| Literature DB >> 11911824 |
A Ioan-Facsinay1, S J de Kimpe, S M M Hellwig, P L van Lent, F M A Hofhuis, H H van Ojik, C Sedlik, S A da Silveira, J Gerber, Y F de Jong, R Roozendaal, L A Aarden, W B van den Berg, T Saito, D Mosser, S Amigorena, S Izui, G J B van Ommen, M van Vugt, J G J van de Winkel, J S Verbeek.
Abstract
The high-affinity receptor for IgG, FcgammaRI, shares its capacity to bind IgG2a immune complexes (IgG2a-IC) with the low-affinity receptor FcgammaRIII and complement factors, hampering the definition of its biological role. Moreover, in vivo, FcgammaRI is occupied by monomeric IgG2a, reducing its accessibility to newly formed IgG2a-IC. By using a variety of FcgammaR(-/-) mice, we demonstrate that in the absence of FcgammaRI, the IgG2a-IC-induced cellular processes of phagocytosis, cytokine release, cellular cytotoxicity, and antigen presentation are impaired. FcgammaRI(-/-) mice showed impaired hypersensitivity responses, strongly reduced cartilage destruction in an arthritis model, and impaired protection from a bacterial infection. We conclude that FcgammaRI contributes substantially to a variety of IgG2a-IC-dependent immune functions and immunopathological responses.Entities:
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Year: 2002 PMID： 11911824 DOI： 10.1016/s1074-7613(02)00294-7
Source DB: PubMed Journal: Immunity ISSN： 1074-7613 Impact factor: 31.745