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细丝蛋白对肌动球蛋白ATP酶活性的双重作用。

Dual effect of filamin on actomyosin ATPase activity.

作者信息

Dabrowska R, Goch A, Osińska H, Szpacenko A, Sosinski J

出版信息

J Muscle Res Cell Motil. 1985 Feb;6(1):29-42. doi: 10.1007/BF00712309.

Abstract

Filamin binds to F-actin and influences the myosin-actin interaction. At relatively low concentrations, filamin activates actomyosin Mg2+-ATPase, whereas higher concentrations of filamin exert an inhibitory effect. Activation of ATPase activity occurs under conditions where a loose meshwork of actin filaments is present and inhibition is associated with the appearance of closely apposed bundles of actin filaments. Maximum activation (about fourfold) of actomyosin ATPase activity by filamin occurs between 30 and 65 mM KCl, at pH 6.5, and at temperatures not less than 30 degrees C. ATPase activation requires higher concentrations of filamin in the presence than in the absence of tropomyosin. Filamin does not activate Mg2+-ATPase activity of acto-subfragment-1 and has only a slight effect on the Mg2+-ATPase of acto-heavy meromyosin, but it inhibits the activity of both these systems under conditions similar to those that inhibit actomyosin ATPase activity.

摘要

细丝蛋白与F-肌动蛋白结合并影响肌球蛋白-肌动蛋白的相互作用。在相对较低的浓度下,细丝蛋白激活肌动球蛋白Mg2 + -ATP酶,而较高浓度的细丝蛋白则发挥抑制作用。ATP酶活性的激活发生在存在松散的肌动蛋白丝网络的条件下,而抑制作用则与紧密排列的肌动蛋白丝束的出现有关。细丝蛋白对肌动球蛋白ATP酶活性的最大激活(约四倍)发生在30至65 mM KCl、pH 6.5以及不低于30摄氏度的温度下。与不存在原肌球蛋白相比,存在时ATP酶激活需要更高浓度的细丝蛋白。细丝蛋白不激活肌动蛋白亚片段-1的Mg2 + -ATP酶活性,对肌动蛋白重酶解肌球蛋白的Mg2 + -ATP酶只有轻微影响,但在类似于抑制肌动球蛋白ATP酶活性的条件下,它会抑制这两个系统的活性。

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