期刊
EXPERIMENTAL GERONTOLOGY
卷 42, 期 10, 页码 931-938出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.exger.2007.06.015
关键词
actin; myosin; aged muscle; enzymatic activity; oxidative modifications
资金
- NIAMS NIH HHS [AR032961, R01 AR032961, R01 AR032961-24] Funding Source: Medline
- NIA NIH HHS [R01 AG017768-03, K02 AG021626-01, K02 AG021626, AG21626, AG026160, R01 AG017768, R01 AG017768-04, R01 AG026160-04, K02 AG021626-04, R37 AG026160, R01 AG026160, K02 AG021626-03, R01 AG017768-02, K02 AG021626-02, R01 AG017768-01A1, AG17768] Funding Source: Medline
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.
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