| Background | Human FcγRs are divided into three classes designated FcγRI (CD64), FcγRII (CD32), and FcγRIII (CD16), which generate multiple isoforms, are recognized. The activating type receptor either has or associates noncovalently with an accessory subunit that has an immunoreceptor tyrosinebased activation motif (ITAM) in its cytoplasmic domain. FcγRI binds IgG with high affinity and functions during early immune responses, whereas FcγRII and RIII are low affinity receptors that recognize IgG as aggregates surrounding multivalent antigens during late immune responses.Human CD32, also known as Low affinity immunoglobulin γ Fc region receptor II-a (IgG Fc receptor II-a), FcγRII A or FCGR2A Protein, is expressed on cells of both myeloid and lymphoid lineages as well as on cells of non-hematopoietic origin. Associated with an ITAM-bearing adapter subunit, FcRγ, CD32a (FcγRII A) delivers an activating signal upon ligand binding, and results in the initiation of inflammatory responses including cytolysis, phagocytosis, degranulation, and cytokine production. The responses can be modulated by signals from the co-expressed inhibitory receptors such as Fcγ RII B, and the strength of the signal is dependent on the ratio of expression of the activating and inhibitory receptors. |
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