The Effect of Experimental Hyperthyroidism on Characteristics of Actin–Myosin Interaction in Fast and Slow Skeletal Muscles

The molecular mechanism of the failure of contractile function of skeletal muscles caused by oxidative damage to myosin in hyperthyroidism is not fully understood. Using an in vitro motility assay, we studied the effect of myosin damage caused by oxidative stress in experimental hyperthyroidism on t...

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Bibliographic Details
Published in:Biochemistry (Moscow) 2018-05, Vol.83 (5), p.527-533
Main Authors: Kopylova, G. V., Shchepkin, D. V., Bershitsky, S. Y.
Format: Article
Language:English
Subjects:
Actin
Actins - metabolism
Animals
Biochemistry
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
Calcium
Calcium - metabolism
Contractility
Filaments
Health aspects
Hyperthyroidism
Hyperthyroidism - metabolism
Life Sciences
Microbiology
Molecular chains
Motility
Muscle Fibers, Fast-Twitch - metabolism
Muscle Fibers, Slow-Twitch - metabolism
Muscles
Myosin
Myosins - metabolism
Oxidation
Oxidative Stress
Physiological aspects
Rabbits
Skeletal muscle
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Summary:The molecular mechanism of the failure of contractile function of skeletal muscles caused by oxidative damage to myosin in hyperthyroidism is not fully understood. Using an in vitro motility assay, we studied the effect of myosin damage caused by oxidative stress in experimental hyperthyroidism on the actin–myosin interaction and its regulation by calcium. We found that hyperthyroidism-induced oxidation of myosin is accompanied by a decrease in the sliding velocity of the regulated thin filaments in the in vitro motility assay, and this effect is increased with the duration of the pathological process.
ISSN:0006-2979
1608-3040
DOI:10.1134/S000629791805005X