM), which visualizes translation in cells via standard immunofluorescence microscopy. The RPM is based on ribosome-catalyzed puromycylation of nascent chains immobilized on ribosomes by antibiotic chain elongation inhibitors followed by detection of puromycylated ribosome-bound nascent chains with a puromycin (PMY)-specific monoclonal antibody in fixed and permeabilized cells. The RPM correlates localized translation with myriad processes in cells and can be applied to any cell whose translation is sensitive to PMY. In this paper, we use the RPM to provide evidence for translation in the nucleoplasm and nucleolus, which is regulated by infectious and chemical stress.
Published: 2012
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44. Autophagy inhibition promotes defective neosynthesized proteins storage in ALIS, and induces redirection toward proteasome processing and MHCI-restricted presentation

Author: Francesca De Angelis Rigotti, Seigo Terawaki, Ronza Abdelrassoul, Nuno Cláudio, Till Wenger, Giovanna Clavarino, Voahirana Camosseto, Aude De Gassart, Nadia Catalan, Philippe Pierre, Anna Mies, Evelina Gatti, Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Haon, Marie Laure, and Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)
Subjects: Sequestosome-1 Protein, Proteasome Endopeptidase Complex, Protein Folding, Transcription, Genetic, [SDV.IMM] Life Sciences [q-bio]/Immunology, NF-E2-Related Factor 2, Recombinant Fusion Proteins, Green Fluorescent Proteins, ATG5, Antigen presentation, Biology, Major histocompatibility complex, Substrate Specificity, 03 medical and health sciences, 0302 clinical medicine, Autophagy, Transcriptional regulation, Humans, Protein Structure, Quaternary, Molecular Biology, Adaptor Proteins, Signal Transducing, 030304 developmental biology, Inclusion Bodies, Antigen Presentation, 0303 health sciences, Ubiquitin, Histocompatibility Antigens Class I, Intracellular Signaling Peptides and Proteins, Proteins, Signal transducing adaptor protein, Cell Biology, Cell biology, Proteasome, Protein Biosynthesis, Proteolysis, biology.protein, [SDV.IMM]Life Sciences [q-bio]/Immunology, Puromycin, Corrigendum, Proteasome Inhibitors, Protein Processing, Post-Translational, Ribosomes, 030217 neurology & neurosurgery, HeLa Cells, Molecular Chaperones, Signal Transduction
Abstract: International audience; A significant portion of newly synthesized protein fails to fold properly and is quickly degraded. These defective ribosomal products (DRiPs) are substrates for the ubiquitin-proteasome system (UPS) and give rise to a large fraction of peptides presented by major histocompatibility complex class I molecules (MHCI). Here, we showed that DRiPs are also autophagy substrates, which accumulate upon autophagy inhibition in aggresome-like-induced structures (ALIS). Aggregation is critically depending on p62/SQSTM1, but occurs in the absence of activation of the NRF2 signaling axis and transcriptional regulation of p62/SQSTM1. We demonstrated that autophagy-targeted DRiPs can become UPS substrates and give rise to MHCI presented peptides upon autophagy inhibition. We further demonstrated that autophagy targeting of DRiPs is controlled by NBR1, but not p62/SQSTM1, CHIP or BAG-1. Active autophagy therefore directly modulates MHCI presentation by constantly degrading endogenous defective neosynthesized antigens, which are submitted to at least two distinct quality control mechanisms.
Published: 2012

45. BAD-LAMP is a novel biomarker of nonactivated human plasmacytoid dendritic cells

Author: Philippe Pierre, Alexandre David, Francesca De Angelis Rigotti, Aude De Gassart, Pierre Brousset, Axel Defays, Voahirana Camossetto, Evelina Gatti, Till Wenger, Marc Dalod, Tony Petrella, Institut de Biologie du Développement de Marseille (IBDM), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Center for Indlejrede Software Systemer (CISS), Aalborg University [Denmark] (AAU), Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), CHU Dijon, Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand (CHU Dijon), and Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)
Subjects: genetic structures, Immunology, Interleukin-3 Receptor alpha Subunit, Oligonucleotides, Golgi Apparatus, Endosomes, Biology, Endoplasmic Reticulum, Transfection, Biochemistry, 03 medical and health sciences, 0302 clinical medicine, Humans, Oligonucleotide Array Sequence Analysis, 030304 developmental biology, 0303 health sciences, Leukemia, Oligonucleotide, Compartment (ship), Endoplasmic reticulum, Brain, Lysosome-Associated Membrane Glycoproteins, Membrane Proteins, Membrane Transport Proteins, hemic and immune systems, Dendritic Cells, Cell Biology, Hematology, Dendritic cell, eye diseases, 3. Good health, Cell biology, CpG site, Membrane protein, 030220 oncology & carcinogenesis, Biomarker (medicine), [SDV.IMM]Life Sciences [q-bio]/Immunology, Interleukin-3, Interleukin-3 receptor, sense organs, Biomarkers, HeLa Cells
Abstract: The brain and dendritic cell (BAD)–associated lysosome-associated membrane protein (LAMP)–like molecule (BAD-LAMP, c20orf103, UNC-46) is a newly identified member of the family of LAMPs. BAD-LAMP expression in the mouse is confined to neurons. We demonstrate here that in humans, BAD-LAMP can specifically be found in the type I IFN-producing plasmacytoid dendritic cells (pDCs). Human BAD-LAMP is localized in the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) of freshly isolated CD123+ pDCs and is rapidly lost upon activation by unmethylated cytosine-phosphate-guanine (CpG) oligonucleotides. The restricted pattern of BAD-LAMP expression allows for the rapid identification of normal and leukemic human pDCs in tissues and blood.
Published: 2011
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46. Integration of ER stress and viral nucleotide sensing in DCs: mounting a response commensurate to the threat?

Author: Marc Dalod, Philippe Pierre, Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), and Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)
Subjects: XBP1, medicine.medical_treatment, Immunology, Stimulation, Biology, Endoplasmic Reticulum, Article, Proinflammatory cytokine, 03 medical and health sciences, 0302 clinical medicine, Immune system, Interferon, Stress, Physiological, MESH: Endoplasmic Reticulum, medicine, Immunology and Allergy, Animals, Humans, MESH: Animals, MESH: Stress, Physiological, Transcription factor, 030304 developmental biology, 0303 health sciences, MESH: Humans, MESH: Dendritic Cells, Dendritic Cells, 3. Good health, MESH: DNA, Viral, Cytokine, MESH: RNA, Viral, DNA, Viral, Unfolded protein response, RNA, Viral, [SDV.IMM]Life Sciences [q-bio]/Immunology, 030215 immunology, medicine.drug
Abstract: Multiple physiological and pathological conditions interfere with the function of Endoplasmic Reticulum (ER). However, much remains unknown regarding the impact of ER stress on inflammatory responses in dendritic cells (DCs) upon the recognition of pathogen molecules. We show that ER stress greatly potentiates the expression of inflammatory cytokines and IFN-β in murine DCs stimulated by polyIC, a synthetic mimic of virus dsRNA. Both toll-like receptor 3 and melanoma differentiation-associated gene-5 are involved in the enhanced IFN-β production, which is associated with increased activation of NF-κB and IRF3 signaling as well as the splicing of X-box binding protein-1 (XBP-1), an important regulator involved in ER stress response. Surprisingly, silencing of XBP-1 reduces polyIC-stimulated IFN-β expression in the presence or absence of ER stress, indicating that XBP-1 may be essential for polyIC signaling and ER stress-amplified IFN-β production. Overexpression of a spliced form of XBP-1(XBP-1s) synergistically augments polyIC-induced inflammatory response. For the first time we show that XBP-1s overexpression-enhanced IFN-β production in DCs markedly suppresses vesicular stomatitis virus infection, revealing a previously unrecognized role of XBP-1 in an antiviral response. Our findings suggest that evolutionarily conserved ER stress response and XBP-1 may function collaboratively with the innate immunity in maintaining cellular homeostasis.
Published: 2011
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47. Systems biology of infectious diseases: a focus on fungal infections

Author: Michael Bromley, Philippe Pierre, Ivo Gut, Lisa Rizzetto, Rodrigo Santamaría, Wanseon Lee, Duccio Cavalieri, Brian Miller, Misha Kapushesky, Teresa Zelante, Luigina Romani, Manuel A. S. Santos, Paul Bowyer, University of Salamanca - Spain, University of Salamanca, Università degli Studi di Firenze = University of Florence [Firenze] (UNIFI), University of Manchester [Manchester], Università degli Studi di Perugia (UNIPG), European Bioinforrmatics Institute (UK) (EBI), École de biologie industrielle (EBI), AlerGenetica (UK), AlerGenetica, Centre National de Génotypage (CNG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Universidade de Aveiro, Universidad de Salamanca, Università degli Studi di Firenze = University of Florence (UniFI), and Università degli Studi di Perugia = University of Perugia (UNIPG)
Subjects: Proteomics, Antifungal Agents, MESH: Th17 Cells, Disease, MESH: Drug Design, Bioinformatics, MESH: Receptors, Pattern Recognition, MESH: Molecular Targeted Therapy, Candida albicans, Immunology and Allergy, MESH: Animals, MESH: Immune Evasion, MESH: Genetic Variation, Molecular Targeted Therapy, Organism, MESH: Cytokines, 0303 health sciences, MESH: Proteomics, Systems Biology, Hematology, 3. Good health, Drug development, MESH: Systems Biology, Receptors, Pattern Recognition, MESH: Genome, Fungal, Host-Pathogen Interactions, MESH: Communicable Diseases, [SDV.IMM]Life Sciences [q-bio]/Immunology, Cytokines, MESH: Aspergillus fumigatus, Genome, Fungal, MESH: Immune Tolerance, Systems biology, Host–pathogen interaction, Immunology, Computational biology, Biology, Communicable Diseases, Underlying infection, 03 medical and health sciences, MESH: Mycoses, Immune Tolerance, Animals, Humans, Immune Evasion, 030304 developmental biology, MESH: Humans, 030306 microbiology, MESH: Candida albicans, Aspergillus fumigatus, MESH: Host-Pathogen Interactions, MESH: Biological Markers, Genetic Variation, Th1 Cells, MESH: Antifungal Agents, Microarray Analysis, MESH: Microarray Analysis, MESH: Th1 Cells, Mycoses, Infectious disease (medical specialty), Drug Design, Th17 Cells, Biomarkers
Abstract: International audience; The study of infectious disease concerns the interaction between the host species and a pathogen organism. The analysis of such complex systems is improving with the evolution of high-throughput technologies and advanced computational resources. This article reviews integrative, systems-oriented approaches to understanding mechanisms underlying infection, immune response and inflammation to find biomarkers of disease and design new drugs. We focus on the systems biology process, especially the data gathering and analysis techniques rather than the experimental technologies or latest computational resources.
Published: 2011
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48. NAD(P)H quinone-oxydoreductase 1 protects eukaryotic translation initiation factor 4GI from degradation by the proteasome

Author: Rodica Anesia, Stéphane Pyronnet, Philippe Pierre, Corinne Bousquet, Bertrand Fabre, Christiane Susini, Amandine Alard, Catherine Marboeuf, Simon, Marie Francoise, Institut de médecine moléculaire de Rangueil (I2MR), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées- Institut Fédératif de Recherche Bio-médicale Institution (IFR150)-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Chirurgie Générale et Digestive [Rangueil], Centre Hospitalier Universitaire de Toulouse (CHU Toulouse), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-IFR150-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU), CHU Toulouse [Toulouse]-Hôpital de Rangueil, CHU Toulouse [Toulouse], and Université de Toulouse (UT)-Université de Toulouse (UT)- Institut Fédératif de Recherche Bio-médicale Institution (IFR150)-Institut National de la Santé et de la Recherche Médicale (INSERM)
Subjects: Small interfering RNA, MESH: NAD(P)H Dehydrogenase (Quinone), Mice, Peptide Initiation Factors, Chlorocebus aethiops, NAD(P)H Dehydrogenase (Quinone), Protein biosynthesis, MESH: Animals, MESH: Peptide Initiation Factors, MESH: Peptide Fragments, 0303 health sciences, MESH: Protease Inhibitors, MESH: Oxidative Stress, Protein Stability, MESH: Proteasome Endopeptidase Complex, 030302 biochemistry & molecular biology, Articles, Transfection, MESH: Eukaryotic Initiation Factor-4G, Biochemistry, MESH: Protein Biosynthesis, Proteasome Inhibitors, Protein Binding, Proteasome Endopeptidase Complex, MESH: NADPH Dehydrogenase, Biology, Cell Line, 03 medical and health sciences, Eukaryotic translation, MESH: Protein Stability, Animals, Humans, Initiation factor, MESH: Protein Binding, Protease Inhibitors, Molecular Biology, MESH: Mice, 030304 developmental biology, MESH: Humans, NADPH Dehydrogenase, Cell Biology, MESH: Cercopithecus aethiops, Peptide Fragments, MESH: Cell Line, Oxidative Stress, Proteasome, Protein Biosynthesis, NAD+ kinase, Eukaryotic Initiation Factor-4G
Abstract: International audience; The eukaryotic translation initiation factor 4GI (eIF4GI) serves as a central adapter in cap-binding complex assembly. Although eIF4GI has been shown to be sensitive to proteasomal degradation, how the eIF4GI steady-state level is controlled remains unknown. Here, we show that eIF4GI exists in a complex with NAD(P)H quinone-oxydoreductase 1 (NQO1) in cell extracts. Treatment of cells with dicumarol (dicoumarol), a pharmacological inhibitor of NQO1 known to preclude NQO1 binding to its protein partners, provokes eIF4GI degradation by the proteasome. Consistently, the eIF4GI steady-state level also diminishes upon the silencing of NQO1 (by transfection with small interfering RNA), while eIF4GI accumulates upon the overexpression of NQO1 (by transfection with cDNA). We further reveal that treatment of cells with dicumarol frees eIF4GI from mRNA translation initiation complexes due to strong activation of its natural competitor, the translational repressor 4E-BP1. As a consequence of cap-binding complex dissociation and eIF4GI degradation, protein synthesis is dramatically inhibited. Finally, we show that the regulation of eIF4GI stability by the proteasome may be prominent under oxidative stress. Our findings assign NQO1 an original role in the regulation of mRNA translation via the control of eIF4GI stability by the proteasome.
Published: 2010
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49. CLIP-170 links endocytic vesicles to microtubules

Author: Jochen Scheel, Thomas E. Kreis, Janet E. Rickard, and Philippe Pierre
Subjects: Base Sequence, Endosome, Binding protein, Vesicle, Molecular Sequence Data, education, Endocytic cycle, Endosomes, Biology, Microtubules, Endocytosis, General Biochemistry, Genetics and Molecular Biology, Neoplasm Proteins, Cell biology, Microtubule plus-end, Endocytic vesicle, Cytoplasm, Microtubule, Sequence Homology, Nucleic Acid, Humans, Amino Acid Sequence, cardiovascular diseases, Cloning, Molecular, Microtubule-Associated Proteins, HeLa Cells
Abstract: Binding of endocytic carrier vesicles to microtubules depends on the microtubule-binding protein CLIP-170 in vitro. In vivo, CLIP-170 colocalizes with a subset of transferrin receptor-positive endocytic structures and, more extensively, with endosomal tubules induced by brefeldin A. The structure of CLIP-170 has been analyzed by cloning its cDNA. The predicted non-helical C- and N-terminal domains of the homodimeric protein are connected by a long coiled-coil domain. We have identified a novel motif present in a tandem repeat in the N-terminal domain of CLIP-170 that is involved in binding to microtubules. This motif is also found in the Drosophila Glued and yeast BIK1 proteins. These features, together with its very elongated structure, suggest that CLIP-170 belongs to a novel class of proteins, cytoplasmic linker proteins (CLIPs), mediating interactions of organelles with microtubules.
Published: 1992
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50. MicroRNA-155 modulates the interleukin-1 signaling pathway in activated human monocyte-derived dendritic cells

Author: EmmanuÃ¨le Barras, Maurizio Ceppi, Philippe Pierre, Manuel A. S. Santos, Walter Reith, Isabelle Dunand-Sauthier, Patricia M. Pereira, Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Universidade de Aveiro, University of Coimbra, Faculty of Medicine, University of Geneva Medical School, Department of Pathology and Immunology, and Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)
Subjects: MESH: Signal Transduction, medicine.medical_treatment, MESH: Base Sequence, ddc:616.07, MESH: Monocytes, Lymphocyte Activation, Monocytes, 0302 clinical medicine, RNA Processing, Post-Transcriptional, Receptor, Cells, Cultured, 0303 health sciences, Multidisciplinary, MESH: Dendritic Cells, Toll-Like Receptors, Signal transducing adaptor protein, Interleukin, Dendritic Cells/ metabolism, Biological Sciences, Signal Transduction/ physiology, Adaptor Proteins, Signal Transducing/genetics/metabolism, Cell biology, Cytokine, 030220 oncology & carcinogenesis, [SDV.IMM]Life Sciences [q-bio]/Immunology, Signal transduction, MESH: Toll-Like Receptors, Signal Transduction, MESH: Cells, Cultured, MESH: RNA Processing, Post-Transcriptional, MESH: DNA Primers, MicroRNAs/ physiology, Biology, Interleukin-1/ metabolism, 03 medical and health sciences, microRNA, medicine, Gene silencing, Humans, MESH: Lymphocyte Activation, Adaptor Proteins, Signal Transducing, 030304 developmental biology, MESH: Adaptor Proteins, Signal Transducing, DNA Primers, MESH: Humans, Base Sequence, Monocytes/ metabolism, MESH: Interleukin-1, Dendritic Cells, MicroRNAs, Gene chip analysis, Toll-Like Receptors/metabolism, MESH: MicroRNAs, Interleukin-1
Abstract: International audience; In response to inflammatory stimulation, dendritic cells (DCs) have a remarkable pattern of differentiation (maturation) that exhibits specific mechanisms to control immunity. Here, we show that in response to Lipopolysaccharides (LPS), several microRNAs (miRNAs) are regulated in human monocyte-derived dendritic cells. Among these miRNAs, miR-155 is highly up-regulated during maturation. Using LNA silencing combined to microarray technology, we have identified the Toll-like receptor/interleukin-1 (TLR/IL-1) inflammatory pathway as a general target of miR-155. We further demonstrate that miR-155 directly controls the level of TAB2, an important signal transduction molecule. Our observations suggest, therefore, that in mature human DCs, miR-155 is part of a negative feedback loop, which down-modulates inflammatory cytokine production in response to microbial stimuli.
Published: 2009
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