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PMID: 1605043 Published · ppublish English Journal Article

Myosin heavy chain isoform transition in ageing fast and slow muscles of the rat.

Acta physiologica Scandinavica ·Vol. 144 ·No. 4 ·1992-04-00 ·Pages 419-23

Sugiura T, Matoba H, Miyata H, Kawai Y, Murakami N

Abstract

Using gradient sodium dodecyl sulphate-polyacrylamide gel electrophoresis, myosin heavy chain (MHC) isoforms were studied in the extensor digitorum longus (EDL) and the soleus muscles of male Wistar rats at different ages (5, 10, 20 weeks, 1 and 2 years). In the EDL muscle, four types of MHC isoforms were observed in all age groups. There was an increase in the percentage of HCIId and a concomitant decrease in the percentage of HCIIb with increasing age. No significant difference was observed in the percentages of HCI and HCIIa isoforms in all the age groups. In contrast, the soleus muscle contained two MHC isoforms, HCI and HCIIa. There was an increase in the percentage of HCI and a concomitant decrease in the percentage of HCIIa with increasing age. These results suggest that age-related changes in the MHC isoforms in both the fast-twitch EDL and the slow-twitch soleus muscles are one factor underlying the age-related decrease in the speed of muscle contraction.

MeSH Terms
Aging/metabolism Animals Electrophoresis, Polyacrylamide Gel Male Muscle Contraction/physiology Muscles/metabolism Myosins/isolation & purification,metabolism Rats Rats, Inbred Strains
Chemicals
Myosins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Sugiura T
Laboratory of Biomechanics and Physiology, Faculty of Liberal Arts, Yamaguchi University, Japan.
Matoba H
Miyata H
Kawai Y
Murakami N
Article Info
Journal
Acta physiologica Scandinavica
Abbr.
Acta Physiol Scand
ISSN
0001-6772
Published
1992-04-00
Pages
419-23
Language
English
Region
England
NLM ID
0370362
Subset
IM
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