Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Monique Synguelakis"'
Autor:
Jean Kanellopoulos, Sonja von Aulock, Andrew N. J. McKenzie, Jean-Michel Sallenave, Elvira Garcia-de-Paco, Ignacio Garcia-Verdugo, Quentin Espinassous, Monique Synguelakis
Publikováno v:
The Journal of Immunology. 183:1446-1455
Bacterial LPS triggers monocytes and macrophages to produce several inflammatory cytokines and mediators. However, once exposed to LPS, they become hyporesponsive to a subsequent endotoxin challenge. This phenomenon is defined as LPS desensitization
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf687b33205cca2e7b04d4b1881f2f65
https://doi.org/10.4049/jimmunol.0803067
https://doi.org/10.4049/jimmunol.0803067
Autor:
Jesús Pérez-Gil, Ignacio Garcia-Verdugo, Richard Chaby, Jean Kanellopoulos, Elvira Garcia de Paco, Quentin Espinassous, Azucena González-Horta, Monique Synguelakis, Luis Rivas
Publikováno v:
Innate Immunity. 15:53-62
Surfactant protein C (SP-C) consists of a hydrophobic α-helix inserted in pulmonary surfactant membranes, and a more polar N-terminal palmitoylated segment exposed to the aqueous phase. Previously, we showed that SP-C inserted in lipid vesicles inte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f649c0586e57c17f1fb152fa53b4654
https://doi.org/10.1177/1753425908100500
https://doi.org/10.1177/1753425908100500
Publikováno v:
Biology of the Cell
Summary A major antigen of the brush border membrane of Torpedo marmorata kidney was identified and purified by immunoprecipitation. The sequence of its 18 N terminal amino acids was determined and found to be very similar to that of mammalian aminop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4ce3bc7ad36413a89016ea7e6650102
http://europepmc.org/articles/PMC7131328
http://europepmc.org/articles/PMC7131328
Structural Basis for Interactions between Lung Surfactant Protein C and Bacterial Lipopolysaccharide
Publikováno v:
Journal of Biological Chemistry. 277:23484-23492
In the respiratory tract, recognition of bacterial endotoxin (lipopolysacharide, LPS) is a critical step of the innate host defense system directed against invading pathogens. Secretions of the airways contain proteins that have direct antimicrobial
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d339ca06be24d982ed59e68adbc20374
https://doi.org/10.1074/jbc.m111925200
https://doi.org/10.1074/jbc.m111925200
Publikováno v:
Neurochemistry International. 29:659-667
Two proteins of the presynaptic plasma membrane, syntaxin and SNAP 25, and VAMP/synaptobrevin, a synaptic vesicle membrane protein, form stable protein complexes which are involved in the docking and fusion of synaptic vesicles at the mammalian brain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f8208851e2fae3b1dbcfc486544ac68
https://doi.org/10.1016/s0197-0186(96)00026-5
https://doi.org/10.1016/s0197-0186(96)00026-5
Autor:
Andrea Ravasio, Elvira Garcia de Paco, Thomas Haller, Ignacio Garcia-Verdugo, Nina Ivanova, Jean Kanellopoulos, Monique Synguelakis
Publikováno v:
American journal of physiology. Lung cellular and molecular physiology. 295(4)
Bacterial LPS is a potent proinflammatory molecule. In the lungs, LPS induces alterations in surfactant pool sizes and phospholipid (PL) contents, although direct actions of LPS on the alveolar type II cells (AT II) are not yet clear. For this reason
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a85ce6d1a6c8196db4b7dd44d27a0862
https://pubmed.ncbi.nlm.nih.gov/18689605
https://pubmed.ncbi.nlm.nih.gov/18689605
Autor:
Benoit Valot, Jeril Degrouard, Richard Chaby, Claudio-Areias Franco, Ignacio Garcia-Verdugo, Michel Zivy, Zahra Tanfin, Monique Synguelakis
Publikováno v:
Biochemistry. 47(18)
Surfactant protein A (SP-A), a member of the collectin family that modulates innate immunity, has recently been involved in the physiology of reproduction. Consistent with the activation of ERK-1/2 and COX-2 induced by SP-A in myometrial cells, we re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7e8bbaee005b599d96051ee4e9c582f
https://pubmed.ncbi.nlm.nih.gov/18407667
https://pubmed.ncbi.nlm.nih.gov/18407667
Autor:
Richard Chaby, Monique Synguelakis, Jan Johansson, Michel Lepoivre, Quentin Espinassous, Luis A. Augusto
Publikováno v:
American journal of respiratory and critical care medicine. 168(3)
The respiratory system is continuously exposed to airborne particles containing lipopolysaccharide. Our laboratory established previously that the hydrophobic surfactant protein C (SP-C) binds to lipopolysaccharide and to one of its cellular receptor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82d625073a0b03e41b897c1f155a4053
https://pubmed.ncbi.nlm.nih.gov/12773323
https://pubmed.ncbi.nlm.nih.gov/12773323
Autor:
Pierre Le Maréchal, Paulette Decottignies, Magali Nicaise, Richard Chaby, Monique Synguelakis, Luis A. Augusto
Publikováno v:
Biochemistry. 42(13)
Unlike soluble and membrane forms of lipopolysaccharide (LPS)-binding proteins, intracellular LPS-binding molecules are poorly documented. We looked for such molecules in a murine lung epithelial cell line. Two proteins with LPS-binding activity were
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a292d2ec5b687962a663ec2a7b2ca6c
https://pubmed.ncbi.nlm.nih.gov/12667084
https://pubmed.ncbi.nlm.nih.gov/12667084
Autor:
Thierry Pedron, Richard Chaby, Luis A. Augusto, Jan Johansson, Robert Girard, Monique Synguelakis
Publikováno v:
Infection and immunity. 71(1)
In addition to their effects on alveolar surface tension, some components of lung surfactant also have immunological functions. We found recently that the hydrophobic lung surfactant protein SP-C specifically binds to the lipid A region of lipopolysa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef084484413de01ecb7c11d6dcdb3699
https://pubmed.ncbi.nlm.nih.gov/12496149
https://pubmed.ncbi.nlm.nih.gov/12496149