THROMBIN-INDUCED HUMAN PLATELET-AGGREGATION IS INHIBITED BY PROTEIN-TYROSINE KINASE INHIBITORS, ST638 AND GENISTEIN

被引：73

作者：

ASAHI, M ^{[1
]}

YANAGI, S ^{[1
]}

OHTA, S ^{[1
]}

INAZU, T ^{[1
]}

SAKAI, K ^{[1
]}

TAKEUCHI, F ^{[1
]}

TANIGUCHI, T ^{[1
]}

YAMAMURA, H ^{[1
]}

机构：

[1] FUKUI MED SCH,DEPT BIOCHEM,MATSUOKA,FUKUI 91011,JAPAN

来源：

FEBS LETTERS | 1992年 / 309卷 / 01期

关键词：

PLATELET AGGREGATION; THROMBIN; PROTEIN-TYROSINE PHOSPHORYLATION; CA2+; ST638; GENISTEIN;

D O I：

10.1016/0014-5793(92)80728-Y

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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-mu-M of ST638 or 25-mu-g/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.

引用

页码：10 / 14

页数：5

共 25 条

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