α1- 衔接蛋白缺陷小鼠在渗透休克后肌肉力量恢复受损。
α1-Syntrophin-deficient mice exhibit impaired muscle force recovery after osmotic shock.
机构信息
Department of Medical Genetics, School of Human Development, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Alberta, Canada; Department of Molecular Therapy, National Institute of Neuroscience, National Center of Neurology and Psychiatry, 4-1-1, Ogawa-higashi, Kodaira, Tokyo, 187-8502, Japan.
出版信息
Muscle Nerve. 2014 May;49(5):728-35. doi: 10.1002/mus.23990.
INTRODUCTION
α1-syntrophin, a member of the dystrophin complex, recruits membrane molecules, including aquaporin-4, at the sarcolemma. The physiological functions of α1-syntrophin are poorly understood.
METHODS
We examined the physiological characteristics of α1-syntrophin-deficient muscles under osmotic stress conditions to test the possibility that mutant muscles are less tolerant of osmotic shock.
RESULTS
Isolated muscle bundles from mutant mice showed markedly reduced force production after hypo-osmotic shock. In addition, the mutant muscle bundles showed delayed recovery of specific gravity after being exposed to hypo-osmotic conditions. Two consecutive exercise tests on the treadmill revealed their performance in the second test was significantly lower than for wild-type mice. Furthermore, mutant mice had higher serum lactate concentrations after treadmill exercise.
CONCLUSIONS
Although the lack of α1-syntrophin from the sarcolemma does not lead to muscle degeneration, our results suggest that it may be partly involved in the pathophysiology of dystrophin-deficient Duchenne muscular dystrophy.
简介
α1- 连接蛋白是抗肌萎缩蛋白复合物的一个成员，它将包括水通道蛋白-4 在内的膜分子募集到肌小节膜。α1- 连接蛋白的生理功能尚未完全了解。
方法
我们在渗透胁迫条件下检查了缺乏α1-连接蛋白的肌肉的生理特征，以测试突变肌肉对渗透冲击的耐受性降低的可能性。
结果
从突变小鼠分离的肌束在低渗休克后显示出明显减少的力产生。此外，突变肌束在暴露于低渗条件后表现出比重恢复延迟。在跑步机上进行的两次连续运动测试显示，它们在第二次测试中的表现明显低于野生型小鼠。此外，突变小鼠在跑步机运动后血清乳酸盐浓度更高。
结论
尽管肌小节膜缺乏α1-连接蛋白不会导致肌肉退化，但我们的结果表明，它可能部分参与了抗肌萎缩蛋白缺乏型杜氏肌营养不良症的病理生理学过程。
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