钙调蛋白特异性抑制原肌球蛋白对血小板中肌动球蛋白系统的作用。
Caldesmon specifically inhibits the effect of tropomyosin on actomyosin system in platelet.
作者信息
Onji T, Takagi M, Shibata N
出版信息
Biochem Biophys Res Commun. 1987 Mar 13;143(2):475-81. doi: 10.1016/0006-291x(87)91378-7.
Caldesmon, a calmodulin and actin binding protein, has been shown to exist in platelet. In this report, it is shown that caldesmon specifically inhibits the effect of tropomyosin to enhance the actomyosin ATPase activity in platelet. Platelet tropomyosin enhances the MgATPase activity of platelet actomyosin. This effect is abolished by platelet caldesmon. In the absence of tropomyosin, however, caldesmon has no effect on the ATPase activity. The inhibition is not due to displacement of the binding of tropomyosin to F-actin by caldesmon. The result indicates that caldesmon is the specific inhibitor of tropomyosin in resting platelet.
钙调蛋白结合蛋白（一种钙调蛋白与肌动蛋白结合蛋白）已被证实在血小板中存在。在本报告中，研究表明钙调蛋白结合蛋白能特异性抑制原肌球蛋白增强血小板中肌动球蛋白ATP酶活性的作用。血小板原肌球蛋白可增强血小板肌动球蛋白的MgATP酶活性。这种作用会被血小板钙调蛋白消除。然而，在没有原肌球蛋白的情况下，钙调蛋白对ATP酶活性没有影响。这种抑制作用并非由于钙调蛋白取代了原肌球蛋白与F - 肌动蛋白的结合。结果表明，钙调蛋白结合蛋白是静息血小板中原肌球蛋白的特异性抑制剂。
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