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Thrombin-induced Human Platelet Aggregation Is Inhibited by Protein-Tyrosine Kinase Inhibitors, ST638 and Genistein

M Asahi, S Yanagi, S Ohta, T Inazu, K Sakai, F Takeuchi, T Taniguchi, H Yamamura

FEBS Lett. 1992 Aug 31;309(1):10-4.

PMID: 1511739

Abstract:

We have investigated the involvement of protein-tyrosine kinases in thrombin-induced aggregation of human platelets, using ST638 and genistein which are known inhibitors of protein-tyrosine kinase. Preincubation of platelets with 50 microM of ST638 or 25 micrograms/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. These results suggest that the protein-tyrosine phosphorylation plays a certain role in platelet activation having some relation to the intracellular Ca2+ concentration.

Chemicals Related in the Paper:

Catalog Number Product Name Structure CAS Number Price
AP107761240 ST638 ST638 107761-24-0 Price
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