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在生理温度下,横纹肌收缩激活的变化。

Changing face of contractile activation in striated muscle at physiological temperature.

机构信息

Department of Chemistry and Biomedical Sciences, Linnaeus University, Kalmar, Sweden.

出版信息

J Gen Physiol. 2023 Dec 4;155(12). doi: 10.1085/jgp.202313494. Epub 2023 Nov 7.

Abstract

Calcium binding to troponin, with subsequent displacement of its linked tropomyosin molecule on the thin filament surface, cooperates with myosin binding to actin in the contractile regulation of striated muscle. The intertwined role of these systems is studied in the present issue of JGP by Ishii et al. (https://doi.org/10.1085/jgp.202313414). A particularly interesting feature of the paper, except for studying both skeletal and cardiac muscle proteins, is that the experiments unlike most other similar studies are performed at physiological temperature (35-40°C).

摘要

钙与肌钙蛋白结合,随后将其连接的原肌球蛋白分子从细肌丝表面置换,这与肌球蛋白结合肌动蛋白一起协作,调节横纹肌的收缩。Ishii 等人在本期 JGP 中研究了这些系统的相互交织作用(https://doi.org/10.1085/jgp.202313414)。除了研究骨骼肌和心肌蛋白外,该论文的一个特别有趣的特点是,与大多数其他类似研究不同,实验是在生理温度(35-40°C)下进行的。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/afe1/10630095/216eda03c77d/JGP_202313494_Fig1.jpg

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