Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia.
Biochemistry (Mosc). 2012 Dec;77(13):1515-35. doi: 10.1134/S0006297912130093.
This review summarizes results of our studies on titin isoform composition in vertebrate striated muscles under normal conditions, during hibernation, real and simulated microgravity, and under pathological conditions (stiff-person syndrome, post-apoplectic spasticity, dilated cardiomyopathy, cardiac hypertrophy). Experimental evidence for the existence in mammalian striated muscles of higher molecular weight isoforms of titin (NT-isoforms) in addition to the known N2A-, N2BA-, and N2B-titin isoforms was obtained. Comparative studies of changes in titin isoform composition and structure-functional properties of human and animal striated muscles during adaptive and pathological processes led to a conclusion about the key role of NT-isoforms of titin in maintenance of sarcomere structure and contractile function of these muscles.
这篇综述总结了我们在正常条件下、冬眠期间、真实和模拟微重力以及病理条件下（僵人综合征、中风后痉挛、扩张型心肌病、心脏肥大）研究脊椎动物横纹肌肌联蛋白异构体组成的结果。实验证据表明，哺乳动物横纹肌中除了已知的 N2A-、N2BA-和 N2B-肌联蛋白异构体外，还存在更高分子量的肌联蛋白异构体（NT-异构体）。对人类和动物横纹肌在适应和病理过程中肌联蛋白异构体组成和结构-功能特性变化的比较研究得出结论，认为肌联蛋白 NT-异构体在维持这些肌肉的肌节结构和收缩功能方面起着关键作用。
