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  1. 原著論文

Nanoscopic changes in the lattice structure of striated muscle sarcomeres involved in the mechanism of spontaneous oscillatory contraction (SPOC)

https://repo.qst.go.jp/records/80634
https://repo.qst.go.jp/records/80634
fa947fd3-2097-4c29-8afe-346461d64b91
Item type 学術雑誌論文 / Journal Article(1)
公開日 2020-09-15
タイトル
タイトル Nanoscopic changes in the lattice structure of striated muscle sarcomeres involved in the mechanism of spontaneous oscillatory contraction (SPOC)
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
アクセス権
アクセス権 metadata only access
アクセス権URI http://purl.org/coar/access_right/c_14cb
著者 Kono, Fumiaki

× Kono, Fumiaki

WEKO 1002437

Kono, Fumiaki

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Kawai, Seitaro

× Kawai, Seitaro

WEKO 1002438

Kawai, Seitaro

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Shimamoto, Yuta

× Shimamoto, Yuta

WEKO 1002439

Shimamoto, Yuta

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Shin'ichi, Ishiwata

× Shin'ichi, Ishiwata

WEKO 1002440

Shin'ichi, Ishiwata

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Fumiaki, Kono

× Fumiaki, Kono

WEKO 1002441

en Fumiaki, Kono

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抄録
内容記述タイプ Abstract
内容記述 Muscles perform a wide range of motile functions in animals. Among various types are skeletal and cardiac muscles, which exhibit a steady auto-oscillation of force and length when they are activated at an intermediate level of contraction. This phenomenon, termed spontaneous oscillatory contraction or SPOC, occurs devoid of cell membranes and at fixed concentrations of chemical substances, and is thus the property of the contractile system per se. We have previously developed a theoretical model of SPOC and proposed that the oscillation emerges from a dynamic force balance along both the longitudinal and lateral axes of sarcomeres, the contractile units of the striated muscle. Here, we experimentally tested this hypothesis by developing an imaging-based analysis that facilitates detection of the structural changes of single sarcomeres at unprecedented spatial resolution. We found that the sarcomere width oscillates anti-phase with the sarcomere length in SPOC. We also found that the oscillatory dynamics can be altered by osmotic compression of the myofilament lattice structure of sarcomeres, but they are unchanged by a proteolytic digestion of titin/connectin – the spring-like protein that provides passive elasticity to sarcomeres. Our data thus reveal the three-dimensional mechanical dynamics of oscillating sarcomeres and suggest a structural requirement of steady auto-oscillation.
書誌情報 Scientific Reports

巻 10, p. 16372, 発行日 2020-10
出版者
出版者 Nature Publishing Group
ISSN
収録物識別子タイプ ISSN
収録物識別子 2045-2322
PubMed番号
識別子タイプ PMID
関連識別子 33009449
DOI
識別子タイプ DOI
関連識別子 10.1038/s41598-020-73247-1
関連サイト
識別子タイプ URI
関連識別子 https://www.nature.com/articles/s41598-020-73247-1
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