Vikhliantsev I M, Alekseeva Iu A, Shpagina M D, Udal'tsov S N, Podlubnaia Z A
Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region, 142290 Russia.
Biofizika. 2002 Jul-Aug;47(4):701-5.
Changes in the molecular weight and functional properties of the C and X proteins from skeletal muscles and the C protein from the cardiac muscle of hibernating ground squirrels Citellus undulatus at different stages of the hibernation were studied. A decrease in the molecular weight of the C protein from fast fibers of skeletal muscles of hibernating ground squirrels compared with awakening and active animals was revealed. The appearance of shorter molecules of the C protein upon hibernation was accompanied by a lowering of its capacity to enhance the actin-activated ATPase activity of control myosin and by the inhibition of its Ca(2+)-sensitivity. No similar changes were observed for the skeletal X protein and the cardiac C protein. The influence of the skeletal C protein on the main functional properties of myosin allows one to draw a conclusion about its contribution to the inhibition of contractile activity of skeletal muscles upon hibernation. The physiological significance of the changes in the C protein upon hibernation is discussed in connection with similar changes in some cardiomyopathies.
研究了冬眠不同阶段的花鼠(Citellus undulatus)骨骼肌中C蛋白和X蛋白以及心肌中C蛋白的分子量和功能特性变化。结果显示,与苏醒和活跃状态的动物相比,冬眠花鼠骨骼肌快肌纤维中C蛋白的分子量有所降低。冬眠时C蛋白出现较短分子,同时其增强对照肌球蛋白肌动蛋白激活的ATP酶活性的能力降低,且其Ca(2+)敏感性受到抑制。骨骼肌X蛋白和心肌C蛋白未观察到类似变化。骨骼肌C蛋白对肌球蛋白主要功能特性的影响使人们能够得出结论,即其对冬眠时骨骼肌收缩活动的抑制有贡献。结合某些心肌病中的类似变化,讨论了冬眠时C蛋白变化的生理意义。