Onji T, Takagi M, Shibata N
Biochem Biophys Res Commun. 1985 Oct 15;132(1):307-12. doi: 10.1016/0006-291x(85)91023-x.
Filamin, an actin cross-linker protein, has been shown to exist in platelet. The role of this protein in the platelet has remained unclear. In this report, we show that filamin inhibits the actin-activated Mg2+ -ATPase activity of platelet myosin. The activation caused by platelet actin is inhibited by 50% at the molar ratio of filamin to actin of 1/50. Platelet tropomyosin, which we showed to enhance the ATPase activity, does not abolish the effect of filamin. The results support the view that filamin stabilizes the actin network in the resting platelet.
细丝蛋白是一种肌动蛋白交联蛋白,已证实在血小板中存在。该蛋白在血小板中的作用尚不清楚。在本报告中,我们表明细丝蛋白可抑制血小板肌球蛋白的肌动蛋白激活的Mg2 + -ATP酶活性。当细丝蛋白与肌动蛋白的摩尔比为1/50时,血小板肌动蛋白引起的激活被抑制50%。我们发现可增强ATP酶活性的血小板原肌球蛋白并不能消除细丝蛋白的作用。这些结果支持了细丝蛋白可稳定静息血小板中肌动蛋白网络的观点。