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Glycoprotein IIIa is phosphorylated in intact human platelets
LV Parise, AB Criss, L Nannizzi and MR Wardell
Gladstone Foundation Laboratories for Cardiovascular Disease, University of
California, San Francisco.
The glycoprotein IIb-IIIa complex (GP IIb-IIIa) is a multifunctional
transmembrane protein on platelets. Its most completely described function
is as a fibrinogen receptor that mediates platelet aggregation, but it is
also involved in clot retraction, signal transduction, calcium transport,
and other events. However, the mechanisms that regulate the functions of GP
IIb-IIIa during platelet activation are largely unknown. One possible
mechanism is phosphorylation, since several other receptors are regulated
by this process. We found that GP IIIa, but not GP IIb, was phosphorylated
in 32P-labeled platelets, predominantly on threonine residues. Furthermore,
GP IIIa phosphorylation increased four-fold in platelets activated with
thrombin or phorbol 12-myristate 13-acetate, but not at all in platelets
treated with prostacyclin, an inhibitor of platelet activation. The
thrombin-induced increase in phosphorylation was inhibited by pretreating
platelets with prostacyclin or with staurosporin, a specific protein kinase
C inhibitor. Thus, there is an increase in the level or turnover of
phosphate on GP IIIa during platelet activation, most likely involving
protein kinase C. This phosphorylation may regulate some aspect(s) of GP
IIb-IIIa function.
Volume 75,
Issue 12,
pp. 2363-2368,
06/15/1990
Copyright © 1990 by The American Society of Hematology
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