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

IF 3.3 2区 医学 Q1 PHYSIOLOGY
Journal of General Physiology Pub Date : 2023-12-04 Epub Date: 2023-11-07 DOI:10.1085/jgp.202313494
Alf Månsson
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引用次数: 0

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).

生理温度下横纹肌收缩激活的变化面。
钙与肌钙蛋白结合,随后其连接的原肌球蛋白分子在细丝表面移位,与肌球蛋白与肌动蛋白结合在一起,共同调节横纹肌的收缩。石井等人在本期JGP中研究了这些系统相互交织的作用(https://doi.org/10.1085/jgp.202313414)。除了研究骨骼肌和心肌蛋白外,这篇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的实验是在生理温度(35-40°C)下进行的。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
CiteScore
6.00
自引率
10.50%
发文量
88
审稿时长
6-12 weeks
期刊介绍: General physiology is the study of biological mechanisms through analytical investigations, which decipher the molecular and cellular mechanisms underlying biological function at all levels of organization. The mission of Journal of General Physiology (JGP) is to publish mechanistic and quantitative molecular and cellular physiology of the highest quality, to provide a best-in-class author experience, and to nurture future generations of independent researchers. The major emphasis is on physiological problems at the cellular and molecular level.
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