Search

Your search keyword '"Pocidalo, Marie-Anne"' showing total 171 results
Start Over Author "Pocidalo, Marie-Anne" Search Limiters Available in Library Collection
171 results on '"Pocidalo, Marie-Anne"'

2. Serpin B1 defect and increased apoptosis of neutrophils in Cohen syndrome neutropenia

Author

Duplomb, Laurence, Rivière, Julie, Jego, Gaëtan, Da Costa, Romain, Hammann, Arlette, Racine, Jessica, Schmitt, Alain, Droin, Nathalie, Capron, Claude, Gougerot-Pocidalo, Marie-Anne, Dubrez, Laurence, Aral, Bernard, Lafon, Arnaud, Edery, Patrick, Ghoumid, Jamal, Blair, Edward, El Chehadeh-Djebbar, Salima, Carmignac, Virginie, Thevenon, Julien, Guy, Julien, Girodon, François, Bastie, Jean-Noël, Delva, Laurent, Faivre, Laurence, Thauvin-Robinet, Christel, and Solary, Eric

Published
2019
Full Text
View/download PDF

3. Pyogenic Bacterial Infections in Humans with IRAK-4 Deficiency

Author

Picard, Capucine, Puel, Anne, Bonnet, Marion, Ku, Cheng-Lung, Bustamante, Jacinta, Yang, Kun, Soudais, Claire, Dupuis, Stéphanie, Feinberg, Jacqueline, Fieschi, Claire, Elbim, Carole, Hitchcock, Remi, Lammas, David, Davies, Graham, Al-Ghonaium, Abdulaziz, Al-Rayes, Hassan, Al-Jumaah, Sulaiman, Al-Hajjar, Sami, Al-Mohsen, Ibrahim Zaid, Frayha, Husn H., Rucker, Rajivi, Hawn, Thomas R., Aderem, Alan, Tufenkeji, Haysam, Haraguchi, Soichi, Day, Noorbibi K., Good, Robert A., Gougerot-Pocidalo, Marie-Anne, Ozinsky, Adrian, and Casanova, Jean-Laurent

Published
2003

7. Impaired p47phox phosphorylation in neutrophils from p67phox-deficient chronic granulomatous disease patients Short title: p67phox regulates p47phox phosphorylation

Author

Belambri, Sahra Amel, Marzaioli, Viviana, Hurtado-Nedelec, Margarita, Pintard, Coralie, Liang, Shiyu, Liu, Yezhou, Boussetta, Tarek, Gougerot-Pocidalo, Marie-Anne, Ye, Richard, Dang, Pham My-Chan, El-Benna, Jamel, DANG, Pham My-Chan, Centre de recherche sur l'Inflammation (CRI (UMR_S_1149 / ERL_8252 / U1149)), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), Laboratoire d'Excellence INFLAMEX [Paris], Université Sorbonne Paris Cité (USPC), AP-HP - Hôpital Bichat - Claude Bernard [Paris], and Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)

Subjects
PHAGOCYTES, GRANULOCYTES, AND MYELOPOIESIS, [SDV.IMM.II] Life Sciences [q-bio]/Immunology/Innate immunity, [SDV.IMM.II]Life Sciences [q-bio]/Immunology/Innate immunity
Abstract

International audience; Abstract Superoxide production by the phagocyte reduced NAD phosphate (NADPH) oxidase is essential for innate immunity as shown in chronic granulomatous disease (CGD), an immunodeficiency disease resulting from mutations in 1 of its genes. The NADPH oxidase is composed of 2 membrane proteins (gp91phox/NOX2 and p22phox) and 4 cytosolic proteins (p47phox, p67phox, p40phox, and Rac1/2). The phosphorylation of p47phox is required for NADPH oxidase activation in cells. As p47phox and p67phox can form a tight complex in cells, we hypothesized that p67phox could regulate p47phox phosphorylation. To investigate this hypothesis, we used phospho-specific antibodies against 5 major p47phox-phosphorylated sites (Ser304, Ser315, Ser320, Ser328, and Ser345) and neutrophils from healthy donors and from p67phox−/− CGD patients. Results showed that formyl-methionyl-leucyl-phenylalanine and phorbol myristate acetate induced a time- and a concentration-dependent phosphorylation of p47phox on Ser304, Ser315, Ser320, and Ser328 in healthy human neutrophils. Interestingly, in neutrophils and Epstein-Barr virus-transformed B lymphocytes from p67phox−/− CGD patients, phosphorylation of p47phox on serine residues was dramatically reduced. In COSphox cells, the presence of p67phox led to increased phosphorylation of p47phox. In vitro studies showed that recombinant p47phox was phosphorylated on Ser304, Ser315, Ser320, and Ser328 by different PKC isoforms and the addition of recombinant p67phox alone or in combination with p40phox potentiated this process. Thus, p67phox and p40phox are required for optimal p47phox phosphorylation on Ser304, Ser315, Ser320, and Ser328 in intact cells. Therefore, p67phox and p40phox are novel regulators of p47phox-phosphorylation.

Published
2022
Full Text
View/download PDF

9. The protein kinase A negatively regulates reactive oxygen species production by phosphorylating gp91phox/NOX2 in human neutrophils

Author

El Benna, Jamel, Raad, Houssam, Mouawia, Hussein, Hassan, Hamad, El-Seblani, Mohamed, Arabi-Derkawi, Riad, Boussetta, Tarek, Gougerot-Pocidalo, Marie-Anne, Dang, Pham My-Chan, El-Benna, Jamel, Lab Excellence Inflamex (CRI INSERM U1149 - Bichat Medical Faculty), Université Paris Diderot - Paris 7 (UPD7), Centre de recherche sur l'Inflammation (CRI (UMR_S_1149 / ERL_8252 / U1149)), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP), and Medical Care Laboratory, Lebanese University, Faculty of the Public Health IV, Zahle, Lebanon

Subjects
0301 basic medicine, Neutrophils, [SDV.IMM.II]Life Sciences [q-bio]/Immunology/Innate immunity, Biochemistry, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Physiology (medical), Humans, Phosphorylation, Protein kinase A, Protein kinase C, ComputingMilieux_MISCELLANEOUS, chemistry.chemical_classification, Reactive oxygen species, Phagocytes, NADPH oxidase, biology, Superoxide, Activator (genetics), NADPH Oxidases, Phosphoproteins, Cyclic AMP-Dependent Protein Kinases, Cell biology, 030104 developmental biology, chemistry, NADPH Oxidase 2, biology.protein, [SDV.IMM]Life Sciences [q-bio]/Immunology, P22phox, Reactive Oxygen Species, 030217 neurology & neurosurgery
Abstract

Superoxide anion production by neutrophils is essential for host defense against microbes. Superoxide anion generates other reactive oxygen species (ROS) that are very toxic for microbes and host cells, therefore their excessive production could induce inflammatory reactions and tissue injury. Cyclic adenosine monophosphate (cAMP) elevating agents are considered to be physiological inhibitors of superoxide production by neutrophils but the mechanisms involved in this inhibitory effect are poorly understood. Superoxide is produced by the phagocyte NADPH oxidase, a complex enzyme composed of two membrane subunits, gp91phox or NOX2 and p22phox, and four cytosolic components p47phox, p67phox, p40phox, and Rac2. Except Rac2, these proteins are known to be phosphorylated upon neutrophil stimulation. Here we show that forskolin, an activator of the adenylate cyclase-cAMP-PKA pathway, induced phosphorylation of gp91phox/NOX2 and inhibited fMLF-induced NADPH oxidase activation in human neutrophils. H89, a PKA inhibitor prevented the forskolin-induced phosphorylation of gp91phox and restored NADPH oxidase activation. Furthermore, PKA phosphorylated the recombinant gp91phox/NOX2-cytosolic C-terminal region in vitro only on a few specific peptides containing serine residues, as compared to PKC. Interestingly, phosphorylation of NOX2-Cter by PKA alone did not induce interaction with the cytosolic components p47phox, p67phox and Rac2, however it induced inhibition of PKC-induced interaction. Furthermore, PKA alone did not induce NOX2 electron transfer activity, however it inhibited PKC-induced activation. These results suggest that PKA phosphorylates NOX2 in human neutrophils, a process essential to limit ROS production and inflammation under physiological conditions. Our data identify the cAMP-PKA-NOX2-axis as a critical gatekeeper of neutrophil ROS production.

Published
2020
Full Text
View/download PDF

10. A specific [p47.sup.phox]-serine phosphorylated by convergent MAPKs mediates neutrophil NADPH oxidase priming at inflammatory sites

Author

Dang, Pham My-Chan, Stensballe, Allan, Boussetta, Tarek, Raad, Houssam, Dewas, Cedric, Kroviarski, Yolande, Hayem, Gilles, Jensen, Ole N., Gougerot-Pocidalo, Marie-Anne, and El-Benna, Jamel

Subjects
Rheumatoid arthritis -- Care and treatment, Enzyme activation -- Methods, Protein kinases -- Chemical properties, Neutrophils -- Chemical properties, NADP (Coenzyme) -- Chemical properties, Phosphorylation -- Methods, Phosphorylation -- Research, Enzymes -- Structure-activity relationship
Abstract

Neutrophil NADPH oxidase plays a key role in host defense and in inflammation by releasing large amounts of superoxide and other ROSs. Proinflammatory cytokines such as GM-CSF and TNF-[alpha] prime [...]

Published
2006

19. Increased neutrophil apoptosis in chronically SIV-infected macaques

Author

Gougerot-Pocidalo Marie-Anne, Hurtrel Bruno, François Stéphanie, Monceaux Valérie, Elbim Carole, and Estaquier Jérome

Subjects
Immunologic diseases. Allergy, RC581-607
Abstract

Abstract Polymorphonuclear neutrophils (PMN) from chronically HIV-infected individuals have been reported to be more prone to die. However, although non-human primates models have been extensively used for improving our knowledge on T cell immunity, the impact of SIV-infection on PMN, in relationships with disease severity, has never been assessed. In our study, we demonstrate that PMN from Rhesus macaques (RMs) of Chinese origin chronically infected with the virulent strain SIVmac251 display increased susceptibility to undergo apoptosis as compared to PMN from RMs infected with the non-pathogenic SIVΔnef strain. PMN apoptosis was significantly increased in RMs progressing faster to AIDS as compared to non-progressors RMs. Furthermore, the percentage of apoptotic cells correlated with PMN activation state reflected by increased CD11b expression and reactive oxygen species production. Interestingly, whereas inflammatory cytokines IL-8 and IL-1β prevent in vitro PMN death, the levels of those cytokines were low in RMs progressing towards AIDS. Altogether, increased PMN death during SIV infection is a new pathogenic effect associated with AIDS progression, adding to the long list of markers associated with disruption of defense against infection.

Published
2009
Full Text
View/download PDF

22. Aspergillus-induced pneumonia in adult without obvious immunodeficiency: test the burst!

Author

Flament, Héloïse, primary, Granger, Vanessa, additional, Vezinet, Corinne, additional, Marzaioli, Viviana, additional, Kannengiesser, Caroline, additional, de Chaisemartin, Luc, additional, Hurtado-Nedelec, Margarita, additional, Litvinova, Elena, additional, Messika, Jonathan, additional, Adam, Nicolas, additional, Gougerot-Pocidalo, Marie-Anne, additional, Dang, Pham My-Chan, additional, Monteiro, Renato, additional, el Benna, Jamel, additional, Langeron, Olivier, additional, Chollet-Martin, Sylvie, additional, and Monsel, Antoine, additional

Published
2018
Full Text
View/download PDF

27. Phosphorylation of p47phox is required for receptor-mediated NADPH oxidase/NOX2 activation in Epstein-Barr virus-transformed human B lymphocytes

Author

Belambri, Sahra Amel, Hurtado-Nedelec, Margarita, Senator, Abderrahmane, Makni-Maalej, Karama, Fay, Michèle, Gougerot-Pocidalo, Marie-Anne, Marie, Jean-Claude, Dang, Pham My-Chan, and El-Benna, Jamel

Subjects
urogenital system, cardiovascular system, Original Article, hormones, hormone substitutes, and hormone antagonists, circulatory and respiratory physiology
Abstract

The phagocyte NADPH oxidase (NOX2) is known to be expressed in Epstein-Barr virus (EBV)-transformed human B lymphocytes. Phosphorylation of the NOX2 cytosolic subunit p47phox is required for phorbol myristate acetate (PMA)-induced NOX2 activation in EBV-transformed B lymphocytes, however the role of this process in receptor-mediated NOX2 activation is not known. Here, we used pansorbin which acts by cross linking cell surface IgG and transfected cells with mutated p47phox to address if the phosphorylation of this subunit is required for receptor-mediated NOX2 activation. We show that pansorbin induced NOX2 activation in a time and concentration-dependent manner, albeit at levels only of 20% of those induced by PMA. GF109203X, a PKC selective inhibitor, inhibited pansorbin as well as PMA-induced NOX2 activation. Using specific anti-phospho serine antibodies we showed that pansorbin induced p47phox phosphorylation on Ser304, 315, 320, 328, and 345 and kinetics of these phosphorylations preceed NOX2 activation. To determine whether the phosphorylation of p47phox is required for pansorbin-induced NOX2 activation, we transfected EBV-transformed lymphocytes deficent in p47phox with a plasmid expressing wild type p47phox or p47phox with all the phosphorylated serines mutated to alanines, p47phoxS(303-379)A. Results show that pansorbin-induced NOX2 activation was greatly decreased in lymphocytes expressing the mutant as compared to the wild-type p47phox. These results show that pansorbin induced p47phox phosphorylation on multiple sites in EBV-transformed B lymphocytes and this process is required for pansorbin-induced NADPH oxidase activation in these cells.

Published
2012

29. Pulmonary manifestations in adult patients with chronic granulomatous disease

Author

Salvator, Hélène, primary, Mahlaoui, Nizar, additional, Catherinot, Emilie, additional, Rivaud, Elisabeth, additional, Pilmis, Benoit, additional, Borie, Raphael, additional, Crestani, Bruno, additional, Tcherakian, Colas, additional, Suarez, Felipe, additional, Dunogue, Bertrand, additional, Gougerot-Pocidalo, Marie-Anne, additional, Hurtado-Nedelec, Margarita, additional, Dreyfus, Jean-François, additional, Durieu, Isabelle, additional, Fouyssac, Fanny, additional, Hermine, Olivier, additional, Lortholary, Olivier, additional, Fischer, Alain, additional, and Couderc, Louis-Jean, additional

Published
2015
Full Text
View/download PDF

30. Gene- and exon-expression profiling reveals an extensive LPS-induced response in immune cells in patients with cirrhosis.

Author

Gandoura, Sonia, Weiss, Emmanuel, Rautou, Pierre-Emmanuel, Fasseu, Magali, Gustot, Thierry, Lemoine, Frédéric, Hurtado-Nedelec, Margarita, Hego, Caroline, Vadrot, Nathalie, Elkrief, Laure, Lettéron, Philippe, Tellier, Zéra, Pocidalo, Marie-Anne, Valla, Dominique, Lebrec, Didier, Groyer, André, Monteiro, Renato C, de la Grange, Pierre, Moreau, Richard, Gandoura, Sonia, Weiss, Emmanuel, Rautou, Pierre-Emmanuel, Fasseu, Magali, Gustot, Thierry, Lemoine, Frédéric, Hurtado-Nedelec, Margarita, Hego, Caroline, Vadrot, Nathalie, Elkrief, Laure, Lettéron, Philippe, Tellier, Zéra, Pocidalo, Marie-Anne, Valla, Dominique, Lebrec, Didier, Groyer, André, Monteiro, Renato C, de la Grange, Pierre, and Moreau, Richard

Abstract

Lipopolysaccharide (LPS)-expressing bacteria cause severe inflammation in cirrhotic patients. The global gene response to LPS is unknown in cirrhotic immune cells., Journal Article, Research Support, Non-U.S. Gov't, info:eu-repo/semantics/published

Published
2013

37. NAD(P)H Oxidase Nox-4 Mediates 7-Ketocholesterol-Induced Endoplasmic Reticulum Stress and Apoptosis in Human Aortic Smooth Muscle Cells

Author

Pedruzzi, Eric, primary, Guichard, Cécile, additional, Ollivier, Véronique, additional, Driss, Fathi, additional, Fay, Michèle, additional, Prunet, Céline, additional, Marie, Jean-Claude, additional, Pouzet, Cécile, additional, Samadi, Mohammad, additional, Elbim, Carole, additional, O'Dowd, Yvonne, additional, Bens, Marcelle, additional, Vandewalle, Alain, additional, Gougerot-Pocidalo, Marie-Anne, additional, Lizard, Gérard, additional, and Ogier-Denis, Eric, additional

Published
2004
Full Text
View/download PDF

41. P40phox associates with the neutrophil Triton X-100-insoluble cytoskeletal fraction and PMA-activated membrane skeleton: a comparative study with P67phox and P47phox

Author

Benna, Jamel El, primary, Dang, Pham My-chan, additional, Andrieu, Valérie, additional, Vergnaud, Sabrina, additional, Dewas, Cedric, additional, Cachia, Odile, additional, Fay, Michèle, additional, Morel, Françoise, additional, Chollet-Martin, Sylvie, additional, Hakim, Jacques, additional, and Gougerot-Pocidalo, Marie-Anne, additional

Published
1999
Full Text
View/download PDF

43. Human Immunodeficiency Virus Induces a Dual Regulation of Bcl-2, Resulting in Persistent Infection of CD4 + T- or Monocytic Cell Lines

Author

Aillet, Fabienne, primary, Masutani, Hiroshi, additional, Elbim, Carole, additional, Raoul, Hervé, additional, Chêne, Laurent, additional, Nugeyre, Marie-Thérèse, additional, Paya, Carlos, additional, Barré-Sinoussi, Françoise, additional, Gougerot-Pocidalo, Marie-Anne, additional, and Israël, Nicole, additional

Published
1998
Full Text
View/download PDF

50. ASK1-p38 MAPK-p47phox activation is essential for inflammatory responses during tuberculosis via TLR2-ROS signalling.

Author

Chul-Su Yang, Dong-Min Shin, Hye-Mi Lee, Ji Woong Son, Sung Joong Lee, Akira, Shizuo, Gougerot-Pocidalo, Marie-Anne, El-Benna, Jamel, Ichijo, Hidenori, and Eun-Kyeong Jo

Subjects
TUBERCULIN, PROTEINS, CELL receptors, APOPTOSIS, TUBERCULOSIS, INFECTION, MITOGEN-activated protein kinases, PATIENTS, REACTIVE oxygen species, INFLAMMATION, MYCOBACTERIAL diseases, MACROPHAGES
Abstract

The roles of intracellular reactive oxygen species (ROS) and related signalling pathways in mycobacterial infection are largely unknown. Here we show that tuberculin purified protein derivative (PPD)/Toll-like receptor (TLR) 2/ROS signalling through activation of apoptosis-regulating signal kinase (ASK) 1 and p47phox pathways is responsible for the induction of proinflammatory responses during tuberculosis (TB) infection. Tuberculin PPD stimulation resulted in rapid activation of mitogen-activated protein kinases (MAPKs) and an early burst of ROS in monocytes/macrophages in a TLR2-dependent manner. PPD-induced ROS production led to robust activation of ASK1 upstream of p38 MAPK, via TLR2. Interestingly, phosphorylation of the cytosolic NADPH oxidase subunit p47phox and ASK1 activation are mutually dependent on PPD/TLR2-mediated signalling. Furthermore, active pulmonary TB patients showed upregulated ROS generation, as well as enhanced activation of ASK1/p38/p47phox pathways in their primary monocytes compared with healthy controls, which suggests a systemic primed status during TB. Taken together, these results indicate that activation of the ASK1/p38 MAPK/p47phox cascade plays a central role in PPD/TLR2-induced ROS generation and suggests the existence of a ‘ROS/ASK1’ inflammatory amplification feedback loop in monocytes/macrophages. The altered regulation of this axis with an increasing free-radical burden may contribute to the immunopathogenesis of human TB. [ABSTRACT FROM AUTHOR]

Published
2008
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results