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肌动蛋白丝柔韧性对骨骼肌纤维弹性特性解读的影响

The effect of actin filament compliance on the interpretation of the elastic properties of skeletal muscle fibres.

作者信息

Blangé T, van der Heide U A, Treijtel B W, de Beer E L

机构信息

University of Amsterdam, Department of Physiology, The Netherlands.

出版信息

J Muscle Res Cell Motil. 1997 Apr;18(2):125-31. doi: 10.1023/a:1018649420778.

DOI:10.1023/a:1018649420778
PMID:9127261
Abstract

Recently, X-ray diffraction studies provided direct evidence for an appreciable length change in the actin filament upon activation. This finding has profound implications on the interpretation of the elastic properties of skeletal muscle fibre. In this study we determined the compliance of the actin filament during activation, using the data obtained previously from quick stretch and release experiments on skeletal muscle fibres of the frog. The effects of filament compliance are demonstrated clearly in the elastic properties of partially activated fibres. The low-frequency elasticity increases linearly with tension, reflecting an increase in the number of force-producing cross-bridges. At higher frequencies, this linearity is lost. In this study we describe the data consistently in terms of a cross-bridge stiffness increasing linearly with tension and a constant Young's modulus for the actin filament of 44 MN m-2. This corresponds to a compliance of 23 pm microns-1 per kN m-2 tension developed. Using this value for the actin filament Young's modulus, its contribution to the elastic properties of skeletal muscle fibre of the frog is considered in rigor and relaxation. The filament compliance hardly affects the overall elasticity of the muscle fibre in relaxation. In contrast, it contributes to a large extent to the overall elasticity in rigor. Taking account of the filament compliance, we find that the Young's modulus in rigor exhibits an increase from 14 MN m-2 at frequencies below 500 Hz to 55 MN m-2 above 40 kHz.

摘要

最近,X射线衍射研究为肌动蛋白丝在激活时发生明显的长度变化提供了直接证据。这一发现对骨骼肌纤维弹性特性的解释具有深远意义。在本研究中,我们利用先前从青蛙骨骼肌纤维的快速拉伸和释放实验中获得的数据,确定了激活过程中肌动蛋白丝的顺应性。在部分激活的纤维的弹性特性中,丝顺应性的影响得到了清晰的证明。低频弹性随张力呈线性增加,反映了产生力的横桥数量的增加。在较高频率下,这种线性关系消失。在本研究中,我们根据横桥刚度随张力线性增加以及肌动蛋白丝的杨氏模量恒定为44 MN m-2来一致地描述这些数据。这对应于每产生1 kN m-2张力时23 pm μm-1的顺应性。利用这个肌动蛋白丝杨氏模量值,在强直收缩和舒张状态下考虑了其对青蛙骨骼肌纤维弹性特性的贡献。在舒张状态下,丝顺应性几乎不影响肌肉纤维的整体弹性。相比之下,在强直收缩状态下,它在很大程度上对整体弹性有贡献。考虑到丝顺应性,我们发现强直收缩状态下的杨氏模量在频率低于500 Hz时从14 MN m-2增加到高于40 kHz时的55 MN m-2。

相似文献

1
The effect of actin filament compliance on the interpretation of the elastic properties of skeletal muscle fibres.肌动蛋白丝柔韧性对骨骼肌纤维弹性特性解读的影响
J Muscle Res Cell Motil. 1997 Apr;18(2):125-31. doi: 10.1023/a:1018649420778.
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The stiffness of skeletal muscle in isometric contraction and rigor: the fraction of myosin heads bound to actin.等长收缩和尸僵状态下骨骼肌的僵硬度:与肌动蛋白结合的肌球蛋白头部比例。
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X-ray diffraction evidence for the extensibility of actin and myosin filaments during muscle contraction.X射线衍射证据表明,在肌肉收缩过程中肌动蛋白丝和肌球蛋白丝具有可伸展性。
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Pflugers Arch. 1992 Apr;420(5-6):434-45. doi: 10.1007/BF00374617.

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