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在用心肌肌钙蛋白C部分替代修饰肌钙蛋白后,皮肤化骨骼肌纤维中张力发展的钙离子依赖性发生改变。

Altered Ca2+ dependence of tension development in skinned skeletal muscle fibers following modification of troponin by partial substitution with cardiac troponin C.

作者信息

Moss R L, Lauer M R, Giulian G G, Greaser M L

出版信息

J Biol Chem. 1986 May 5;261(13):6096-9.

PMID:3700385
Abstract

Binding of Ca2+ to the troponin C (TnC) subunit of troponin is necessary for tension development in skeletal and cardiac muscles. Tension was measured in skinned fibers from rabbit skeletal muscle at various [Ca2+] before and after partial substitution of skeletal TnC with cardiac TnC. Following substitution, the tension-pCa relationship was altered in a manner consistent with the differences in the number of low-affinity Ca2+-binding sites on the two types of TnC and their affinities for Ca2+. The alterations in the tension-pCa relationship were for the most part reversed by reextraction of cardiac TnC and readdition of skeletal TnC into the fiber segments. These findings indicate that the type of TnC present plays an important role in determining the Ca2+ dependence of tension development in striated muscle.

摘要

钙离子与肌钙蛋白的肌钙蛋白C(TnC)亚基结合是骨骼肌和心肌产生张力所必需的。在用心肌TnC部分替代骨骼肌TnC之前和之后,在不同钙离子浓度下测量了来自兔骨骼肌的脱膜纤维中的张力。替代后,张力-pCa关系发生了改变,其方式与两种类型的TnC上低亲和力钙离子结合位点的数量差异及其对钙离子的亲和力一致。通过重新提取心肌TnC并将骨骼肌TnC重新添加到纤维段中,张力-pCa关系的改变在很大程度上得到了逆转。这些发现表明,存在的TnC类型在决定横纹肌中张力发展的钙离子依赖性方面起着重要作用。

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