Polymorphism of myofibrillar proteins of rabbit skeletal-muscle fibres. An electrophoretic study of single fibres
- 1 November 1982
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 207 (2), 261-272
- https://doi.org/10.1042/bj2070261
Abstract
Rabbit predominantly fast-twitch-fibre and predominantly slow-twitch-fibre skeletal muscles of the hind limbs, the psoas, the diaphragm and the masseter muscles were fibre-typed by one-dimensional polyacrylamide-gel electrophoresis of the myofibrillar proteins of chemically skinned single fibres. Investigation of the distribution of fast-twitch-fibre and slow-twitch-fibre isoforms of myosin light chains and the type of myosin heavy chains, based on peptide ‘maps’ published in Cleveland. Fischer, Kirschner & Laemmli [(1977) J. Biol. Chem. 252, 1102-1106], allowed a classification of muscle fibres into four classes, corresponding to histochemical types I, IIA, IIB and IIC. Type I fibres with a pure slow-twitch-type of myosin were found to be characterized by a unique set of isoforms of troponins I, C and T, in agreement with the immunological data of Dhoot & Perry [(1979) Nature (London) 278, 714-718], by predominance of the beta-tropomyosin subunit and by the presence of a small amount of an additional tropomyosin subunit, apparently dissimilar from fast-twitch-fibre alpha-tropomyosin subunit. The myofibrillar composition of type IIB fast-twitch white fibres was the mirror image of that found for slow-twitch fibres in that the fast-twitch-fibre isoforms only of the troponin subunits were present and the alpha-tropomyosin subunit predominated. Type IIA fast-twitch red fibres showed a troponin subunit composition identical with that of type IIB fast-twitch white fibres. On the other hand, a unique type of myosin heavy chains was found to be associated with type IIA fibres. Furthermore, the myosin light-chain composition of these fibres was invariably characterized by a small amount of LC3F light chain and by a pattern that was either a pure fast-twitch-fibre light-chain pattern or a hybrid LC1F/LC2F/LC3F/LC1Sb light-chain pattern. By these criteria type IIA fibres could be distinguished from type IIC intermediate fibres, which showed coexistence of fast-twitch-fibre and slow-twitch-fibre forms of myosin light chains and of troponin subunits.This publication has 42 references indexed in Scilit:
- Gene Expression of Myofibrillar Proteins in Single Muscle Fibers of Adult Chicken: Micro Two Dimensional Gel Electrophoretic Analysis1The Journal of Biochemistry, 1981
- Electrophoretic analysis of proteins from single bovine muscle fibresBiochemical Journal, 1981
- A highly sensitive silver stain for detecting proteins and peptides in polyacrylamide gelsAnalytical Biochemistry, 1979
- Changes in tropomyosin subunit pattern in chronic electrically stimulated rabbit fast musclesBiochemical and Biophysical Research Communications, 1979
- Immunohistochemical evidence for myosin polymorphism in the chicken heartNature, 1978
- Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.Journal of Biological Chemistry, 1977
- Discrimination between fiber populations in mammalian skeletal muscle by using ultrastructural parametersJournal of Ultrastructure Research, 1976
- Characterization of myosin light chains from histochemically identified fibres of rabbit psoas muscleFEBS Letters, 1975
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Qualitative differences between actomyosin ATPase of slow and fast mammalian muscleExperimental Neurology, 1969