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261 results on '"Korkmaz, Brice"'

1. Pharmacological inhibition of cathepsin S and of NSPs-AAP-1 (a novel, alternative protease driving the activation of neutrophil serine proteases)

Author

Domain, Roxane, Seren, Seda, Jerke, Uwe, Makridakis, Manousos, Chen, Kuan-Ju, Zoidakis, Jérôme, Rhimi, Moez, Zhang, Xian, Bonvent, Tillia, Croix, Cécile, Gonzalez, Loïc, Li, Dedong, Basso, Jessica, Paget, Christophe, Viaud-Massuard, Marie-Claude, Lalmanach, Gilles, Shi, Guo-Ping, Aghdassi, Ali, Vlahou, Antonia, McDonald, Patrick P., Couillin, Isabelle, Williams, Rich, Kettritz, Ralph, and Korkmaz, Brice

Published
2024
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12. Preservation solution Custodiol containing human alpha-1-antitrypsin improves graft recovery after prolonged cold ischemic storage in a rat model of heart transplantation

Author

Korkmaz-Icöz, Sevil, primary, Abulizi, Sophia, additional, Li, Kunsheng, additional, Korkmaz, Brice, additional, Georgevici, Adrian-Iustin, additional, Sayour, Alex Ali, additional, Loganathan, Sivakkanan, additional, Canoglu, Hansa, additional, Karck, Matthias, additional, and Szabó, Gábor, additional

Published
2023
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16. Additional file 1 of Dipeptidyl peptidase-1 inhibition with brensocatib reduces the activity of all major neutrophil serine proteases in patients with bronchiectasis: results from the WILLOW trial

Author

Cipolla, David, Zhang, Jimin, Korkmaz, Brice, Chalmers, James D., Basso, Jessica, Lasala, Daniel, Fernandez, Carlos, Teper, Ariel, Mange, Kevin C., Perkins, Walter R., and Sullivan, Eugene J.

Abstract

Additional file 1: Figure S1. Distribution Analysis of NE Activity in WBCs Collected Over the Trial Duration. NE activity from WBCs is shown in a quantile-quantile plot of measured values versus predicted standard normal distribution values, in a distribution plot, and in a relative frequency histogram plot. The height of the outlined box in panel B indicates the mean value for each arm. Median values for WBC NE are 5772, 4947, 3392 and 4776 ng/mL for placebo, 10 mg brensocatib, 25 mg brensocatib and all arms combined, respectively. Figure S2. Distribution Analysis of Sputum NE Activity Collected Over the Trial Duration. NE activity in sputum is shown in a quantile-quantile plot of measured values versus predicted standard normal distribution values, in a distribution plot, and in a relative frequency histogram plot. The bar in panel B indicates the mean NE activity for each arm. Median activity values for each group in the analysis are 3.32, 2.21, 1.50 and 2.30 log (ng/mL) for sputum NE for placebo, 10 mg brensocatib, 25 mg brensocatib and all arms combined, respectively. When converted back from log transformation, the median values are 2089, 162, 32 and 200 ng/mL for sputum NE, respectively. Figure S3. Distribution Analysis of Sputum PR3 Activity Collected Over the Trial Duration. PR3 activity in sputum is shown in a quantile-quantile plot of measured values versus predicted standard normal distribution values, in a distribution plot, and in a relative frequency histogram plot. The bar in panel B indicates the mean PR3 activity for each arm. Median activity values are 3.63, 3.60, 3.46, and 3.55 log (ng/mL) for sputum PR3 for placebo, 10 mg brensocatib, 25 mg brensocatib and all arms combined, respectively. When converted back from log transformation, the median values are 4266, 3981, 2884 and 3548 ng/mL for sputum PR3, respectively. Figure S4. Distribution Analysis of Sputum CatG Activity Collected Over the Trial Duration. CatG activity in sputum is shown in a quantile-quantile plot of measured values versus predicted standard normal distribution values, in a distribution plot, and in a relative frequency histogram plot. The bar in panel B indicates the mean CatG activity for each arm. Median activity values are 1.29, 0.29, 0.29 and 0.29 log (ng/mL) for sputum PR3 for placebo, 10 mg brensocatib, 25 mg brensocatib and all arms combined, respectively. When converted back from log transformation, the median values are 19, 1.9, 1.9 and 1.9 ng/mL for sputum PR3, respectively.

Published
2023
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17. Neutrophils initiate the destruction of the olfactory epithelium during SARS-CoV-2 infection in hamsters

Author

Bourgon Clara, St Albin Audrey, Ando-Grard Ophélie, Da Costa Bruno, Domain Roxane, Korkmaz Brice, Klonjkowski Bernard, Le Poder Sophie, and Meunier Nicolas

Abstract

The loss of smell related to SARS-CoV-2 infection is one of the most prevalent symptoms of COVID-19. It is now clear that this symptom is related to the massive infection by SARS-CoV-2 of the olfactory epithelium leading to its desquamation. However, the molecular mechanism behind the destabilization of the olfactory epithelium is less clear. Using golden Syrian hamster, we show here that while apoptosis remains at a low level in damaged infected epithelium, the latter is invaded by innate immunity cells. By depleting the neutrophil population or blocking the activity of neutrophil elastase-like proteinases, we reduced the damage induced by the SARS-CoV-2 infection. Surprisingly, the impairment of neutrophil activity led to a decrease of SARS-CoV-2 infection levels in the nasal cavity. Our results indicate a counterproductive role of neutrophils leading to the release of infected cells in the lumen of the nasal cavity and thereby enhanced spreading of the virus.

Published
2022

18. Development of a long-acting version of Alpha1 antitrypsin for augmentation therapy in Alpha1 antitrypsin deficiency

Author

UCL - SSS/LDRI - Louvain Drug Research Institute, UCL - Faculty of Pharmacy and Biomedical Sciences, Vanbever, Rita, Van Bambeke, Françoise, Leal, Teresinha, Soumillion, Patrice, Delporte, Cédric, Korkmaz, Brice, Liu, Xiao, UCL - SSS/LDRI - Louvain Drug Research Institute, UCL - Faculty of Pharmacy and Biomedical Sciences, Vanbever, Rita, Van Bambeke, Françoise, Leal, Teresinha, Soumillion, Patrice, Delporte, Cédric, Korkmaz, Brice, and Liu, Xiao

Abstract

Alpha-1 antitrypsin (AAT) is a serine protease inhibitor. A low level of serum AAT (<11 µM) is defined as AAT deficiency. The limitations of the current treatments for AAT deficiency-related lung disease are the low AAT lung penetration rate following intravenous infusion and the rapid AAT clearance from the lung following inhalation. Here, we present a PEGylated version of AAT, which shows improved resistance to proteolysis in vitro. In vivo, PEGylated AAT exhibits prolonged body residency after delivery by the intravenous and intratracheal routes. In a murine COPD model, a low intranasal dose of PEGylated AAT achieves better efficacy than a 45-fold higher intravenous dose of AAT. PEGylated AAT represents a promising alternative for AAT augmentation therapy., (BIFA - Sciences biomédicales et pharmaceutiques) -- UCL, 2022

Published
2022

19. Targeting Cathepsin C in PR3-ANCA Vasculitis

Author

Jerke, Uwe, primary, Eulenberg-Gustavus, Claudia, additional, Rousselle, Anthony, additional, Nicklin, Paul, additional, Kreideweiss, Stefan, additional, Grundl, Marc A., additional, Eickholz, Peter, additional, Nickles, Katrin, additional, Schreiber, Adrian, additional, Korkmaz, Brice, additional, and Kettritz, Ralph, additional

Published
2022
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20. Bile Acids: Key Players in Inflammatory Bowel Diseases?

Author

Kriaa, Aicha, primary, Mariaule, Vincent, additional, Jablaoui, Amin, additional, Rhimi, Soufien, additional, Mkaouar, Hela, additional, Hernandez, Juan, additional, Korkmaz, Brice, additional, Lesner, Adam, additional, Maguin, Emmanuelle, additional, Aghdassi, Ali, additional, and Rhimi, Moez, additional

Published
2022
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22. Cathepsin C inhibition as a potential treatment strategy in cancer

Author

Korkmaz, Brice, primary, Lamort, Anne-Sophie, additional, Domain, Roxane, additional, Beauvillain, Céline, additional, Gieldon, Artur, additional, Yildirim, Ali Önder, additional, Stathopoulos, Georgios T., additional, Rhimi, Moez, additional, Jenne, Dieter E., additional, and Kettritz, Ralph, additional

Published
2021
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23. Analysis of urinary cathepsin C for diagnosing Papillon–Lefèvre syndrome

Author

Hamon, Yveline, Legowska, Monika, Fergelot, Patricia, Dallet-Choisy, Sandrine, Newell, Louise, Vanderlynden, Lise, Valeshabad, Ali Kord, Acrich, Karina, Kord, Hadi, Charalampos, Tsamakis, Morice-Picard, Fanny, Surplice, Ian, Zoidakis, Jerome, David, Karen, Vlahou, Antonia, Ragunatha, Shivanna, Nagy, Nikoletta, Farkas, Katalin, Széll, Márta, Goizet, Cyril, Schacher, Beate, Battino, Maurizio, Al Farraj Aldosari, Abdullah, Wang, Xinwen, Liu, Yang, Marchand-Adam, Sylvain, Lesner, Adam, Kara, Elodie, Korkmaz-Icöz, Sevil, Moss, Celia, Eickholz, Peter, Taieb, Alain, Kavukcu, Salih, Jenne, Dieter E., Gauthier, Francis, and Korkmaz, Brice

Published
2016
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26. Gut Serpinome: Emerging Evidence in IBD

Author

Mkaouar, Héla, primary, Mariaule, Vincent, additional, Rhimi, Soufien, additional, Hernandez, Juan, additional, Kriaa, Aicha, additional, Jablaoui, Amin, additional, Akermi, Nizar, additional, Maguin, Emmanuelle, additional, Lesner, Adam, additional, Korkmaz, Brice, additional, and Rhimi, Moez, additional

Published
2021
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28. 4C3 Human Monoclonal Antibody: A Proof of Concept for Non-pathogenic Proteinase 3 Anti-neutrophil Cytoplasmic Antibodies in Granulomatosis With Polyangiitis

Author

Granel, Jérôme, Lemoine, Roxane, Morello, Eric, Gallais, Yann, Mariot, Julie, Drapeau, Marion, Musnier, Astrid, Poupon, Anne, Pugnière, Martine, Seren, Seda, Nouar, Dalila, Gouilleux-Gruart, Valérie, Watier, Herve, Korkmaz, Brice, Hoarau, Cyrille, EA4245 - Transplantation, Immunologie, Inflammation [Tours] (T2i), Université de Tours, Infectiologie et Santé Publique (UMR ISP), Université de Tours-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), MAbSilico SAS, Dynamiques de populations multi-échelles pour des systèmes physiologiques (MUSCA), Inria Saclay - Ile de France, Institut National de Recherche en Informatique et en Automatique (Inria)-Institut National de Recherche en Informatique et en Automatique (Inria)-Physiologie de la reproduction et des comportements [Nouzilly] (PRC), Institut Français du Cheval et de l'Equitation [Saumur]-Université de Tours-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Institut Français du Cheval et de l'Equitation [Saumur]-Université de Tours-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Mathématiques et Informatique Appliquées du Génome à l'Environnement [Jouy-En-Josas] (MaIAGE), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Physiologie de la reproduction et des comportements [Nouzilly] (PRC), Institut Français du Cheval et de l'Equitation [Saumur]-Université de Tours-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Institut de Recherche en Cancérologie de Montpellier (IRCM - U1194 Inserm - UM), CRLCC Val d'Aurelle - Paul Lamarque-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), Centre d’Etude des Pathologies Respiratoires (CEPR), UMR 1100 (CEPR), Université de Tours-Institut National de la Santé et de la Recherche Médicale (INSERM), Service de néphrologie et immunologie clinique [CHRU Tours] (EA4245 UT), Centre Hospitalier Régional Universitaire de Tours (CHRU Tours)-Hôpital Bretonneau-Université de Tours, Region Centre-Val-de-Loire (program Ambition Research and Development 'Biopharmaceuticals'), University of Tours, ANR-10-LABX-0053,MAbImprove,Optimization of therapeutic monoclonal antibodies development Better antibodies, better developed AND better used(2010), Université de Tours (UT), Université de Tours (UT)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Institut Français du Cheval et de l'Equitation [Saumur] (IFCE)-Université de Tours (UT)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Institut Français du Cheval et de l'Equitation [Saumur] (IFCE)-Université de Tours (UT)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Mathématiques et Informatique Appliquées du Génome à l'Environnement [Jouy-En-Josas] (MaIAGE), Institut Français du Cheval et de l'Equitation [Saumur] (IFCE)-Université de Tours (UT)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Université de Tours (UT)-Institut National de la Santé et de la Recherche Médicale (INSERM), Service de néphrologie et immunologie clinique [CHRU Tours], Centre Hospitalier Régional Universitaire de Tours (CHRU Tours)-Hôpital Bretonneau-Université de Tours (UT), Institut Français du Cheval et de l'Equitation [Saumur]-Université de Tours (UT)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Institut Français du Cheval et de l'Equitation [Saumur]-Université de Tours (UT)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Mathématiques et Informatique Appliquées du Génome à l'Environnement [Jouy-En-Josas] (MaIAGE), and Institut Français du Cheval et de l'Equitation [Saumur]-Université de Tours (UT)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)

Subjects
Male, Glycosylation, human neutrophils, biologie computationnelle, [SDV]Life Sciences [q-bio], Myeloblastin, Immunology, Antibody Affinity, Proof of Concept Study, Neutrophil Activation, Antibodies, Antineutrophil Cytoplasmic, Cell Line, Epitopes, immune system diseases, Antibody Specificity, Humans, Immunology and Allergy, cardiovascular diseases, skin and connective tissue diseases, Aged, Original Research, B-Lymphocytes, epitope, granulomatosis with polyangiitis, Antibodies, Monoclonal, Middle Aged, respiratory tract diseases, proteinase 3, Case-Control Studies, anti-neutrophil cytoplasmic antibodies, Female, Binding Sites, Antibody, Biomarkers, Epitope Mapping
Abstract

International audience; Granulomatosis with polyangiitis (GPA) is a severe autoimmune vasculitis associated with the presence of anti-neutrophil cytoplasmic antibodies (ANCA) mainly targeting proteinase 3 (PR3), a neutrophilic serine proteinase.PR3-ANCA binding to membrane-bound PR3 on neutrophils induce their auto-immune activation responsible for vascular lesions. However, the correlation between PR3-ANCA level and disease activity remains inconsistent, suggesting the existence of non-pathogenic PR3-ANCA. In order to prove their existence, we immortalized B lymphocytes from blood samples of GPA patients in remission having persistent PR3-ANCA to isolate non-activating PR3-ANCA. We obtained for the first time a non-activating human IgG1κanti-PR3 monoclonal antibody (mAb) named 4C3. This new mAb binds soluble PR3 with a high affinity and membrane-bound PR3 on an epitope close to the PR3 hydrophobic patch and in the vicinity of the active site. 4C3 is able to bind FcγRIIA and FcγRIIIB and has a G2F glycosylation profile on asparagine 297. 4C3 did not induce activation of neutrophils and could inhibit human polyclonal PR3-ANCA-induced activation suggesting that 4C3 is non-pathogenic This characteristic relies on the recognized epitope on PR3 rather than to the Fc portion properties. The existence of non-pathogenic PR3-ANCA, which do not activate neutrophils, could explain the persistence of high PR3-ANCA levels in some GPA patients in remission and why PR3-ANCA would not predict relapse. Finally, these results offer promising perspectives particularly regarding the understanding of PR3-ANCA pathogenicity and the development of new diagnostic and therapeutic strategies in GPA

Published
2020
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30. Contributors

Author

Abbott, Catherine Anne, primary, Abraham, Carmela R., additional, Adachi, Hideki, additional, Adachi, Osao, additional, Adam, Zach, additional, Adams, Michael W.W., additional, Adang, Michael J., additional, Adham, Ibrahim M., additional, Aducci, Patrizia, additional, Agard, David A., additional, Agranovsky, Alexey A., additional, Akamatsu, Tetsuya, additional, Akiyama, Yoshinori, additional, Albrechtsen, Reidar, additional, Alejo, Alí, additional, Amberg, Sean M., additional, Amerik, Alexander Y., additional, Amparyup, Piti, additional, Andrade, Felipe, additional, Andrés, Germán, additional, Andrews, Daniel M., additional, Andrews, Robert K., additional, Antalis, Toni M., additional, Anthony, Colin S., additional, Aoki, Naoya, additional, Apte, Suneel S., additional, Arima, Kazunari, additional, Arlaud, Gérard, additional, Arni, Raghuvir Krishnaswamy, additional, Arnoux, Pascal, additional, Aronson, Nathan N., additional, Arthur, Michel, additional, Asano, Yasuhisa, additional, Ascenzi, Paolo, additional, Assakura, Marina T., additional, Auld, David S., additional, Ávila, Veridiana de Melo Rodrigues, additional, Avilés, Francesc X., additional, Awad, William M., additional, Bachhawat, Anand K., additional, Bai, Shan, additional, Baird, Teaster T., additional, Bajaj, S. Paul, additional, Baker, Susan C., additional, Banbula, Agnieszka, additional, Barrett, Alan J., additional, Barrowman, Jemima, additional, Bartlett, John D., additional, Bartsch, Jörg W., additional, Baschuk, Nikola, additional, Baskova, Isolda P., additional, Batra, Jyotsna, additional, Bauer, Karl, additional, Baumann, Ulrich, additional, Baumeister, Wolfgang, additional, Bauvois, Cédric, additional, Bayés, Alex, additional, Beauvais, Anne, additional, Becker-Pauly, Christoph, additional, Begley, Tadhg P., additional, Békés, Miklós, additional, Belas, Robert, additional, Beleford, Daniah, additional, Beppu, Teruhiko, additional, Bergmann, Ernst M., additional, Bernard, Bruno A., additional, Bernard, Dominique, additional, Berndt, Michael C., additional, Berruti, Giovanna, additional, Berry, Colin, additional, Bertenshaw, Greg P., additional, Betzel, Christian, additional, Bhaskarla, Chetana, additional, Bhosale, Manoj, additional, Bierbaum, Gabriele, additional, Bjarnason Jón, B., additional, Blaber, Michael, additional, Blackman, Michael J., additional, Blinkovsky, Alexander, additional, Boeke, Jef D., additional, Bogyo, Matthew, additional, Bohn, Stefan, additional, Boileau, Guy, additional, Boland, Mike, additional, Bolken, Tové C., additional, Bond, Judith S., additional, Bondeson, Jan, additional, Bordallo, Javier, additional, Borelli, Claudia, additional, Botelho, Tiago O., additional, Bott, Richard R., additional, Bourne, David G., additional, Bovenschen, Niels, additional, Bradshaw, Ralph A., additional, Breddam, Klaus, additional, Brew, Keith, additional, Brindley, Paul J., additional, Brinkman, Diane L., additional, Britton, Collette, additional, Broadbent, Jeff R., additional, Broadhurst, Anne, additional, Brómme, Dieter, additional, Broom, Murray, additional, Brown, Jeremy S., additional, Brown, Mark A., additional, Bruchhaus, Iris, additional, Burleigh, Barbara A., additional, Burns, Kristin E., additional, Burrows, James F., additional, Butler, Michael J., additional, Buttle, David J., additional, Byrd, Chelsea M., additional, Byun, Tony, additional, Cadel, Sandrine, additional, Caffrey, Conor R., additional, Cal, Santiago, additional, Caldentey, Javier, additional, Candela, Thomas, additional, Capasso, Clemente, additional, Capriogilio, Daniel R., additional, Carginale, Vincenzo, additional, Carmona, Adriana Karaoglanovic, additional, Carruthers, Vern B., additional, Castellino, Francis J., additional, Catanese, Joseph J., additional, Caterson, Bruce, additional, Caughey, George H., additional, Cawley, Naimh X., additional, Cawston, Tim E., additional, Cazzulo, Juan José, additional, Chai, Jijie, additional, Chai, Karl X., additional, Chaim, Olga Meiri, additional, Chang, L.S., additional, Chao, Julie, additional, Chapot-Chartier, Marie-Pierre, additional, Charli, Jean-Louis, additional, Charlier, Paulette, additional, Chave, Karen J., additional, Chen, Jian-Min, additional, Chen, Jinq-May, additional, Chen, Li-Mei, additional, Chen, Ya-Wen, additional, Chen, Yu-Yen, additional, Chevrier, Bernard, additional, Chich, Jean-François, additional, Chien, Jeremy, additional, Chimalapati, Suneeta, additional, Cho, Ki Joon, additional, Choi, Kwan Yong, additional, Chuang, Woei-Jer, additional, Chung, Chin Ha, additional, Chung, Ivy Yeuk Wah, additional, Clamagirand, Christine, additional, Clark, Ian M., additional, Clarke, Adrian K., additional, Clarke, Nicola E., additional, Clarke, Steven Gerard, additional, Clauziat, Philippe, additional, Clements, Judith A., additional, Coffinier, Catherine, additional, Cohen, Paul, additional, Colige, Alain, additional, Collignon, Anne, additional, Colloms, Sean D., additional, Conzelmann, Andreas, additional, Coombs, Graham H., additional, Cooney, Jakki C., additional, Cooper, Jonathan B., additional, Cooper, Max D., additional, Copeland, Nikki A., additional, Cottrell, Graeme S., additional, Coyle, Joseph T., additional, Craik, Charles S., additional, Creemers, John W.M., additional, Cretu, Daniela, additional, Croce, Jenifer, additional, Cross, Keith J., additional, Cueva, Rosario, additional, Cui, Sheng, additional, Cunha, Luis, additional, Cutting, Simon, additional, d’Enfert, Christophe, additional, D’Orchymont, Hugues, additional, Dahlbäck, Björn, additional, Dai, Shujia, additional, Dalbey, Ross E., additional, Dalton, John P., additional, Dando, Pam M., additional, Daniel, R.M., additional, Danilov, Sergei M., additional, Davies, Donna E., additional, De Araujo, Heloisa S., additional, De los Santos, Teresa, additional, de Luca, Viviana, additional, De Meester, Ingrid, additional, de Oliveira, Ana Karina, additional, de Oliveira, Eduardo Brandt, additional, De Oliveira, Pedro Lagerblad, additional, de Vos, Sarah, additional, Declercq, Jeroen, additional, Declercq, Wim, additional, Deghmane, Ala-Eddine, additional, Dekker, Niek, additional, Del Prete, Sonia, additional, Del Rosal, Marina, additional, Delmas, Bernard, additional, DeLotto, Robert, additional, Demidyuk, Ilya V., additional, Denison, Mark R., additional, Deussing, Jan M., additional, Devi, Lakshmi A., additional, Diamandis, Eleftherios P., additional, Diaz, Isabel, additional, Díaz-Perales, Araceli, additional, Dijkstra, Bauke W., additional, Ding, Yan, additional, Dixon, Jack E., additional, Dodt, Johannes, additional, Dokland, Terje, additional, Dolenc, Iztok, additional, Dong, Ningzheng, additional, Dong, Tran Cat, additional, Dong, Ying, additional, Dongre, Mitesh, additional, Donovan, Mark, additional, Dore, Timothy M., additional, Dorstyn, Loretta, additional, Dou, Hong, additional, Dou, Zhicheng, additional, Dougall, Annette M., additional, Drag, Marcin, additional, Dudley, Edward G., additional, Dunn, Ben M., additional, Dupuy, Bruno, additional, Duque-Magalhāes, Maria Conceicāo, additional, Durá, M. Asunción, additional, Eeckhout, Yves, additional, Eijsink, Vincent, additional, Eisen, Arthur Z., additional, Eissa, Azza, additional, Eklund, Sandra, additional, Eletr, Ziad M., additional, Ellis, Vincent, additional, Engel, Wolfgang, additional, Erdös, Ervin G., additional, Escalante, Teresa, additional, Estell, David A., additional, Etscheid, Michael, additional, Evans, Herbert J., additional, Everett, Roger D., additional, Faesen, Alex C., additional, Fahrenholz, Falk, additional, Fanjul-Fernández, Miriam, additional, Farady, Christopher J., additional, Feller, Georges, additional, Feng, Hong, additional, Fenster, Kurt M., additional, Férec, Claude, additional, Ferrari, Silvia, additional, Fingleton, Barbara, additional, Fisher, Jed F., additional, Fives-Taylor, Paula M., additional, Fong, Loren G., additional, Forneris, F., additional, Forster, Brian M., additional, Forster, Friedrich, additional, Foster, Simon J., additional, Foulon, Thierry, additional, Foundling, Stephen I., additional, Fox, Jay William, additional, Franzetti, Bruno, additional, Frasch, Alejandra P., additional, Freeze, Hudson H., additional, Frère, Jean-Marie, additional, Frey, Teryl K., additional, Fricke, Beate, additional, Fricker, Lloyd D., additional, Fridman, Rafael, additional, Froelich, Christopher J., additional, Fröhlich, Camilla, additional, Fu, Hsueh-Liang, additional, Fuhrmann, Cynthia N., additional, Fujimura, Satoshi, additional, Fujiwara, Hiroshi, additional, Fukushima, Jun, additional, Fukuyama, Keiichi, additional, Fuller, Robert S., additional, Fusek, Martin, additional, Gaboriaud, Christine, additional, Gache, Christian, additional, Gakh, Oleksandr, additional, Gal, Peter, additional, Gao, Junjun, additional, García-Sastre, Adolfo, additional, Gardiner, Donald L., additional, Gatehouse, John A., additional, Gaucher, G.M., additional, Gauthier, Francis, additional, Ghuysen, Jean-Marie, additional, Gibson, Wade, additional, Gillies, Jennifer, additional, Glaser, Elzbieta, additional, Glaser, Fabian, additional, Glickman, Michael H., additional, Goettig, Peter, additional, Goffin, Colette, additional, Gohda, Eiichi, additional, Goldberg, Alfred L., additional, Goldberg, Daniel E., additional, Goldberg, Gregory I., additional, Goldfarb, Nathan E., additional, Gomis-Rüth, F. Xavier, additional, Gopal, B., additional, Gorbalenya, Alexander E., additional, Gordon, Stuart G., additional, Gorrell, Mark D., additional, Götz, Friedrich, additional, Goulas, Theodoros, additional, Gouzy-Darmon, Cécile, additional, Govind, K., additional, Gráf, Lászlo, additional, Granados, Robert R., additional, Gräwert, Melissa Ann, additional, Gray, Douglas A., additional, Graycar, Thomas P., additional, Green, Jonathan A., additional, Gremski, Luiza Helena, additional, Groll, Michael, additional, Gromova, Tania Yu, additional, Gros, P., additional, Grubman, Marvin J., additional, Grunden, Amy M., additional, Gudmundsdóttir, Ágústa, additional, Guinand, Micheline, additional, Gully, Djamel, additional, Gustchina, Alla, additional, Gutiérrez, José María, additional, Ha, Byung Hak, additional, Haeggström, Jesper Z., additional, Hageman, James H., additional, Haiko, Johanna, additional, Hailfinger, Stephan, additional, Haitchi, Hans Michael, additional, Han, Ji Seon, additional, Hanquez, Chantal, additional, Harada, Minoru, additional, Hara-Nishimura, Ikuko, additional, Harboe, Marianne, additional, Härd, Torleif, additional, Harris, David A., additional, Hassiepen, Ulrich, additional, Hata, Shoji, additional, Hattori, Akira, additional, He, Rong-Qiao, additional, Heck, Albert J.R., additional, Hendricks, Dirk F., additional, Henrich, Bernhard, additional, Henriet, Patrick, additional, Hernández-Arana, Andrés, additional, Herrera-Camacho, Irma, additional, Heussipp, Gerhard, additional, Hibino, Toshihiko, additional, Hicks, P.M., additional, Hillman, Bradley I., additional, Hiraoka, B. 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F., additional, Prehna, Gerd, additional, Prévost, Gilles, additional, Pshezhetsky, Alexey V., additional, Qasim, Mohammad A., additional, Qian, Feng, additional, Qiu, Jiazhou, additional, Quesada, Víctor, additional, Radisky, Evette S., additional, Rader, Stephen D., additional, Raman, Kavita, additional, Ramsay, Andrew J., additional, Rancourt, Derrick E., additional, Ranjit, Najju, additional, Rao, Narayanam V., additional, Ratia, Kiira, additional, Rawlings, Neil D., additional, Rawson, Robert B., additional, Reddy, Vijay, additional, Redman, Colvin M., additional, Regonesi, Maria Elena, additional, Reichert, Andreas S., additional, Reichl, Antonia P., additional, Remaut, Han, additional, Remington, S. James, additional, Renatus, Martin, additional, Reverter, David, additional, Reynolds, Eric C., additional, Rholam, Mohamed, additional, Rice, Charles M., additional, Ridky, Todd W., additional, Riezman, Howard, additional, Rijken, D.C., additional, Rio, Marie-Christine, additional, Ritchie, Alison, additional, Robert-Baudouy, Janine, additional, Robinson, Mark W., additional, Robinson, Michael, additional, Rodriguez-Romero, Adela, additional, Rodriques, Renata Santos, additional, Rogers, John C., additional, Rojas, Camilo, additional, Romesberg, Floyd E., additional, Roper, David J., additional, Rosas-Murrieta, Nora, additional, Rose, A.M., additional, Rosenthal, Philip J., additional, Rosing, J., additional, Rossetto, Ornella, additional, Rossi, Véronique, additional, Roth, Richard A., additional, Rottensteiner, Hanspeter, additional, Rowan, Andrew D., additional, Rozanov, Mikhail, additional, Rucavado, Alexandra, additional, Ruecker, Andrea, additional, Rul, Françoise, additional, Rümenapf, Till, additional, Russo, Ilaria, additional, Ryan, Martin D., additional, Sacco, Elena, additional, Sadler, J. Evan, additional, Saenger, W., additional, Sahl, Hans-Georg, additional, Sajid, Mohammed, additional, Sakaguchi, Masayoshi, additional, Sakiyama, Fumio, additional, Salas, Maria L., additional, Salgado, Maria Cristina O., additional, Salvesen, Guy S., additional, Sánchez, Edith, additional, Sanchez, Eladio F., additional, Sang, Qing-Xiang Amy, additional, Sankaran, Krishnan, additional, Sarkar, Susanta K., additional, Sarras, Michael P., additional, Sasagawa, Yoshikiyo, additional, Satohiko, Araki, additional, Sauvage, Eric, additional, Saveanu, Loredana, additional, Savithri, H.S., additional, Sawada, Hitoshi, additional, Sawers, R. Gary, additional, Scarisbrick, Isobel A., additional, Schaller, Andreas, additional, Scheer, Justin M., additional, Scheiflinger, Friedrich, additional, Schiene-Fischer, Cordelia, additional, Schlomann, Uwe, additional, Schlösser, Manfred, additional, Schmaier, Alvin H., additional, Schmidt, Walter K., additional, Schneemann, Anette, additional, Schnellmann, Rick G., additional, Scholze, Henning, additional, Schomburg, Lutz, additional, Schwaeble, Wilhelm J., additional, Scott, Christopher J., additional, Scudiero, Rosaria, additional, Sehara-Fujisawa, Atsuko, additional, Seidah, Nabil G., additional, Seiki, Motoharu, additional, Sekiguchi, Junichi, additional, Senff-Ribeiro, Andrea, additional, Seong, Ihn Sik, additional, Serpe, Mihaela, additional, Serrano, Solange M.T., additional, Setlow, Peter, additional, Shahian, Tina, additional, Shanks, M., additional, Shao, Feng, additional, Shapiro, Steven D., additional, Sharma, Navneet, additional, Shaw, Lindsey N., additional, Shen, 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Published
2013
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34. Proteinase release from activated neutrophils in mechanically ventilated patients with non-COVID-19 and COVID-19 pneumonia

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Seren, Seda, primary, Derian, Lohann, additional, Keleş, Irem, additional, Guillon, Antoine, additional, Lesner, Adam, additional, Gonzalez, Loïc, additional, Baranek, Thomas, additional, Si-Tahar, Mustapha, additional, Marchand-Adam, Sylvain, additional, Jenne, Dieter E., additional, Paget, Christophe, additional, Jouan, Youenn, additional, and Korkmaz, Brice, additional

Published
2021
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39. Human proteinase 3 resistance to inhibition extends to alpha‐2 macroglobulin

Author

N’Guessan, Koffi, primary, Grzywa, Renata, additional, Seren, Seda, additional, Gabant, Guillaume, additional, Juliano, Maria A., additional, Moniatte, Marc, additional, van Dorsselaer, Alain, additional, Bieth, Joseph G., additional, Kellenberger, Christine, additional, Gauthier, Francis, additional, Wysocka, Magdalena, additional, Lesner, Adam, additional, Sienczyk, Marcin, additional, Cadene, Martine, additional, and Korkmaz, Brice, additional

Published
2020
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43. Consequences of cathepsin C inactivation for membrane exposure of proteinase 3, the target antigen in autoimmune vasculitis

Author

Seren, Seda, Rashed Abouzaid, Maha, Eulenberg-Gustavus, Claudia, Hirschfeld, Josefine, Nasr Soliman, Hala, Jerke, Uwe, N'Guessan, Koffi, Dallet-Choisy, Sandrine, Lesner, Adam, Lauritzen, Conni, Schacher, Beate, Eickholz, Peter, Nagy, Nikoletta, Szell, Marta, Croix, Cécile, Viaud-Massuard, Marie-Claude, Al Farraj Aldosari, Abdullah, Ragunatha, Shivanna, Ibrahim Mostafa, Mostafa, Giampieri, Francesca, Battino, Maurizio, Cornillier, Hélène, Lorette, Gérard, Stephan, Jean-Louis, Goizet, Cyril, Pedersen, John, Gauthier, Francis, Jenne, Dieter E., Marchand-Adam, Sylvain, Chapple, Iain L., Kettritz, Ralph, Korkmaz, Brice, Pathologies Respiratoires : Protéolyse et Aérosolthérapie, Université de Tours (UT)-Institut National de la Santé et de la Recherche Médicale (INSERM), National Research Center, Helmholtz-Gemeinschaft = Helmholtz Association, University of Birmingham, Medical & Molecular Genetics, University of Birmingham, School of Clinical and Experimental Medicine, Faculty of Chemistry, Technion - Israel Institute of Technology [Haifa], Unizyme Laboratories A/S, Partenaires INRAE, Department of Periodontology, People's Liberation Army No. 309 Hospital, Department of Medical Genetics, University Hospital of North-Norway, Centre National de la Recherche Scientifique (CNRS), King Saud University [Riyadh] (KSU), Department of Dermatology, Venereology, and Leprosy, Sri Siddhartha Medical College, Department of Clinical Sciences, Swedish University of Agricultural Sciences (SLU), Service de dermatologie, Infectiologie et Santé Publique (UMR ISP), Institut National de la Recherche Agronomique (INRA)-Université de Tours (UT), Centre Hospitalier Universitaire de Saint-Etienne (CHU de Saint-Etienne), Laboratoire Maladies Rares: Génétique et Métabolisme (Bordeaux) (U1211 INSERM/MRGM), Université de Bordeaux (UB)-Groupe hospitalier Pellegrin-Institut National de la Santé et de la Recherche Médicale (INSERM), German Centre for Lung Research, Max Planck Institute of Neurobiology, Charité - UniversitätsMedizin = Charité - University Hospital [Berlin], Ministère de l'Enseignement Supérieur et de la Recherche, the 'Région Centre-Val de Loire' (Project BPCO-Lyse), European Project: 668036,H2020,H2020-PHC-2015-two-stage,RELENT(2015), ProdInra, Migration, RELapses prevENTion in chronic autoimmune disease: common mechanisms and co-morbidities - RELENT - - H20202015-11-01 - 2020-04-30 - 668036 - VALID, Université de Tours-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre Hospitalier Régional Universitaire de Tours (CHRU TOURS), Institut National de la Recherche Agronomique (INRA)-Université de Tours, Centre Hospitalier Universitaire de Saint-Etienne [CHU Saint-Etienne] (CHU ST-E), and Centre Hospitalier Régional Universitaire de Tours (CHRU Tours)

Subjects
Adult, Male, neutrophile, Adolescent, Neutrophils, cathepsin C, Myeloblastin, Papillon-Lefèvre syndrome, Médecine humaine et pathologie, cathepsine, autoimmune disease, Cysteine Proteinase Inhibitors, activation cellulaire, protease inhibitor, Young Adult, antigen, genetic disease, cellule souche, Humans, cardiovascular diseases, Child, hématopoïèse, aminopeptidase, granulomatosis with polyangiitis, neutrophil, protease, proteinase 3, maladie autoimmune, [SDV.MHEP] Life Sciences [q-bio]/Human health and pathology, Cell Membrane, inhibiteur pharmacologique, Case-Control Studies, Child, Preschool, Proteolysis, Enzymology, Female, Human health and pathology, [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
Abstract

International audience; Membrane-bound proteinase 3 (PR3m) is the main target antigen of anti-neutrophil cytoplasmic autoantibodies (ANCA) in granulomatosis with polyangiitis, a systemic small-vessel vasculitis. Binding of ANCA to PR3m triggers neutrophil activation with the secretion of enzymatically active PR3 and related neutrophil serine proteases, thereby contributing to vascular damage. PR3 and related proteases are activated from pro-forms by the lysosomal cysteine protease cathepsin C (CatC) during neutrophil maturation. We hypothesized that pharmacological inhibition of CatC provides an effective measure to reduce PR3m and therefore has implications as a novel therapeutic approach in granulomatosis with polyangiitis. We first studied neutrophilic PR3 from 24 patients with Papillon-Lefèvre syndrome (PLS), a genetic form of CatC deficiency. PLS neutrophil lysates showed a largely reduced but still detectable (0.5-4%) PR3 activity when compared with healthy control cells. Despite extremely low levels of cellular PR3, the amount of constitutive PR3m expressed on the surface of quiescent neutrophils and the typical bimodal membrane distribution pattern were similar to what was observed in healthy neutrophils. However, following cell activation, there was no significant increase in the total amount of PR3m on PLS neutrophils, whereas the total amount of PR3m on healthy neutrophils was significantly increased. We then explored the effect of pharmacological CatC inhibition on PR3 stability in normal neutrophils using a potent cell-permeable CatC inhibitor and a CD34+ hematopoietic stem cell model. Human CD34+ hematopoietic stem cells were treated with the inhibitor during neutrophil differentiation over 10 days. We observed strong reductions in PR3m, cellular PR3 protein, and proteolytic PR3 activity, whereas neutrophil differentiation was not compromised.

Published
2018

49. Human proteinase 3 resistance to inhibition extends to alpha‐2 macroglobulin.

Author

N'Guessan, Koffi, Grzywa, Renata, Seren, Seda, Gabant, Guillaume, Juliano, Maria A., Moniatte, Marc, Dorsselaer, Alain, Bieth, Joseph G., Kellenberger, Christine, Gauthier, Francis, Wysocka, Magdalena, Lesner, Adam, Sienczyk, Marcin, Cadene, Martine, and Korkmaz, Brice

Subjects
ELASTASES, SERINE proteinases, MASS spectrometry, LEUCOCYTE elastase, GRANULOMATOSIS with polyangiitis, ENDOPEPTIDASES, PROTEINASES, PEPTIDASE
Abstract

Polymorphonuclear neutrophils contain at least four serine endopeptidases, namely neutrophil elastase (NE), proteinase 3 (PR3), cathepsin G (CatG), and NSP4, which contribute to the regulation of infection and of inflammatory processes. In physiological conditions, endogenous inhibitors including α2‐macroglobulin (α2‐M), serpins [α1‐proteinase inhibitor (α1‐PI)], monocyte neutrophil elastase inhibitor (MNEI), α1‐antichymotrypsin, and locally produced chelonianins (elafin, SLPI) control excessive proteolytic activity of neutrophilic serine proteinases. In contrast to human NE (hNE), hPR3 is weakly inhibited by α1‐PI and MNEI but not by SLPI. α2‐M is a large spectrum inhibitor that traps a variety of proteinases in response to cleavage(s) in its bait region. We report here that α2‐M was more rapidly processed by hNE than hPR3 or hCatG. This was confirmed by the observation that the association between α2‐M and hPR3 is governed by a kass in the ≤ 105 m−1·s−1 range. Since α2‐M‐trapped proteinases retain peptidase activity, we first predicted the putative cleavage sites within the α2‐M bait region (residues 690–728) using kinetic and molecular modeling approaches. We then identified by mass spectrum analysis the cleavage sites of hPR3 in a synthetic peptide spanning the 39‐residue bait region of α2‐M (39pep‐α2‐M). Since the 39pep‐α2‐M peptide and the corresponding bait area in the whole protein do not contain sequences with a high probability of specific cleavage by hPR3 and were indeed only slowly cleaved by hPR3, it can be concluded that α2‐M is a poor inhibitor of hPR3. The resistance of hPR3 to inhibition by endogenous inhibitors explains at least in part its role in tissue injury during chronic inflammatory diseases and its well‐recognized function of major target autoantigen in granulomatosis with polyangiitis. [ABSTRACT FROM AUTHOR]

Published
2020
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50. Therapeutic targeting of cathepsin C: from pathophysiology to treatment

Author

Korkmaz, Brice, primary, Caughey, George H., additional, Chapple, Iain, additional, Gauthier, Francis, additional, Hirschfeld, Josefine, additional, Jenne, Dieter E., additional, Kettritz, Ralph, additional, Lalmanach, Gilles, additional, Lamort, Anne-Sophie, additional, Lauritzen, Conni, additional, Łȩgowska, Monika, additional, Lesner, Adam, additional, Marchand-Adam, Sylvain, additional, McKaig, Sarah J., additional, Moss, Celia, additional, Pedersen, John, additional, Roberts, Helen, additional, Schreiber, Adrian, additional, Seren, Seda, additional, and Thakker, Nalin S., additional

Published
2018
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