van der Pol W, van de Winkel J G
Department of Immunology, Utrecht University, G04.614, Heidelberglaan 100, 3584 CX Utrecht, The Netherlands.
Immunogenetics. 1998 Aug;48(3):222-32. doi: 10.1007/s002510050426.
Two groups of receptors for immunoglobulin G (FcgammaR) can be distinguished. Endothelial cells and placental syncytiotrophoblasts express an MHC class I-like FcgammaR important for regulation of IgG half-life and IgG transport, respectively. FcgammaR expressed on leukocytes constitute a heterogeneous family of membrane bound and soluble proteins. The various FcgammaR (sub) classes of this family differ in ligand affinity and specificity, which is determined by primary structure, glycosylation, association with signaling subunits, and environmental factors (such as serine proteases). The finding that polymorphisms of FcgammaRIIa, FcgammaRIIIa, and FcgammaRIIIb critically affect interaction with antibodies has prompted analysis in patients which provided tantalizing evidence for the relevance of FcgammaR polymorphisms as risk factors for a number of infectious and autoimmune diseases.
