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疲劳后骨骼肌收缩装置和肌浆网的功能方面

Functional aspects of skeletal muscle contractile apparatus and sarcoplasmic reticulum after fatigue.

作者信息

Williams J H, Ward C W, Spangenburg E E, Nelson R M

机构信息

Muscular Function Laboratory, Department of Human Nutrition, Foods, and Exercise, Virginia Polytechnic Institute and State University, Blacksburg, Virginia 24061-0430, USA.

出版信息

J Appl Physiol (1985). 1998 Aug;85(2):619-26. doi: 10.1152/jappl.1998.85.2.619.

Abstract

This study examined the effects of fatigue on the functional aspects of the contractile apparatus and sarcoplasmic reticulum (SR). Frog semitendinosus muscles were stimulated to fatigue, and skinned fibers or a homogenate fraction was prepared from both fatigued and rested contralateral muscles. In fatigued fibers, maximal Ca2+-activated force of the contractile apparatus was unaltered, whereas maximal actomyosin-ATPase activity was depressed by 20%. The Ca2+ sensitivity of force was increased, whereas that of actomyosin-ATPase was not altered. Also, the rate constant for tension redevelopment was decreased at submaximal Ca2+ concentration. These latter findings suggest that fatigue slows the dissociation of force-generating myosin cross bridges. Ca2+ uptake and Ca2+-ATPase activity of the SR were depressed by 46 and 21%, respectively, in the fatigued muscles. Fatigue also reduced the rates of SR Ca2+ release evoked by AgNO3 and 4-chloro-m-cresol by 38 and 45%, respectively. During fatigue, the contractile apparatus and SR undergo intrinsic functional alterations. These changes likely result in altered force production and energy consumption by the intact muscle.

摘要

本研究考察了疲劳对收缩装置和肌浆网(SR)功能方面的影响。刺激青蛙半腱肌使其疲劳,然后从疲劳和未疲劳的对侧肌肉制备去皮纤维或匀浆组分。在疲劳纤维中,收缩装置的最大Ca2+激活力未改变,而最大肌动球蛋白ATP酶活性降低了20%。力的Ca2+敏感性增加,而肌动球蛋白ATP酶的Ca2+敏感性未改变。此外,在亚最大Ca2+浓度下,张力重建的速率常数降低。这些结果表明,疲劳会减缓产生力的肌球蛋白横桥的解离。疲劳肌肉中,SR的Ca2+摄取和Ca2+-ATP酶活性分别降低了46%和21%。疲劳还分别使由AgNO3和4-氯间甲酚诱发的SR Ca2+释放速率降低了38%和45%。在疲劳过程中,收缩装置和SR会发生内在功能改变。这些变化可能导致完整肌肉的力产生和能量消耗发生改变。

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