Relationships between alkali light-chain complement and myosin heavy-chain isoforms in single fast-twitch fibers of rat and rabbit.
The present study compares the alkali myosin light chain (LC) complement of the fast fiber types IIB, IID and IIA in single fibers from rat muscle, as well as in type IID and type IIA fibers from rabbit muscle. Single fibers were classified according to their electrophoretically determined myosin heavy chain (HC) isoforms, HCIIb, HCIId, and HCIIa. Alkali myosin light chains were analysed by densitometric evaluation of two-dimensional electrophoresis performed on extracts from the same fibers. On the average, the fraction of LC3f, i.e. LC3f/(LC1f+LC3f), was highest in type IIB fibers and lowest in type IIA fibers. Type IID fibers occupied an intermediate position. Also in the rabbit, type IID fibers displayed a higher fraction of LC3f than type IIA fibers. Large scattering of the LC3f fraction in IIB, IID, and IIA fibers indicated that each fiber type is composed of fibers identical with regard to their specific myosin heavy chain complement, but heterogeneous with regard to their fast alkali light chain composition and the resulting light-chain-based isomyosins. It is suggested that the variable proportions of the two alkali light chains in the three fast fiber populations serve as a fine tuning of contractile velocities within the ranges determined by the three fast myosin heavy-chain isoforms.
Fakultät für Biologie, Universität Konstanz, Germany.
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Wada
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D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D008297:Male; D009132:Muscles / Q000737:chemistry*; D009218:Myosins / Q000032:analysis*; D011817:Rabbits; D051381:Rats; D017208:Rats, Wistar; D013237:Stereoisomerism
D009218:Myosins