FcgammaRI (CD64) contributes substantially to severity of arthritis, hypersensitivity responses, and protection from bacterial infection

Autor: M van Vugt, Takashi Saito, H.H van Ojik, Shozo Izui, Sandra M. M. Hellwig, G-J B van Ommen, Lucien A. Aarden, J. Gerber, R. Roozendaal, W.B. van den Berg, David M. Mosser, S.A da Silveira, S. de Kimpe, Andreea Ioan-Facsinay, Y.F de Jong, Christine Sedlik, Frans M. A. Hofhuis, J.G.J. van de Winkel, J. S. Verbeek, Sebastian Amigorena, P.L.E.M. van Lent
Přispěvatelé: Landsteiner Laboratory, Infectious diseases
Rok vydání: 2002
Předmět:
Zdroj: Immunity, 16, 391-402
Immunity, Vol. 16, No 3 (2002) pp. 391-402
Immunity, 16(3), 391-402. Cell Press
Immunity, 16, 3, pp. 391-402
ISSN: 1074-7613
Popis: Item does not contain fulltext 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.
Databáze: OpenAIRE