Myosin and tropomyosin-troponin complementarily regulate thermal activation of muscles.

IF 3.3 2区 医学 Q1 PHYSIOLOGY Journal of General Physiology Pub Date : 2023-12-04 Epub Date: 2023-10-23 DOI:10.1085/jgp.202313414
Shuya Ishii, Kotaro Oyama, Fuyu Kobirumaki-Shimozawa, Tomohiro Nakanishi, Naoya Nakahara, Madoka Suzuki, Shin'ichi Ishiwata, Norio Fukuda
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引用次数: 1

Abstract

Ishii et al. analyze the microheating-induced sliding movements of reconstituted thin filaments in an in vitro motility assay. They find that the temperature dependence of thin filament sliding is complementarily regulated by myosin and tropomyosin–troponin within the body temperature range.
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肌球蛋白和原肌球蛋白肌钙蛋白互补调节肌肉的热激活。
横纹肌的收缩是由胞浆Ca2+浓度的增加引起的,这是由肌节水平上作用于肌动蛋白丝的原肌球蛋白和肌钙蛋白调节的。也就是说,Ca2+与肌钙蛋白C的结合使细丝状态的“开关”平衡向“打开”状态转变,促进肌动蛋白的相互作用;同样,即使在没有Ca2+的情况下,温度升高到体温范围内也会将平衡转变为开启状态。在这里,我们使用光学加热显微镜研究了肌节缩短沿着分离的快速骨骼肌纤维的温度依赖性。在2秒内快速加热(25至41.5°C)可在松弛溶液中诱导可逆的肌节缩短。此外,我们在体温范围内的体外运动测定中研究了重建的快速骨骼或心脏细丝对快速骨骼或β-心肌肌球蛋白的滑动速度的温度依赖性。我们发现(a)对于快速骨骼肌球蛋白上的快速骨骼细丝,其温度依赖性与快速骨骼肌原纤维(Q10~8)中肌节缩短所获得的温度依赖性相当,和(c)与任一类型肌球蛋白上的快速骨骼细丝相比,心脏细丝在较低温度下滑动。因此,根据各种情况的生理需求,哺乳动物的横纹肌可以通过肌球蛋白和原肌球蛋白肌钙蛋白在体温范围内的互补调节进行微调,以有效收缩。
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.
期刊最新文献
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