牛血小板肌动蛋白聚合的特异性脱敏作用。

Specific desensitization of actin polymerization of bovine platelets.

作者信息

Imada T, Kikuchi T, Shimada H, Inada Y, Saito Y

出版信息

Biochem Biophys Res Commun. 1984 May 16;120(3):846-50. doi: 10.1016/s0006-291x(84)80184-9.

Abstract

Polymerization of actin induced by activation of platelets was investigated using deoxyribonuclease I inhibition assay. When platelets were activated with ADP or 5-hydroxytryptamine, actin was polymerized quickly followed by rapid depolymerization to the initial level. Reactivation with the same agonist, however, did not cause the polymerization of actin, though with different agonists actin polymerized quite normally. The mechanism for this agonist-specific desensitization of actin polymerization was investigated by the use of a calcium ionophore A23187. It was suggested that the cause for the desensitization is the inability of platelets to mobilize Ca2+ in response to specific agonist.

摘要

使用脱氧核糖核酸酶I抑制试验研究了血小板活化诱导的肌动蛋白聚合。当血小板用ADP或5-羟色胺活化时，肌动蛋白迅速聚合，随后迅速解聚至初始水平。然而，用相同激动剂再次激活并不会导致肌动蛋白聚合，尽管使用不同激动剂时肌动蛋白聚合相当正常。通过使用钙离子载体A23187研究了这种肌动蛋白聚合的激动剂特异性脱敏机制。结果表明，脱敏的原因是血小板无法响应特定激动剂动员Ca2+。