Thrombin-induced human platelet aggregation is inhibited by protein-tyrosine kinase inhibitors, ST638 (cas 107761-24-0) and genistein

Add time:08/16/2019    Source:sciencedirect.com

We have investigated the involvement of protein-tyrosine kinases in thrombin-induced aggregation of human platelets, using ST638 (cas 107761-24-0) and genistein which are known inhibitors of protein-tyrosine kinase. Preincubation of platelets with 50 μM of ST638 or 25 μg/ml of genistein completely blocked the platelet aggregation induced with 0.05 unit/ml of thrombin. The increase of protein-tyrosine phosphorylation bands (135-, 124-, 76-, 64-, and 60-kDa) induced with thrombin was also inhibited by these inhibitors in a dose-dependent manner. These inhibitors also blocked the platelet aggregation and protein-tyrosine phosphorylation induced with thrombin in aspirin-treated platelets. Increase of the intracellular Ca2+ concentration induced by thrombin was also inhibited by higher concentrations of genistein. The results suggest that the protein-tyrosine phosphorylation plays a certain role in platelet activation having some relation to the intracellular Ca2+ concentration.

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