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RIIA in Human Neutrophils: Stimulated Insolubilization, Translocation to Detergent-Resistant Domains, and Degradation of FcRIIA1
Centre de Recherche en Rhumatologie et Immunologie, Canadian Institutes for Health Research Group on the Molecular Mechanisms of Inflammation, Centre de Recherche du Centre Hospitalier de l’Université Laval, and Department of Medicine, Faculty of Medicine, Laval University, Sainte-Foy, Québec, Canada
The signal transduction mechanisms associated with the ligation of
Fc
RIIA in human neutrophils are as yet only incompletely
characterized. In the present study, we have investigated the
distribution and fate of FcRIIA following its cross-linking. The
results obtained indicate that cross-linking of FcRIIA led, within a
few seconds, to its translocation into a nonionic detergent-insoluble
fraction. This was followed, within a couple of minutes, by a
substantial loss of immunoreactive FcRIIA in the cells. The
stimulated degradation of FcRIIA was blocked by the Src kinase
inhibitor PP1 but not by wortmannin, ST-638, piceatannol, or
cytochalasin B. Cross-linked FcRIIA could be solubilized by saponin
(in the presence of Nonidet P-40) and by 
-octylglucoside. Sucrose
gradient analysis of the distribution of FcRIIA revealed that its
cross-linking led to its translocation into the pellets and not the
light buoyant density fractions classically associated with lipid
rafts. Disruption of cholesterol-containing membrane microdomains with
filipin prevented the degradation of FcRIIA but did not inhibit the
stimulation of the pattern of tyrosine phosphorylation or the
mobilization of calcium that followed FcRIIA cross-linking. These
data suggest that both cholesterol-rich domains and Src kinases are
required for the degradation of the activated FcRIIA and provide new
insights into the early events following FcRIIA
cross-linking.
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