(~10-8‑10-9 M) capable of binding monomeric IgG, whereas the CD16 and CD32 proteins bind IgG with lower affinities (~10-6‑10-7 M) only recognizing IgG aggregates surrounding multivalent antigens (1, 4). Fc gamma Rs that deliver an activating signal either have an intrinsic immunoreceptor tyrosine-based activation motif (ITAM) within their cytoplasmic domains or associate with one of the ITAM-bearing adapter subunits, FcR gamma or zeta (3, 5). The only inhibitory member in human and mouse, Fc gamma RIIB, has an intrinsic cytoplasmic immunoreceptor tyrosine-based inhibitory motif (ITIM). The coordinated functioning of activating and inhibitory receptors is necessary for successful initiation, amplification, and termination of immune responses (5).
Three distinct genes encode the human CD32 group, and the protein products are designated Fc gamma RIIA, B, and C (1). These receptors are glycoproteins of approximately 40 kDa having two extracellular Ig-like domains. The Fc gamma RII proteins share 94‑99% amino acid identity in their extracellular domains but differ substantially in their transmembrane and cytoplasmic domains. Fc gamma RIIA associates with FcR gamma, and delivers an activating signal upon ligand binding (3, 5). In contrast, Fc gamma RIIB delivers an inhibitory signal. Fc gamma RIIC represents an unequal cross-over event between the IIA and IIB genes. Its extracellular domain shares 99% amino acid identity with Fc gamma RIIB, but a portion of the cytoplasmic domain is closely related to Fc gamma RIIA. Fc gamma RII proteins are expressed on cells of both myeloid and lymphoid lineages as well as on cells of non-hematopoietic origin.
Powered by Bioz
