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Myosin isoforms, muscle fiber types, and transitions
Author(s) -
Pette Dirk,
Staron Robert S.
Publication year - 2000
Publication title -
microscopy research and technique
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.536
H-Index - 118
eISSN - 1097-0029
pISSN - 1059-910X
DOI - 10.1002/1097-0029(20000915)50:6<500::aid-jemt7>3.0.co;2-7
Subject(s) - myosin , gene isoform , fiber type , skeletal muscle , fiber , chemistry , biophysics , microbiology and biotechnology , biology , biochemistry , anatomy , gene , organic chemistry
Skeletal muscle is an extremely heterogeneous tissue composed of a variety of fast and slow fiber types and subtypes. Moreover, muscle fibers are versatile entities capable of adjusting their phenotypic properties in response to altered functional demands. Major differences between muscle fiber types relate to their myosin complement, i.e., isoforms of myosin light and heavy chains. Myosin heavy chain (MHC) isoforms appear to represent the most appropriate markers for fiber type delineation. On this basis, pure fiber types are characterized by the expression of a single MHC isoform, whereas hybrid fiber type express two or more MHC isoforms. Hybrid fibers bridge the gap between the pure fiber types. The fiber population of skeletal muscles, thus, encompasses a continuum of pure and hybrid fiber types. Under certain conditions, changes can be induced in MHC isoform expression heading in the direction of either fast‐to‐slow or slow‐to‐fast. Increased neuromuscular activity, mechanical loading, and hypothyroidism are conditions that induce fast‐to‐slow transitions, whereas reduced neuromuscular activity, mechanical unloading, and hyperthyroidism cause transitions in the slow‐to‐fast direction. Microsc. Res. Tech. 50:500–509, 2000. © 2000 Wiley‐Liss, Inc.