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血清素对人血小板中40 kDa和20 kDa蛋白质磷酸化的刺激作用。

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

作者信息

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

出版信息

FEBS Lett. 1984 Jun 11;171(2):289-92. doi: 10.1016/0014-5793(84)80506-2.

DOI:10.1016/0014-5793(84)80506-2
PMID:6233173
Abstract

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.

摘要

在人血小板中,已知血清素会引发形态变化,随后(可逆地)聚集。最近发现,这种胺会引发胞质游离钙升高并激活磷脂酶C。在用血清素刺激人血小板时,我们发现蛋白激酶C活性立即增加,使其40 kDa底物蛋白磷酸化。一种20 kDa蛋白,很可能是肌球蛋白轻链,也被磷酸化到相同程度。酮色林,一种高度选择性的血清素-S2拮抗剂,在亚纳摩尔浓度下抑制了这两个磷酸化过程。

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