Human IgG Fc receptor heterogeneity: molecular aspects and clinical implications.
Receptors for the Fc domain of IgG (Fc gamma R) provide a critical link between specific humoral responses and the cellular branch of the immune system. When hFc gamma R interact with immunoglobulin, a variety of biological responses are triggered. These include phagocytosis, endocytosis, antibody-dependent cellular cytotoxicity (ADCC), release of inflammatory mediators, and enhancement of antigen presentation. In the last few years our understanding of the Fc gamma receptor structure has increased dramatically, due to the availability of monoclonal antibodies (mAb) and cDNA probes. Fc gamma R are members of the immunoglobulin superfamily and three main classes, hFc gamma RI, hFc gamma RII, and hFc gamma RIII are recognized in man generating at least 12 different isoforms. A further level of complexity is introduced by various genetic polymorphisms and, importantly, recent evidence points at the relevance of this Fc gamma R heterogeneity.
Dept of Immunology, University Hospital Utrecht, The Netherlands.
J G
JG
van de Winkel
P J
PJ
Capel
D000920:Antibody-Dependent Cell Cytotoxicity / Q000276:immunology; D000938:Antigen-Presenting Cells / Q000276:immunology; D004705:Endocytosis / Q000276:immunology; D005803:Genes, Immunoglobulin; D006801:Humans; D007074:Immunoglobulin G / Q000235:genetics / Q000276:immunology*; D016130:Immunophenotyping; D010587:Phagocytosis / Q000276:immunology; D011110:Polymorphism, Genetic; D017452:Receptors, IgG / Q000235:genetics / Q000276:immunology*
D007074:Immunoglobulin G; D017452:Receptors, IgG