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Vol. 289, Issue 2, 721-728, May 1999
Departments of Pharmacology & Therapeutics and Oral Biology,
University of Manitoba, Winnipeg, Manitoba, Canada
Activation of phospholipase C (PLC) is a central component of the
signal transduction process in numerous cells, including platelets.
U73122 has been widely used as a selective PLC inhibitor. In the
present study, the effects of U73122 on platelet function have been
further examined. Platelets were stimulated with collagen (via
PLC-
), the stable thromboxane mimetic U46619 (via PLC-
), or
phorbol myristate acetate (PMA) via protein kinase C (PKC). Consistent
with inhibition of PLC, U73122 inhibited platelet aggregation and
[3H]-serotonin release in response to collagen and U46619
in a concentration-dependent manner. Similarly, U73122 blocked
collagen-induced release of thromboxane A2. U73122 also
inhibited U46619-induced [32P]phosphatidic acid
production and phosphorylation of the major PKC substrate, pleckstrin.
U73122 had no effect on PMA-induced pleckstrin phosphorylation,
[3H]-serotonin release, or intracellular vacuole
formation. However, U73122 did inhibit PMA-induced platelet aggregation
and fibrinogen binding. Overall, these results suggest that U73122, in
addition to its inhibition of PLC, also affects PKC-independent events that interfere with platelet aggregation.
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