Age-related decline in actomyosin structure and function

被引：42
|
作者：
Prochniewicz, Ewa [1 ]
Thompson, LaDora V.
Thomas, David D.
机构：
[1] Univ Minnesota, Dept Biochem, Minneapolis, MN 55455 USA
[2] Univ Minnesota, Dept Mol Biol & Biophys, Minneapolis, MN 55455 USA
[3] Univ Minnesota, Dept Phys Med & Rehabil, Minneapolis, MN 55455 USA
来源：
EXPERIMENTAL GERONTOLOGY | 2007年 / 42卷 / 10期
关键词：
actin; myosin; aged muscle; enzymatic activity; oxidative modifications;
D O I：
10.1016/j.exger.2007.06.015
中图分类号：
R592 [老年病学]; C [社会科学总论];
学科分类号：
03 ; 0303 ; 100203 ;
摘要：
This review focuses on the role of changes in the contractile proteins actin and myosin in age-related deterioration of skeletal muscle function. Functional and structural changes in contractile proteins have been determined indirectly from specific force and unloaded shortening velocity of permeabilized muscle fibers, and were detected directly from site-directed spectroscopy in muscle fibers and from biochemical analysis of purified actin and myosin. Contractile proteins from aged and young muscle differ in (a) myosin and actomyosin ATPase activities, (b) structural states of myosin in contracting muscle, (c) the state of oxidative modifications. The extent of age-related physiological and molecular changes is dependent on the studied animal, the animal's age, and the type of muscle. Therefore, understanding the aging process requires systematic, multidisciplinary studies on physiological, biochemical, structural, and chemical changes in specific muscles. (C) 2007 Elsevier Inc. All rights reserved.
引用
收藏
页码：931 / 938
页数：8
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