Stimulation by serotonin of 40 kDa and 20 kDa protein phosphorylation in human platelets

FEBS Letters

de Chaffoy de Courcelles, D.¹  Roevens, P.¹  van Belle, H.¹ 

[1] Department of Biochemistry, Janssen Pharmaceutica, B-2340 Beerse, Belgium

关键词: Serotonin-S2 receptor;    Protein phosphorylation;    Platelet;    Ketanserin;    PA;    phosphatidic acid;    DAG;    diacylglycerol;   

DOI  :  10.1016/0014-5793(84)80506-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In human platelets, serotonin is known to induce a shape change followed by (reversible) aggregation. Recently, it was found that the amine triggers the elevation of cytosolic free calcium and activates phospholipase C. On stimulation of human platelets with serotonin we found an immediate increase in protein kinase C activity, phosphorylating its 40 kDa substrate protein. A 20 kDa protein, most likely the myosin light chain, was phosphorylated to the same extent. Ketanserin, a highly selective serotonin-S₂ antagonist inhibited both phosphorylation processes at subnanomolar concentrations.

【 授权许可】

Unknown