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