Comparison of Functional Characteristics of Myosin in Fast and Slow Skeletal Muscles

被引：0
作者：
Shchepkin, D., V [1 ]
Nabiev, S. R. [1 ]
Koubassova, N. A. [2 ]
Bershitsky, S. Y. [1 ]
Kopylova, G., V [1 ]
机构：
[1] Russian Acad Sci, Inst Immunol & Physiol, Ural Div, Ekaterinburg, Russia
[2] Moscow MV Lomonosov State Univ, Inst Mech, Moscow, Russia
来源：
BULLETIN OF EXPERIMENTAL BIOLOGY AND MEDICINE | 2020年 / 169卷 / 03期
基金：
俄罗斯基础研究基金会;
关键词：
skeletal myosin; myosin isoforms; actin-myosin interaction; optical trap; in vitro motility assay; HEAVY-CHAIN; FIBER TYPES; ISOFORMS; FILAMENTS; VELOCITY;
D O I：
10.1007/s10517-020-04882-x
中图分类号：
R-3 [医学研究方法]; R3 [基础医学];
学科分类号：
1001 ;
摘要：
Myosins of fast and slow skeletal muscles differ by the isoform composition of the heavy and light chains. We compared functional characteristics of myosin from the fast (m. psoas) and slow (m. soleus) muscles of rabbits. The parameters of single actin-myosin interaction were measured in an optical trap, and the characteristics of the Ca(2+)regulation of actin-myosin interaction were studied using anin vitromotility assay. The duration of interaction of myosin from the fast muscle with actin was shorter and the filament sliding velocity over this myosin was higher than the corresponding parameters for myosin from the slow muscle. The dependencepCa-velocity for myosin from the fast muscle was less sensitive to Ca(2+)than that of slow muscle myosin. Thus, functional properties of myosin determine not only mechanical and kinetic characteristics of muscle contraction, but also the peculiarities of its Ca(2+)regulation.
引用
收藏
页码：338 / 341
页数：4
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