PHOSPHOLIPID TURNOVER AS A POSSIBLE TRANSMEMBRANE SIGNAL FOR PROTEIN-PHOSPHORYLATION DURING HUMAN-PLATELET ACTIVATION BY THROMBIN
PHOSPHOLIPID TURNOVER AS A POSSIBLE TRANSMEMBRANE SIGNAL FOR PROTEIN-PHOSPHORYLATION DURING HUMAN-PLATELET ACTIVATION BY THROMBIN
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DOI：
10.1016/s0006-291x(80)80169-0
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发表时间：
1980-01-01
影响因子：
3.1
通讯作者：
NISHIZUKA, Y
中科院分区：
文献类型：
--
作者：
KAWAHARA, Y;TAKAI, Y;NISHIZUKA, Y
人血小板含有大量的钙激活的磷脂依赖性蛋白激酶（蛋白激酶C）。这种酶的激活是由凝血酶诱导的磷脂酰肌醇水解产生的不饱和二酰甘油引发的。蛋白激酶C在体外优先磷酸化MW约为40，000的多肽（40K蛋白）。该蛋白在凝血酶和外源性磷脂酶C刺激的血小板中被迅速标记，并且二酰基甘油形成总是伴随着40K蛋白磷酸化。氯丙嗪和地布卡因可选择性抑制凝血酶诱导的体内40K蛋白磷酸化，这两种药物是蛋白激酶C的有效抑制剂。凝血酶引起的磷脂酰肌醇周转似乎是血小板活化过程中蛋白磷酸化的跨膜信号。
Human platelets contain a large amount of Ca2+-activated, phospholipid-dependent protein kinase (protein kinase C). The activation of this enzyme is initiated by unsaturated diacylglycerol which results from the thrombin-induced phphosphatidylinositol hydrolysis. Protein kinase C preferentially phosphorylates in vitro a polypeptide having a MW of about 40,000 (40K protein). This protein was labeled rapidly in platelets stimulated by thrombin as well as by exogenous phospholipase C, and diacylglycerol formation always accompanies 40K protein phosphorylation. The phosphorylation of 40K protein in vivo induced by thrombin is selectively inhibited by chlorpromazine and dibucaine, which are potent inhibitors for protein kinase C. Phosphatidylinositol turnover provoked by thrombin seems to serve as a transmembrane signal for protein phosphorylation during platelet activation.