Abstract

The changes in the content of the giant sarcomeric cytoskeletal proteins titin (3000–3700 kDa) and nebulin (770 kDa) in skeletal muscles (m. soleus, m. gastrocnemius), and titin in the left ventricular myocardium, as well as of the submembrane cytoskeletal protein dystrophin (427 kDa) in m. soleus and m. extensor digitorum longus (EDL), have been studied in the edible dormouse Glis glis during hibernation. The animals were divided into two experimental groups: “Summer activity” and “Hypothermia”. It was found that the development of atrophic changes in the skeletal muscles of hibernating animals is accompanied by a decrease in the dystrophin content. Specifically, the fluorescence intensity in skeletal muscle cross sections labeled with primary antibodies to dystrophin and Alexa Fluor^® 488 conjugated secondary antibodies decreased in animals of the “Hypothermia” group by 2.7 times (p < 0.05) and 2.0 times (p < 0.05) in m. soleus and m. EDL, respectively. SDS electrophoresis of proteins in agarose-strengthened macroporous 2.2%-polyacrylamide gel revealed an insignificant decrease (by 15%, p ≤ 0.01) in the titin content compared to the myosin heavy chain content in m. gastrocnemius of animals of the “Hypothermia” group. The titin content in m. soleus and cardiac muscle, as well as the nebulin content in m. soleus and m. gastrocnemius, did not decrease during hibernation. These results are consistent with our previous data for other hibernators: long-tailed ground squirrel, brown and Himalayan black bears. It can be assumed that during evolution, hibernating animals developed the molecular mechanisms responsible for maintaining a stable level of giant sarcomeric cytoskeletal proteins during hibernation.

中文翻译：

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冬眠期间食用睡鼠 Glis glis 横纹肌中巨肌节细胞骨架蛋白的稳定水平

摘要

骨骼肌（比目鱼肌、腓肠肌）中巨型肌节细胞骨架蛋白titin（3000-3700 kDa）和nebulin（770 kDa）以及左心室心肌中titin含量的变化，以及亚膜细胞骨架蛋白肌营养不良蛋白 (427 kDa)，单位为m。比目鱼和米。趾长伸肌( EDL )，已在可食用的睡鼠Glis glis 中进行了研究在冬眠期间。将动物分为两个实验组：“夏季活动”和“低温”。发现冬眠动物骨骼肌萎缩变化的发展伴随着抗肌萎缩蛋白含量的减少。具体地，在标记的第一抗体，以抗肌萎缩蛋白和Alexa Fluor骨骼肌的横截面的荧光强度^® 488缀合的二抗在“低温”组的动物降低了2.7倍（p <0.05）和2.0倍（p <0.05）米。比目鱼和米。EDL，分别。琼脂糖强化大孔 2.2% 聚丙烯酰胺凝胶中蛋白质的 SDS 电泳显示降低不显着（降低 15%，p ≤ 0.01) 中肌球蛋白含量与m 中的肌球蛋白重链含量相比。“低温”组动物的腓肠肌。以米为单位的肌联蛋白含量。比目鱼肌和心肌，以及m 中的 nebulin 含量。比目鱼和米。腓肠肌在冬眠期间没有减少。这些结果与我们之前对其他冬眠动物的数据一致：长尾地松鼠、棕熊和喜马拉雅黑熊。可以假设，在进化过程中，冬眠动物发展了负责在冬眠期间维持稳定水平的巨型肌节细胞骨架蛋白的分子机制。