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dc.contributor.authorBonnerot, Cfr_FR
dc.contributor.authorFriedmann, Hfr_FR
dc.date.accessioned2013-02-18T16:16:58Z
dc.date.available2013-02-18T16:16:58Z
dc.date.issued1993fr_FR
dc.identifier.citationBonnerot, C ; Friedmann, H, Bases moléculaires de la diversité fonctionnelle des récepteurs des anticorps., Med Sci (Paris), 1993, Vol. 9, N° 11; p.1236-42.fr_FR
dc.identifier.issn1958-5381fr_FR
dc.identifier.urihttp://hdl.handle.net/10608/2837
dc.description.abstractThe low-affinity receptors for the Fe portion of IgC (Fc gamma R) are expressed on most of the cells of the immune system. They bind immune complexes but not monomeric IgC. These receptors are a family of surface glycoproteins tells with homologous extrac lar domains and different transmembrane and cytoplasmic portion. They mediate the biological activities of antibodies bound at the surface of all the immune cells: Fc gamma Rs activate macrophages, neutrophils and NK cells, participating in antibody-dependent cellular cytotoxicity; Fc gamma Rs activate mast cells, resulting in the release of inflammation mediators and the induction of cytokines; in B cells, on the contrary, cross-linking of Fc gamma R and IgM blocks cellular activation, inhibiting Ige production. Fc gamma Rs are also involved in ligand internalization and the clearing of immune complexes.fr
dc.language.isofrfr_FR
dc.publisherJohn Libbey Eurotext, Montrougefr_FR
dc.rightsArticle en libre accèsfr
dc.rightsMédecine/Sciences - Inserm - SRMSfr
dc.sourceM/S. Médecine sciences [revue papier, ISSN : 0767-0974], 1993, Vol. 9, N° 11; p.1236-42.fr_FR
dc.titleBases moléculaires de la diversité fonctionnelle des récepteurs des anticorps.fr
dc.typeArticlefr_FR
dc.identifier.doi10.4267/10608/2837


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