Vikhliantsev I M, makarenko I V, Khalina Ia N, Malyshev S L, Podlubnaia Z A
Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region, Russia.
Biofizika. 2000 Sep-Oct;45(5):831-5.
Changes in the isoform composition of the elastic protein titin from skeletal and cardiac muscles of hibernating ground squirrels were revealed for the first time. It was shown that, upon hibernation, the molecular mass of titin decreases and its functional properties change as compared with the active state of the animal. The physiological significance of the changes in titin isoform composition for the inhibition of muscle contractile activity upon hibernation is discussed in connection with similar changes during some cardiomyopathies.
首次揭示了冬眠地松鼠骨骼肌和心肌中弹性蛋白肌联蛋白的同工型组成变化。结果表明，与动物的活跃状态相比，冬眠时肌联蛋白的分子量降低，其功能特性发生改变。结合某些心肌病期间的类似变化，讨论了冬眠时肌联蛋白同工型组成变化对抑制肌肉收缩活动的生理意义。
