Two groups of receptors for immunoglobulin G (Fc gamma R) can be disti
nguished. Endothelial cells and placental syncytiotrophoblasts express
an MHC class I-like Fc gamma R important for regulation of IgG half-l
ife and IgG transport, respectively. Fc gamma R expressed on leukocyte
s constitute a heterogeneous family of membrane bound and soluble prot
eins. The various Fc gamma R (sub) classes of this family differ in li
gand affinity and specificity, which is determined by primary structur
e, glycosylation, association with signaling subunits, and environment
al factors (such as serine proteases). The finding that polymorphisms
of Fc gamma RIIa. Fc gamma RIIIa, and Fc gamma RIIIb critically affect
interaction with antibodies has prompted analysis in patients which p
rovided tantalizing evidence for the relevance of Fc gamma R polymorph
isms as risk factors for a number of infectious and autoimmune disease
s.