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Volume 270, Number 38, Issue of September 22, pp. 22301-22307, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.

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The Ca Dependence of Human Fc Receptor-initiated Phagocytosis

(Received for publication, June 20, 1995; and in revised form, July 24, 1995)

Jeffrey C. Edberg ,&nbsp;<WBR> Ching-Tai Lin ,&nbsp;<WBR> Dana Lau ,&nbsp;<WBR> Jay C. Unkeless ,&nbsp;<WBR> Robert P. Kimberly

Differing roles for transients in FcR-mediated phagocytosis have been suggested based on the observations that antibody-opsonized erythrocyte phagocytosis by human neutrophils shows a [Ca] dependence, while that by murine macrophages appears [Ca]-independent. To explore whether this difference might reflect different receptor isoforms or different cell types, we studied the [Ca] dependence of receptor-initiated phagocytosis by human FcRIIa and a panel of FcRIIa cytoplasmic domain mutants expressed in murine P388D1 cells and by human FcR endogenously expressed on human neutrophils and monocytes. Wild-type and point mutants of huFcRIIa stably transfected into murine P388D1 cells have different capacities to initiate a [Ca] transient, which are closely correlated with quantitative phagocytosis (r = 0.94, p < 0.0001). Phagocytosis both by huFcRIIa in P388D1 cells and by huFcRIIa endogenously expressed on neutrophils and blood monocytes shows [Ca] dependence. Phagocytosis of antibody-opsonized erythrocytes by neutrophils demonstrated greater susceptibility to [Ca] quenching compared with FcRIIa-specific internalization with E-IV.3, suggesting that the phagocytosis activating property of FcRIIIb in neutrophils also engages a [Ca]-dependent element. In contrast, phagocytosis by human FcRIa, endogenously expressed on blood monocytes, is [Ca]-independent. Despite the importance of a consensus tyrosine activation motif for both receptors, FcRIa and FcRIIa engage at least some distinct signaling elements to initiate phagocytosis. The recognition that both of the phagocytic receptors on murine macrophages and human FcRIa associate with the FcRI -chain, which contains a tyrosine activation motif distinct from that in the FcRIIa cytoplasmic domain, suggests that [Ca]-independent phagocytosis is a property associated with the utilization of -chains by FcR.

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