首页> 外文期刊>Journal of Muscle Research and Cell Motility >Non-crossbridge calcium-dependent stiffness in slow and fast skeletal fibres from mouse muscle
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Non-crossbridge calcium-dependent stiffness in slow and fast skeletal fibres from mouse muscle

机译:小鼠肌肉的慢速和快速骨骼纤维的非横桥钙依赖性刚度

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摘要

We showed previously that force development in frog and FDB mouse skeletal muscle fibres is preceded by an increase of fibre stiffness occurring well before crossbridge attachment and force generation. This stiffness increase, referred to as static stiffness, is due to a Ca2+-dependent stiffening of a non-crossbridge sarcomere structure which we suggested could be attributed to the titin filaments. To investigate further the role of titin in static stiffness, we measured static stiffness properties at 24 and 35°C in soleus and EDL mouse muscle fibres which are known to express different titin isoforms. We found that static stiffness was present in both soleus and EDL fibres, however, its value was about five times greater in EDL than in soleus fibres. The rate of development of static stiffness on stimulation increased with temperature and was slightly faster in EDL than in soleus in agreement with previously published data on the time course of the intracellular Ca2+ transients in these muscles. The present results show that the presence of a non-crossbridge Ca2+-dependent stiffening of the muscle fibre is a physiological general characteristic of skeletal muscle. Static stiffness depends on fibre type, being greater and developing faster in fast than in slow fibres. Our observations are consistent with the idea that titin stiffening on contraction improves the sarcomere structure stability. Such an action in fact seems to be more important in EDL fast fibre than in soleus slow fibres.
机译:我们以前表明青蛙和FDB小鼠骨骼肌纤维中的力量发展是在刚好跨桥附着和力量产生之前发生纤维刚度的增加。这种刚度的增加,称为静态刚度,是由于非横桥肌节结构的Ca2 +依赖性刚度所致,我们认为这可能归因于纤丝。为了进一步研究titin在静态刚度中的作用,我们测量了比目鱼和EDL小鼠肌肉纤维在24和35°C时的静态刚度特性,已知它们表达不同的titin亚型。我们发现比目鱼纤维和EDL纤维都存在静态刚度,但是,其值在EDL中比比目鱼纤维大约5倍。刺激时静态刚度的发展速率随温度增加而增加,在EDL中比比目鱼肌中稍快,这与先前发表的有关这些肌肉中细胞内Ca2 + 瞬变时间过程的数据一致。目前的结果表明,肌纤维非横桥Ca 2+依赖性的硬化的存在是骨骼肌的生理总体特征。静态刚度取决于纤维类型,它的强度更大,并且在快速中比在慢速纤维中发展更快。我们的观察结果与钛蛋白在收缩时变硬可改善肌节结构稳定性的观点一致。实际上,这种作用在EDL快纤维中比在比目鱼慢纤维中似乎更为重要。

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  • 来源
    《Journal of Muscle Research and Cell Motility》 |2012年第6期|p.403-409|共7页
  • 作者单位

    Dipartimento di Scienze Fisiologiche, Università degli Studi di Firenze, Viale G.B. Morgagni 63, 50134, Florence, Italy;

    Dipartimento di Scienze Fisiologiche, Università degli Studi di Firenze, Viale G.B. Morgagni 63, 50134, Florence, Italy;

    Dipartimento di Scienze Fisiologiche, Università degli Studi di Firenze, Viale G.B. Morgagni 63, 50134, Florence, Italy;

    Department of Physiology and Pharmacology, Karolinska Institutet, 171 77, Stockholm, Sweden;

    Dipartimento di Scienze Fisiologiche, Università degli Studi di Firenze, Viale G.B. Morgagni 63, 50134, Florence, Italy;

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  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

    Stiffness; Static stiffness; Titin; Fast mouse muscle; Slow mouse muscle;

    机译:刚度;静态刚度;钛;快小鼠肌肉;慢小鼠肌肉;

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