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PMID: 6508759 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Myofibrillar-protein isoforms and sarcoplasmic-reticulum Ca2+-transport activity of single human muscle fibres.

The Biochemical journal ·Vol. 224 ·No. 1 ·1984-11-15 ·Pages 215-25

Salviati G, Betto R, Danieli Betto D, Zeviani M

Abstract

In this study the polymorphism of myofibrillar proteins and the Ca2+-uptake activity of sarcoplasmic reticulum were analysed in single fibres from human skeletal muscles. Two populations of histochemically identified type-I fibres were found differing in the number of light-chain isoforms of the constituent myosin, whereas the pattern of light chains of fast myosin of type-IIA and type-IIB fibres was indistinguishable. Regulatory proteins, troponin and tropomyosin, and other myofibrillar proteins, such as M- and C-proteins, showed specific isoforms in type-I and type-II fibres. Furthermore, tropomyosin presented different stoichiometries of the alpha- and beta-subunits between the two types of fibres. Sarcoplasmic-reticulum volume, as indicated by the maximum capacity for calcium oxalate accumulation, was almost identical in type-I and type-II fibres, whereas the rate of Ca2+ transport was twice as high in type-II as compared with type-I fibres. It is concluded that, in normal human muscle fibres, there is a tight segregation of fast and slow isoforms of myofibrillar proteins that is very well co-ordinated with the relaxing activity of the sarcoplasmic reticulum. These findings may thus represent a molecular correlation with the differences of the twitch-contraction time between fast and slow human motor units. This tight segregation is partially lost in the muscle fibres of elderly individuals.

MeSH Terms
Age Factors Biological Transport Calcium/metabolism Electrophoresis, Polyacrylamide Gel Female Humans Muscle Proteins/genetics,metabolism Muscles/metabolism Myofibrils/metabolism Myosins/metabolism Polymorphism, Genetic Sarcoplasmic Reticulum/metabolism
Chemicals
Muscle Proteins Myosins Calcium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Salviati G
Betto R
Danieli Betto D
Zeviani M
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46 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2240215
Published
1984-11-15
Pages
215-25
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1144416
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2240215 PMC Full Text View journal details
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