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Thermal Activation of Thin Filaments in Striated Muscle

In skeletal and cardiac muscles, contraction is triggered by an increase in the intracellular Ca(2+) concentration. During Ca(2+) transients, Ca(2+)-binding to troponin C shifts the “on–off” equilibrium of the thin filament state toward the “on” sate, promoting actomyosin interaction. Likewise, rece...

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Autores principales: Ishii, Shuya, Oyama, Kotaro, Shintani, Seine A., Kobirumaki-Shimozawa, Fuyu, Ishiwata, Shin’ichi, Fukuda, Norio
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7179743/
https://www.ncbi.nlm.nih.gov/pubmed/32372968
http://dx.doi.org/10.3389/fphys.2020.00278
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author Ishii, Shuya
Oyama, Kotaro
Shintani, Seine A.
Kobirumaki-Shimozawa, Fuyu
Ishiwata, Shin’ichi
Fukuda, Norio
author_facet Ishii, Shuya
Oyama, Kotaro
Shintani, Seine A.
Kobirumaki-Shimozawa, Fuyu
Ishiwata, Shin’ichi
Fukuda, Norio
author_sort Ishii, Shuya
collection PubMed
description In skeletal and cardiac muscles, contraction is triggered by an increase in the intracellular Ca(2+) concentration. During Ca(2+) transients, Ca(2+)-binding to troponin C shifts the “on–off” equilibrium of the thin filament state toward the “on” sate, promoting actomyosin interaction. Likewise, recent studies have revealed that the thin filament state is under the influence of temperature; viz., an increase in temperature increases active force production. In this short review, we discuss the effects of temperature on the contractile performance of mammalian striated muscle at/around body temperature, focusing especially on the temperature-dependent shift of the “on–off” equilibrium of the thin filament state.
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spelling pubmed-71797432020-05-05 Thermal Activation of Thin Filaments in Striated Muscle Ishii, Shuya Oyama, Kotaro Shintani, Seine A. Kobirumaki-Shimozawa, Fuyu Ishiwata, Shin’ichi Fukuda, Norio Front Physiol Physiology In skeletal and cardiac muscles, contraction is triggered by an increase in the intracellular Ca(2+) concentration. During Ca(2+) transients, Ca(2+)-binding to troponin C shifts the “on–off” equilibrium of the thin filament state toward the “on” sate, promoting actomyosin interaction. Likewise, recent studies have revealed that the thin filament state is under the influence of temperature; viz., an increase in temperature increases active force production. In this short review, we discuss the effects of temperature on the contractile performance of mammalian striated muscle at/around body temperature, focusing especially on the temperature-dependent shift of the “on–off” equilibrium of the thin filament state. Frontiers Media S.A. 2020-04-16 /pmc/articles/PMC7179743/ /pubmed/32372968 http://dx.doi.org/10.3389/fphys.2020.00278 Text en Copyright © 2020 Ishii, Oyama, Shintani, Kobirumaki-Shimozawa, Ishiwata and Fukuda. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Physiology
Ishii, Shuya
Oyama, Kotaro
Shintani, Seine A.
Kobirumaki-Shimozawa, Fuyu
Ishiwata, Shin’ichi
Fukuda, Norio
Thermal Activation of Thin Filaments in Striated Muscle
title Thermal Activation of Thin Filaments in Striated Muscle
title_full Thermal Activation of Thin Filaments in Striated Muscle
title_fullStr Thermal Activation of Thin Filaments in Striated Muscle
title_full_unstemmed Thermal Activation of Thin Filaments in Striated Muscle
title_short Thermal Activation of Thin Filaments in Striated Muscle
title_sort thermal activation of thin filaments in striated muscle
topic Physiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7179743/
https://www.ncbi.nlm.nih.gov/pubmed/32372968
http://dx.doi.org/10.3389/fphys.2020.00278
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