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Receptor-Mediated Activation of Phospholipase D Regulates Macrophage Phagocytosis of IgG-Opsonized Particles1
,
,
*
Department of Medicine, the
Inflammation Program, and the
Graduate Program in Immunology at the University of Iowa and Veterans Affairs Medical Center, Iowa City, IA 52242
Receptors for the Fc portion of IgG (Fc
Rs) integrate the innate
and acquired components of immunity by coupling the specific
recognition of IgG Abs to the activation of phagocytic leukocytes.
Knowledge of the molecular mechanisms that regulate phagocyte
stimulation by FcRs may permit therapeutic modulation to augment
immunoprotective aspects and minimize damage to host tissues in diverse
inflammatory diseases. Since phospholipase D (PLD) has been linked to
the stimulation of cytotoxic leukocyte responses, we characterized
FcR-dependent activation of PLD in human macrophages. IgG-coated
SRBCs (EIgG) stimulated a 9.4-fold increase in PLD activity compared
with SRBCs treated with control Ab (p < 0.001),
determined by formation of the PLD-specific product phosphatidylethanol
in the presence of 0.5% ethanol. Levels of phosphatidic acid, the
physiologic product of PLD-mediated catalyzis, were significantly
increased in the absence of ethanol (6.4-fold, p <
0.001). PLD activity was also stimulated by immune complex-coated latex
beads or cross-linking of Abs specific for FcRI, FcRII, or
FcRIII. Phagocytosis of EIgG was reduced by two inhibitors of
PLD-mediated signaling, 2,3-diphosphoglycerate or 1-butanol. Addition
of purified PLD restored control levels of phagocytosis in cells in
which endogenous PLD was inhibited. The tyrosine kinase inhibitors
genistein and herbimycin A caused concordant reductions in
FcR-stimulated PLD activity and phagocytosis. These studies
demonstrate that FcR-mediated phagocytosis is accompanied by
tyrosine kinase-dependent activation of PLD and support the hypothesis
that stimulation of PLD functions to regulate the ingestion of
IgG-opsonized particles.
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