| First Author | Ioan-Facsinay A | Year | 2002 |
| Journal | Immunity | Volume | 16 |
| Issue | 3 | Pages | 391-402 |
| PubMed ID | 11911824 | Mgi Jnum | J:83995 |
| Mgi Id | MGI:2664488 | Doi | 10.1016/s1074-7613(02)00294-7 |
| Citation | Ioan-Facsinay A, et al. (2002) FcgammaRI (CD64) contributes substantially to severity of arthritis, hypersensitivity responses, and protection from bacterial infection. Immunity 16(3):391-402 |
| abstractText | 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. |
