Seasonal changes in the isoform composition of the myosin heavy chains in skeletal muscles of hibernating ground squirrels Spermophilus undulatus

被引：13
|
作者：
Lazareva M.V. [1 ]
Trapeznikova K.O. [1 ]
Vikhlyantsev I.M. [2 ]
Bobylev A.G. [2 ]
Klimov A.A. [2 ]
Podlubnaya Z.A. [2 ,3 ]
机构：
[1] Belgorod State University, Belgorod
[2] Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region
[3] Pushchino State Institute of Natural Sciences, Pushchino, Moscow Region
来源：
Biophysics | 2012年 / 57卷 / 6期
基金：
俄罗斯基础研究基金会;
关键词：
hibernation; isoforms of myosin heavy chains; skeletal muscles;
D O I：
10.1134/S0006350912060085
中图分类号：
学科分类号：
摘要：
Seasonal changes of the isoform composition of myosin heavy chains in skeletal muscles (m. triceps, m. longissimus dorsi, m. soleus, m. gastrocnemius, m. vastus lateralis) of hibernating ground squirrels Spermophilus undulatus were studied. Functional properties of myosin (the actin-activated ATPase activity and its Ca2+-sensitivity in vitro) were also examined. It was observed that the content of slow myosin heavy chain I isoform increased and the content of fast IIx/d isoform decreased in muscles of torpid ground squirrels and animals which are active in autumn and winter. In muscles of these animals the content of N2A-titin isoform decreased although the relative content of NT-titin isoform, observed in striated muscles of mammals in our previous experimental works, increased. Actin-activated ATPase activity and Ca2+-sensitivity of myosin isolated from skeletal muscles of torpid and interbout ground squirrels were found to reduce. The changes observed are discussed in the context of adaptation of skeletal muscles of ground squirrels to hibernation conditions. © 2012 Pleiades Publishing, Ltd.
引用
收藏
页码：764 / 768
页数：4
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