Search

Your search keyword '"Bertrand, Mathieu J.M."' showing total 41 results
Start Over Author "Bertrand, Mathieu J.M."
41 results on '"Bertrand, Mathieu J.M."'

4. Apoptotic cell death in disease—Current understanding of the NCCD 2023

Author

Vitale, Ilio, Pietrocola, Federico, Guilbaud, Emma, Aaronson, Stuart A., Abrams, John M., Adam, Dieter, Agostini, Massimiliano, Agostinis, Patrizia, Alnemri, Emad S., Altucci, Lucia, Amelio, Ivano, Andrews, David W., Aqeilan, Rami I., Arama, Eli, Baehrecke, Eric H., Balachandran, Siddharth, Bano, Daniele, Barlev, Nickolai A., Bartek, Jiri, Bazan, Nicolas G., Becker, Christoph, Bernassola, Francesca, Bertrand, Mathieu J.M., Bianchi, Marco E., Blagosklonny, Mikhail V., Blander, J. Magarian, Blandino, Giovanni, Blomgren, Klas, Borner, Christoph, Bortner, Carl D., Bove, Pierluigi, Boya, Patricia, Brenner, Catherine, Broz, Petr, Brunner, Thomas, Damgaard, Rune Busk, Calin, George A., Campanella, Michelangelo, Candi, Eleonora, Carbone, Michele, Carmona-Gutierrez, Didac, Cecconi, Francesco, Chan, Francis K.M., Chen, Guo Qiang, Chen, Quan, Chen, Youhai H., Cheng, Emily H., Chipuk, Jerry E., Cidlowski, John A., Ciechanover, Aaron, Ciliberto, Gennaro, Conrad, Marcus, Cubillos-Ruiz, Juan R., Czabotar, Peter E., D’Angiolella, Vincenzo, Daugaard, Mads, Dawson, Ted M., Dawson, Valina L., De Maria, Ruggero, De Strooper, Bart, Debatin, Klaus Michael, Deberardinis, Ralph J., Degterev, Alexei, Del Sal, Giannino, Deshmukh, Mohanish, Di Virgilio, Francesco, Diederich, Marc, Dixon, Scott J., Dynlacht, Brian D., El-Deiry, Wafik S., Elrod, John W., Engeland, Kurt, Fimia, Gian Maria, Galassi, Claudia, Ganini, Carlo, Garcia-Saez, Ana J., Garg, Abhishek D., Garrido, Carmen, Gavathiotis, Evripidis, Gerlic, Motti, Ghosh, Sourav, Green, Douglas R., Greene, Lloyd A., Gronemeyer, Hinrich, Häcker, Georg, Hajnóczky, György, Hardwick, J. Marie, Haupt, Ygal, He, Sudan, Heery, David M., Hengartner, Michael O., Hetz, Claudio, Hildeman, David A., Ichijo, Hidenori, Inoue, Satoshi, Jäättelä, Marja, Janic, Ana, Joseph, Bertrand, Jost, Philipp J., Kanneganti, Thirumala Devi, Karin, Michael, Kashkar, Hamid, Kaufmann, Thomas, Kelly, Gemma L., Kepp, Oliver, Kimchi, Adi, Kitsis, Richard N., Klionsky, Daniel J., Kluck, Ruth, Krysko, Dmitri V., Kulms, Dagmar, Kumar, Sharad, Lavandero, Sergio, Lavrik, Inna N., Lemasters, John J., Liccardi, Gianmaria, Linkermann, Andreas, Lipton, Stuart A., Lockshin, Richard A., López-Otín, Carlos, Luedde, Tom, MacFarlane, Marion, Madeo, Frank, Malorni, Walter, Manic, Gwenola, Mantovani, Roberto, Marchi, Saverio, Marine, Jean Christophe, Martin, Seamus J., Martinou, Jean Claude, Mastroberardino, Pier G., Medema, Jan Paul, Mehlen, Patrick, Meier, Pascal, Melino, Gerry, Melino, Sonia, Miao, Edward A., Moll, Ute M., Muñoz-Pinedo, Cristina, Murphy, Daniel J., Niklison-Chirou, Maria Victoria, Novelli, Flavia, Núñez, Gabriel, Oberst, Andrew, Ofengeim, Dimitry, Opferman, Joseph T., Oren, Moshe, Pagano, Michele, Panaretakis, Theocharis, Pasparakis, Manolis, Penninger, Josef M., Pentimalli, Francesca, Pereira, David M., Pervaiz, Shazib, Peter, Marcus E., Pinton, Paolo, Porta, Giovanni, Prehn, Jochen H.M., Puthalakath, Hamsa, Rabinovich, Gabriel A., Rajalingam, Krishnaraj, Ravichandran, Kodi S., Rehm, Markus, Ricci, Jean Ehrland, Rizzuto, Rosario, Robinson, Nirmal, Rodrigues, Cecilia M.P., Rotblat, Barak, Rothlin, Carla V., Rubinsztein, David C., Rudel, Thomas, Rufini, Alessandro, Ryan, Kevin M., Sarosiek, Kristopher A., Sawa, Akira, Sayan, Emre, Schroder, Kate, Scorrano, Luca, Sesti, Federico, Shao, Feng, Shi, Yufang, Sica, Giuseppe S., Silke, John, Simon, Hans Uwe, Sistigu, Antonella, Stephanou, Anastasis, Stockwell, Brent R., Strapazzon, Flavie, Strasser, Andreas, Sun, Liming, Sun, Erwei, Sun, Qiang, Szabadkai, Gyorgy, Tait, Stephen W.G., Tang, Daolin, Tavernarakis, Nektarios, Troy, Carol M., Turk, Boris, Urbano, Nicoletta, Vandenabeele, Peter, Vanden Berghe, Tom, Vander Heiden, Matthew G., Vanderluit, Jacqueline L., Verkhratsky, Alexei, Villunger, Andreas, von Karstedt, Silvia, Voss, Anne K., Vousden, Karen H., Vucic, Domagoj, Vuri, Daniela, Wagner, Erwin F., Walczak, Henning, Wallach, David, Wang, Ruoning, Wang, Ying, Weber, Achim, Wood, Will, Yamazaki, Takahiro, Yang, Huang Tian, Zakeri, Zahra, Zawacka-Pankau, Joanna E., Zhang, Lin, Zhang, Haibing, Zhivotovsky, Boris, Zhou, Wenzhao, Piacentini, Mauro, Kroemer, Guido, Galluzzi, Lorenzo, Vitale, Ilio, Pietrocola, Federico, Guilbaud, Emma, Aaronson, Stuart A., Abrams, John M., Adam, Dieter, Agostini, Massimiliano, Agostinis, Patrizia, Alnemri, Emad S., Altucci, Lucia, Amelio, Ivano, Andrews, David W., Aqeilan, Rami I., Arama, Eli, Baehrecke, Eric H., Balachandran, Siddharth, Bano, Daniele, Barlev, Nickolai A., Bartek, Jiri, Bazan, Nicolas G., Becker, Christoph, Bernassola, Francesca, Bertrand, Mathieu J.M., Bianchi, Marco E., Blagosklonny, Mikhail V., Blander, J. Magarian, Blandino, Giovanni, Blomgren, Klas, Borner, Christoph, Bortner, Carl D., Bove, Pierluigi, Boya, Patricia, Brenner, Catherine, Broz, Petr, Brunner, Thomas, Damgaard, Rune Busk, Calin, George A., Campanella, Michelangelo, Candi, Eleonora, Carbone, Michele, Carmona-Gutierrez, Didac, Cecconi, Francesco, Chan, Francis K.M., Chen, Guo Qiang, Chen, Quan, Chen, Youhai H., Cheng, Emily H., Chipuk, Jerry E., Cidlowski, John A., Ciechanover, Aaron, Ciliberto, Gennaro, Conrad, Marcus, Cubillos-Ruiz, Juan R., Czabotar, Peter E., D’Angiolella, Vincenzo, Daugaard, Mads, Dawson, Ted M., Dawson, Valina L., De Maria, Ruggero, De Strooper, Bart, Debatin, Klaus Michael, Deberardinis, Ralph J., Degterev, Alexei, Del Sal, Giannino, Deshmukh, Mohanish, Di Virgilio, Francesco, Diederich, Marc, Dixon, Scott J., Dynlacht, Brian D., El-Deiry, Wafik S., Elrod, John W., Engeland, Kurt, Fimia, Gian Maria, Galassi, Claudia, Ganini, Carlo, Garcia-Saez, Ana J., Garg, Abhishek D., Garrido, Carmen, Gavathiotis, Evripidis, Gerlic, Motti, Ghosh, Sourav, Green, Douglas R., Greene, Lloyd A., Gronemeyer, Hinrich, Häcker, Georg, Hajnóczky, György, Hardwick, J. Marie, Haupt, Ygal, He, Sudan, Heery, David M., Hengartner, Michael O., Hetz, Claudio, Hildeman, David A., Ichijo, Hidenori, Inoue, Satoshi, Jäättelä, Marja, Janic, Ana, Joseph, Bertrand, Jost, Philipp J., Kanneganti, Thirumala Devi, Karin, Michael, Kashkar, Hamid, Kaufmann, Thomas, Kelly, Gemma L., Kepp, Oliver, Kimchi, Adi, Kitsis, Richard N., Klionsky, Daniel J., Kluck, Ruth, Krysko, Dmitri V., Kulms, Dagmar, Kumar, Sharad, Lavandero, Sergio, Lavrik, Inna N., Lemasters, John J., Liccardi, Gianmaria, Linkermann, Andreas, Lipton, Stuart A., Lockshin, Richard A., López-Otín, Carlos, Luedde, Tom, MacFarlane, Marion, Madeo, Frank, Malorni, Walter, Manic, Gwenola, Mantovani, Roberto, Marchi, Saverio, Marine, Jean Christophe, Martin, Seamus J., Martinou, Jean Claude, Mastroberardino, Pier G., Medema, Jan Paul, Mehlen, Patrick, Meier, Pascal, Melino, Gerry, Melino, Sonia, Miao, Edward A., Moll, Ute M., Muñoz-Pinedo, Cristina, Murphy, Daniel J., Niklison-Chirou, Maria Victoria, Novelli, Flavia, Núñez, Gabriel, Oberst, Andrew, Ofengeim, Dimitry, Opferman, Joseph T., Oren, Moshe, Pagano, Michele, Panaretakis, Theocharis, Pasparakis, Manolis, Penninger, Josef M., Pentimalli, Francesca, Pereira, David M., Pervaiz, Shazib, Peter, Marcus E., Pinton, Paolo, Porta, Giovanni, Prehn, Jochen H.M., Puthalakath, Hamsa, Rabinovich, Gabriel A., Rajalingam, Krishnaraj, Ravichandran, Kodi S., Rehm, Markus, Ricci, Jean Ehrland, Rizzuto, Rosario, Robinson, Nirmal, Rodrigues, Cecilia M.P., Rotblat, Barak, Rothlin, Carla V., Rubinsztein, David C., Rudel, Thomas, Rufini, Alessandro, Ryan, Kevin M., Sarosiek, Kristopher A., Sawa, Akira, Sayan, Emre, Schroder, Kate, Scorrano, Luca, Sesti, Federico, Shao, Feng, Shi, Yufang, Sica, Giuseppe S., Silke, John, Simon, Hans Uwe, Sistigu, Antonella, Stephanou, Anastasis, Stockwell, Brent R., Strapazzon, Flavie, Strasser, Andreas, Sun, Liming, Sun, Erwei, Sun, Qiang, Szabadkai, Gyorgy, Tait, Stephen W.G., Tang, Daolin, Tavernarakis, Nektarios, Troy, Carol M., Turk, Boris, Urbano, Nicoletta, Vandenabeele, Peter, Vanden Berghe, Tom, Vander Heiden, Matthew G., Vanderluit, Jacqueline L., Verkhratsky, Alexei, Villunger, Andreas, von Karstedt, Silvia, Voss, Anne K., Vousden, Karen H., Vucic, Domagoj, Vuri, Daniela, Wagner, Erwin F., Walczak, Henning, Wallach, David, Wang, Ruoning, Wang, Ying, Weber, Achim, Wood, Will, Yamazaki, Takahiro, Yang, Huang Tian, Zakeri, Zahra, Zawacka-Pankau, Joanna E., Zhang, Lin, Zhang, Haibing, Zhivotovsky, Boris, Zhou, Wenzhao, Piacentini, Mauro, Kroemer, Guido, and Galluzzi, Lorenzo

Abstract

Apoptosis is a form of regulated cell death (RCD) that involves proteases of the caspase family. Pharmacological and genetic strategies that experimentally inhibit or delay apoptosis in mammalian systems have elucidated the key contribution of this process not only to (post-)embryonic development and adult tissue homeostasis, but also to the etiology of multiple human disorders. Consistent with this notion, while defects in the molecular machinery for apoptotic cell death impair organismal development and promote oncogenesis, the unwarranted activation of apoptosis promotes cell loss and tissue damage in the context of various neurological, cardiovascular, renal, hepatic, infectious, neoplastic and inflammatory conditions. Here, the Nomenclature Committee on Cell Death (NCCD) gathered to critically summarize an abundant pre-clinical literature mechanistically linking the core apoptotic apparatus to organismal homeostasis in the context of disease.

Published
2023

6. From PERK to RIPK1: Design, synthesis and evaluation of novel potent and selective necroptosis inhibitors

Author

Scarpellini, Camilla, Valembois, Sophie, Goossens, Kenneth, Vadi, Mike, Lanthier, Caroline, Klejborowska, Greta, van der Veken, Pieter, De Winter, Hans, Bertrand, Mathieu J.M., and Augustyns, Koen

Subjects
Chemistry, General Chemistry
Abstract

Receptor-Interacting serine/threonine-Protein Kinase 1 (RIPK1) emerged as an important driver of inflammation and, consequently, inflammatory pathologies. The enzymatic activity of RIPK1 is known to indirectly promote inflammation by triggering cell death, in the form of apoptosis, necroptosis and pyroptosis. Small molecule Receptor-Interacting serine/threonine-Protein Kinase 1 inhibitors have therefore recently entered clinical trials for the treatment of a subset of inflammatory pathologies. We previously identified GSK2656157 (GSK’157), a supposedly specific inhibitor of protein kinase R (PKR)-like ER kinase (PERK), as a much more potent type II Receptor-Interacting serine/threonine-Protein Kinase 1 inhibitor. We now performed further structural optimisation on the GSK’157 scaffold in order to develop a novel class of more selective Receptor-Interacting serine/threonine-Protein Kinase 1 inhibitors. Based on a structure-activity relationship (SAR) reported in the literature, we anticipated that introducing a substituent on the para-position of the pyridinyl ring would decrease the interaction with PERK. Herein, we report a series of novel GSK’157 analogues with different para-substituents with increased selectivity for Receptor-Interacting serine/threonine-Protein Kinase 1. The optimisation led to UAMC-3861 as the best compound of this series in terms of activity and selectivity for Receptor-Interacting serine/threonine-Protein Kinase 1 over PERK. The most selective compounds were screened in vitro for their ability to inhibit RIPK1-dependent apoptosis and necroptosis. With this work, we successfully synthesised a novel series of potent and selective type II Receptor-Interacting serine/threonine-Protein Kinase 1 inhibitors based on the GSK’157 scaffold.

Published
2023

7. RIPK1 kinase-dependent inflammation and cell death contribute to the pathogenesis of COPD

Author

Van Eeckhoutte, Hannelore P., primary, Donovan, Chantal, additional, Kim, Richard Y., additional, Conlon, Thomas M., additional, Ansari, Meshal, additional, Khan, Haroon, additional, Jayaraman, Ranjith, additional, Hansbro, Nicole G., additional, Dondelinger, Yves, additional, Delanghe, Tom, additional, Beal, Allison M., additional, Geddes, Brad, additional, Bertin, John, additional, Vanden Berghe, Tom, additional, De Volder, Joyceline, additional, Maes, Tania, additional, Vandenabeele, Peter, additional, Vanaudenaerde, Bart M., additional, Deforce, Dieter, additional, Škevin, Sonja, additional, Van Nieuwerburgh, Filip, additional, Verhamme, Fien M., additional, Joos, Guy F., additional, Idrees, Sobia, additional, Schiller, Herbert B., additional, Yildirim, Ali Önder, additional, Faiz, Alen, additional, Bertrand, Mathieu J.M., additional, Brusselle, Guy G., additional, Hansbro, Philip M., additional, and Bracke, Ken R., additional

Published
2022
Full Text
View/download PDF

8. Endocytic membrane repair by ESCRT-III controls antigen export to the cytosol during antigen cross-presentation

Author

Gros, Marine, primary, Segura, Elodie, additional, Rookhuizen, Derek C., additional, Baudon, Blandine, additional, Heurtebise-Chrétien, Sandrine, additional, Burgdorf, Nina, additional, Maurin, Mathieu, additional, Kapp, Eugene A., additional, Simpson, Richard J., additional, Kozik, Patrycja, additional, Villadangos, Jose A., additional, Bertrand, Mathieu J.M., additional, Burbage, Marianne, additional, and Amigorena, Sebastian, additional

Published
2022
Full Text
View/download PDF

10. RIPK1 ensures intestinal homeostasis by protecting the epithelium against apoptosis

Author

Takahashi, Nozomi, Vereecke, Lars, Bertrand, Mathieu J.M., Duprez, Linde, Berger, Scott B., Divert, Tatyana, Goncalves, Amanda, Sze, Mozes, Gilbert, Barbara, Kourula, Stephanie, Goossens, Vera, Lefebvre, Sylvie, Gunther, Claudia, Becker, Christoph, Bertin, John, Gough, Peter J., Declercq, Wim, van Loo, Geert, and Vandenabeele, Peter

Subjects
Epithelium -- Physiological aspects, Homeostasis -- Research, Protein research, Protein kinases -- Physiological aspects, Apoptosis -- Research, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Receptor interacting protein kinase 1 (RIPK1) has an essential role in the signalling triggered by death receptors and pattern recognition receptors (1,2). RIPK1 is believed to function as a node driving NF-κB-mediated cell survival and inflammation as well as caspase8 (CASP8)-dependent apoptotic or RIPK3/MLKL-dependent necroptotic cell death. The physiological relevance of this dual function has remained elusive because of the perinatal death of RIPK1 full knockout mice (3). To circumvent this problem, we generated RIPK1 conditional knockout mice, and show that mice lacking RIPK1 in intestinal epithelial cells (IECs) spontaneously develop severe intestinal inflammation associated with IEC apoptosis leading to early death. This early lethality was rescued by antibiotic treatment, MYD88 deficiency or tumour-necrosis factor (TNF) receptor 1 deficiency, demonstrating the importance of commensal bacteria and TNF in the IEC Ripk1 knockout phenotype. CASP8 deficiency, but not RIPK3 deficiency, rescued the inflammatory phenotype completely, indicating the indispensable role of RIPK1 in suppressing CASP8-dependent apoptosis but not RIPK3-dependent necroptosis in the intestine. RIPK1 kinase-dead knock-in mice did not exhibit any sign of inflammation, suggesting that RIPK1-mediated protection resides in its kinase-independent platform function. Depletion of RIPK1 in intestinal organoid cultures sensitized them to TNF-induced apoptosis, confirming the invivoobservations. Unexpectedly, TNF-mediated NF-κB activation remained intact in these organoids. Our results demonstrate that RIPK1 is essential for survival of IECs, ensuring epithelial homeostasis by protecting the epithelium from CASP8mediated IEC apoptosis independently of its kinase activity and NF-κB activation., RIPK1 is a serine/threonine kinase that is an upstream regulator of the cellular responses initiated by members of the death receptor families, such as TNF receptor (TNFR), and pattern recognition [...]

Published
2014

11. Polyhydramnios, Transient Antenatal Bartterʼs Syndrome, and MAGED2 Mutations

Author

Laghmani, Kamel, Beck, Bodo B., Yang, Sung-Sen, Seaayfan, Elie, Wenzel, Andrea, Reusch, Björn, Vitzthum, Helga, Priem, Dario, Demaretz, Sylvie, Bergmann, Klasien, Duin, Leonie K., Göbel, Heike, Mache, Christoph, Thiele, Holger, Bartram, Malte P., Dombret, Carlos, Altmüller, Janine, Nürnberg, Peter, Benzing, Thomas, Levtchenko, Elena, Seyberth, Hannsjörg W., Klaus, Günter, Yigit, Gökhan, Lin, Shih-Hua, Timmer, Albert, de Koning, Tom J., Scherjon, Sicco A., Schlingmann, Karl P., Bertrand, Mathieu J.M., Rinschen, Markus M., de Backer, Olivier, Konrad, Martin, and Kömhoff, Martin

Published
2016
Full Text
View/download PDF

12. Respiratory Syncytial Virus Infection Promotes Necroptosis and HMGB1 Release by Airway Epithelial Cells

Author

Simpson, Jennifer, Loh, Zhixuan, Ullah, Md Ashik, Lynch, Jason P., Werder, Rhiannon B., Collinson, Natasha, Zhang, Vivian, Dondelinger, Yves, Bertrand, Mathieu J.M., Everard, Mark L., Blyth, Christopher C., Hartel, Gunter, Van Oosterhout, Antoon J., Gough, Peter J., Bertin, John, Upham, John W., Spann, Kirsten M., Phipps, Simon, Simpson, Jennifer, Loh, Zhixuan, Ullah, Md Ashik, Lynch, Jason P., Werder, Rhiannon B., Collinson, Natasha, Zhang, Vivian, Dondelinger, Yves, Bertrand, Mathieu J.M., Everard, Mark L., Blyth, Christopher C., Hartel, Gunter, Van Oosterhout, Antoon J., Gough, Peter J., Bertin, John, Upham, John W., Spann, Kirsten M., and Phipps, Simon

Abstract

Rationale: Respiratory syncytial virus (RSV) bronchiolitis causes significant infant mortality. Bronchiolitis is characterized by airway epithelial cell (AEC) death; however, the mode of death remains unknown. Objectives: To determine whether necroptosis contributes to RSV bronchiolitis pathogenesis via HMGB1 (high mobility group box 1) release. Methods: Nasopharyngeal samples were collected from children presenting to the hospital with acute respiratory infection. Primary humanAECs andneonatalmicewere inoculatedwithRSVandmurine Pneumovirus, respectively. Necroptosis was determined via viability assays and immunohistochemistry for RIPK1 (receptor-interacting protein kinase-1), MLKL (mixed lineage kinase domain-like pseudokinase) protein, and caspase-3. Necroptosis was blocked using pharmacological inhibitors and RIPK1 kinase-dead knockin mice. Measurements and Main Results: HMGB1 levels were elevated in nasopharyngeal samples of children with acute RSV infection. RSV-induced epithelial cell death was associated with increased phosphorylated RIPK1 and phosphorylated MLKL but not active caspase-3 expression. Inhibition of RIPK1 or MLKL attenuated RSV-induced HMGB1 translocation and release, and lowered viral load. MLKL inhibition increased active caspase-3 expression in a caspase-8/9 dependent manner. In susceptible mice, Pneumovirus infection upregulated RIPK1 and MLKL expression in the airway epithelium at 8 to 10 days after infection, coinciding with AEC sloughing, HMGB1 release, and neutrophilic inflammation. Genetic or pharmacological inhibition of RIPK1 or MLKL attenuated these pathologies, lowered viral load, and prevented type 2 inflammation and airway remodeling. Necroptosis inhibition in early life ameliorated asthma progression induced by viral or allergen challenge in later life. Conclusions: Pneumovirus infection induces AEC necroptosis. Inhibition of necroptosis may be a viable strategy to limit the severity of viral bronchiolitis and break its nexus

Published
2020

16. OTULIN Prevents Liver Inflammation and Hepatocellular Carcinoma by Inhibiting FADD- and RIPK1 Kinase-Mediated Hepatocyte Apoptosis

Author

Verboom, Lien, primary, Martens, Arne, additional, Priem, Dario, additional, Hoste, Esther, additional, Sze, Mozes, additional, Vikkula, Hanna, additional, Van Hove, Lisette, additional, Voet, Sofie, additional, Roels, Jana, additional, Maelfait, Jonathan, additional, Bongiovanni, Laura, additional, de Bruin, Alain, additional, Scott, Charlotte L., additional, Saeys, Yvan, additional, Pasparakis, Manolis, additional, Bertrand, Mathieu J.M., additional, and van Loo, Geert, additional

Published
2020
Full Text
View/download PDF

18. Type III collagen affects dermal and vascular collagen fibrillogenesis and tissue integrity in a mutant Col3a1 transgenic mouse model

Author

D'hondt, Sanne, primary, Guillemyn, Brecht, additional, Syx, Delfien, additional, Symoens, Sofie, additional, De Rycke, Riet, additional, Vanhoutte, Leen, additional, Toussaint, Wendy, additional, Lambrecht, Bart N., additional, De Paepe, Anne, additional, Keene, Douglas R., additional, Ishikawa, Yoshihiro, additional, Bächinger, Hans Peter, additional, Janssens, Sophie, additional, Bertrand, Mathieu J.M., additional, and Malfait, Fransiska, additional

Published
2018
Full Text
View/download PDF

20. Correction: Experimental African trypanosome infection suppresses the development of multiple myeloma in mice by inducing intrinsic apoptosis of malignant plasma cells

Author

De Beule, Nathan, primary, Menu, Eline, additional, Bertrand, Mathieu J.M., additional, Favreau, Mérédis, additional, De Bruyne, Elke, additional, Maes, Ken, additional, De Veirman, Kim, additional, Radwanska, Magdalena, additional, Samali, Afshin, additional, Magez, Stefan, additional, Vanderkerken, Karin, additional, and De Trez, Carl, additional

Published
2018
Full Text
View/download PDF

22. Experimental African trypanosome infection suppresses the development of multiple myeloma in mice by inducing intrinsic apoptosis of malignant plasma cells

Author

De Beule, Nathan, primary, Menu, Eline, additional, Bertrand, Mathieu J.M., additional, Favreau, Mérédis, additional, De Bruyne, Elke, additional, Maes, Ken, additional, De Veirman, Kim, additional, Radwanska, Magdalena, additional, Samali, Afshin, additional, Magez, Stefan, additional, Vanderkerken, Karin, additional, and De Trez, Carl, additional

Published
2017
Full Text
View/download PDF

24. The Tumor Suppressor Hace1 Is a Critical Regulator of TNFR1-Mediated Cell Fate

Author

Tortola, Luigi, primary, Nitsch, Roberto, additional, Bertrand, Mathieu J.M., additional, Kogler, Melanie, additional, Redouane, Younes, additional, Kozieradzki, Ivona, additional, Uribesalgo, Iris, additional, Fennell, Lilian M., additional, Daugaard, Mads, additional, Klug, Helene, additional, Wirnsberger, Gerald, additional, Wimmer, Reiner, additional, Perlot, Thomas, additional, Sarao, Renu, additional, Rao, Shuan, additional, Hanada, Toshikatsu, additional, Takahashi, Nozomi, additional, Kernbauer, Elisabeth, additional, Demiröz, Duygu, additional, Lang, Michaela, additional, Superti-Furga, Giulio, additional, Decker, Thomas, additional, Pichler, Andrea, additional, Ikeda, Fumiyo, additional, Kroemer, Guido, additional, Vandenabeele, Peter, additional, Sorensen, Poul H., additional, and Penninger, Josef M., additional

Published
2016
Full Text
View/download PDF

25. Vaccination with Necroptotic Cancer Cells Induces Efficient Anti-tumor Immunity

Author

Aaes, Tania Løve, primary, Kaczmarek, Agnieszka, additional, Delvaeye, Tinneke, additional, De Craene, Bram, additional, De Koker, Stefaan, additional, Heyndrickx, Liesbeth, additional, Delrue, Iris, additional, Taminau, Joachim, additional, Wiernicki, Bartosz, additional, De Groote, Philippe, additional, Garg, Abhishek D., additional, Leybaert, Luc, additional, Grooten, Johan, additional, Bertrand, Mathieu J.M., additional, Agostinis, Patrizia, additional, Berx, Geert, additional, Declercq, Wim, additional, Vandenabeele, Peter, additional, and Krysko, Dmitri V., additional

Published
2016
Full Text
View/download PDF

26. NF-κB-Independent Role of IKKα/IKKβ in Preventing RIPK1 Kinase-Dependent Apoptotic and Necroptotic Cell Death during TNF Signaling

Author

Dondelinger, Yves, primary, Jouan-Lanhouet, Sandrine, additional, Divert, Tatyana, additional, Theatre, Emilie, additional, Bertin, John, additional, Gough, Peter J., additional, Giansanti, Piero, additional, Heck, Albert J.R., additional, Dejardin, Emmanuel, additional, Vandenabeele, Peter, additional, and Bertrand, Mathieu J.M., additional

Published
2015
Full Text
View/download PDF

28. Cellules souches et choix éthiques

Author

Bertrand, Mathieu J.M., Centre de recherche en droit constitutionnel (CRDC), and Université Paris 1 Panthéon-Sorbonne (UP1)

Subjects
[SHS.DROIT]Humanities and Social Sciences/Law, OS
Published
2006

29. Textes constitutionnels de la Vème République

Author

Bertrand, Mathieu J.M., Verpeaux, Michel, Rials, S., Centre de recherche en droit constitutionnel (CRDC), Université Paris 1 Panthéon-Sorbonne (UP1), Presses universitaires de France, and Matringe, Sophie

Subjects
[SHS.DROIT]Humanities and Social Sciences/Law, [SHS.DROIT] Humanities and Social Sciences/Law, ComputingMilieux_MISCELLANEOUS
Abstract

National audience

Published
2005

30. Chronique de jurisprudence constitutionnelle

Author

Bertrand, Mathieu J.M., Verpeaux, Michel, Centre de recherche en droit constitutionnel (CRDC), Université Paris 1 Panthéon-Sorbonne (UP1), and Matringe, Sophie

Subjects
[SHS.DROIT]Humanities and Social Sciences/Law, [SHS.DROIT] Humanities and Social Sciences/Law, ACLN
Published
2005

33. MLKL Compromises Plasma Membrane Integrity by Binding to Phosphatidylinositol Phosphates

Author

Dondelinger, Yves, primary, Declercq, Wim, additional, Montessuit, Sylvie, additional, Roelandt, Ria, additional, Goncalves, Amanda, additional, Bruggeman, Inge, additional, Hulpiau, Paco, additional, Weber, Kathrin, additional, Sehon, Clark A., additional, Marquis, Robert W., additional, Bertin, John, additional, Gough, Peter J., additional, Savvides, Savvas, additional, Martinou, Jean-Claude, additional, Bertrand, Mathieu J.M., additional, and Vandenabeele, Peter, additional

Published
2014
Full Text
View/download PDF

38. Smac Mimetic Bypasses Apoptosis Resistance in FADD- or Caspase-8-Deficient Cells by Priming for Tumor Necrosis Factor α-Induced Necroptosis

Author

Laukens, Bram, primary, Jennewein, Claudia, additional, Schenk, Barbara, additional, Vanlangenakker, Nele, additional, Schier, Alexander, additional, Cristofanon, Silvia, additional, Zobel, Kerry, additional, Deshayes, Kurt, additional, Vucic, Domagoj, additional, Jeremias, Irmela, additional, Bertrand, Mathieu J.M., additional, Vandenabeele, Peter, additional, and Fulda, Simone, additional

Published
2011
Full Text
View/download PDF

41. The autophagy protein RUBCNL/PACER represses RIPK1 kinase-dependent apoptosis and necroptosis.

Author

Rojas-Rivera, Diego, Beltrán, Sebastián, Muñoz-Carvajal, Francisco, Ahumada-Montalva, Pablo, Abarzúa, Lorena, Gomez, Laura, Hernandez, Fernanda, Bergmann, Cristian A., Labrador, Luis, Calegaro-Nassif, Melissa, Bertrand, Mathieu J.M., Manque, Patricio A., and Woehlbier, Ute

Abstract

Mesenchymal stem cells (MSCs) are used in cell therapy; nonetheless, their application is limited by their poor survival after transplantation in a proinflammatory microenvironment. Macroautophagy/autophagy activation in MSCs constitutes a stress adaptation pathway, promoting cellular homeostasis. Our proteomics data indicate that RUBCNL/PACER (RUN and cysteine rich domain containing beclin 1 interacting protein like), a positive regulator of autophagy, is also involved in cell death. Hence, we screened MSC survival upon various cell death stimuli under loss or gain of function of RUBCNL. MSCs were protected from TNF (tumor necrosis factor)-induced regulated cell death when RUBCNL was expressed. TNF promotes inflammation by inducing RIPK1 kinase-dependent apoptosis or necroptosis. We determine that MSCs succumb to RIPK1 kinase-dependent apoptosis upon TNF sensing and necroptosis when caspases are inactivated. We show that RUBCNL is a negative regulator of both RIPK1-dependent apoptosis and necroptosis. Furthermore, RUBCNL mutants that lose the ability to regulate autophagy, retain their function in negatively regulating cell death. We also found that RUBCNL forms a complex with RIPK1, which disassembles in response to TNF. In line with this finding, RUBCNL expression limits assembly of RIPK1-TNFRSF1A/TNFR1 complex I, suggesting that complex formation between RUBCNL and RIPK1 represses TNF signaling. These results provide new insights into the crosstalk between the RIPK1-mediated cell death and autophagy machineries and suggest that RUBCNL, due to its functional duality in autophagy and apoptosis/necroptosis, could be targeted to improve the therapeutic efficacy of MSCs. Abbreviations: BAF: bafilomycin A1; CASP3: caspase 3; Caspases: cysteine-aspartic proteases; cCASP3: cleaved CASP3; CQ: chloroquine; CHX: cycloheximide; cPARP: cleaved poly (ADP-ribose) polymerase; DEPs: differential expressed proteins; ETO: etoposide; MEF: mouse embryonic fibroblast; MLKL: mixed lineage kinase domain-like; MSC: mesenchymal stem cell; MTORC1: mechanistic target of rapamycin kinase complex 1; Nec1s: necrostatin 1s; NFKB/NF-kB: nuclear factor of kappa light polypeptide gene enhancer in B cells; PLA: proximity ligation assay; RCD: regulated cell death; RIPK1: receptor (TNFRSF)-interacting serine-threonine kinase 1; RIPK3: receptor-interacting serine-threonine kinase 3; RUBCNL/PACER: RUN and cysteine rich domain containing beclin 1 interacting protein like; siCtrl: small interfering RNA nonsense; siRNA: small interfering RNA; TdT: terminal deoxynucleotidyl transferase; Tm: tunicamycin; TNF: tumor necrosis factor; TNFRSF1A/TNFR1: tumor necrosis factor receptor superfamily, member 1a [ABSTRACT FROM AUTHOR]

Published
2024
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results