Author: "Jung, Stephanie" / Database: OpenAIRE - Searchworks@Jio Institute Digital Library Search Results

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1. Factor XIII is a newly identified binding partner for platelet collagen receptor GPVI-dimer-An interaction that may modulate fibrin crosslinking

Author: Moroi, Masaaki, Induruwa, Isuru, Farndale, Richard W, Jung, Stephanie M, Moroi, Masaaki [0000-0003-4656-2319], Induruwa, Isuru [0000-0002-7020-8179], Farndale, Richard W [0000-0001-6130-8808], Jung, Stephanie M [0000-0002-7409-9715], and Apollo - University of Cambridge Repository
Subjects: GPVI, GPVI‐dimer, crosslinking, factor XIII, fibrin, γ‐dimer, fibrin clot, γ‐chain
Abstract: BACKGROUND: In the fibrin-forming process, thrombin cleaves fibrinogen to fibrin, which form fibrils and then fibers, producing a gel-like clot. Thrombin also activates coagulation factor XIII (FXIII), which crosslinks fibrin γ-chains and α-chains, stabilizing the clot. Many proteins bind to fibrin, including FXIII, an established regulation of clot structure, and platelet glycoprotein VI (GPVI), whose contribution to clot function is largely unknown. FXIII is present in plasma, but the abundant FXIII in platelet cytosol becomes exposed to the surface of strongly activated platelets. OBJECTIVES: We determined if GPVI interacts with FXIII and how this might modulate clot formation. METHODS: We measured interactions between recombinant proteins of the GPVI extracellular domain: GPVI-dimer (GPVI-Fc2) or monomer (GPVIex) and FXIII proteins (nonactivated and thrombin-activated FXIII, FXIII subunits A and B) by ELISA. Binding to fibrin clots and fibrin γ-chain crosslinking were analyzed by immunoblotting. RESULTS: GPVI-dimer, but not GPVI-monomer, bound to FXIII. GPVI-dimer selectively bound to the FXIII A-subunit, but not to the B-subunit, an interaction that was decreased or abrogated by the GPVI-dimer-specific antibody mFab-F. The GPVI-dimer-FXIII interaction decreased the extent of γ-chain crosslinking, indicating a role in the regulation of clot formation. CONCLUSIONS: This is the first report of the specific interaction between GPVI-dimer and the A-subunit of FXIII, as determined in an in vitro system with defined components. GPVI-dimer-FXIII binding was inhibitory toward FXIII-catalyzed crosslinking of fibrin γ-chains in fibrin clots. This raises the possibility that GPVI-dimer may negatively modulate fibrin crosslinking induced by FXIII, lessening clot stability., British Heart Foundation SP/10/011/28199 NIHR Academic Clinical Lectureship RG85316
Published: 2022
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2. Activation-induced changes in platelet surface receptor expression and the contribution of the large-platelet subpopulation to activation

Author: Moroi, Masaaki, Farndale, Richard W, Jung, Stephanie M, Jung, Stephanie M [0000-0002-7409-9715], and Apollo - University of Cambridge Repository
Subjects: IIbIIIa, large platelets, GPVI, GPIb, receptors, activation, αIIbβ3
Abstract: OBJECTIVE: Platelet surface receptors are also present subcellularly in organelle membranes and can be expressed on the surface upon platelet activation. However, some receptors were reported to be decreased after activation. We analyzed the mechanism of activation-dependent expression for different receptors. METHODS: Flow cytometry using platelet-rich plasma or washed platelets was used to analyze receptor-expression changes after platelet activation by glycoprotein (GP) VI-specific agonists, crosslinked collagen-related peptide (CRP-XL) and convulxin (Cvx), and thrombin. Platelets prelabeled with fluorescent antibody specific for a receptor were allowed to adhere on immobilized collagen or fibrinogen and post-stained with antibody against the same receptor labeled with another fluorophore, allowing us to differentiate preexisting receptors from newly expressed receptors. RESULTS: Surface expression of αIIbβ3 increased in CRP-XL-, Cvx-, or thrombin-stimulated platelets, but GPIb decreased due to shedding and internalization. Both total and dimeric GPVI increased in thrombin-induced platelets, but decreased in platelets stimulated by Cvx, as a result of internalization. The larger platelets showed a greater increase in surface receptor (α2β1, αIIbβ3, GPVI, GPIb) expression upon activation compared to the smaller ones. Pre- and postlabeling with antibody specific for the same receptor, but conjugated with different fluorophores, allowed us to differentiate the receptors expressed on the surface of resting platelets from receptors newly exposed to the surface upon platelet activation. CONCLUSIONS: Increased receptor expressions after activation are mainly manifested in the larger platelets. On platelets adhered on fibrinogen, the newly expressed receptors, especially GPVI, are localized in the lamellipodia of the spread platelets.
Published: 2020

3. Extracellular vesicles derived from Hepatitis-D Virus infected cells induce a proinflammatory cytokine response in human peripheral blood mononuclear cells and macrophages

Author: Jung, Stephanie, Altstetter, Sebastian Maximilian, Wilsch, Florian, Shein, Mikhail, Schütz, Anne Kathrin, and Protzer, Ulrike
Subjects: viruses, FOS: Biological sciences, proinflammatory cytokines, virus diseases, Hepatitis D Virus, biochemical phenomena, metabolism, and nutrition, extracellular vesicles, innate immunity, FOS: Medical and health sciences
Abstract: Hepatitis D Virus (HDV) is a satellite virus requiring a Hepatitis B Virus (HBV) envelope proteins for productive infection. Hepatitis D is the most severe form of viral hepatitis and is a global health threat affecting 15 to 20 million humans. In contrast to the Hep atitis B Virus mono-infection, against which only a minor innate immune response is mounted at most, HBV-HDV coinfection is characterized by strong activation of innate immune responses. To shed light on poorly understood mechanisms of HDV-triggered disease progression, we focussed on the question how immune cells may be activated by HDV. We hypothesized that extracellular vesicles (EVs) released from infected cells me diate this activation. We, therefore, purified EVs from the supernatant of HDV-infected and non-infected cells and incubated them with human peripheral blood mononuclear cells (PBMC) and macrophages. Here we show for the first time that HDV infection leads to the production of EVs which subsequently mediate a proinflammatory cytokine response in primary human immune cells. These data might help to understand how HDV can be sensed by non-infected immune cells.
Published: 2020
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4. A comprehensive UHPLC ion mobility QTOF method for profiling and quantification of eicosanoids, other oxylipins and fatty acids

Author: Hinz, Christine, Liggi, Sonia, Mocciaro, Gabriele, Jung, Stephanie M., Induruwa, Isuru, Pereira, Milton C.D.A., Bryant, Clare E., Meckelmann, Sven W., O'Donnell, Valerie B., Farndale, Richard W., Fjeldsted, John C., and Griffin, Julian L.
Subjects: Mice, Inbred C57BL, Tandem Mass Spectrometry, Fatty Acids, Ion Mobility Spectrometry, Animals, Eicosanoids, Humans, Oxylipins, Article, Cells, Cultured, Chromatography, High Pressure Liquid
Abstract: Analysis of oxylipins by liquid chromatography mass spectrometry (LC-MS) is challenging because of the small mass range occupied by this diverse lipid class, the presence of numerous structural isomers, and their low abundance in biological samples. Although highly sensitive LC-MS/MS methods are commonly used, further separation is achievable by using drift tube ion mobility coupled with high-resolution mass spectrometry (DTIM-MS). Herein, we present a combined analytical and computational method for the identification of oxylipins and fatty acids. We use a reversed-phase LC-DTIM-MS workflow able to profile and quantify (based on chromatographic peak area) the oxylipin and fatty acid content of biological samples while simultaneously acquiring full scan and product ion spectra. The information regarding accurate mass, collision-cross section values in nitrogen ((DT)CCS(N2)) and retention times of the species found are compared to an internal library of lipid standards as well as the LIPID MAPS Structure Database by using specifically developed processing tools. Features detected within the (DT)CCS(N2) and m/z ranges of the analyzed standards are flagged as oxylipin-like species, which can be further characterized using drift time alignment of product and precursor ions distinctive of DTIM-MS. This not only helps identification by reducing the number of annotations from LIPID MAPS, but also guides discovery studies of potentially novel species. Testing the methodology on Salmonella enterica serovar Typhimurium infected murine bone-marrow derived macrophages and thrombin activated human platelets yields results in agreement with literature. This workflow has also annotated features as potentially novel oxylipins, confirming its ability in providing further insights into lipid analysis of biological samples.
Published: 2019

5. Data on hyper-activation of GPVI signalling in obese patients: Towards the identification of novel antiplatelet targets in obesity

Author: Barrachina, María N, Izquierdo, Irene, Hermida-Nogueira, Lidia, Sueiro, Aurelio M, Guitián, Esteban, Casanueva, Felipe F, Farndale, Richard W, Moroi, Masaaki, Jung, Stephanie M, Pardo, María, García, Ángel, Farndale, Richard [0000-0001-6130-8808], and Apollo - University of Cambridge Repository
Subjects: 2 Aetiology, 32 Biomedical and Clinical Sciences, Hematology, 3101 Biochemistry and Cell Biology, Cardiovascular, lcsh:Computer applications to medicine. Medical informatics, Stroke, Clinical Research, 2.1 Biological and endogenous factors, lcsh:R858-859.7, Obesity, lcsh:Science (General), 31 Biological Sciences, Nutrition, Cancer, lcsh:Q1-390
Abstract: This data article is associated with the manuscript "GPVI surface expression and signalling pathway activation are increased in platelets from obese patients: elucidating potential anti-atherothrombotic targets in obesity" [1]. The study refers to a combination of different approaches in order to identify platelet-derived biomarkers in obesity. A total of 34 obese patients and their lean-matched controls were included in the study. We carried out a proteomic and functional (aggregation assays) analysis to find alterations in platelet-derived signalling pathways. After that, biochemical and mechanistic (flow cytometry assays) approaches were done in order to confirm a hyperactivation of the GPVI-related signalling pathway.
Published: 2019

6. GPVI surface expression and signalling pathway activation are increased in platelets from obese patients: Elucidating potential anti-atherothrombotic targets in obesity

Author: Núñez Barrachina, María, Sueiro, Aurelio M., Izquierdo Berjano, Irene, Hermida Nogueira, Lidia, Guitián Fernández, Esteban, Casanueva Freijo, Felipe, Farndale, Richard W., Masaaki, Moroi, Jung, Stephanie M., Pardo Pérez, María, García Alonso, Ángel, Farndale, Richard [0000-0001-6130-8808], Apollo - University of Cambridge Repository, Universidade de Santiago de Compostela. Centro de Investigación en Medicina Molecular e Enfermidades Crónicas, and Universidade de Santiago de Compostela. Departamento de Farmacoloxía, Farmacia e Tecnoloxía Farmacéutica
Subjects: Platelets, Proteomics, Adult, Blood Platelets, Male, Drug targets, Adolescent, Platelet Aggregation, Phospholipase C gamma, GPVI signalling, Platelet Membrane Glycoproteins, Platelet Activation, Article, Body Mass Index, Up-Regulation, Young Adult, Case-Control Studies, Humans, Female, Obesity, Phosphorylation, SFK-Mediated signalling pathways, Signal Transduction
Abstract: Background and aims Platelets play a fundamental role in the increased atherothrombotic risk related to central obesity since they show hyperactivation and lower sensitivity to antiplatelet therapy in obese patients. The main goal of this study was to identify platelet biomarkers related to the risk of atherothrombosis in obese patients, confirm platelet activation levels in these patients, and identify altered activation pathways. Methods Platelets were obtained from cohorts of obese patients and age- and sex-matched lean controls. Biochemical and proteome analyses were done by two-dimensional differential in-gel electrophoresis (2D-DIGE), mass spectrometry, and immunoblotting. Functional and mechanistic studies were conducted with aggregation assays and flow cytometry. Results We confirmed an up-regulation of αIIb and fibrinogen isoforms in platelets from obese patients. A complementary platelet aggregation approach showed platelets from obese patients are hyper-reactive in response to collagen and collagen-related peptide (CRP), revealing the collagen receptor Glycoprotein VI (GPVI) signalling as one of the altered pathways. We also found the active form of Src (pTyr418) is up-regulated in platelets from obese individuals, which links proteomics to aggregation data. Moreover, we showed that CRP-activated platelets present higher levels of tyrosine phosphorylated PLCγ2 in obese patients, confirming alterations in GPVI signalling. In line with the above, flow cytometry studies show higher surface expression levels of total GPVI and GPVI-dimer in obese platelets, both correlating with BMI. Conclusions Our results suggest a higher activation state of SFKs-mediated signalling pathways in platelets from obese patients, with a primary involvement of GPVI signalling., Graphical abstract Image 1, Highlights • Higher expression of the active form of Src (pTyr418) in obese patients platelets. • Increased aggregation levels of obese platelets in response to GPVI activation. • GPVI-activated platelets show higher levels of tyr-phosphorylated PLCγ2 in obesity. • Higher surface expression levels of GPVI in obese platelets, correlating with BMI.
Published: 2019

7. Data on hyper-activation of GPVI signalling inobese patients: towards the identification ofnovel antiplatelet targets in obesity

Author: Núñez Barrachina, María, Berjano Izquierdo, Irene, Hermida Nogueira, Lidia, Sueiro, Aurelio M., Guitián Fernández, Esteban, Casanueva Freijo, Felipe, Farndale, Richard W., Masaaki, Moroi, Jung, Stephanie M., Pardo Pérez, María, García Alonso, Ángel, Universidade de Santiago de Compostela. Centro de Investigación en Medicina Molecular e Enfermidades Crónicas, and Universidade de Santiago de Compostela. Departamento de Farmacoloxía, Farmacia e Tecnoloxía Farmacéutica
Abstract: This data article is associated with the manuscript "GPVI surface expression and signalling pathway activation are increased in platelets from obese patients: elucidating potential anti-atherothrombotic targets in obesity" [1]. The study refers to a combination of different approaches in order to identify platelet-derived biomarkers in obesity. A total of 34 obese patients and their lean-matched controls were included in the study. We carried out a proteomic and functional (aggregation assays) analysis to find alterations in platelet-derived signalling pathways. After that, biochemical and mechanistic (flow cytometry assays) approaches were done in order to confirm a hyperactivation of the GPVI-related signalling pathway. This work was supported by the Spanish Ministry of Economy andCompetitiveness (MINECO) [grant No. SAF2016-79662-R], co-funded by the European RegionalDevelopment Fund (ERDF). Financial support from the Consellería de Cultura, Educación e OrdenaciónUniversitaria, Xunta de Galicia (Centro Singular de investigación de Galicia accreditation 2016e2019,ED431G/05), and the European Regional Development Fund (ERDF) is also gratefully acknowledged.SMJ and RWF were supported by British Heart Foundation, grants SP/13/7/30575, PG/18/36/338, andRG/15/4/31268 SI
Published: 2019

8. Minimal information for studies of extracellular vesicles 2018 (MISEV2018):a position statement of the International Society for Extracellular Vesicles and update of the MISEV2014 guidelines

Author: Théry, Clotilde, Witwer, Kenneth W, Aikawa, Elena, Alcaraz, Maria Jose, Anderson, Johnathon D, Andriantsitohaina, Ramaroson, Antoniou, Anna, Arab, Tanina, Archer, Fabienne, Atkin-Smith, Georgia K, Ayre, D Craig, Bach, Jean-Marie, Bachurski, Daniel, Baharvand, Hossein, Balaj, Leonora, Baldacchino, Shawn, Bauer, Natalie N, Baxter, Amy A, Bebawy, Mary, Beckham, Carla, Bedina Zavec, Apolonija, Benmoussa, Abderrahim, Berardi, Anna C, Bergese, Paolo, Bielska, Ewa, Blenkiron, Cherie, Bobis-Wozowicz, Sylwia, Boilard, Eric, Boireau, Wilfrid, Bongiovanni, Antonella, Borràs, Francesc E, Bosch, Steffi, Boulanger, Chantal M, Breakefield, Xandra, Breglio, Andrew M, Brennan, Meadhbh Á, Brigstock, David R, Brisson, Alain, Broekman, Marike Ld, Bromberg, Jacqueline F, Bryl-Górecka, Paulina, Buch, Shilpa, Buck, Amy H, Burger, Dylan, Busatto, Sara, Buschmann, Dominik, Bussolati, Benedetta, Buzás, Edit I, Byrd, James Bryan, Camussi, Giovanni, Carter, David Rf, Caruso, Sarah, Chamley, Lawrence W, Chang, Yu-Ting, Chen, Chihchen, Chen, Shuai, Cheng, Lesley, Chin, Andrew R, Clayton, Aled, Clerici, Stefano P, Cocks, Alex, Cocucci, Emanuele, Coffey, Robert J, Cordeiro-da-Silva, Anabela, Couch, Yvonne, Coumans, Frank Aw, Coyle, Beth, Crescitelli, Rossella, Criado, Miria Ferreira, D'Souza-Schorey, Crislyn, Das, Saumya, Datta Chaudhuri, Amrita, de Candia, Paola, De Santana, Eliezer F, De Wever, Olivier, Del Portillo, Hernando A, Demaret, Tanguy, Deville, Sarah, Devitt, Andrew, Dhondt, Bert, Di Vizio, Dolores, Dieterich, Lothar C, Dolo, Vincenza, Dominguez Rubio, Ana Paula, Dominici, Massimo, Dourado, Mauricio R, Driedonks, Tom Ap, Duarte, Filipe V, Duncan, Heather M, Eichenberger, Ramon M, Ekström, Karin, El Andaloussi, Samir, Elie-Caille, Celine, Erdbrügger, Uta, Falcón-Pérez, Juan M, Fatima, Farah, Fish, Jason E, Flores-Bellver, Miguel, Försönits, András, Frelet-Barrand, Annie, Fricke, Fabia, Fuhrmann, Gregor, Gabrielsson, Susanne, Gámez-Valero, Ana, Gardiner, Chris, Gärtner, Kathrin, Gaudin, Raphael, Gho, Yong Song, Giebel, Bernd, Gilbert, Caroline, Gimona, Mario, Giusti, Ilaria, Goberdhan, Deborah Ci, Görgens, André, Gorski, Sharon M, Greening, David W, Gross, Julia Christina, Gualerzi, Alice, Gupta, Gopal N, Gustafson, Dakota, Handberg, Aase, Haraszti, Reka A, Harrison, Paul, Hegyesi, Hargita, Hendrix, An, Hill, Andrew F, Hochberg, Fred H, Hoffmann, Karl F, Holder, Beth, Holthofer, Harry, Hosseinkhani, Baharak, Hu, Guoku, Huang, Yiyao, Huber, Veronica, Hunt, Stuart, Ibrahim, Ahmed Gamal-Eldin, Ikezu, Tsuneya, Inal, Jameel M, Isin, Mustafa, Ivanova, Alena, Jackson, Hannah K, Jacobsen, Soren, Jay, Steven M, Jayachandran, Muthuvel, Jenster, Guido, Jiang, Lanzhou, Johnson, Suzanne M, Jones, Jennifer C, Jong, Ambrose, Jovanovic-Talisman, Tijana, Jung, Stephanie, Kalluri, Raghu, Kano, Shin-Ichi, Kaur, Sukhbir, Kawamura, Yumi, Keller, Evan T, Khamari, Delaram, Khomyakova, Elena, Khvorova, Anastasia, Kierulf, Peter, Kim, Kwang Pyo, Kislinger, Thomas, Klingeborn, Mikael, Klinke, David J, Kornek, Miroslaw, Kosanović, Maja M, Kovács, Árpád Ferenc, Krämer-Albers, Eva-Maria, Krasemann, Susanne, Krause, Mirja, Kurochkin, Igor V, Kusuma, Gina D, Kuypers, Sören, Laitinen, Saara, Langevin, Scott M, Languino, Lucia R, Lannigan, Joanne, Lässer, Cecilia, Laurent, Louise C, Lavieu, Gregory, Lázaro-Ibáñez, Elisa, Le Lay, Soazig, Lee, Myung-Shin, Lee, Yi Xin Fiona, Lemos, Debora S, Lenassi, Metka, Leszczynska, Aleksandra, Li, Isaac Ts, Liao, Ke, Libregts, Sten F, Ligeti, Erzsebet, Lim, Rebecca, Lim, Sai Kiang, Linē, Aija, Linnemannstöns, Karen, Llorente, Alicia, Lombard, Catherine A, Lorenowicz, Magdalena J, Lörincz, Ákos M, Lötvall, Jan, Lovett, Jason, Lowry, Michelle C, Loyer, Xavier, Lu, Quan, Lukomska, Barbara, Lunavat, Taral R, Maas, Sybren Ln, Malhi, Harmeet, Marcilla, Antonio, Mariani, Jacopo, Mariscal, Javier, Martens-Uzunova, Elena S, Martin-Jaular, Lorena, Martinez, M Carmen, Martins, Vilma Regina, Mathieu, Mathilde, Mathivanan, Suresh, Maugeri, Marco, McGinnis, Lynda K, McVey, Mark J, Meckes, David G, Meehan, Katie L, Mertens, Inge, Minciacchi, Valentina R, Möller, Andreas, Møller Jørgensen, Malene, Morales-Kastresana, Aizea, Morhayim, Jess, Mullier, François, Muraca, Maurizio, Musante, Luca, Mussack, Veronika, Muth, Dillon C, Myburgh, Kathryn H, Najrana, Tanbir, Nawaz, Muhammad, Nazarenko, Irina, Nejsum, Peter, Neri, Christian, Neri, Tommaso, Nieuwland, Rienk, Nimrichter, Leonardo, Nolan, John P, Nolte-'t Hoen, Esther NM, Noren Hooten, Nicole, O'Driscoll, Lorraine, O'Grady, Tina, O'Loghlen, Ana, Ochiya, Takahiro, Olivier, Martin, Ortiz, Alberto, Ortiz, Luis A, Osteikoetxea, Xabier, Østergaard, Ole, Ostrowski, Matias, Park, Jaesung, Pegtel, D Michiel, Peinado, Hector, Perut, Francesca, Pfaffl, Michael W, Phinney, Donald G, Pieters, Bartijn Ch, Pink, Ryan C, Pisetsky, David S, Pogge von Strandmann, Elke, Polakovicova, Iva, Poon, Ivan Kh, Powell, Bonita H, Prada, Ilaria, Pulliam, Lynn, Quesenberry, Peter, Radeghieri, Annalisa, Raffai, Robert L, Raimondo, Stefania, Rak, Janusz, Ramirez, Marcel I, Raposo, Graça, Rayyan, Morsi S, Regev-Rudzki, Neta, Ricklefs, Franz L, Robbins, Paul D, Roberts, David D, Rodrigues, Silvia C, Rohde, Eva, Rome, Sophie, Rouschop, Kasper Ma, Rughetti, Aurelia, Russell, Ashley E, Saá, Paula, Sahoo, Susmita, Salas-Huenuleo, Edison, Sánchez, Catherine, Saugstad, Julie A, Saul, Meike J, Schiffelers, Raymond M, Schneider, Raphael, Schøyen, Tine Hiorth, Scott, Aaron, Shahaj, Eriomina, Sharma, Shivani, Shatnyeva, Olga, Shekari, Faezeh, Shelke, Ganesh Vilas, Shetty, Ashok K, Shiba, Kiyotaka, Siljander, Pia R-M, Silva, Andreia M, Skowronek, Agata, Snyder, Orman L, Soares, Rodrigo Pedro, Sódar, Barbara W, Soekmadji, Carolina, Sotillo, Javier, Stahl, Philip D, Stoorvogel, Willem, Stott, Shannon L, Strasser, Erwin F, Swift, Simon, Tahara, Hidetoshi, Tewari, Muneesh, Timms, Kate, Tiwari, Swasti, Tixeira, Rochelle, Tkach, Mercedes, Toh, Wei Seong, Tomasini, Richard, Torrecilhas, Ana Claudia, Tosar, Juan Pablo, Toxavidis, Vasilis, Urbanelli, Lorena, Vader, Pieter, van Balkom, Bas Wm, van der Grein, Susanne G, Van Deun, Jan, van Herwijnen, Martijn Jc, Van Keuren-Jensen, Kendall, van Niel, Guillaume, van Royen, Martin E, van Wijnen, Andre J, Vasconcelos, M Helena, Vechetti, Ivan J, Veit, Tiago D, Vella, Laura J, Velot, Émilie, Verweij, Frederik J, Vestad, Beate, Viñas, Jose L, Visnovitz, Tamás, Vukman, Krisztina V, Wahlgren, Jessica, Watson, Dionysios C, Wauben, Marca Hm, Weaver, Alissa, Webber, Jason P, Weber, Viktoria, Wehman, Ann M, Weiss, Daniel J, Welsh, Joshua A, Wendt, Sebastian, Wheelock, Asa M, Wiener, Zoltán, Witte, Leonie, Wolfram, Joy, Xagorari, Angeliki, Xander, Patricia, Xu, Jing, Yan, Xiaomei, Yáñez-Mó, María, Yin, Hang, Yuana, Yuana, Zappulli, Valentina, Zarubova, Jana, Žėkas, Vytautas, Zhang, Jian-Ye, Zhao, Zezhou, Zheng, Lei, Zheutlin, Alexander R, Zickler, Antje M, Zimmermann, Pascale, Zivkovic, Angela M, Zocco, Davide, Zuba-Surma, Ewa K, dB&C I&I, LS Celbiologie-Algemeen, Celbiologie, Afd Pharmaceutics, Sub General Pharmaceutics, Sub Biomol.Mass Spect. and Proteomics, Afd Pharmacology, Urology, Pathology, Medical Oncology, Immunité et cancer, Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Johns Hopkins University School of Medicine [Baltimore], Stress Oxydant et Pathologies Métaboliques (SOPAM), Université d'Angers (UA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U 1192 (PRISM), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), Infections Virales et Pathologie Comparée - UMR 754 (IVPC), Institut National de la Recherche Agronomique (INRA)-École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon, Immuno-Endocrinologie Cellulaire et Moléculaire [Nantes] (IECM), Institut National de la Recherche Agronomique (INRA)-Université de Nantes (UN)-École nationale vétérinaire, agroalimentaire et de l'alimentation Nantes-Atlantique (ONIRIS), Department for Molecular Biology and Nanobiotechnology, National Institute of chemitry, Slovenia, Biologie, génétique et thérapies ostéoarticulaires et respiratoires (BIOTARGEN), Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU), Institut de pharmacologie moléculaire et cellulaire (IPMC), Université Nice Sophia Antipolis (1965 - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Centre National de la Recherche Scientifique (CNRS), Franche-Comté Électronique Mécanique, Thermique et Optique - Sciences et Technologies (UMR 6174) (FEMTO-ST), Université de Technologie de Belfort-Montbeliard (UTBM)-Ecole Nationale Supérieure de Mécanique et des Microtechniques (ENSMM)-Centre National de la Recherche Scientifique (CNRS)-Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC), Immuno-Endocrinologie Cellulaire et Moléculaire (IECM), Institut National de la Recherche Agronomique (INRA)-Université de Nantes (UN)-Ecole Nationale Vétérinaire de Nantes, Paris-Centre de Recherche Cardiovasculaire (PARCC - UMR-S U970), Hôpital Européen Georges Pompidou [APHP] (HEGP), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Physiopathologie des Adaptations Nutritionnelles (PhAN), Université de Nantes - UFR de Médecine et des Techniques Médicales (UFR MEDECINE), Université de Nantes (UN)-Université de Nantes (UN)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Imagerie Moléculaire et Nanobiotechnologies - Institut Européen de Chimie et Biologie (IECB), Université Sciences et Technologies - Bordeaux 1-Centre National de la Recherche Scientifique (CNRS), Molecular Biotechnology Center, Università degli studi di Torino = University of Turin (UNITO), Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Centre for Sustainable Tropical Fisheries and Aquaculture, James Cook University (JCU), Department of Oncology - Pathology, Cancer Center Karolinska [Karolinska Institutet] (CCK), Karolinska Institutet [Stockholm]-Karolinska Institutet [Stockholm], Departamento de Ciências Biológicas, Universidade do Porto = University of Porto, Laboratory of Experimental Cancer Research, Department of Radiation Oncology and Experimental Cancer Research, Cancer Research Institute Ghent (CRIG), Universiteit Gent = Ghent University [Belgium] (UGENT), Department of Medical and Surgical Sciences for Children and Adults [Modena, Italy] (Laboratory of Cellular Therapy), Università degli Studi di Modena e Reggio Emilia (UNIMORE), Clinical Research Center, Department of Laboratory Medicine, Karolinska Institutet, Karolinska University Hospital Huddinge, Huddinge, Sweden, Karolinska Institutet [Stockholm]-Karolinska University Hospital [Stockholm], Center for Cooperative Research in Biosciences (CIC bioGUNE), Partner site Munich, German Centre for Infection Research (DZIF), Institute for Transfusion Medicine, University Hospital Essen, Universität Duisburg-Essen [Essen], Mécanismes Adaptatifs et Evolution (MECADEV), Muséum national d'Histoire naturelle (MNHN)-Centre National de la Recherche Scientifique (CNRS), Psychiatry, Institute of Biological, Environmental and Rural Sciences (IBERS), Aberystwyth University, Department of Bacteriology and Immunology [Helsinki], Haartman Institute [Helsinki], Faculty of Medecine [Helsinki], Helsingin yliopisto = Helsingfors universitet = University of Helsinki-Helsingin yliopisto = Helsingfors universitet = University of Helsinki-Faculty of Medecine [Helsinki], Helsingin yliopisto = Helsingfors universitet = University of Helsinki-Helsingin yliopisto = Helsingfors universitet = University of Helsinki, Rigshospitalet [Copenhagen], Copenhagen University Hospital, Dalhousie University [Halifax], Department of Biology, Molecular Cell Biology, University of Mainz, Johannes Gutenberg - Universität Mainz = Johannes Gutenberg University (JGU), Glycobiologie et signalisation cellulaire, Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM), Krefting Research Centre, Department of Internal Medicine and Clinical Nutrition, University of Gothenburg (GU), Universidad de Alicante, École supérieure du professorat et de l'éducation - Académie de Créteil (UPEC ESPE Créteil), Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12), University of Antwerp (UA), Université Catholique de Louvain = Catholic University of Louvain (UCL), Research Institute, IRCCS Ospedale Pediatrico Bambino Gesù [Roma], Department of Veterinary Disease Biology [Copenhagen], Faculty of Health and Medical Sciences, University of Copenhagen = Københavns Universitet (KU)-University of Copenhagen = Københavns Universitet (KU), Biologie et Pathologie du Neurone (Brain-C), Adaptation Biologique et Vieillissement = Biological Adaptation and Ageing (B2A), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), 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)-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)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), 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)-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)-Centre National de la Recherche Scientifique (CNRS), Department of Mathematics and Statistics, American University, University of Pretoria [South Africa], Ecole des Ingénieurs de la Ville de Paris (EIVP), Universitat Pompeu Fabra [Barcelona] (UPF), Instituto de Investigaciones Biomedicas, Universidad Nacional Autónoma de México (UNAM), Istituto Ortopedico Rizzoli, Department of Molecular Therapeutics, The Scripps Research Institute, Laboratoire d'Informatique de Grenoble (LIG ), Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP )-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Montreal Children's Hospital, McGill University Health Center [Montreal] (MUHC), Compartimentation et dynamique cellulaires (CDC), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut Curie [Paris]-Centre National de la Recherche Scientifique (CNRS), National Cancer Institute [Bethesda] (NCI-NIH), National Institutes of Health [Bethesda] (NIH), Cardiovasculaire, métabolisme, diabétologie et nutrition (CarMeN), Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Hospices Civils de Lyon (HCL)-Institut National de la Santé et de la Recherche Médicale (INSERM), Cardiovascular Research Center, Massachusetts General Hospital [Boston], University Medical Center [Utrecht], University of Toronto, Fiocruz Minas - René Rachou Research Center / Instituto René Rachou [Belo Horizonte, Brésil], Fundação Oswaldo Cruz (FIOCRUZ), Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), 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), Federal University of Sao Paulo (Unifesp), Functional Genomics / Genómica Funcional [Montevideo], Institut Pasteur de Montevideo, Dipartimento di Medicina Sperimentale e Scienze Biochimiche, Università degli Studi di Perugia (UNIPG), Hospital Santa Cristina Instituto de Investigación Sanitaria Princesa C, Unidad de Investigación, Institut Curie [Paris]-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Ingénierie Moléculaire et Physiopathologie Articulaire (IMoPA), Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), Department of Physiology, University of California [San Francisco] (UCSF), University of California-University of California, University of Vermont [Burlington], Peking University [Beijing], Shandong Agricultural University (SDAU), State Key Laboratory of Quality Research in Chinese Medicine Taipa, Macau SAR, (Institute of Chinese Medical Sciences), Human Genetics, Universität Ulm - Ulm University [Ulm, Allemagne], INSERM, Institut Curie, INCa [INCA-11548], French National Research Agency [ANR-10-IDEX-0001-02 PSL*, ANR-11-LABX-0043], SIDACTION [17-1-AAE-1138], Fondation ARC [PGA1 RF20180206962, PJA 20171206453], NIDA [DA040385, DA047807], Ministry of Education, NIA [AG057430], NIMH [MH118164], Institut National de la Recherche Agronomique (INRA)-École Pratique des Hautes Études (EPHE), Institut National de la Recherche Agronomique (INRA)-Université de Nantes (UN)-Ecole Nationale Vétérinaire de Nantes-École nationale vétérinaire, agroalimentaire et de l'alimentation Nantes-Atlantique (ONIRIS), Institut National de la Recherche Agronomique (INRA)-Université de Nantes (UN), Université Sciences et Technologies - Bordeaux 1 (UB)-Centre National de la Recherche Scientifique (CNRS), Universiteit Gent = Ghent University (UGENT), Università degli Studi di Modena e Reggio Emilia = University of Modena and Reggio Emilia (UNIMORE), Universität Duisburg-Essen = University of Duisburg-Essen [Essen], Biotechnology and Biological Sciences Research Council (BBSRC)-Aberystwyth University, University of Copenhagen = Københavns Universitet (UCPH)-University of Copenhagen = Københavns Universitet (UCPH), Universidad Nacional Autónoma de México = National Autonomous University of Mexico (UNAM), The Scripps Research Institute [La Jolla, San Diego], Fundação Oswaldo Cruz / Oswaldo Cruz Foundation (FIOCRUZ), Università degli Studi di Perugia = University of Perugia (UNIPG), Instituto de Investigacion Sanitaria del Hospital de la Princesa, Hospital Universitario de La Princesa, University of California [San Francisco] (UC San Francisco), University of California (UC)-University of California (UC), ANR-17-CE09-0025,MADNESS,Une approche microfluidique générique pour la qualification des nanoparticules biologiques(2017), Institut National de la Recherche Agronomique (INRA)-École pratique des hautes études (EPHE)-Université Claude Bernard Lyon 1 (UCBL), Biomedical Engineering and Physics, ACS - Atherosclerosis & ischemic syndromes, ACS - Microcirculation, Laboratory Specialized Diagnostics & Research, Radiotherapie, RS: GROW - R2 - Basic and Translational Cancer Biology, Université de Lille-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), Institut National de la Recherche Agronomique (INRA)-Université de Nantes (UN)-Ecole Nationale Vétérinaire, Agroalimentaire et de l'alimentation Nantes-Atlantique (ONIRIS), Université Nice Sophia Antipolis (... - 2019) (UNS), Université de Technologie de Belfort-Montbeliard (UTBM)-Ecole Nationale Supérieure de Mécanique et des Microtechniques (ENSMM)-Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC)-Centre National de la Recherche Scientifique (CNRS), Ecole Nationale Vétérinaire de Nantes-Université de Nantes (UN)-Institut National de la Recherche Agronomique (INRA), Università degli studi di Torino (UNITO), Universidade do Porto, University of Helsinki-University of Helsinki-Faculty of Medecine [Helsinki], University of Helsinki-University of Helsinki, Johannes Gutenberg - Universität Mainz (JGU), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-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 Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Institut Curie [Paris]-Université Pierre et Marie Curie - Paris 6 (UPMC), Hospices Civils de Lyon (HCL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Université de Lyon-Institut National des Sciences Appliquées (INSA)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Institut National de la Recherche Agronomique (INRA), Université de Toronto [Canada], Institut Curie-Institut National de la Santé et de la Recherche Médicale (INSERM), Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U1192 (PRISM), Université de Lille-Institut National de la Santé et de la Recherche Médicale (INSERM), Université Côte d'Azur (UCA)-Université Côte d'Azur (UCA)-Centre National de la Recherche Scientifique (CNRS), Université de Franche-Comté (UFC)-Centre National de la Recherche Scientifique (CNRS)-Ecole Nationale Supérieure de Mécanique et des Microtechniques (ENSMM)-Université de Technologie de Belfort-Montbeliard (UTBM), Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Physiopathologie de la Résorption Osseuse et Thérapie des Tumeurs Osseuses Primitives, Université de Nantes (UN)-Institut National de la Santé et de la Recherche Médicale (INSERM), Universidade do Porto [Porto], Ghent University [Belgium] (UGENT), FEMTO-ST Institute, Université de Technologie de Belfort-Montbeliard (UTBM)-Université de Franche-Comté (UFC)-CNRS : UMR6174, Mécanismes adaptatifs : des organismes aux communautés (MECADEV), Centre National de la Recherche Scientifique (CNRS)-Muséum national d'Histoire naturelle (MNHN), Johannes Gutenberg - University of Mainz (JGU), Université Catholique de Louvain (UCL), Universitat Pompeu Fabra [Barcelona], Laboratoire d'Informatique de Grenoble (LIG), Université Pierre Mendès France - Grenoble 2 (UPMF)-Université Joseph Fourier - Grenoble 1 (UJF)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP)-Institut National Polytechnique de Grenoble (INPG)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), Centre National de la Recherche Scientifique (CNRS)-Institut Curie-Université Pierre et Marie Curie - Paris 6 (UPMC), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Hospices Civils de Lyon (HCL), Laboratoire Réactions et Génie des Procédés (LRGP), Fiocruz Minas - René Rachou Research Center / Instituto René Rachou, 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), Functional Genomics Unit, Institut Curie-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), University of Vermont College of Medicine [Burlington, VT, USA], Extracellular Vesicles, Molecular and Integrative Biosciences Research Programme, Thery, C., Witwer, K. W., Aikawa, E., Alcaraz, M. J., Anderson, J. D., Andriantsitohaina, R., Antoniou, A., Arab, T., Archer, F., Atkin-Smith, G. K., Ayre, D. C., Bach, J. -M., Bachurski, D., Baharvand, H., Balaj, L., Baldacchino, S., Bauer, N. N., Baxter, A. A., Bebawy, M., Beckham, C., Bedina Zavec, A., Benmoussa, A., Berardi, A. C., Bergese, P., Bielska, E., Blenkiron, C., Bobis-Wozowicz, S., Boilard, E., Boireau, W., Bongiovanni, A., Borras, F. E., Bosch, S., Boulanger, C. M., Breakefield, X., Breglio, A. M., Brennan, M. A., Brigstock, D. R., Brisson, A., Broekman, M. L. D., Bromberg, J. F., Bryl-Gorecka, P., Buch, S., Buck, A. H., Burger, D., Busatto, S., Buschmann, D., Bussolati, B., Buzas, E. I., Byrd, J. B., Camussi, G., Carter, D. R. F., Caruso, S., Chamley, L. W., Chang, Y. -T., Chaudhuri, A. D., Chen, C., Chen, S., Cheng, L., Chin, A. R., Clayton, A., Clerici, S. P., Cocks, A., Cocucci, E., Coffey, R. J., Cordeiro-da-Silva, A., Couch, Y., Coumans, F. A. W., Coyle, B., Crescitelli, R., Criado, M. F., D'Souza-Schorey, C., Das, S., de Candia, P., De Santana, E. F., De Wever, O., del Portillo, H. A., Demaret, T., Deville, S., Devitt, A., Dhondt, B., Di Vizio, D., Dieterich, L. C., Dolo, V., Dominguez Rubio, A. P., Dominici, M., Dourado, M. R., Driedonks, T. A. P., Duarte, F. V., Duncan, H. M., Eichenberger, R. M., Ekstrom, K., EL Andaloussi, S., Elie-Caille, C., Erdbrugger, U., Falcon-Perez, J. M., Fatima, F., Fish, J. E., Flores-Bellver, M., Forsonits, A., Frelet-Barrand, A., Fricke, F., Fuhrmann, G., Gabrielsson, S., Gamez-Valero, A., Gardiner, C., Gartner, K., Gaudin, R., Gho, Y. S., Giebel, B., Gilbert, C., Gimona, M., Giusti, I., Goberdhan, D. C. I., Gorgens, A., Gorski, S. M., Greening, D. W., Gross, J. C., Gualerzi, A., Gupta, G. N., Gustafson, D., Handberg, A., Haraszti, R. A., Harrison, P., Hegyesi, H., Hendrix, A., Hill, A. F., Hochberg, F. H., Hoffmann, K. F., Holder, B., Holthofer, H., Hosseinkhani, B., Hu, G., Huang, Y., Huber, V., Hunt, S., Ibrahim, A. G. -E., Ikezu, T., Inal, J. M., Isin, M., Ivanova, A., Jackson, H. K., Jacobsen, S., Jay, S. M., Jayachandran, M., Jenster, G., Jiang, L., Johnson, S. M., Jones, J. C., Jong, A., Jovanovic-Talisman, T., Jung, S., Kalluri, R., Kano, S. -I., Kaur, S., Kawamura, Y., Keller, E. T., Khamari, D., Khomyakova, E., Khvorova, A., Kierulf, P., Kim, K. P., Kislinger, T., Klingeborn, M., Klinke, D. J., Kornek, M., Kosanovic, M. M., Kovacs, A. F., Kramer-Albers, E. -M., Krasemann, S., Krause, M., Kurochkin, I. V., Kusuma, G. D., Kuypers, S., Laitinen, S., Langevin, S. M., Languino, L. R., Lannigan, J., Lasser, C., Laurent, L. C., Lavieu, G., Lazaro-Ibanez, E., Le Lay, S., Lee, M. -S., Lee, Y. X. F., Lemos, D. S., Lenassi, M., Leszczynska, A., Li, I. T. S., Liao, K., Libregts, S. F., Ligeti, E., Lim, R., Lim, S. K., Line, A., Linnemannstons, K., Llorente, A., Lombard, C. A., Lorenowicz, M. J., Lorincz, A. M., Lotvall, J., Lovett, J., Lowry, M. C., Loyer, X., Lu, Q., Lukomska, B., Lunavat, T. R., Maas, S. L. N., Malhi, H., Marcilla, A., Mariani, J., Mariscal, J., Martens-Uzunova, E. S., Martin-Jaular, L., Martinez, M. C., Martins, V. R., Mathieu, M., Mathivanan, S., Maugeri, M., Mcginnis, L. K., Mcvey, M. J., Meckes, D. G., Meehan, K. L., Mertens, I., Minciacchi, V. R., Moller, A., Moller Jorgensen, M., Morales-Kastresana, A., Morhayim, J., Mullier, F., Muraca, M., Musante, L., Mussack, V., Muth, D. C., Myburgh, K. H., Najrana, T., Nawaz, M., Nazarenko, I., Nejsum, P., Neri, C., Neri, T., Nieuwland, R., Nimrichter, L., Nolan, J. P., Nolte-'t Hoen, E. N. M., Noren Hooten, N., O'Driscoll, L., O'Grady, T., O'Loghlen, A., Ochiya, T., Olivier, M., Ortiz, A., Ortiz, L. A., Osteikoetxea, X., Ostegaard, O., Ostrowski, M., Park, J., Pegtel, D. M., Peinado, H., Perut, F., Pfaffl, M. W., Phinney, D. G., Pieters, B. C. H., Pink, R. C., Pisetsky, D. S., Pogge von Strandmann, E., Polakovicova, I., Poon, I. K. H., Powell, B. H., Prada, I., Pulliam, L., Quesenberry, P., Radeghieri, A., Raffai, R. L., Raimondo, S., Rak, J., Ramirez, M. I., Raposo, G., Rayyan, M. S., Regev-Rudzki, N., Ricklefs, F. L., Robbins, P. D., Roberts, D. D., Rodrigues, S. C., Rohde, E., Rome, S., Rouschop, K. M. A., Rughetti, A., Russell, A. E., Saa, P., Sahoo, S., Salas-Huenuleo, E., Sanchez, C., Saugstad, J. A., Saul, M. J., Schiffelers, R. M., Schneider, R., Schoyen, T. H., Scott, A., Shahaj, E., Sharma, S., Shatnyeva, O., Shekari, F., Shelke, G. V., Shetty, A. K., Shiba, K., Siljander, P. R. -M., Silva, A. M., Skowronek, A., Snyder, O. L., Soares, R. P., Sodar, B. W., Soekmadji, C., Sotillo, J., Stahl, P. D., Stoorvogel, W., Stott, S. L., Strasser, E. F., Swift, S., Tahara, H., Tewari, M., Timms, K., Tiwari, S., Tixeira, R., Tkach, M., Toh, W. S., Tomasini, R., Torrecilhas, A. C., Tosar, J. P., Toxavidis, V., Urbanelli, L., Vader, P., van Balkom, B. W. M., van der Grein, S. G., Van Deun, J., van Herwijnen, M. J. C., Van Keuren-Jensen, K., van Niel, G., van Royen, M. E., van Wijnen, A. J., Vasconcelos, M. H., Vechetti, I. J., Veit, T. D., Vella, L. J., Velot, E., Verweij, F. J., Vestad, B., Vinas, J. L., Visnovitz, T., Vukman, K. V., Wahlgren, J., Watson, D. C., Wauben, M. H. M., Weaver, A., Webber, J. P., Weber, V., Wehman, A. M., Weiss, D. J., Welsh, J. A., Wendt, S., Wheelock, A. M., Wiener, Z., Witte, L., Wolfram, J., Xagorari, A., Xander, P., Xu, J., Yan, X., Yanez-Mo, M., Yin, H., Yuana, Y., Zappulli, V., Zarubova, J., Zekas, V., Zhang, J. -Y., Zhao, Z., Zheng, L., Zheutlin, A. R., Zickler, A. M., Zimmermann, P., Zivkovic, A. M., Zocco, D., Zuba-Surma, E. K., dB&C I&I, LS Celbiologie-Algemeen, Celbiologie, Afd Pharmaceutics, Sub General Pharmaceutics, Sub Biomol.Mass Spect. and Proteomics, Afd Pharmacology, CCA - Imaging and biomarkers, Amsterdam Neuroscience - Neuroinfection & -inflammation, and Amsterdam Neuroscience - Cellular & Molecular Mechanisms
Subjects: ectosome, ectosomes, exosomes, extracellular vesicles, guidelines, microparticles, microvesicles, minimal information requirements, reproducibility, rigor, standardization, Histology, Cell Biology, [SDV]Life Sciences [q-bio], size-exclusion, Medicine and Health Sciences, CELL-DERIVED MICROPARTICLES, FIELD-FLOW FRACTIONATION, requirements, circulating, ComputingMilieux_MISCELLANEOUS, Manchester Cancer Research Centre, lcsh:Cytology, PROSTATE-CANCER, microparticle, Cell interaction, microvesicle, chromatography, Position Paper, guideline, Life Sciences & Biomedicine, ectosomes, exosomes, extracellular vesicles, guidelines, microparticles, microvesicles, minimal information requirements, reproducibility, rigor, standardization, MEMBRANE-VESICLES, FETAL BOVINE, Ectosomes, Exosomes, Extracellular Vesicles, Guidelines, Microparticles, Microvesicles, Minimal Information Requirements, Reproducibility, Rigor, Standardization, CIRCULATING MICROPARTICLES, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, ddc:570, exosome, SURFACE-PLASMON RESONANCE, ddc:610, lcsh:QH573-671, Biology, Interacció cel·lular, Science & Technology, ResearchInstitutes_Networks_Beacons/mcrc, Cell membranes, HUMAN URINARY EXOSOMES, PREANALYTICAL PARAMETERS, minimal information requirement, SIZE-EXCLUSION CHROMATOGRAPHY, 1182 Biochemistry, cell and molecular biology, extracellular vesicle, Human medicine, Membranes cel·lulars
Abstract: The last decade has seen a sharp increase in the number of scientific publications describing physiological and pathological functions of extracellular vesicles (EVs), a collective term covering various subtypes of cell-released, membranous structures, called exosomes, microvesicles, microparticles, ectosomes, oncosomes, apoptotic bodies, and many other names. However, specific issues arise when working with these entities, whose size and amount often make them difficult to obtain as relatively pure preparations, and to characterize properly. The International Society for Extracellular Vesicles (ISEV) proposed Minimal Information for Studies of Extracellular Vesicles ("MISEV") guidelines for the field in 2014. We now update these "MISEV2014" guidelines based on evolution of the collective knowledge in the last four years. An important point to consider is that ascribing a specific function to EVs in general, or to subtypes of EVs, requires reporting of specific information beyond mere description of function in a crude, potentially contaminated, and heterogeneous preparation. For example, claims that exosomes are endowed with exquisite and specific activities remain difficult to support experimentally, given our still limited knowledge of their specific molecular machineries of biogenesis and release, as compared with other biophysically similar EVs. The MISEV2018 guidelines include tables and outlines of suggested protocols and steps to follow to document specific EV-associated functional activities. Finally, a checklist is provided with summaries of key points.
Published: 2018

9. Two novel, putative mechanisms of action for citalopram-induced platelet inhibition

Author: Roweth, Harvey G, Cook, Aaron A, Moroi, Masaaki, Bonna, Arkadiusz M, Jung, Stephanie M, Bergmeier, Wolfgang, Sage, Stewart O, Jarvis, Gavin E, Bonna, Arkadiusz M [0000-0002-3957-7849], Jarvis, Gavin E [0000-0003-4362-1133], Apollo - University of Cambridge Repository, and Jarvis, Gavin E.
Subjects: sub_pharmacyandpharmacology, L-Lactate Dehydrogenase, Platelet Aggregation, Neutrophils, lcsh:R, lcsh:Medicine, Platelet Membrane Glycoproteins, Citalopram, behavioral disciplines and activities, Models, Biological, Article, Cytosol, 15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid, mental disorders, Humans, lcsh:Q, Calcium, lcsh:Science, sub_biomedicalsciences, Platelet Aggregation Inhibitors
Abstract: Citalopram, a selective serotonin reuptake inhibitor (SSRI), inhibits platelet function in vitro. We have previously shown that this action is independent of citalopram’s ability to block serotonin uptake by the serotonin transporter and must therefore be mediated via distinct pharmacological mechanisms. We now report evidence for two novel and putative mechanisms of citalopram-induced platelet inhibition. Firstly, in platelets, citalopram blocked U46619-induced Rap1 activation and subsequent platelet aggregation, but failed to inhibit U46619-induced increases in cytosolic Ca2+. Similarly, in neutrophils, citalopram inhibited Rap1 activation and downstream functions but failed to block PAF-induced Ca2+ mobilisation. In a cell-free system, citalopram also reduced CalDAG-GEFI-mediated nucleotide exchange on Rap1B. Secondly, the binding of anti-GPVI antibodies to resting platelets was inhibited by citalopram. Furthermore, citalopram-induced inhibition of GPVI-mediated platelet aggregation was instantaneous, reversible and displayed competitive characteristics, suggesting that these effects were not caused by a reduction in GPVI surface expression, but by simple competitive binding. In conclusion, we propose two novel, putative and distinct inhibitory mechanisms of action for citalopram: (1) inhibition of CalDAG-GEFI/Rap1 signalling, and (2) competitive antagonism of GPVI in platelets. These findings may aid in the development of novel inhibitors of CalDAG-GEFI/Rap1-dependent nucleotide exchange and novel GPVI antagonists.
Published: 2018

10. Differential Inhibition of Human Atherosclerotic Plaque–Induced Platelet Activation by Dimeric GPVI-Fc and Anti-GPVI Antibodies

Author: Jamasbi, Janina, Megens, Remco T.A., Bianchini, Mariaelvy, Münch, Götz, Ungerer, Martin, Faussner, Alexander, Sherman, Shachar, Walker, Adam, Goyal, Pankaj, Jung, Stephanie, Brandl, Richard, Weber, Christian, Lorenz, Reinhard, Farndale, Richard, Elia, Natalie, and Siess, Wolfgang
Subjects: Cardiology and Cardiovascular Medicine
Published: 2015
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11. Beyond antiplatelets: The role of glycoprotein VI in ischemic stroke

Author: Induruwa, Isuru, Jung, Stephanie M, Warburton, Elizabeth A, Induruwa, Isuru [0000-0002-7020-8179], and Apollo - University of Cambridge Repository
Subjects: Stroke, glycoprotein VI, Blood Platelets, platelets, Animals, Humans, antiplatelets, Collagen, Platelet Membrane Glycoproteins, Platelet Aggregation Inhibitors, Brain Ischemia
Abstract: BACKGROUND: Platelets are essential to physiological hemostasis or pathological thrombus formation. Current antiplatelet agents inhibit platelet aggregation but leave patients at risk of systemic side-effects such as hemorrhage. Newer therapeutic strategies could involve targeting this cascade earlier during platelet adhesion or activation via inhibitory effects on specific glycoproteins, the thrombogenic collagen receptors found on the platelet surface. AIMS: Glycoprotein VI (GPVI) is increasingly being recognized as the main platelet-collagen receptor involved in arterial thrombosis. This review summarizes the crucial role GPVI plays in ischemic stroke as well as the current strategies used to attempt to inhibit its activity. SUMMARY OF REVIEW: In this review, we discuss the normal hemostatic process, and the role GPVI plays at sites of atherosclerotic plaque rupture. We discuss how the unique structure of GPVI allows for its interaction with collagen and creates downstream signaling that leads to thrombus formation. We summarize the current strategies used to inhibit GPVI activity and how this could translate to a clinically viable entity that may compete with current antiplatelet therapy. CONCLUSION: From animal models, it is clear that GPVI inhibition leads to an abolished platelet response to collagen and reduced platelet aggregation, culminating in smaller arterial thrombi. There is now an increasing body of evidence that these findings can be translated into the development of a bleeding free pharmacological entity specific to sites of plaque rupture in humans.
Published: 2016
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12. Differential Inhibition of Human Atherosclerotic Plaque-Induced Platelet Activation by Dimeric GPVI-Fc and Anti-GPVI Antibodies: Functional and Imaging Studies

Author: Jamasbi, Janina, Megens, Remco T. A., Bianchini, Mariaelvy, Muench, Goetz, Ungerer, Martin, Faussner, Alexander, Sherman, Shachar, Walker, Adam, Goyal, Pankaj, Jung, Stephanie, Brandl, Richard, Weber, Christian, Lorenz, Reinhard, Farndale, Richard, Elia, Natalie, Siess, Wolfgang, Farndale, Richard [0000-0001-6130-8808], Apollo - University of Cambridge Repository, Fysiologie, Biochemie, RS: CARIM - R1 - Thrombosis and haemostasis, RS: CARIM - R3 - Vascular biology, Biomedische Technologie, and Pathologie
Subjects: plaque rupture, Platelet Membrane Glycoproteins, antithrombotic, Platelet Activation, Plaque, Atherosclerotic, Rats, glycoprotein VI, Immunoglobulin Fab Fragments, Carotid Arteries, atherothrombosis, Animals, Humans, Immunologic Factors, Carotid Stenosis, Blood Flow Velocity
Abstract: BACKGROUND: Glycoprotein VI (GPVI) is the essential platelet collagen receptor in atherothrombosis, but its inhibition causes only a mild bleeding tendency. Thus, targeting this receptor has selective antithrombotic potential. OBJECTIVES: This study sought to compare compounds interfering with platelet GPVI-atherosclerotic plaque interaction to improve current antiatherothrombotic therapy. METHODS: Human atherosclerotic plaque-induced platelet aggregation was measured in anticoagulated blood under static and arterial flow conditions (550/s, 1,100/s, and 1,500/s). Inhibition by dimeric GPVI fragment crystallizable region of IgG (Fc) masking GPVI binding sites on collagen was compared with that of 3 anti-GPVI antibodies: BLO8-1, a human domain antibody; 5C4, a fragment antigen-binding (Fab fragment) of monoclonal rat immunoglobulin G; and m-Fab-F, a human recombinant sFab against GPVI dimers. RESULTS: GPVI-Fc reduced plaque-triggered platelet aggregation in static blood by 51%, BLO8-1 by 88%, and 5C4 by 93%. Under arterial flow conditions, BLO8-1 and 5C4 almost completely inhibited platelet aggregation while preserving platelet adhesion on plaque. Inhibition by GPVI-Fc, even at high concentrations, was less marked but increased with shear rate. Advanced optical imaging revealed rapid persistent GPVI-Fc binding to collagen under low and high shear flow, upstream and downstream of plaque fragments. At low shear particularly, platelets adhered in plaque flow niches to GPVI-Fc-free segments of collagen fibers and recruited other platelets onto aggregates via ADP and TxA2 release. CONCLUSIONS: Anti-GPVI antibodies inhibit atherosclerotic plaque-induced platelet aggregation under static and flow conditions more effectively than GPVI-Fc. However, potent platelet inhibition by GPVI-Fc at a higher shear rate (1,500/s) suggests localized antithrombotic efficacy at denuded or fissured stenotic high-risk lesions without systemic bleeding. The compound-specific differences have relevance for clinical trials targeting GPVI-collagen interaction combined with established antiplatelet therapies in patients with spontaneous plaque rupture or intervention-associated plaque injury.
Published: 2015

13. Immunerkennung endogener RNA-Liganden

Author: Jung, Stephanie and Bauer, Stefan (Prof. Dr.)
Subjects: Medical sciences, Medicine -- Medizin, Gesundheit, ITS2, modification, Modifikationen, RNase L, RIG I, 45S rRNA, RNase A, TLR8, 2014, ddc:610
Abstract: Das angeborene Immunsystem verfügt über eine Vielzahl keimbahnkodierter Rezeptoren, die pathogenspezifische Muster erkennen und so eine Immunantwort auslösen können. Verantwortlich für die Detektion doppelsträngiger RNA im Zytoplasma ist die Familie der RIG I ähnlichen Rezeptoren, zu der u.a. RIG I und MDA5 gehören; im Endosomen wird doppel- und einzelsträngige RNA durch die Toll-ähnlichen Rezeptoren („Toll like receptors“, TLRs) 3, 7 und 8 erkannt. Diese Rezeptoren können unter physiologischen Bedingungen anhand von Struktur und Modifikationen zwischen zelleigener und zellfremder RNA unterscheiden, unter pathologischen Bedingungen kann es aber auch zu einer Erkennung körpereigener RNA kommen. Der Hauptteil dieser Arbeit beschäftigt sich mit der Erkennung zelleigener RNA im Zytoplasma. Während einer Virusinfektion kann doppelsträngige virale RNA nicht nur direkt durch die RIG I ähnlichen Rezeptoren erkannt werden, sondern auch indirekt über 2‘5‘ Oligoadenylat-aktivierte RNase L aktivieren. Dies führt zum Schneiden zelleigener RNA, wobei die gebildeten Fragmente wiederum von keimbahn-kodierten Rezeptoren erkannt werden. Diese Verstärkung des Gefahrensignals nimmt eine grundlegende Rolle in der Virusabwehr ein. Im Rahmen dieser Arbeit konnte gezeigt werden, dass die Erkennung zelleigener RNase-generierter RNA-Fragmente ausschließlich über RIG I verläuft. Die Existenz spezifischer endogener RIG I Liganden wurde belegt und die Sequenzen der betreffenden Fragmente wurden mittels Next Generation Sequencing ermittelt. Hierbei handelt es sich um Strukturen aus der 28S rRNA und der ITS2, einem Prozessierungsprodukt der 45S rRNA. Der spezifische RIG I aktivierende Effekt dieser Sequenzen konnte in verschiedenen Stimulationsexperimenten nachgewiesen werden. Interessanterweise tragen die endogenen stimulatorischen RNA-Spezies im Gegensatz zum Prototyp eines RIG I Liganden kein 5' Triphosphat, sondern ein 3' Monophosphat, auch weisen sie keine typische Basenzusammensetzung mit hohem Uridingehalt auf. Stattdessen werden die außergewöhnlich GC-reichen Sequenzen vermutlich aufgrund ihrer Doppelsträngigkeit und einer Ringstruktur nahe der Schnittstelle von RIG I erkannt. Die besondere Bedeutung dieser Sequenzen wird durch die evolutionäre Konservierung dieser Strukturen belegt, auch könnten sie nicht nur eine Funktion in der Virusabwehr, sondern auch als Tumorsupressor haben. Die intrazelluläre Generierung immunstimulatorischer RNA-Spezies erfolgt nicht nur über die virusinduzierte RNase L, sondern auch über eine artifiziell in die Zelle transfizierte RNase A. Dies eröffnet die Möglichkeit zur Etablierung von RNase A als neue Adjuvansspezies. Im zweiten Teil dieser Arbeit wurde untersucht, welchen Einfluss verschiedene Modifikationen des 18S rRNA Abkömmlings RNA63 auf dessen Erkennung durch die endosomalen TLRs 7 und 8 haben. Eine nichtmodifizierte RNA63 und solche mit einer 2'-O-Deoxy- oder Fluorgruppe werden sowohl durch TLR7 als auch durch TLR8 erkannt. Durch eine 2'-O-Methylierung allerdings lässt sich die Erkennung der RNA63 durch TLR7 hemmen, nicht aber die Erkennung durch TLR8. Somit handelt es sich bei 2'-methylierter RNA63 um einen spezifischen TLR8-aktivierenden Liganden.
Published: 2014

14. Japan Series

Author: Jung, Stephanie
Subjects: Japan, Vision, Urban Landscape, Japón, City, Photography, Visión, Ciudad, Paisaje Urbano, Fotografía
Abstract: My work now mainly is inspired by life itself, by walking through cities and watching life. Another huge inspiration is simply music. Sometimes when I walk around to take pictures, I listen to my current favorite songs, they create the mood I need to get new ideas. But I’m also looking at several art blogs or communities, to see what other artists are doing, that’s really important! Not to copy any style, but to see what’s possible and to use it as a motivation to create new work. ResumenMi trabajo está mayormente inspirado en la vida misma, camino por las ciudades admirando su vida.Otra gran inspiración es música. A veces cuando camino para tomar fotografías, escucho mis canciones favoritas, crean el ambiente necesario para que las ideas fluyan. Pero también busco inspiración en varios blogs de arte o comunidades, para ver que hacen otros artistas, esto es muy importante para mí. No con el fin de copiar estilos, pero sí para observar lo que es posible y cómo utilizarlo como motivación para mi propio trabajo.
Published: 2014

15. Immunerkennung endogener RNA-Liganden

Author: Jung, Stephanie
Subjects: Modifikationen, modification, RIG I, ITS2, 45S rRNA, RNase A, RNase L, Medizin, Gesundheit, TLR8
Abstract: Innate immunity has evolved different pattern recognition receptors to detect pathogen associated molecular patterns (PAMPs) and to elicit an immune response. Whereas double stranded RNA in the cytoplasm is detected by RIG I and MDA5, double- and single stranded RNA in the endosome is recognized by Toll like Receptors (TLRs) 3, 7 and 8. Under physiological conditions, these receptors discriminate between foreign and self RNA based on certain structures and modification patters. Under pathological conditons, these receptors can also recognize self RNA. The major part of this thesis deals with the detection of self RNA as a potential danger signal in the cytoplasm. In the case of viral infection, in addition to the activation of RIG I and MDA5, double stranded RNA also leads to the activation of RNase L. Subsequently, cellular RNA is digested and fragments bound to pattern recognition receptors, which results in an amplification of the danger signal. In this thesis, it could be shown that the fragments of self-RNA are exclusively recognized by RIG I. It was proven that this RIG I activation is not a common effect of digested RNA but caused by specific RNA structures. The sequences of these molecules were obtained by Next Generation Sequencing. The endogenous RIG I ligands are derived from expansion segments in the 28S rRNA and from ITS2, a processing product of the 45S rRNA. Their specific RIG I activating effect could be shown in different immunostimulation experiments. Unlike the common model of an ultimate RIG I ligand, they do not bear a 5’ triphosphate but a 3’ monophosphate and are not rich in uridine but in guanosine and cytosine. Instead, the endogenous RIG I ligands seem to be detected due to their double-strandness and a certain loop structure. Involvement of ITS2 indicates a further link not only between antiviral response and RNase L but also between RNase L, rRNA biogenesis and cancer development. Generation of immunostimulatory RNA species is not only limited to virus induced RNase L but can also be obtained by artificial transfection of RNase A into a cell. Consequently, RNase A might be established as a novel species of adjuvant. In the second part of this thesis, the impact of modifications on the TLR7 and 8 mediated recognition of 18S rRNA derived RNA63 was analysed. Unmodified RNA63 and RNA63 bearing a 2’-O-deoxy or 2’-O-fluor modification all activate TLR7 and TLR8 while 2’-O-methylation inhibits TLR7 depended signaling and is solely detected by TLR8. This is why TLR8 activation is more resistent to RNA-modifications than TLR7activation. Consequently, 2’-O-methylated RNA63 is a specific TLR8 ligand., Das angeborene Immunsystem verfügt über eine Vielzahl keimbahnkodierter Rezeptoren, die pathogenspezifische Muster erkennen und so eine Immunantwort auslösen können. Verantwortlich für die Detektion doppelsträngiger RNA im Zytoplasma ist die Familie der RIG I ähnlichen Rezeptoren, zu der u.a. RIG I und MDA5 gehören; im Endosomen wird doppel- und einzelsträngige RNA durch die Toll-ähnlichen Rezeptoren („Toll like receptors“, TLRs) 3, 7 und 8 erkannt. Diese Rezeptoren können unter physiologischen Bedingungen anhand von Struktur und Modifikationen zwischen zelleigener und zellfremder RNA unterscheiden, unter pathologischen Bedingungen kann es aber auch zu einer Erkennung körpereigener RNA kommen. Der Hauptteil dieser Arbeit beschäftigt sich mit der Erkennung zelleigener RNA im Zytoplasma. Während einer Virusinfektion kann doppelsträngige virale RNA nicht nur direkt durch die RIG I ähnlichen Rezeptoren erkannt werden, sondern auch indirekt über 2‘5‘ Oligoadenylat-aktivierte RNase L aktivieren. Dies führt zum Schneiden zelleigener RNA, wobei die gebildeten Fragmente wiederum von keimbahn-kodierten Rezeptoren erkannt werden. Diese Verstärkung des Gefahrensignals nimmt eine grundlegende Rolle in der Virusabwehr ein. Im Rahmen dieser Arbeit konnte gezeigt werden, dass die Erkennung zelleigener RNase-generierter RNA-Fragmente ausschließlich über RIG I verläuft. Die Existenz spezifischer endogener RIG I Liganden wurde belegt und die Sequenzen der betreffenden Fragmente wurden mittels Next Generation Sequencing ermittelt. Hierbei handelt es sich um Strukturen aus der 28S rRNA und der ITS2, einem Prozessierungsprodukt der 45S rRNA. Der spezifische RIG I aktivierende Effekt dieser Sequenzen konnte in verschiedenen Stimulationsexperimenten nachgewiesen werden. Interessanterweise tragen die endogenen stimulatorischen RNA-Spezies im Gegensatz zum Prototyp eines RIG I Liganden kein 5' Triphosphat, sondern ein 3' Monophosphat, auch weisen sie keine typische Basenzusammensetzung mit hohem Uridingehalt auf. Stattdessen werden die außergewöhnlich GC-reichen Sequenzen vermutlich aufgrund ihrer Doppelsträngigkeit und einer Ringstruktur nahe der Schnittstelle von RIG I erkannt. Die besondere Bedeutung dieser Sequenzen wird durch die evolutionäre Konservierung dieser Strukturen belegt, auch könnten sie nicht nur eine Funktion in der Virusabwehr, sondern auch als Tumorsupressor haben. Die intrazelluläre Generierung immunstimulatorischer RNA-Spezies erfolgt nicht nur über die virusinduzierte RNase L, sondern auch über eine artifiziell in die Zelle transfizierte RNase A. Dies eröffnet die Möglichkeit zur Etablierung von RNase A als neue Adjuvansspezies. Im zweiten Teil dieser Arbeit wurde untersucht, welchen Einfluss verschiedene Modifikationen des 18S rRNA Abkömmlings RNA63 auf dessen Erkennung durch die endosomalen TLRs 7 und 8 haben. Eine nichtmodifizierte RNA63 und solche mit einer 2'-O-Deoxy- oder Fluorgruppe werden sowohl durch TLR7 als auch durch TLR8 erkannt. Durch eine 2'-O-Methylierung allerdings lässt sich die Erkennung der RNA63 durch TLR7 hemmen, nicht aber die Erkennung durch TLR8. Somit handelt es sich bei 2'-methylierter RNA63 um einen spezifischen TLR8-aktivierenden Liganden.
Published: 2014
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16. Microchip HPLC: Experimental investigation of separation efficiency, column characteristics, and coupling with mass spectrometry

Author: Jung, Stephanie and Tallarek, Ulrich (Prof. Dr.)
Subjects: ddc:540, Chemistry and allied sciences -- Chemie, Chromatographie, Porosität, Lab-on-a-chip, Electrospray ionisation, Lab on a Chip, Microchip, Elektrospray-Ionisation, Chromatogaphy, Chip, Porosity, 2012
Abstract: Die vorliegende Arbeit beschäftigt sich mit verschiedenen Aspekten, welche die chromatographische Effizienz in der miniaturisierten HPLC beeinflussen. Der Einfluss der Kanalgeometrie auf die chromatographische Effizienz von gepackten Mikrochipkanälen wurde untersucht. Es wurden HPLC/UV Mikrochips mit Trennkanälen von quadratischem, trapezoidalen und gaußförmigen Querschnitt eingesetzt. Die Mikrochips wurden Laserablation und Lamination der Polyimidfolien hergestellt. Als Packungsmaterialien wurden 3 oder 5 µm-große sphärische C8-Kieselgelpartikel verwendet und unter optimierten Bedingungen in den Trennkanal gepackt. Die Dispersionseigenschaften der ungepackten Trennkanäle wurden vermessen und mit berechneten Daten der axialen Dispersionseigenschaften von Zylindern verglichen. Packungsdichten und Bodenhöhen der verschiedenen gepackten Betten werden miteinander verglichen und deren Unterschiede erklärt. Die Packungen der 3 µm Partikel reflektieren das Dispersionsverhalten der Leerkanäle. Die Dispersion in den 5 µm Packungen korreliert mit den erhaltenen Packungsdichten, die wiederum durch die Anzahl und die Erreichbarkeit der Ecken in den jeweiligen Kanalquerschnitten limitiert sind. Interpartikuläre Porositäten und Zwischenkornvolumina von gepackten Kapillarsäulen und kommerziell erhältlichen analytischen Umkehrphasensäulen wurden mittels intrapartikulärem Donnan-Ausschluss einer kleinen, nicht-retardierten und ko-ionischen Verbindung (Nitrationen) bestimmt. Die Anwendbarkeit der Methode wurde für Kieselgel, Umkehrphasen- und Kationenaustauschermaterialien mit unterschiedlichen Partikelgrößen, Porendurchmessern und Partikelkonstruktion (vollporös und core-shell) in Abhängigkeit der Ionenstärke der mobilen Phase untersucht. Die Nitrationen werden bei niedrigen Pufferkonzentrationen vollständig von dem intrapartikulären Porenraum der Partikel ausgeschlossen, deutlich sichtbar durch eine Plateauregion, in welche die Elutionsvolumina der Nitrationen laufen. Für die kommerziellen HPLC-Säulen wurden deutliche Plateauregionen beobachtet, sogar im Falle von sehr dicht gepackten core-shell und 1,8 µm Partikeln. Dies zeigt, dass die Donnan-Ausschlussmethode sehr gut geeignet ist, die interpartikulären Porositäten schnell und einfach bis auf die dritte Nachkommastelle zu bestimmen. Die erhaltenen interpartikulären Porositäten stimmen mit den Werten der inversen Größenausschlussmethode gut überein. Einschränkungen in der Anwendbarkeit treten erst auf, wenn der Donnan-Ausschluss (elektrostatischer Ausschluss) oder der mechanische Ausschluss der inversen Größenausschlusschromatographie auch im Zwischenkornraum der gepackten Betten auftreten. Dies ist der Fall für sehr kleine, hochgeladene Partikel oder sehr großen Porendurchmessern. Graduelle Änderungen in der Zusammensetzung der mobilen Phase während einer Gradientenelution beeinflusst die Elektrosprayionisation bei direkter Kopplung mit einem Massenspektrometer. Der Einfluss der Eluentzusammensetzung auf den Elektrospraymodus und die damit einhergehenden Änderungen der Spraystabilität und des MS-Signals werden mittels Infusions- und Injektionsexperimenten untersucht. Die verwendete HPLC/ESI-MS Konfiguration bestand aus einem Mikrochip mit Anreicherungssäule, Trennkanal und Make-up Flusskanal. Eine Nanopumpe wurde an den Trennkanal angeschlossen, eine zweite bediente den Make-up Flusskanal mit einem inversen Lösungmittelgradienten. Die beiden Lösungsmittelströme wurden vor der Elektrosprayspitze zusammengeführt, so dass an der Elektrosprayspitze eine identische Eluentzusammensetzung über den gesamten Gradientenlauf vorlag. Signalparameter eines Analyten wurden mit und ohne Kompensation über den Make-up Fluss aufgezeichnet und mit der Spraystabilität und dem jeweiligen Elektrospraymodus korreliert. Die Anwendung des post-column Make-up Flusses verbesserte die Spray- und Signalstabilität erheblich, ohne die chromatographische Effizienz zu beeinträchtigen.
Published: 2012

17. Microchip HPLC: Experimental investigation of separation efficiency, column characteristics, and coupling with mass spectrometry

Author: Jung, Stephanie
Subjects: Elektrospray-Ionisation, Chromatogaphy, Lab-on-a-chip, Chromatographie, Porosität, Microchip, Chip, Chemie, Electrospray ionisation, Lab on a Chip, Porosity
Abstract: Die vorliegende Arbeit beschäftigt sich mit verschiedenen Aspekten, welche die chromatographische Effizienz in der miniaturisierten HPLC beeinflussen. Der Einfluss der Kanalgeometrie auf die chromatographische Effizienz von gepackten Mikrochipkanälen wurde untersucht. Es wurden HPLC/UV Mikrochips mit Trennkanälen von quadratischem, trapezoidalen und gaußförmigen Querschnitt eingesetzt. Die Mikrochips wurden Laserablation und Lamination der Polyimidfolien hergestellt. Als Packungsmaterialien wurden 3 oder 5 µm-große sphärische C8-Kieselgelpartikel verwendet und unter optimierten Bedingungen in den Trennkanal gepackt. Die Dispersionseigenschaften der ungepackten Trennkanäle wurden vermessen und mit berechneten Daten der axialen Dispersionseigenschaften von Zylindern verglichen. Packungsdichten und Bodenhöhen der verschiedenen gepackten Betten werden miteinander verglichen und deren Unterschiede erklärt. Die Packungen der 3 µm Partikel reflektieren das Dispersionsverhalten der Leerkanäle. Die Dispersion in den 5 µm Packungen korreliert mit den erhaltenen Packungsdichten, die wiederum durch die Anzahl und die Erreichbarkeit der Ecken in den jeweiligen Kanalquerschnitten limitiert sind. Interpartikuläre Porositäten und Zwischenkornvolumina von gepackten Kapillarsäulen und kommerziell erhältlichen analytischen Umkehrphasensäulen wurden mittels intrapartikulärem Donnan-Ausschluss einer kleinen, nicht-retardierten und ko-ionischen Verbindung (Nitrationen) bestimmt. Die Anwendbarkeit der Methode wurde für Kieselgel, Umkehrphasen- und Kationenaustauschermaterialien mit unterschiedlichen Partikelgrößen, Porendurchmessern und Partikelkonstruktion (vollporös und core-shell) in Abhängigkeit der Ionenstärke der mobilen Phase untersucht. Die Nitrationen werden bei niedrigen Pufferkonzentrationen vollständig von dem intrapartikulären Porenraum der Partikel ausgeschlossen, deutlich sichtbar durch eine Plateauregion, in welche die Elutionsvolumina der Nitrationen laufen. Für die kommerziellen HPLC-Säulen wurden deutliche Plateauregionen beobachtet, sogar im Falle von sehr dicht gepackten core-shell und 1,8 µm Partikeln. Dies zeigt, dass die Donnan-Ausschlussmethode sehr gut geeignet ist, die interpartikulären Porositäten schnell und einfach bis auf die dritte Nachkommastelle zu bestimmen. Die erhaltenen interpartikulären Porositäten stimmen mit den Werten der inversen Größenausschlussmethode gut überein. Einschränkungen in der Anwendbarkeit treten erst auf, wenn der Donnan-Ausschluss (elektrostatischer Ausschluss) oder der mechanische Ausschluss der inversen Größenausschlusschromatographie auch im Zwischenkornraum der gepackten Betten auftreten. Dies ist der Fall für sehr kleine, hochgeladene Partikel oder sehr großen Porendurchmessern. Graduelle Änderungen in der Zusammensetzung der mobilen Phase während einer Gradientenelution beeinflusst die Elektrosprayionisation bei direkter Kopplung mit einem Massenspektrometer. Der Einfluss der Eluentzusammensetzung auf den Elektrospraymodus und die damit einhergehenden Änderungen der Spraystabilität und des MS-Signals werden mittels Infusions- und Injektionsexperimenten untersucht. Die verwendete HPLC/ESI-MS Konfiguration bestand aus einem Mikrochip mit Anreicherungssäule, Trennkanal und Make-up Flusskanal. Eine Nanopumpe wurde an den Trennkanal angeschlossen, eine zweite bediente den Make-up Flusskanal mit einem inversen Lösungmittelgradienten. Die beiden Lösungsmittelströme wurden vor der Elektrosprayspitze zusammengeführt, so dass an der Elektrosprayspitze eine identische Eluentzusammensetzung über den gesamten Gradientenlauf vorlag. Signalparameter eines Analyten wurden mit und ohne Kompensation über den Make-up Fluss aufgezeichnet und mit der Spraystabilität und dem jeweiligen Elektrospraymodus korreliert. Die Anwendung des post-column Make-up Flusses verbesserte die Spray- und Signalstabilität erheblich, ohne die chromatographische Effizienz zu beeinträchtigen., This work deals with separation efficiency and column characteristics of particle-packed HPLC microchips. The impact of conduit geometry on the chromatographic performance of typical particulate microchip packings is investigated. For this purpose, HPLC/UV-microchips with separation channels of quadratic, trapezoidal, or Gaussian cross-section were fabricated by direct laser ablation and lamination of multiple polyimide layers and then slurry-packed with either 3 or 5 µm spherical porous C8-silica particles under optimized packing conditions. Experimentally determined plate height curves for the empty microchannels are compared with dispersion coefficients from theoretical calculations. Packing densities and plate height curves for the various microchip packings are presented and conclusively explained. 3 µm packings display a high packing density irrespective of their conduit geometries and their performance reflects the dispersion behaviour of the empty channels. Dispersion in 5 µm packings correlates with the achieved packing densities, which are limited by the number and accessibility of corners in a given conduit shape. Interparticle void volumes and porosities of packed capillaries and of commercially available, analytical, reversed-phase HPLC columns have been determined using intraparticle Donnan exclusion of a small, unretained, co-ionic tracer (nitrate ions). The operational domain of this approach has been characterized for bare silica, reversed-phase, and strong cation-exchange materials with different particle sizes, intraparticle pore sizes, and construction (fully porous or core-shell) in dependence of the mobile phase ionic strength. At low buffer concentrations nitrate ions are completely electrostatically excluded from the intraparticle mesopore space, which is reflected by a plateau region in the elution curves. The elution volume in the plateau region equals the interparticle void volume. Clearly defined plateau regions were observed for all columns, even those densely packed with core-shell and sub-2 µm particles, enabling the accurate determination of interparticle porosities to three decimal places in a fast and convenient way. Interparticle porosities agree well with those analyzed by inverse size-exclusion chromatography (ISEC). Limitations to the use of Donnan exclusion (electrostatic exclusion) and ISEC (mechanical exclusion) arise as either type of exclusion becomes noticeable also in the cusp regions between particles, or as the intraparticle pores are so large that complete electrostatic and size exclusion are difficult to realize. Dynamic changes in mobile phase composition during high performance liquid chromatography (HPLC) gradient elution coupled to mass spectrometry (MS) sensitively affect electrospray modes. The impact of the eluent composition on spray stability and MS response by infusion and injection experiments with a small tetrapeptide in water-acetonitrile mixtures was investigated. The employed HPLC/ESI-MS configuration uses a microchip equipped with enrichment column, separation column, and make-up flow (MUF) channel. One nano pump is connected to the separation column, while a second one delivers solvent of exactly inverted composition to the MUF channel. Both solvent streams are united behind the separation column, before the ESI tip, such that the resulting electrosprayed solution always has identical composition during a gradient elution. Analyte peak parameters without and with MUF compensation are determined and discussed with respect to the electrospray mode and eluent composition. The post-column MUF significantly improves spray and signal stability over the entire solvent gradient, without compromising the performance of the HPLC separation column. It can also be conveniently implemented on microchip platforms.
Published: 2012
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18. Expanding the UBC Farm Market

Author: Bishop, Breanna, Drescher, Alana, Jung, Stephanie, Lee, Jason, Liu, Winnie (Wan-Ju), Snow, Diana, and Wedemire, Courtney
Abstract: Currently, costs at the UBC Farm exceed revenues with the deficit being met with grant money deeming the Farm unsustainable. To amend this, the UBC Farm is exploring the option of expanding the current Farm Market to a larger multi-vendor market. This option could generate additional income for the farm and help meet consumer demand. After conversing with representatives, creating and analyzing surveys for stakeholders, examining relevant policies, and investigating research papers from previous years, it was realized that there is an ample consumer base to encourage the expansion of the UBC Farm Market provided the market expand their product selection to include other products with a preference for those locally grown. The vendors who were surveyed indicated that they could provide the desired products, but many have difficulty overcoming barriers such as time constraints and labour requirements. Addressing these issues would likely increase vendor participation, and in turn, increase market popularity and consumer traffic. With time and consistent effort, the UBC Farm Market can aid in turning the UBC Farm into a sustainable and viable project at UBC. Disclaimer: “UBC SEEDS provides students with the opportunity to share the findings of their studies, as well as their opinions, conclusions and recommendations with the UBC community. The reader should bear in mind that this is a student project/report and is not an official document of UBC. Furthermore readers should bear in mind that these reports may not reflect the current status of activities at UBC. We urge you to contact the research persons mentioned in a report or the SEEDS Coordinator about the current status of the subject matter of a project/report.”
Published: 2007
Full Text: View/download PDF

19. Minimal information for studies of extracellular vesicles 2018 (MISEV2018): a position statement of the International Society for Extracellular Vesicles and update of the MISEV2014 guidelines

Author: Théry, Clotilde, Witwer, Kenneth W., Aikawa, Elena, Alcaraz, Maria Jose, Anderson, Johnathon D., Andriantsitohaina, Ramaroson, Antoniou, Anna, Arab, Tanina, Archer, Fabienne, Atkin-Smith, Georgia K., Ayre, D Craig, Bach, Jean-Marie, Bachurski, Daniel, Baharvand, Hossein, Balaj, Leonora, Baldacchino, Shawn, Bauer, Natalie N., Baxter, Amy A., Bebawy, Mary, Beckham, Carla, Bedina Zavec, Apolonija, Benmoussa, Abderrahim, Berardi, Anna C., Bergese, Paolo, Bielska, Ewa, Blenkiron, Cherie, Bobis-Wozowicz, Sylwia, Boilard, Eric, Boireau, Wilfrid, Bongiovanni, Antonella, Borràs, Francesc E., Bosch, Steffi, Boulanger, Chantal M., Breakefield, Xandra, Breglio, Andrew M., Brennan, Meadhbh Á., Brigstock, David R., Brisson, Alain, Broekman, Marike Ld., Bromberg, Jacqueline F., Bryl-Górecka, Paulina, Buch, Shilpa, Buck, Amy H., Burger, Dylan, Busatto, Sara, Buschmann, Dominik, Bussolati, Benedetta, Buzás, Edit I., Byrd, James Bryan, Camussi, Giovanni, Carter, David Rf., Caruso, Sarah, Chamley, Lawrence W., Chang, Yu-Ting, Chen, Chihchen, Chen, Shuai, Cheng, Lesley, Chin, Andrew R., Clayton, Aled, Clerici, Stefano P., Cocks, Alex, Cocucci, Emanuele, Coffey, Robert J., Cordeiro-Da-Silva, Anabela, Couch, Yvonne, Coumans, Frank Aw., Coyle, Beth, Crescitelli, Rossella, Criado, Miria Ferreira, D'Souza-Schorey, Crislyn, Das, Saumya, Datta Chaudhuri, Amrita, De Candia, Paola, De Santana, Eliezer F., De Wever, Olivier, Del Portillo, Hernando A., Demaret, Tanguy, Deville, Sarah, Devitt, Andrew, Dhondt, Bert, Di Vizio, Dolores, Dieterich, Lothar C., Dolo, Vincenza, Dominguez Rubio, Ana Paula, Dominici, Massimo, Dourado, Mauricio R., Driedonks, Tom Ap., Duarte, Filipe V., Duncan, Heather M., Eichenberger, Ramon M., Ekström, Karin, El Andaloussi, Samir, Elie-Caille, Celine, Erdbrügger, Uta, Falcón-Pérez, Juan M., Fatima, Farah, Fish, Jason E., Flores-Bellver, Miguel, Försönits, András, Frelet-Barrand, Annie, Fricke, Fabia, Fuhrmann, Gregor, Gabrielsson, Susanne, Gámez-Valero, Ana, Gardiner, Chris, Gärtner, Kathrin, Gaudin, Raphael, Gho, Yong Song, Giebel, Bernd, Gilbert, Caroline, Gimona, Mario, Giusti, Ilaria, Goberdhan, Deborah Ci, Görgens, André, Gorski, Sharon M., Greening, David W., Gross, Julia Christina, Gualerzi, Alice, Gupta, Gopal N., Gustafson, Dakota, Handberg, Aase, Haraszti, Reka A., Harrison, Paul, Hegyesi, Hargita, Hendrix, An, Hill, Andrew F., Hochberg, Fred H., Hoffmann, Karl F., Holder, Beth, Holthofer, Harry, Hosseinkhani, Baharak, Hu, Guoku, Huang, Yiyao, Huber, Veronica, Hunt, Stuart, Ibrahim, Ahmed Gamal-Eldin, Ikezu, Tsuneya, Inal, Jameel M., Isin, Mustafa, Ivanova, Alena, Jackson, Hannah K., Jacobsen, Soren, Jay, Steven M, Jayachandran, Muthuvel, Jenster, Guido, Jiang, Lanzhou, Johnson, Suzanne M., Jones, Jennifer C., Jong, Ambrose, Jovanovic-Talisman, Tijana, Jung, Stephanie, Kalluri, Raghu, Kano, Shin-Ichi, Kaur, Sukhbir, Kawamura, Yumi, Keller, Evan T., Khamari, Delaram, Khomyakova, Elena, Khvorova, Anastasia, Kierulf, Peter, Kim, Kwang Pyo, Kislinger, Thomas, Klingeborn, Mikael, Klinke, David J., Kornek, Miroslaw, Kosanović, Maja M., Kovács, Árpád Ferenc, Krämer-Albers, Eva-Maria, Krasemann, Susanne, Krause, Mirja, Kurochkin, Igor V., Kusuma, Gina D., Kuypers, Sören, Laitinen, Saara, Langevin, Scott M., Languino, Lucia R., Lannigan, Joanne, Lässer, Cecilia, Laurent, Louise C., Lavieu, Gregory, Lázaro-Ibáñez, Elisa, Le Lay, Soazig, Lee, Myung-Shin, Lee, Yi Xin Fiona, Lemos, Debora S., Lenassi, Metka, Leszczynska, Aleksandra, Li, Isaac Ts, Liao, Ke, Libregts, Sten F., Ligeti, Erzsebet, Lim, Rebecca, Lim, Sai Kiang, Linē, Aija, Linnemannstöns, Karen, Llorente, Alicia, Lombard, Catherine A., Lorenowicz, Magdalena J., Lörincz, Ákos M., Lötvall, Jan, Lovett, Jason, Lowry, Michelle C., Loyer, Xavier, Lu, Quan, Lukomska, Barbara, Lunavat, Taral R., Maas, Sybren Ln, Malhi, Harmeet, Marcilla, Antonio, Mariani, Jacopo, Mariscal, Javier, Martens-Uzunova, Elena S., Martin-Jaular, Lorena, Martinez, M Carmen, Martins, Vilma Regina, Mathieu, Mathilde, Mathivanan, Suresh, Maugeri, Marco, McGinnis, Lynda K., McVey, Mark J., Meckes, David G., Meehan, Katie L., Mertens, Inge, Minciacchi, Valentina R., Möller, Andreas, Møller Jørgensen, Malene, Morales-Kastresana, Aizea, Morhayim, Jess, Mullier, François, Muraca, Maurizio, Musante, Luca, Mussack, Veronika, Muth, Dillon C., Myburgh, Kathryn H., Najrana, Tanbir, Nawaz, Muhammad, Nazarenko, Irina, Nejsum, Peter, Neri, Christian, Neri, Tommaso, Nieuwland, Rienk, Nimrichter, Leonardo, Nolan, John P., Nolte-'T Hoen, Esther Nm, Noren Hooten, Nicole, O'Driscoll, Lorraine, O'Grady, Tina, O'Loghlen, Ana, Ochiya, Takahiro, Olivier, Martin, Ortiz, Alberto, Ortiz, Luis A., Osteikoetxea, Xabier, Østergaard, Ole, Ostrowski, Matias, Park, Jaesung, Pegtel, D Michiel, Peinado, Hector, Perut, Francesca, Pfaffl, Michael W., Phinney, Donald G., Pieters, Bartijn Ch., Pink, Ryan C., Pisetsky, David S., Pogge Von Strandmann, Elke, Polakovicova, Iva, Poon, Ivan Kh, Powell, Bonita H., Prada, Ilaria, Pulliam, Lynn, Quesenberry, Peter, Radeghieri, Annalisa, Raffai, Robert L., Raimondo, Stefania, Rak, Janusz, Ramirez, Marcel I., Raposo, Graça, Rayyan, Morsi S., Regev-Rudzki, Neta, Ricklefs, Franz L., Robbins, Paul D., Roberts, David D., Rodrigues, Silvia C., Rohde, Eva, Rome, Sophie, Rouschop, Kasper Ma, Rughetti, Aurelia, Russell, Ashley E., Saá, Paula, Sahoo, Susmita, Salas-Huenuleo, Edison, Sánchez, Catherine, Saugstad, Julie A., Saul, Meike J., Schiffelers, Raymond M., Schneider, Raphael, Schøyen, Tine Hiorth, Scott, Aaron, Shahaj, Eriomina, Sharma, Shivani, Shatnyeva, Olga, Shekari, Faezeh, Shelke, Ganesh Vilas, Shetty, Ashok K., Shiba, Kiyotaka, Siljander, Pia R-M, Silva, Andreia M., Skowronek, Agata, Snyder, Orman L., Soares, Rodrigo Pedro, Sódar, Barbara W., Soekmadji, Carolina, Sotillo, Javier, Stahl, Philip D., Stoorvogel, Willem, Stott, Shannon L., Strasser, Erwin F., Swift, Simon, Tahara, Hidetoshi, Tewari, Muneesh, Timms, Kate, Tiwari, Swasti, Tixeira, Rochelle, Tkach, Mercedes, Toh, Wei Seong, Tomasini, Richard, Torrecilhas, Ana Claudia, Tosar, Juan Pablo, Toxavidis, Vasilis, Urbanelli, Lorena, Vader, Pieter, Van Balkom, Bas Wm, Van Der Grein, Susanne G., Van Deun, Jan, Van Herwijnen, Martijn Jc, Van Keuren-Jensen, Kendall, Van Niel, Guillaume, Van Royen, Martin E., Van Wijnen, Andre J., Vasconcelos, M Helena, Vechetti, Ivan J., Veit, Tiago D., Vella, Laura J., Velot, Émilie, Verweij, Frederik J., Vestad, Beate, Viñas, Jose L., Visnovitz, Tamás, Vukman, Krisztina V., Wahlgren, Jessica, Watson, Dionysios C., Wauben, Marca Hm, Weaver, Alissa, Webber, Jason P., Weber, Viktoria, Wehman, Ann M., Weiss, Daniel J., Welsh, Joshua A., Wendt, Sebastian, Wheelock, Asa M., Wiener, Zoltán, Witte, Leonie, Wolfram, Joy, Xagorari, Angeliki, Xander, Patricia, Xu, Jing, Yan, Xiaomei, Yáñez-Mó, María, Yin, Hang, Yuana, Yuana, Zappulli, Valentina, Zarubova, Jana, Žėkas, Vytautas, Zhang, Jian-Ye, Zhao, Zezhou, Zheng, Lei, Zheutlin, Alexander R., Zickler, Antje M., Zimmermann, Pascale, Zivkovic, Angela M., Zocco, Davide, and Zuba-Surma, Ewa K.
Subjects: 3. Good health

20. Minimal information for studies of extracellular vesicles 2018 (MISEV2018): a position statement of the International Society for Extracellular Vesicles and update of the MISEV2014 guidelines

Author: Théry, Clotilde, Witwer, Kenneth W, Aikawa, Elena, Alcaraz, Maria Jose, Anderson, Johnathon D, Andriantsitohaina, Ramaroson, Antoniou, Anna, Arab, Tanina, Archer, Fabienne, Atkin-Smith, Georgia K, Ayre, D Craig, Bach, Jean-Marie, Bachurski, Daniel, Baharvand, Hossein, Balaj, Leonora, Baldacchino, Shawn, Bauer, Natalie N, Baxter, Amy A, Bebawy, Mary, Beckham, Carla, Bedina Zavec, Apolonija, Benmoussa, Abderrahim, Berardi, Anna C, Bergese, Paolo, Bielska, Ewa, Blenkiron, Cherie, Bobis-Wozowicz, Sylwia, Boilard, Eric, Boireau, Wilfrid, Bongiovanni, Antonella, Borràs, Francesc E, Bosch, Steffi, Boulanger, Chantal M, Breakefield, Xandra, Breglio, Andrew M, Brennan, Meadhbh Á, Brigstock, David R, Brisson, Alain, Broekman, Marike LD, Bromberg, Jacqueline F, Bryl-Górecka, Paulina, Buch, Shilpa, Buck, Amy H, Burger, Dylan, Busatto, Sara, Buschmann, Dominik, Bussolati, Benedetta, Buzás, Edit I, Byrd, James Bryan, Camussi, Giovanni, Carter, David RF, Caruso, Sarah, Chamley, Lawrence W, Chang, Yu-Ting, Chen, Chihchen, Chen, Shuai, Cheng, Lesley, Chin, Andrew R, Clayton, Aled, Clerici, Stefano P, Cocks, Alex, Cocucci, Emanuele, Coffey, Robert J, Cordeiro-Da-Silva, Anabela, Couch, Yvonne, Coumans, Frank AW, Coyle, Beth, Crescitelli, Rossella, Criado, Miria Ferreira, D’Souza-Schorey, Crislyn, Das, Saumya, Datta Chaudhuri, Amrita, De Candia, Paola, De Santana, Eliezer F, De Wever, Olivier, Del Portillo, Hernando A, Demaret, Tanguy, Deville, Sarah, Devitt, Andrew, Dhondt, Bert, Di Vizio, Dolores, Dieterich, Lothar C, Dolo, Vincenza, Dominguez Rubio, Ana Paula, Dominici, Massimo, Dourado, Mauricio R, Driedonks, Tom AP, Duarte, Filipe V, Duncan, Heather M, Eichenberger, Ramon M, Ekström, Karin, EL Andaloussi, Samir, Elie-Caille, Celine, Erdbrügger, Uta, Falcón-Pérez, Juan M, Fatima, Farah, Fish, Jason E, Flores-Bellver, Miguel, Försönits, András, Frelet-Barrand, Annie, Fricke, Fabia, Fuhrmann, Gregor, Gabrielsson, Susanne, Gámez-Valero, Ana, Gardiner, Chris, Gärtner, Kathrin, Gaudin, Raphael, Gho, Yong Song, Giebel, Bernd, Gilbert, Caroline, Gimona, Mario, Giusti, Ilaria, Goberdhan, Deborah CI, Görgens, André, Gorski, Sharon M, Greening, David W, Gross, Julia Christina, Gualerzi, Alice, Gupta, Gopal N, Gustafson, Dakota, Handberg, Aase, Haraszti, Reka A, Harrison, Paul, Hegyesi, Hargita, Hendrix, An, Hill, Andrew F, Hochberg, Fred H, Hoffmann, Karl F, Holder, Beth, Holthofer, Harry, Hosseinkhani, Baharak, Hu, Guoku, Huang, Yiyao, Huber, Veronica, Hunt, Stuart, Ibrahim, Ahmed Gamal-Eldin, Ikezu, Tsuneya, Inal, Jameel M, Isin, Mustafa, Ivanova, Alena, Jackson, Hannah K, Jacobsen, Soren, Jay, Steven M, Jayachandran, Muthuvel, Jenster, Guido, Jiang, Lanzhou, Johnson, Suzanne M, Jones, Jennifer C, Jong, Ambrose, Jovanovic-Talisman, Tijana, Jung, Stephanie, Kalluri, Raghu, Kano, Shin-Ichi, Kaur, Sukhbir, Kawamura, Yumi, Keller, Evan T, Khamari, Delaram, Khomyakova, Elena, Khvorova, Anastasia, Kierulf, Peter, Kim, Kwang Pyo, Kislinger, Thomas, Klingeborn, Mikael, Klinke, David J, Kornek, Miroslaw, Kosanović, Maja M, Kovács, Árpád Ferenc, Krämer-Albers, Eva-Maria, Krasemann, Susanne, Krause, Mirja, Kurochkin, Igor V, Kusuma, Gina D, Kuypers, Sören, Laitinen, Saara, Langevin, Scott M, Languino, Lucia R, Lannigan, Joanne, Lässer, Cecilia, Laurent, Louise C, Lavieu, Gregory, Lázaro-Ibáñez, Elisa, Le Lay, Soazig, Lee, Myung-Shin, Lee, Yi Xin Fiona, Lemos, Debora S, Lenassi, Metka, Leszczynska, Aleksandra, Li, Isaac TS, Liao, Ke, Libregts, Sten F, Ligeti, Erzsebet, Lim, Rebecca, Lim, Sai Kiang, Linē, Aija, Linnemannstöns, Karen, Llorente, Alicia, Lombard, Catherine A, Lorenowicz, Magdalena J, Lörincz, Ákos M, Lötvall, Jan, Lovett, Jason, Lowry, Michelle C, Loyer, Xavier, Lu, Quan, Lukomska, Barbara, Lunavat, Taral R, Maas, Sybren LN, Malhi, Harmeet, Marcilla, Antonio, Mariani, Jacopo, Mariscal, Javier, Martens-Uzunova, Elena S, Martin-Jaular, Lorena, Martinez, M Carmen, Martins, Vilma Regina, Mathieu, Mathilde, Mathivanan, Suresh, Maugeri, Marco, McGinnis, Lynda K, McVey, Mark J, Meckes, David G, Meehan, Katie L, Mertens, Inge, Minciacchi, Valentina R, Möller, Andreas, Møller Jørgensen, Malene, Morales-Kastresana, Aizea, Morhayim, Jess, Mullier, François, Muraca, Maurizio, Musante, Luca, Mussack, Veronika, Muth, Dillon C, Myburgh, Kathryn H, Najrana, Tanbir, Nawaz, Muhammad, Nazarenko, Irina, Nejsum, Peter, Neri, Christian, Neri, Tommaso, Nieuwland, Rienk, Nimrichter, Leonardo, Nolan, John P, Nolte-’T Hoen, Esther NM, Noren Hooten, Nicole, O’Driscoll, Lorraine, O’Grady, Tina, O’Loghlen, Ana, Ochiya, Takahiro, Olivier, Martin, Ortiz, Alberto, Ortiz, Luis A, Osteikoetxea, Xabier, Ostegaard, Ole, Ostrowski, Matias, Park, Jaesung, Pegtel, D. Michiel, Peinado, Hector, Perut, Francesca, Pfaffl, Michael W, Phinney, Donald G, Pieters, Bartijn CH, Pink, Ryan C, Pisetsky, David S, Pogge Von Strandmann, Elke, Polakovicova, Iva, Poon, Ivan KH, Powell, Bonita H, Prada, Ilaria, Pulliam, Lynn, Quesenberry, Peter, Radeghieri, Annalisa, Raffai, Robert L, Raimondo, Stefania, Rak, Janusz, Ramirez, Marcel I, Raposo, Graça, Rayyan, Morsi S, Regev-Rudzki, Neta, Ricklefs, Franz L, Robbins, Paul D, Roberts, David D, Rodrigues, Silvia C, Rohde, Eva, Rome, Sophie, Rouschop, Kasper MA, Rughetti, Aurelia, Russell, Ashley E, Saá, Paula, Sahoo, Susmita, Salas-Huenuleo, Edison, Sánchez, Catherine, Saugstad, Julie A, Saul, Meike J, Schiffelers, Raymond M, Schneider, Raphael, Schøyen, Tine Hiorth, Scott, Aaron, Shahaj, Eriomina, Sharma, Shivani, Shatnyeva, Olga, Shekari, Faezeh, Shelke, Ganesh Vilas, Shetty, Ashok K, Shiba, Kiyotaka, Siljander, Pia R-M, Silva, Andreia M, Skowronek, Agata, Snyder, Orman L, Soares, Rodrigo Pedro, Sódar, Barbara W, Soekmadji, Carolina, Sotillo, Javier, Stahl, Philip D, Stoorvogel, Willem, Stott, Shannon L, Strasser, Erwin F, Swift, Simon, Tahara, Hidetoshi, Tewari, Muneesh, Timms, Kate, Tiwari, Swasti, Tixeira, Rochelle, Tkach, Mercedes, Toh, Wei Seong, Tomasini, Richard, Torrecilhas, Ana Claudia, Tosar, Juan Pablo, Toxavidis, Vasilis, Urbanelli, Lorena, Vader, Pieter, Van Balkom, Bas WM, Van Der Grein, Susanne G, Van Deun, Jan, Van Herwijnen, Martijn JC, Van Keuren-Jensen, Kendall, Van Niel, Guillaume, Van Royen, Martin E, Van Wijnen, Andre J, Vasconcelos, M Helena, Vechetti, Ivan J, Veit, Tiago D, Vella, Laura J, Velot, Émilie, Verweij, Frederik J, Vestad, Beate, Viñas, Jose L, Visnovitz, Tamás, Vukman, Krisztina V, Wahlgren, Jessica, Watson, Dionysios C, Wauben, Marca HM, Weaver, Alissa, Webber, Jason P, Weber, Viktoria, Wehman, Ann M, Weiss, Daniel J, Welsh, Joshua A, Wendt, Sebastian, Wheelock, Asa M, Wiener, Zoltán, Witte, Leonie, Wolfram, Joy, Xagorari, Angeliki, Xander, Patricia, Xu, Jing, Yan, Xiaomei, Yáñez-Mó, María, Yin, Hang, Yuana, Yuana, Zappulli, Valentina, Zarubova, Jana, Žėkas, Vytautas, Zhang, Jian-Ye, Zhao, Zezhou, Zheng, Lei, Zheutlin, Alexander R, Zickler, Antje M, Zimmermann, Pascale, Zivkovic, Angela M, Zocco, Davide, and Zuba-Surma, Ewa K
Subjects: 3. Good health
Abstract: Journal of extracellular vesicles 7(1), 1535750 (2018). doi:10.1080/20013078.2018.1535750, Published by Co-Action Publ., [S.l.]

21. Minimal information for studies of extracellular vesicles 2018 (MISEV2018): a position statement of the International Society for Extracellular Vesicles and update of the MISEV2014 guidelines

Author: Thery, Clotilde, Witwer, Kenneth W, Aikawa, Elena, Alcaraz, Maria Jose, Anderson, Johnathon D, Andriantsitohaina, Ramaroson, Antoniou, Anna, Arab, Tanina, Archer, Fabienne, Atkin-Smith, Georgia, Ayre, D Craig, Bach, Jean-Marie, Bachurski, Daniel, Baharvand, Hossein, Balaj, Leonora, Baldacchino, Shawn, Bauer, Natalie N, Baxter, Amy, Bebawy, Mary, Beckham, Carla, Zavec, Apolonija Bedina, Benmoussa, Abderrahim, Berardi, Anna C, Bergese, Paolo, Bielska, Ewa, Blenkiron, Cherie, Bobis-Wozowicz, Sylwia, Boilard, Eric, Boireau, Wilfrid, Bongiovanni, Antonella, Borras, Francesc E, Bosch, Steffi, Boulanger, Chantal M, Breakefield, Xandra, Breglio, Andrew M, Brennan, Meadhbh A, Brigstock, David R, Brisson, Alain, Broekman, Marike LD, Bromberg, Jacqueline F, Bryl-Gorecka, Paulina, Buch, Shilpa, Buck, Amy H, Burger, Dylan, Busatto, Sara, Buschmann, Dominik, Bussolati, Benedetta, Buzas, Edit, Byrd, James Bryan, Camussi, Giovanni, Carter, David RF, Caruso, Sarah, Chamley, Lawrence W, Chang, Yu-Ting, Chen, Chihchen, Chen, Shuai, Sim, Lesley, Chin, Andrew R, Clayton, Aled, Clerici, Stefano P, Cocks, Alex, Cocucci, Emanuele, Coffey, Robert J, Cordeiro-da-Silva, Anabela, Couch, Yvonne, Coumans, Frank AW, Coyle, Beth, Crescitelli, Rossella, Criado, Miria Ferreira, D'Souza-Schorey, Crislyn, Das, Saumya, Chaudhuri, Amrita Datta, de Candia, Paola, De Santana Junior, Eliezer F, De Wever, Olivier, del Portillo, Hernando A, Demaret, Tanguy, Deville, Sarah, Devitt, Andrew, Dhondt, Bert, Di Vizio, Dolores, Dieterich, Lothar C, Dolo, Vincenza, Rubio, Ana Paula Dominguez, Dominici, Massimo, Dourado, Mauricio R, Driedonks, Tom AP, Duarte, Filipe, Duncan, Heather M, Eichenberger, Ramon M, Ekstrom, Karin, Andaloussi, Samir EL, Elie-Caille, Celine, Erdbrugger, Uta, Falcon-Perez, Juan M, Fatima, Farah, Fish, Jason E, Flores-Bellver, Miguel, Forsonits, Andras, Frelet-Barrand, Annie, Fricke, Fabia, Fuhrmann, Gregor, Gabrielsson, Susanne, Gamez-Valero, Ana, Gardiner, Chris, Gaertner, Kathrin, Gaudin, Raphael, Gho, Yong Song, Giebel, Bernd, Gilbert, Caroline, Gimona, Mario, Giusti, Ilaria, Goberdhan, Deborah C, Goergens, Andre, Gorski, Sharon M, Greening, David, Gross, Julia Christina, Gualerzi, Alice, Gupta, Gopal N, Gustafson, Dakota, Handberg, Aase, Haraszti, Reka A, Harrison, Paul, Hegyesi, Hargita, Hendrix, An, Hill, Andrew, Hochberg, Fred H, Hoffmann, Karl F, Holder, Beth, Holthofer, Harry, Hosseinkhani, Baharak, Hu, Guoku, Huang, Yiyao, Huber, Veronica, Hunt, Stuart, Ibrahim, Ahmed Gamal-Eldin, Ikezu, Tsuneya, Inal, Jameel M, Isin, Mustafa, Ivanova, Alena, Jackson, Hannah K, Jacobsen, Soren, Jay, Steven M, Jayachandran, Muthuvel, Jenster, Guido, Jiang, Lanzhou, Johnson, Suzanne M, Jones, Jennifer C, Jong, Ambrose, Jovanovic-Talisman, Tijana, Jung, Stephanie, Kalluri, Raghu, Kano, Shin-ichi, Kaur, Sukhbir, Kawamura, Yumi, Keller, Evan T, Khamari, Delaram, Khomyakova, Elena, Khvorova, Anastasia, Kierulf, Peter, Kim, Kwang Pyo, Kislinger, Thomas, Klingeborn, Mikael, Klinke, David J, Kornek, Miroslaw, Kosanovic, Maja M, Kovacs, Arpad Ferenc, Kraemer-Albers, Eva-Maria, Krasemann, Susanne, Krause, Mirja, Kurochkin, Igor, Kusuma, Gina D, Kuypers, Soren, Laitinen, Saara, Langevin, Scott M, Languino, Lucia R, Lannigan, Joanne, Lasser, Cecilia, Laurent, Louise C, Lavieu, Gregory, Lazaro-Ibanez, Elisa, Le Lay, Soazig, Lee, Myung-Shin, Lee, Yi Xin Fiona, Lemos, Debora S, Lenassi, Metka, Leszczynska, Aleksandra, Li, Isaac TS, Liao, Ke, Libregts, Sten F, Ligeti, Erzsebet, Lim, Rebecca, Lim, Sai Kiang, Line, Aija, Linnemannstoens, Karen, Llorente, Alicia, Lombard, Catherine A, Lorenowicz, Magdalena J, Lorincz, Akos M, Lotvall, Jan, Lovett, Jason, Lowry, Michelle C, Loyer, Xavier, Lu, Quan, Lukomska, Barbara, Lunavat, Taral R, Maas, Sybren LN, Malhi, Harmeet, Marcilla, Antonio, Mariani, Jacopo, Mariscal, Javier, Martens-Uzunova, Elena S, Martin-Jaular, Lorena, Martinez, M Carmen, Martins, Vilma Regina, Mathieu, Mathilde, Mathivanan, Suresh, Maugeri, Marco, McGinnis, Lynda K, McVey, Mark J, Meckes, David G, Meehan, Katie L, Mertens, Inge, Minciacchi, Valentina R, Moller, Andreas, Jorgensen, Malene Moller, Morales-Kastresana, Aizea, Morhayim, Jess, Mullier, Francois, Muraca, Maurizio, Musante, Luca, Mussack, Veronika, Muth, Dillon C, Myburgh, Kathryn H, Najrana, Tanbir, Nawaz, Muhammad, Nazarenko, Irina, Nejsum, Peter, Neri, Christian, Neri, Tommaso, Nieuwland, Rienk, Nimrichter, Leonardo, Nolan, John P, Hoen, Esther NM Nolte-'t, Hooten, Nicole Noren, O'Driscoll, Lorraine, O'Grady, Tina, O'Loghlen, Ana, Ochiya, Takahiro, Olivier, Martin, Ortiz, Alberto, Ortiz, Luis A, Osteikoetxea, Xabier, Ostegaard, Ole, Ostrowski, Matias, Park, Jaesung, Pegtel, D Michiel, Peinado, Hector, Perut, Francesca, Pfaffl, Michael W, Phinney, Donald G, Pieters, Bartijn CH, Pink, Ryan C, Pisetsky, David S, von Strandmann, Elke Pogge, Polakovicova, Iva, Poon, Ivan, Powell, Bonita H, Prada, Ilaria, Pulliam, Lynn, Quesenberry, Peter, Radeghieri, Annalisa, Raffai, Robert L, Raimondo, Stefania, Rak, Janusz, Ramirez, Marcel, Raposo, Graca, Rayyan, Morsi S, Regev-Rudzki, Neta, Ricklefs, Franz L, Robbins, Paul D, Roberts, David D, Rodrigues, Silvia C, Rohde, Eva, Rome, Sophie, Rouschop, Kasper MA, Rughetti, Aurelia, Russell, Ashley E, Saa, Paula, Sahoo, Susmita, Salas-Huenuleo, Edison, Sanchez, Catherine, Saugstad, Julie A, Saul, Meike J, Schiffelers, Raymond M, Schneider, Raphael, Schoyen, Tine Hiorth, Scott, Aaron, Shahaj, Eriomina, Sharma, Shivani, Shatnyeva, Olga, Shekari, Faezeh, Shelke, Ganesh Vilas, Shetty, Ashok K, Shiba, Kiyotaka, Siljander, Pia R-M, Silva, Andreia M, Skowronek, Agata, Snyder, Orman L, Soares, Rodrigo Pedro, Sodar, Barbara W, Soekmadji, Carolina, Sotillo, Javier, Stahl, Philip D, Stoorvogel, Willem, Stott, Shannon L, Strasser, Erwin F, Swift, Simon, Tahara, Hidetoshi, Tewari, Muneesh, Timms, Kate, Tiwari, Swasti, Tixeira, Rochelle, Tkach, Mercedes, Toh, Wei Seong, Tomasini, Richard, Torrecilhas, Ana Claudia, Tosar, Juan Pablo, Toxavidis, Vasilis, Urbanelli, Lorena, Vader, Pieter, van Balkom, Bas WM, van der Grein, Susanne G, Van Deun, Jan, van Herwijnen, Martijn JC, Van Keuren-Jensen, Kendall, van Niel, Guillaume, van Royen, Martin E, van Wijnen, Andre J, Vasconcelos, M Helena, Vechetti, Ivan J, Veit, Tiago D, Vella, Laura J, Velot, Emilie, Verweij, Frederik J, Vestad, Beate, Vinas, Jose L, Visnovitz, Tamas, Vukman, Krisztina V, Wahlgren, Jessica, Watson, Dionysios C, Wauben, Marca HM, Weaver, Alissa, Webber, Jason P, Weber, Viktoria, Wehman, Ann M, Weiss, Daniel J, Welsh, Joshua A, Wendt, Sebastian, Wheelock, Asa M, Wiener, Zoltan, Witte, Leonie, Wolfram, Joy, Xagorari, Angeliki, Xander, Patricia, Xu, Jing, Yan, Xiaomei, Yanez-Mo, Maria, Yin, Hang, Yuana, Yuana, Zappulli, Valentina, Zarubova, Jana, Zekas, Vytautas, Zhang, Jian-ye, Zhao, Zezhou, Zheng, Lei, Zheutlin, Alexander R, Zickler, Antje M, Zimmermann, Pascale, Zivkovic, Angela M, Zocco, Davide, and Zuba-Surma, Ewa K
Subjects: 3. Good health, Uncategorized
Abstract: The last decade has seen a sharp increase in the number of scientific publications describing physiological and pathological functions of extracellular vesicles (EVs), a collective term covering various subtypes of cell-released, membranous structures, called exosomes, microvesicles, microparticles, ectosomes, oncosomes, apoptotic bodies, and many other names. However, specific issues arise when working with these entities, whose size and amount often make them difficult to obtain as relatively pure preparations, and to characterize properly. The International Society for Extracellular Vesicles (ISEV) proposed Minimal Information for Studies of Extracellular Vesicles (“MISEV”) guidelines for the field in 2014. We now update these “MISEV2014” guidelines based on evolution of the collective knowledge in the last four years. An important point to consider is that ascribing a specific function to EVs in general, or to subtypes of EVs, requires reporting of specific information beyond mere description of function in a crude, potentially contaminated, and heterogeneous preparation. For example, claims that exosomes are endowed with exquisite and specific activities remain difficult to support experimentally, given our still limited knowledge of their specific molecular machineries of biogenesis and release, as compared with other biophysically similar EVs. The MISEV2018 guidelines include tables and outlines of suggested protocols and steps to follow to document specific EV-associated functional activities. Finally, a checklist is provided with summaries of key points.

22. MMP-13 binds to platelet receptors αIIbβ3 and GPVI and impairs aggregation and thrombus formation

Author: Richard W. Farndale, Samir W. Hamaia, Joanna-Marie Howes, Stephanie M. Jung, Vera Knäuper, Nicholas Pugh, Jean-Daniel Malcor, Jung, Stephanie M [0000-0002-7409-9715], and Apollo - University of Cambridge Repository
Subjects: 0301 basic medicine, GPVI collagen receptor, Matrix metalloproteinase, Platelet membrane glycoprotein, 03 medical and health sciences, 0302 clinical medicine, matrix metalloproteinase‐13, medicine, Platelet, Platelet activation, cardiovascular diseases, Thrombus, Receptor, thrombosis, Original Articles: Haemostasis, Chemistry, Hematology, medicine.disease, Thrombosis, 030104 developmental biology, platelets, Cancer research, Original Article, Integrin alphaIIbbeta3 (αIIbβ3), GPVI, 030217 neurology & neurosurgery
Abstract: Essentials MMP‐13 has the potential to influence platelet function and thrombus formation directly.We sought to elucidate whether MMP‐13 is able to bind to specific platelet receptors.MMP‐13 is able to bind to platelet alphaIIbbeta3 (αIIbβ3) and glycoprotein (GP)VI.These interactions are sufficient to inhibit platelet aggregation and thrombus formation. Background Acute thrombotic syndromes lead to atherosclerotic plaque rupture with subsequent thrombus formation, myocardial infarction and stroke. Following rupture, flowing blood is exposed to plaque components, including collagen, which triggers platelet activation and aggregation. However, plaque rupture releases other components into the surrounding vessel which have the potential to influence platelet function and thrombus formation. Objectives Here we sought to elucidate whether matrix metalloproteinase‐13 (MMP‐13), a collagenolytic metalloproteinase up‐regulated in atherothrombotic and inflammatory conditions, affects platelet aggregation and thrombus formation. Results We demonstrate that MMP‐13 is able to bind to platelet receptors alphaIIbbeta3 (αIIbβ3) and platelet glycoprotein (GP)VI. The interactions between MMP‐13, GPVI and αIIbβ3 are sufficient to significantly inhibit washed platelet aggregation and decrease thrombus formation on fibrillar collagen. Conclusions Our data demonstrate a role for MMP‐13 in the inhibition of both platelet aggregation and thrombus formation in whole flowing blood, and may provide new avenues of research into the mechanisms underlying the subtle role of MMP‐13 in atherothrombotic pathologies.
Published: 2018
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22 results on '"Jung, Stephanie"'

1. Factor XIII is a newly identified binding partner for platelet collagen receptor GPVI-dimer-An interaction that may modulate fibrin crosslinking

2. Activation-induced changes in platelet surface receptor expression and the contribution of the large-platelet subpopulation to activation

3. Extracellular vesicles derived from Hepatitis-D Virus infected cells induce a proinflammatory cytokine response in human peripheral blood mononuclear cells and macrophages

4. A comprehensive UHPLC ion mobility QTOF method for profiling and quantification of eicosanoids, other oxylipins and fatty acids

5. Data on hyper-activation of GPVI signalling in obese patients: Towards the identification of novel antiplatelet targets in obesity

6. GPVI surface expression and signalling pathway activation are increased in platelets from obese patients: Elucidating potential anti-atherothrombotic targets in obesity

7. Data on hyper-activation of GPVI signalling inobese patients: towards the identification ofnovel antiplatelet targets in obesity

8. Minimal information for studies of extracellular vesicles 2018 (MISEV2018):a position statement of the International Society for Extracellular Vesicles and update of the MISEV2014 guidelines

9. Two novel, putative mechanisms of action for citalopram-induced platelet inhibition

10. Differential Inhibition of Human Atherosclerotic Plaque–Induced Platelet Activation by Dimeric GPVI-Fc and Anti-GPVI Antibodies

11. Beyond antiplatelets: The role of glycoprotein VI in ischemic stroke

12. Differential Inhibition of Human Atherosclerotic Plaque-Induced Platelet Activation by Dimeric GPVI-Fc and Anti-GPVI Antibodies: Functional and Imaging Studies

13. Immunerkennung endogener RNA-Liganden

14. Japan Series

15. Immunerkennung endogener RNA-Liganden

16. Microchip HPLC: Experimental investigation of separation efficiency, column characteristics, and coupling with mass spectrometry

17. Microchip HPLC: Experimental investigation of separation efficiency, column characteristics, and coupling with mass spectrometry

18. Expanding the UBC Farm Market

19. Minimal information for studies of extracellular vesicles 2018 (MISEV2018): a position statement of the International Society for Extracellular Vesicles and update of the MISEV2014 guidelines

20. Minimal information for studies of extracellular vesicles 2018 (MISEV2018): a position statement of the International Society for Extracellular Vesicles and update of the MISEV2014 guidelines

21. Minimal information for studies of extracellular vesicles 2018 (MISEV2018): a position statement of the International Society for Extracellular Vesicles and update of the MISEV2014 guidelines

22. MMP-13 binds to platelet receptors αIIbβ3 and GPVI and impairs aggregation and thrombus formation

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