Reference Database

YearReference
2002
FcgammaRI (CD64) contributes substantially to severity of arthritis, hypersensitivity responses, and protection from bacterial infection.
Ioan-Facsinay, A
de Kimpe, S J
Hellwig, S M M
van Lent, P L
Hofhuis, F M A
van Ojik, H H
Sedlik, C
da Silveira, S A
Gerber, J
de Jong, Y F
Roozendaal, R
Aarden, L A
van den Berg, W B
Saito, T
Mosser, D
Amigorena, S
Izui, S
van Ommen, G J B
van Vugt, M
van de Winkel, J G J
Verbeek, J S
Immunity 2002 Mar;16: 391-402
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.

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