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1. Targeting Glycosylation Aberrations to Improve the Efficiency of Cancer Phototherapy

Author

Hervé Benoist, Annick Barre, Guillaume Poiroux, Pierre Rougé, Centre de Recherches en Cancérologie de Toulouse (CRCT), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Pharmacochimie et Biologie pour le Développement (PHARMA-DEV), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie de Toulouse (ICT-FR 2599), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie du CNRS (INC)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Institut de Chimie du CNRS (INC)-Institut de Recherche pour le Développement (IRD), Université de Toulouse (UT)-Université de Toulouse (UT)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut de Recherche pour le Développement (IRD)-Institut de Chimie de Toulouse (ICT), Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université de Toulouse (UT)-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), and Université de Toulouse (UT)

Subjects
Cancer Research, Glycosylation, medicine.drug_class, medicine.medical_treatment, PhotoDynamic Therapy (PDT), [SDV]Life Sciences [q-bio], aptamers, Photodynamic therapy, [SDV.CAN]Life Sciences [q-bio]/Cancer, Monoclonal antibody, T/Tn antigens, Metastasis, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Antigen, Antigens, Neoplasm, Neoplasms, Drug Discovery, medicine, Animals, Humans, metastasis, Photosensitizer, 030304 developmental biology, Pharmacology, O-glycosylation, 0303 health sciences, Photosensitizing Agents, Cancer, medicine.disease, monoclonal Antibodies (moAbs), lectins, 3. Good health, PhotoSensitizer (PS), Oncology, chemistry, Photochemotherapy, 030220 oncology & carcinogenesis, Cancer cell, Cancer research, cancer cells
Abstract

The use of photodynamic therapy in cancer still remains limited, partly because of the lack of photosensitizer (PS) specificity for the cancerous tissues. Various molecular tools are available to increase PS efficiency by targeting the cancer cell molecular alterations. Most strategies use the protein-protein interactions, e.g. monoclonal antibodies directed toward tumor antigens, such as HER2 or EGFR. An alternative could be the targeting of the tumor glycosylation aberrations, e.g. T/Tn antigens that are truncated O-glycans over-expressed in numerous tumors. Thus, to achieve an effective targeting, PS can be conjugated to molecules that specifically recognize the Oglycosylation aberrations at the cancer cell surface.

Published
2019
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2. Plant Lectins Targeting O-Glycans at the Cell Surface as Tools for Cancer Diagnosis, Prognosis and Therapy

Author

Guillaume Poiroux, Els J.M. Van Damme, Pierre Rougé, Annick Barre, Hervé Benoist, Centre de Recherches en Cancérologie de Toulouse (CRCT), Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM), Pharmacochimie et Biologie pour le Développement (PHARMA-DEV), Institut de Recherche pour le Développement (IRD)-Institut de Chimie de Toulouse (ICT-FR 2599), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie du CNRS (INC)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie du CNRS (INC), Ghent University Hospital, Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie de Toulouse (ICT-FR 2599), Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Institut de Chimie du CNRS (INC)-Institut de Recherche pour le Développement (IRD), Université de Toulouse (UT)-Université de Toulouse (UT)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut de Recherche pour le Développement (IRD)-Institut de Chimie de Toulouse (ICT), Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université de Toulouse (UT)-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées, and Pagès, Nathalie

Subjects
0301 basic medicine, HUMAN BREAST-CANCER, diagnosis, [SDV]Life Sciences [q-bio], Tn antigen, Gene Expression, Review, WHEAT-GERM-AGGLUTININ, Epitope, Substrate Specificity, BAUHINIA-FORFICATA LECTIN, MUSHROOM AGARICUS-BISPORUS, Neoplasms, peanut lectin, Spectroscopy, O-glycosylation, CARBOHYDRATE-BINDING SPECIFICITIES, MOLUCCELLA-LAEVIS, General Medicine, 3. Good health, Computer Science Applications, [SDV] Life Sciences [q-bio], Biochemistry, photodynamic therapy, Plant Lectins, AMARANTHUS-LEUCOCARPUS LECTIN, ANTIGEN, Biology, Catalysis, Inorganic Chemistry, Structure-Activity Relationship, 03 medical and health sciences, Glycolipid, Antigen, Polysaccharides, RIBOSOME-INACTIVATING PROTEIN, medicine, Humans, cancer, Antigens, Tumor-Associated, Carbohydrate, Physical and Theoretical Chemistry, Molecular Biology, Morniga G, THOMSEN-FRIEDENREICH, Cell Membrane, Organic Chemistry, Biology and Life Sciences, Lectin, Cancer, SCLEROTIUM-ROLFSII LECTIN, LECTIN, T antigen, medicine.disease, Molecular biology, 030104 developmental biology, Photochemotherapy, Cancer cell, Jacalin, biology.protein, lectin, peanut, prognosis
Abstract

International audience; Aberrant O-glycans expressed at the surface of cancer cells consist of membrane-tethered glycoproteins (T and Tn antigens) and glycolipids (Lewis a, Lewis x and Forssman antigens). All of these O-glycans have been identified as glyco-markers of interest for the diagnosis and the prognosis of cancer diseases. These epitopes are specifically detected using T/Tn-specific lectins isolated from various plants such as jacalin from Artocarpus integrifola, and fungi such as the Agaricus bisporus lectin. These lectins accommodate T/Tn antigens at the monosaccharide-binding site; residues located in the surrounding extended binding-site of the lectins often participate in the binding of more extended epitopes. Depending on the shape and size of the extended carbohydrate-binding site, their fine sugar-binding specificity towards complex O-glycans readily differs from one lectin to another, resulting in a great diversity in their sugar-recognition capacity. T/Tn-specific lectins have been extensively used for the histochemical detection of cancer cells in biopsies and for the follow up of the cancer progression and evolution. T/Tn-specific lectins also induce a caspase-dependent apoptosis in cancer cells, often associated with a more or less severe inhibition of proliferation. Moreover, they provide another potential source of molecules adapted to the building of photosensitizer-conjugates allowing a specific targeting to cancer cells, for the photodynamic treatment of tumors.

Published
2017
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3. Molecular basis of cross-reactivity between Act c 12 and other seed 11S-globulin allergens

Author

Hervé Benoist, Pierre Rougé, Aleksandra Delplanque, Annick Barre, Mathias Simplicien, Pharmacochimie et Biologie pour le Développement (PHARMA-DEV), Institut de Recherche pour le Développement (IRD)-Institut de Chimie de Toulouse (ICT-FR 2599), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie du CNRS (INC)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie du CNRS (INC), Institut de Recherche pour le Développement (IRD)-Institut de Chimie de Toulouse (ICT), Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université de Toulouse (UT)-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie de Toulouse (ICT-FR 2599), and Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Institut de Chimie du CNRS (INC)-Institut de Recherche pour le Développement (IRD)

Subjects
2. Zero hunger, 0301 basic medicine, Legumin, [SDV]Life Sciences [q-bio], food and beverages, 11S globulins, Biology, 11s globulin, Molecular biology, 03 medical and health sciences, IgE-binding cross-reactivity, 030104 developmental biology, B-cell epitopes, Three-dimensional structures, Immunology and Allergy, B-Cell Epitopes, Act c 12
Abstract

International audience; Kiwi fruit (Actinidia deliciosa, A. chinensis) is an important source of food allergy in children and adults in Western countries. The allergens responsible for this food allergy consist primarily of typical fruit allergens, e.g. the PR 10 Bet v 1-like allergen Act d 8, the cysteine protease actinidin Act d 1, the TLP Act d 2, and a chitinase. All of these allergens from A. deliciosa fruits have their counterparts in A. chinensis fruits. Recently, two other allergens belonging to the cupin superfamily (Act c 12) and the 2S albumin family (Act c 13), found in the kernels of A. chinensis fruit, have been identified as hidden fruit allergens responsible for IgE-binding cross-reactivity with peanuts and tree nuts. The sequential IgE-binding epitope regions of Act c 12 were predicted using a combination of in silico predictive approaches. Sequential IgE-binding epitopes of Act c 12 were predicted on a three-dimensional model of the protein from the amino acid sequence comparisons of the IgE-binding regions of cross-reacting cupins of peanuts and tree nuts. Residues of the sequence stretches exposed at the molecular surface were assigned as cross-reacting IgE-binding regions of Act c 12. In addition to their conformational similarities, these putative IgE-binding epitopes share a high degree of sequence similarity with the corresponding IgE-binding regions of peanut and tree-nut cupin allergens. The Act c 12 allergen offers an interesting example of a hidden fruit allergen likely to trigger allergic responses in individuals previously sensitized to peanut and other three-nut cupin allergens.(C) 2017 Elsevier Masson SAS. All rights reserved.

Published
2017
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4. Bases moléculaires de la réactivité croisée des cupines 11S

Author

Annick Barre, Hervé Benoist, Pierre Rougé, Stéphanie Caze-Subra, Pharmacochimie et Biologie pour le Développement (PHARMA-DEV), Institut de Recherche pour le Développement (IRD)-Institut de Chimie de Toulouse (ICT-FR 2599), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie du CNRS (INC)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Institut de Chimie du CNRS (INC), Institut de Recherche pour le Développement (IRD)-Institut de Chimie de Toulouse (ICT), Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique (Toulouse) (Toulouse INP), Université de Toulouse (UT)-Institut de Recherche pour le Développement (IRD)-Université Toulouse III - Paul Sabatier (UT3), and Université de Toulouse (UT)

Subjects
2. Zero hunger, 030207 dermatology & venereal diseases, 03 medical and health sciences, 0302 clinical medicine, 030228 respiratory system, [SDV]Life Sciences [q-bio], Immunology and Allergy, ComputingMilieux_MISCELLANEOUS
Abstract

Introduction Les globulines 11S (legumines) des graines constituent un groupe important d’allergenes. On les retrouve dans de tres nombreuses graines comestibles : arachide (Ara h 3), pistache (Pis v 2), noix de Cajou (Ana o 2), noix (Jug r 4), noisette (Cor a 9), amande (Pru du 6), soja (Gly m), sesame (Ses i 6), sarrasin (Fag e 13), etc. Ces allergenes presentent souvent une reactivite croisee importante. Recemment, une reactivite croisee a ete mise en evidence entre l’allergene masque Act d 12 des graines de kiwi et les cupines 11S de l’arachide, de l’amande, de la noisette et, plus rarement, de la noix. Methodes Une comparaison de la conformation des regions epitopiques sur la surface moleculaire de ces allergenes a ete entreprise afin de preciser les bases moleculaires qui sous-tendent cette reactivite croisee. Resultats La recherche d’allergenes homologues d’Act c 12 dans les banques d’allergenes fournit de nombreux homologues et tous ces allergenes possedent la structure tridimensionnelle typique des cupines 11S, constituee de deux homotrimeres superposes. Les sequences d’acides amines de ces allergenes montrent des taux eleves d’identite (55 %) et d’homologie (85 %) avec la sequence d’Act c 12. En particulier, ces identites/homologies s’observent dans certaines des regions epitopiques identifiees dans les allergenes homologues comme Ana o 2 de la noix de Cajou, Cor a 9 de la noisette, Jug r 4 de la noix. Ces regions epitopiques a fort pourcentage d’identite/homologie montrent des conformations tres similaires quand on les observe sur les modeles tridimensionnels d’Act c 12 et des autres allergenes Ana o 2, Cor a 9 et Jug r 4. Conclusion Ces conformations voisines rendent compte de la reactivite croisee observee entre Act d 12 et les autres allergenes de la superfamille des cupines 11S. Les regions epitopiques homologues identifiees sur la surface moleculaire des differents cupines 11S correspondent vraisemblablement a des epitopes consensuels presents chez une majorite de cupines 11S.

Published
2016

5. Caspase-mediated inhibition of sphingomyelin synthesis is involved in FasL-triggered cell death

Author

Z-X Jin, Stéphane Carpentier, Hisanori Umehara, Klaus Schulze-Osthoff, Thierry Levade, Hervé Benoist, Bruno Ségui, Elodie Lafont, Virginie Garcia, Toshiro Okazaki, Delphine Milhas, 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), Division of Hematology and Immunology, Kanazawa Medical University, Department of Clinical Laboratory, Medicine/Hematology, Tottori University, Interfaculty Institute for Biochemistry, Eberhard Karls Universität Tübingen = Eberhard Karls University of Tuebingen, Faculté des Sciences Pharmaceutiques, Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-IFR150-Institut National de la Santé et de la Recherche Médicale (INSERM), and Service d'Immunologie (UPS III)

Subjects
Ceramide, Programmed cell death, Fas Ligand Protein, Golgi Apparatus, Transferases (Other Substituted Phosphate Groups), Apoptosis, Nerve Tissue Proteins, chemical and pharmacologic phenomena, Ceramides, Amino Acid Chloromethyl Ketones, Jurkat Cells, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Humans, Enzyme Inhibitors, RNA, Small Interfering, Molecular Biology, Lipid raft, Caspase, 030304 developmental biology, 0303 health sciences, Leukemia, Dose-Response Relationship, Drug, Phospholipase C, biology, Cell growth, technology, industry, and agriculture, Membrane Proteins, hemic and immune systems, Cell Biology, Fas receptor, Sphingomyelins, Cell biology, carbohydrates (lipids), chemistry, Caspases, 030220 oncology & carcinogenesis, biology.protein, RNA Interference, lipids (amino acids, peptides, and proteins), HeLa Cells, Signal Transduction
Abstract

International audience; Ceramide can be converted into sphingomyelin by sphingomyelin synthases (SMS) 1 and 2. In this study, we show that in human leukemia Jurkat cells, which express mainly SMS1, Fas ligand (FasL) treatment inhibited SMS activity in a dose- and time-dependent manner before nuclear fragmentation. The SMS inhibition elicited by FasL (1) was abrogated by benzyloxycarbonyl valyl-alanyl-aspartyl-(O-methyl)-fluoromethylketone (zVAD-fmk), a broad-spectrum caspase inhibitor; (2) did not occur in caspase-8-deficient cells and (3) was not affected in caspase-9-deficient cells. Western blot experiments showed SMS1 cleavage in a caspase-dependent manner upon FasL treatment. In a cell-free system, caspase-2, -7, -8 and -9, but not caspase-3 and -10, cleaved SMS1. In HeLa cells, SMS1 was Golgi localized and relocated throughout the cytoplasm in cells exhibiting an early apoptotic phenotype on FasL treatment. zVAD-fmk prevented FasL-induced SMS1 relocation. Thus, FasL-mediated SMS1 inhibition and relocation depend on caspase activation and likely represent proximal events in Fas signaling. FasL-induced ceramide production and cell death were enhanced in cells stably expressing an siRNA against SMS1. Conversely, in cells stably overexpressing SMS1, FasL neither increased ceramide generation nor efficiently induced cell death. Altogether, our data show that SMS1 is a novel caspase target that is functionally involved in the regulation of FasL-induced apoptosis.

Published
2010
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6. FAN (factor associated with neutral sphingomyelinase activation), a moonlighting protein in TNF-R1 signaling

Author

Bruno Ségui, Hervé Benoist, Pascal G.P. Martin, Anne Montfort, Thierry Levade, 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), Laboratoire de Pharmacologie et Toxicologie, Institut National de la Recherche Agronomique (INRA), Service d'Allergologie et d'Immunologie [CHU Toulouse], 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), Service d'immunologie, and Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées

Subjects
Protein moonlighting, Cell signaling, medicine.medical_treatment, Cellular differentiation, [SDV]Life Sciences [q-bio], Immunology, Mice, Transgenic, Biology, Autoimmune Diseases, Proinflammatory cytokine, Mice, 03 medical and health sciences, 0302 clinical medicine, medicine, Animals, Humans, Immunology and Allergy, 030304 developmental biology, Inflammation, Mice, Knockout, 0303 health sciences, Tumor Necrosis Factor-alpha, Signal transducing adaptor protein, Cell Biology, Cell biology, Enzyme Activation, Molecular Weight, [SDV] Life Sciences [q-bio], Sphingomyelin Phosphodiesterase, Cytokine, Receptors, Tumor Necrosis Factor, Type I, Signal transduction, 030217 neurology & neurosurgery, Intracellular, Signal Transduction
Abstract

Review discusses recent findings on the role of FAN, a TNF receptor 1 adaptor protein, in TNFα-induced cell signaling and biological responses. TNF-α is a pleiotropic cytokine involved in the regulation of various biological effects, including cell survival and proliferation, cell differentiation, and cell death. Moreover, TNF-α triggers proinflammatory responses, essentially through its ability to promote the expression of various proinflammatory genes. Most of the biological effects initiated by TNF-α rely on its ability to bind to and activate TNF-R1. As a consequence, molecular complexes are being formed, resulting from the recruitment of multiple adaptor proteins to the intracellular TNF-R1 DD. The adaptor protein FAN constitutively binds to a proximal membrane domain of TNF-R1 called NSD. Herein, the role of FAN in TNF-α-induced cell signaling and biological responses is discussed.

Published
2010
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7. FAN stimulates TNF(alpha)-induced gene expression, leukocyte recruitment, and humoral response

Author

Marie-Antoinette Bertrand, Pascal G.P. Martin, Caroline Nevoit, Thierry Levade, Marie-Claude Trombe, Hervé Benoist, Victorine Douin-Echinard, Marie-Hélène Bessières, Bruno Ségui, Nicole Therville, Anne Montfort, Virginie Garcia, Jason S. Iacovoni, Bénédicte de Badts, Institut de médecine moléculaire de Rangueil (I2MR), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-IFR150-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de Pharmacologie et Toxicologie, Institut National de la Recherche Agronomique (INRA), IFR 31 Louis Bugnard (IFR 31), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-CHU Toulouse [Toulouse]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Service d'Immunologie, Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, Service de Parasitologie-Mycologie [Toulouse], Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-CHU Toulouse [Toulouse]-Hôpital Purpan [Toulouse], CHU Toulouse [Toulouse], Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU Toulouse [Toulouse]-Université Toulouse III - Paul Sabatier (UT3), Service de Parasitologie et Mycologie, CHU Toulouse [Toulouse]-Institut Fédératif de Biologie (IFB) - Hôpital Purpan, Hôpital Purpan [Toulouse], CHU Toulouse [Toulouse]-CHU Toulouse [Toulouse]-Hôpital Purpan [Toulouse], Simon, Marie Francoise, 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), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre Hospitalier Universitaire de Toulouse (CHU Toulouse)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Faculté des Sciences Pharmaceutiques, Service de Parasitologie et Mycologie [CHU Toulouse], Institut Fédératif de Biologie (IFB), Centre Hospitalier Universitaire de Toulouse (CHU Toulouse)-Centre Hospitalier Universitaire de Toulouse (CHU Toulouse)-Pôle Biologie [CHU Toulouse], and Centre Hospitalier Universitaire de Toulouse (CHU Toulouse)

Subjects
Chemokine, Chemokine CXCL2, Type I, Gene Expression, Inbred C57BL, MESH: Listeria monocytogenes, MESH: Mice, Knockout, MESH: Recombinant Proteins, Mice, 0302 clinical medicine, Gene expression, Receptors, Immunology and Allergy, Listeriosis, MESH: Animals, MESH: Pneumococcal Infections, Peritoneal Cavity, Cells, Cultured, Mice, Knockout, Listeria Infections, MESH: Receptors, Tumor Necrosis Factor, Type I, 0303 health sciences, Cultured, biology, MESH: Toxoplasma, Intracellular Signaling Peptides and Proteins, MESH: Peritoneal Cavity, Acquired immune system, Recombinant Proteins, MESH: Antibody Formation, medicine.anatomical_structure, Streptococcus pneumoniae, Neutrophil Infiltration, Receptors, Tumor Necrosis Factor, Type I, 030220 oncology & carcinogenesis, Knockout mouse, MESH: Toxoplasmosis, Tumor necrosis factor alpha, Toxoplasma, MESH: Listeria Infections, Toxoplasmosis, MESH: Streptococcus pneumoniae, MESH: Cells, Cultured, MESH: Gene Expression, Knockout, Cells, Immunology, Spleen, Pneumococcal Infections, 03 medical and health sciences, Peritoneal cavity, MESH: Mice, Inbred C57BL, MESH: Intracellular Signaling Peptides and Proteins, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, medicine, Animals, MESH: Chemokine CXCL2, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH: Mice, 030304 developmental biology, Microarray analysis techniques, Interleukin-6, Tumor Necrosis Factor-alpha, Fibroblasts, Microarray Analysis, Molecular biology, Listeria monocytogenes, MESH: Interleukin-6, Mice, Inbred C57BL, MESH: Microarray Analysis, MESH: Neutrophil Infiltration, MESH: Fibroblasts, MESH: Tumor Necrosis Factor-alpha, Antibody Formation, biology.protein, Tumor Necrosis Factor, human activities
Abstract

Factor associated with neutral sphingomyelinase activation (FAN) is an adaptor protein that constitutively binds to TNF-R1. Microarray analysis was performed in fibroblasts derived from wild-type or FAN knockout mouse embryos to evaluate the role of FAN in TNF-induced gene expression. Approximately 70% of TNF-induced genes exhibited lower expression levels in FAN-deficient than in wild-type fibroblasts. Of particular interest, TNF-induced expression of cytokines/chemokines, such as IL-6 and CXCL-2, was impaired in FAN-deficient cells. This was confirmed by real time RT-PCR and ELISA. Upon i.p. TNF or thioglycollate injection, neutrophil recruitment into the peritoneal cavity was reduced by more than 50% in FAN-deficient mice. Nevertheless, FAN-deficient animals did not exhibit an increased susceptibility to different microorganisms including bacteria and parasites, indicating that FAN is not essential for pathogen clearance. Specific Ab response to BSA was substantially impaired in FAN-deficient mice and this was associated with a reduced content of leukocytes in the spleen of BSA-challenged FAN-deficient mice as compared with their wild-type counterparts. Altogether, our results indicate the involvement of FAN in TNF-induced gene expression and leukocyte recruitment, contributing to the establishment of the specific immune response.

Published
2009
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8. Two structurally identical mannose-specific jacalin-related lectins display different effects on human T lymphocyte activation and cell death

Author

Raphaël Culerrier, Pierre Rougé, Annick Barre, Bruno Ségui, Hervé Benoist, Els J.M. Van Damme, Alain Jauneau, Willy J. Peumans, Guillaume Poiroux, 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), Faculté des Sciences Pharmaceutiques, Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, Surfaces Cellulaires et Signalisation chez les Végétaux (SCSV), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS), Laboratory of Biochemistry and Glycobiology, Chent University, Simon, Marie Francoise, Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-IFR150-Institut National de la Santé et de la Recherche Médicale (INSERM), Services d'Immunologie et Biologie Cellulaire, and Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3)

Subjects
Programmed cell death, Lymphocyte, T-Lymphocytes, Immunology, Lymphocyte Activation, Jurkat cells, 03 medical and health sciences, Structure-Activity Relationship, 0302 clinical medicine, Adjuvants, Immunologic, medicine, Immunology and Allergy, Humans, FADD, Cells, Cultured, 030304 developmental biology, 0303 health sciences, biology, Cell Death, Antibody-Dependent Cell Cytotoxicity, Cell Biology, Cell biology, medicine.anatomical_structure, Mannose-Binding Lectins, Concanavalin A, Cell culture, Apoptosis, 030220 oncology & carcinogenesis, biology.protein, Morus, Plant Lectins, Artocarpus, CD8
Abstract

Subtle changes in cell surface N-glycan recognition can modulate the T lymphocyte fate. Plant lectins displaying similar single sugar-binding specificity and identical molecular structure might present various biological effects. To explore this possibility, the effects on human lymphocytes of two mannose-specific and structurally closely related lectins, Morniga M from Morus nigra and artocarpin from Artocarpus integrifolia were investigated. In silico analysis revealed that Morniga M presents a more largely open carbohydrate-binding cavity than artocarpin, probably allowing interactions with a broader spectrum of carbohydrate moieties. In vitro, Morniga M interacted strongly with the lymphocyte surface and was uptaken quickly by cells. Morniga M and artocarpin triggered the proliferation and activation of human T and NK lymphocytes. A minority of B lymphocytes was activated in artocarpin-treated culture, whereas Morniga M favored the emergence of CD4+ CD8+ T lymphocytes. Moreover, cell death occurred in activated PBMC, activated T lymphocytes, and Jurkat T leukemia cells incubated with Morniga M only. The biological effects of both lectins were dependent on carbohydrate recognition. The Morniga M-induced cell death resulted, at least in part, from caspase-dependent apoptosis and FADD-dependent receptor-mediated cell death. Finally, Morniga M, but not artocarpin, triggered AICD of T lymphocytes. In conclusion, both lectins trigger lymphocyte activation, but only Morniga M induces cell death. In spite of similar in vitro mannose-binding specificities and virtually identical structure, only Morniga M probably interacts with carbohydrate moieties bound to molecules able to induce cell death. The present data suggest that subtle alterations in N-glycans can distinguish activation and cell death molecules at the lymphocyte surface.

Published
2009
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9. Interleukin-6 deficiency fails to prevent chronic rejection after aortic allografts in apolipoprotein E-deficient mice

Author

Denis Calise, Nicole Therville, Jean Claude Thiers, Bruno Ségui, Hervé Benoist, Mogens Thomsen, Talal Al Saati, Houda Yacoub-Youssef, Nelly Blaes, Institut de médecine moléculaire de Rangueil (I2MR), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-IFR150-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de microchirurgie, IFR 31 Louis Bugnard (IFR 31), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU Toulouse [Toulouse]-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU Toulouse [Toulouse]-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, Plateau technique d'histopathologie expérimentale, Institut Claude de Préval (ICP), 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), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre Hospitalier Universitaire de Toulouse (CHU Toulouse)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre Hospitalier Universitaire de Toulouse (CHU Toulouse)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), and Simon, Marie Francoise

Subjects
Graft Rejection, Apolipoprotein E, MESH: Vascular Resistance, 030204 cardiovascular system & hematology, MESH: Mice, Knockout, Mice, 0302 clinical medicine, Isoantibodies, Deficient mouse, MESH: Animals, Aorta, Dominance (genetics), Mice, Knockout, 0303 health sciences, biology, MESH: Aorta, MESH: Apolipoproteins E, 3. Good health, Titer, medicine.anatomical_structure, Mice, Inbred DBA, Antibody, Cardiology and Cardiovascular Medicine, Pulmonary and Respiratory Medicine, medicine.medical_specialty, T cell, MESH: Graft Rejection, 03 medical and health sciences, Apolipoproteins E, Internal medicine, medicine, MESH: Transplantation, Homologous, Animals, Transplantation, Homologous, Interleukin 6, MESH: Mice, 030304 developmental biology, Transplantation, MESH: Mice, Inbred DBA, Interleukin-6, Cell growth, business.industry, MESH: Interleukin-6, MESH: Isoantibodies, Endocrinology, Immunology, biology.protein, Vascular Resistance, Surgery, business
Abstract

International audience; BACKGROUND: Chronic vascular rejection (CVR) is characterized by an intimal thickening in the arteries of allografts due to immunoinflammatory reactions and smooth muscle cell proliferation. Interleukin 6 (IL-6) levels are increased in patients with graft rejection, however the role of IL-6 in CVR is not known. We investigated if IL-6 deficiency in the recipient could prevent CVR after an aortic allograft. METHODS: Donor aortas from wild-type DBA/2 mice were transplanted into C57BL/6 recipients, either wild-type mice or mice deficient for IL-6 (IL-6(-/-)), apolipoprotein E (ApoE(-/-)), or both (IL-6(-/-)ApoE(-/-)). Alloantibody titers were determined at Day 30, 60, or 90 after grafting. The grafts were examined for CVR lesions by morphometry and immunohistology. RESULTS: All recipient allografts displayed lesions typical for CVR. The lesions were larger in IL-6-deficient strains, and significantly so in IL-6(-/-)ApoE(-/-) recipients. Early immunoglobulin (Ig) G1 alloantibody deposits were observed in the grafts of ApoE-deficient strains and late IgG2a deposits in the grafts of IL-6-deficient strains. A rapid and sustained type 1 helper T cell (Th1; IgG2a) alloresponse in IL-6(-/-) mice, and a strong type 2 helper T cell (Th2; IgG1) response in ApoE(-/-) mice were observed. IL-6(-/-)ApoE(-/-) mice displayed the highest alloantibody titer, with a Th1 dominance. CONCLUSIONS: Unexpectedly, IL-6 deficiency in the recipient mice did not prevent CVR lesions but even aggravated them in IL-6(-/-)ApoE(-/-) recipients. This was associated with increased local and systemic alloresponses.

Published
2009
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