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(Received for publication, January 25, 1996, and in revised form, July 31, 1996)
From the Department of Pharmacology, University of North Carolina,
Chapel Hill, North Carolina 27599
Although there are multiple
potential collagen-binding proteins on platelets, the contribution of
each to collagen-induced signaling events and platelet activation is
unclear. We investigated which early platelet signaling events, if any,
could be attributed specifically to the binding of collagen to one of
its receptors, the
Volume 271, Number 43,
Issue of October 25, 1996
pp. 26668-26676
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
2
1 Integrin Is a Necessary
Co-receptor for Collagen-induced Activation of Syk and the Subsequent
Phosphorylation of Phospholipase C
2 in Platelets
2
1 integrin. Treatment
of platelets with collagen induced a rapid activation of the
non-receptor tyrosine kinase, Syk, as measured by an increase in
phosphorylation and kinase activity. Collagen also induced the rapid
phosphorylation of phospholipase C
2 (PLC2). The phosphorylation
of both Syk and PLC2, as well as platelet aggregation, was blocked
by an anti-21 integrin monoclonal
antibody (P1E6), demonstrating that collagen binding to
21 is necessary for signaling.
Cross-linking of the 21 integrin with
stimulatory monoclonal antibody against either the 1 or
2 subunit stimulated the phosphorylation of both Syk and
PLC2. However, antibody stimulation was dependent on co-stimulation
of the FcII receptor (CD32) since specific F(ab
)2
fragments did not induce Syk and PLC2 phosphorylation. Thus, these
results suggest that occupancy of 21 by
collagen is necessary, but that a co-receptor, in addition to
21, is required for these
collagen-induced signaling events. Moreover, the P1E6 antibody did not
inhibit all collagen-induced tyrosine phosphorylation events,
demonstrating that collagen also induces phosphorylation events that
are independent of the 21 integrin. In
addition to Syk and PLC2, we identified the FcII receptor
(FcRII) as being rapidly phosphorylated in response to collagen
stimulation, even in the absence of antibodies. Finally, to determine
if Syk activation precedes and directly contributes to the
phosphorylation of PLC2, platelets were preincubated with the
Syk-selective kinase inhibitor, piceatannol. A concentration of
piceatannol that inhibited the phosphorylation and kinase activity of
Syk, but had no effect on Src kinase activity, blocked the
collagen-induced phosphorylation of PLC2 and also inhibited
collagen-induced platelet aggregation. Our results begin to delineate a
signaling pathway whereby occupancy of the
21 integrin is required, but not
sufficient, for collagen-induced activation of Syk and the subsequent
phosphorylation of PLC2. These events are necessary for platelet
activation and aggregation in response to collagen.
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