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Protein kinase C regulates tyrosine phosphorylation of pp125FAK in
platelets adherent to fibrinogen
B Haimovich, N Kaneshiki and P Ji
Department of Surgery, UMDNJ-Robert Wood Johnson Medical School, New
Brunswick, NJ, USA.
Platelet adhesion to immobilized fibrinogen stimulates the induction of
tyrosine phosphorylation of multiple proteins. However, platelet spreading
and tyrosine phosphorylation of three proteins, the focal adhesion kinase
pp125FAK and proteins of 101 and 105 kD (pp101 and pp105), require a second
adenosine diphosphate (ADP)-dependent costimulatory event. In this study we
show that protein kinase C (PKC) inhibitors prevented the induction of
tyrosine phosphorylation of pp125FAK, pp101 and pp105, and abolished
spreading. These inhibitory effects were not observed after treatment of
the platelets with the intracellular Ca2+ chelator BAPTA-AM. This suggested
that in platelets, PKC regulates spreading and related protein tyrosine
phosphorylation. In addition, the inhibitory effects of apyrase, an ADP
scavenger, on spreading and tyrosine phosphorylation of pp125FAK, pp101,
and pp105, were not observed in the presence of phorbol 12-myristate
13-acetate (PMA). These data implied that in fibrinogen-adherent platelets
integrin ligation and an agonist receptor occupancy are required for the
functional association of PKC and the alpha IIb beta 3-mediated signaling
pathways. Taken together these results show that PKC plays a central role
in the transduction of intracellular signals downstream from alpha IIb beta
3 that regulate spreading and pp125FAK phosphorylation.
Volume 87,
Issue 1,
pp. 152-161,
01/01/1996
Copyright © 1996 by The American Society of Hematology
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