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J Biol Chem, Vol. 273, Issue 14, 8071-8079, April 3, 1998

Differential Regulation of Human Neutrophil FcRIIa (CD32) and FcRIIIb (CD16)-induced Ca²⁺ Transients

From the Division of Clinical Immunology and Rheumatology, Departments of Medicine and Microbiology, University of Alabama, Birmingham, Alabama 35294

Human neutrophils express two structurally distinct receptors for the Fc region of IgG, FcRIIa and FcRIIIb. Although earlier studies have suggested that the functional properties of these receptors are similar, mounting evidence suggests that these receptors are capable of inducing distinct functional responses. Accordingly, we have examined the regulation of intracellular Ca²⁺ transients induced by each of these receptors alone (homotypic receptor cross-linking) and together (heterotypic receptor cross-linking). The glycosylphosphatidylinositol-anchored FcRIIIb induces a rise in [Ca²⁺] after homotypic cross-linking that is independent of ligand-mediated engagement of the transmembrane FcRIIa. Both receptors were sensitive to the protein-tyrosine kinase inhibitor methyl 2,5-dihydroxycinnamate, but FcRIIa-induced signaling was uniquely sensitive to the protein-tyrosine kinase inhibitor genistein. FcRIIa but not FcRIIIb engages a cAMP-sensitive and inositol 1,4,5-trisphosphate-dependent pathway(s) that results in the Ca²⁺-transient. When these receptors are cross-linked into heterotypic clusters, a synergistic rise in [Ca²⁺] is observed that is accompanied by synergistic increases in the phospholipase C-breakdown products inositol 1,4,5-trisphosphate and diglyceride. These data provide a mechanism for the functional differences between these two receptors and suggest the possibility that they can be differentially modulated.

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