ELEVATION OF CAMP, BUT NOT CGMP, INHIBITS THROMBIN-STIMULATED TYROSINE PHOSPHORYLATION IN HUMAN PLATELETS

被引：32

作者：

PUMIGLIA, KM ^{[1
]}

HUANG, CK ^{[1
]}

FEINSTEIN, MB ^{[1
]}

机构：

[1] UNIV CONNECTICUT, CTR HLTH, DEPT PATHOL, FARMINGTON, CT 06030 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 171卷 / 02期

关键词：

D O I：

10.1016/0006-291X(90)91208-A

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：

Platelets have abundant tyrosine kinase activities, and activation of platelets results in the increased tyrosine phosphorylation of numerous protein substrates. The stimulation of tyrosine phosphorylation elicited by thrombin can be completely inhibited by preincubation with 10nm prostacyclin (PGI2), 1μM PGD2, or 1mM N2, 2′-O-dibutyryl-cAMP. In contrast, incubation of platelets with agents that increase cGMP (sodium nitroprusside or with 1mM 8-Bromo-cGMP) was without effect. The inhibition by prostacyclin was dose dependent, with an IC50 of approximately 3nM, corresponding to the dose range necessary to inhibit other platelet activation processes. These results demonstrate a novel pathway by which agents which raise cAMP may inhibit platelet signal transduction and differential mechanism of action between compounds which raise cAMP and those which elevate cGMP. © 1990.

引用

页码：738 / 745

页数：8