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Receptor IIa and Fc Receptor IIIb Determines the Activation Phenotype of Human Neutrophils1
,
Departments of
*
Medicine and
Biochemistry and Molecular Biology, University of Louisville Health Sciences Center, Louisville, KY 40202; and
Veterans Affairs Medical Center, Louisville, KY 40204
Fc
Rs mediate immune complex-induced tissue injury. The
hypothesis that FcRIIa and FcRIIIb control neutrophil responses
by activating mitogen-activated protein kinases was examined. Homotypic
and heterotypic cross-linking of FcRIIa and/or FcRIIIb resulted
in a rapid, transient increase in ERK and p38 activity, with maximal
stimulation between 1 and 3 min. FcRIIa and FcRIIIb stimulated
distinct patterns of ERK and p38 activity, and heterotypic
cross-linking failed to stimulate synergistic activation of either ERK
or p38 activity. Both FcRIIa and FcRIIIb required activation of a
nonreceptor tyrosine kinase and phosphatidylinositol 3-kinase for
stimulation of ERK and p38. Inhibition of ERK activation with PD98059
enhanced H2O2 production stimulated by
homotypic and heterotypic FcR cross-linking. Inhibition of p38 with
SB203580 attenuated H2O2 production stimulated
by FcRIIIb or heterotypic cross-linking, but had no effect on
FcRIIa-stimulated H2O2 production. On the
other hand, PD98059 inhibited actin polymerization stimulated by FcR
cross-linking, while SB203580 had no effect. Inhibition of actin
polymerization with cytochalasin D enhanced p38 activity stimulated by
either FcRIIa or FcRIIIb, but cytochalasin D only enhanced
H2O2 production stimulated by FcRIIIb. Our
data indicate that FcRIIa and FcRIIIb independently activate ERK
and p38. The two receptors demonstrate different efficacies for ERK and
p38 activation, and they do not act cooperatively. ERK and p38 provide
stimulatory and inhibitory signals for neutrophil responses to immune
complexes. In addition, these data indicate that actin reorganization
may play a role in mediating p38-dependent activation of respiratory
burst upon stimulation of FcRIIIb in
neutrophils.
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