Unloaded shortening velocity and myosin heavy chain and alkali light chain isoform composition in rat skeletal muscle fibres.
- 15 July 1994
- journal article
- Published by Wiley in The Journal of Physiology
- Vol. 478 (2) , 341-349
- https://doi.org/10.1113/jphysiol.1994.sp020254
Abstract
1. This study aims to assess the role of myosin heavy chain (MHC) and alkali myosin light chain (MLC) isoforms in determining maximum velocity of shortening in fast skeletal muscle fibres. 2. The maximum velocity of shortening as determined by the slack test (Vo) was tested for its relationship with MHC composition and with alkali MLC isoform ratio of fast fibres of known MHC composition. 3. MHC isoform composition was determined using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and monoclonal antibodies against MHCs, and combining the results obtained using the two methods. Three groups of fast fibres containing only one MHC isoform were identified: IIA, IIX and IIB fibres containing respectively IIA MHC, IIX MHC and IIB MHC. Fibres containing more than one MHC isoform were discarded. 4. The mean Vo value of IIA fibres was 2.33 +/- 0.29 muscle lengths per second (L s-1; mean +/- S.D.), this was significantly lower than that for IIX fibres (3.07 +/- 0.70 L s-1) which in turn had a mean Vo value significantly lower than that for IIB fibres (3.69 +/- 1.01 L s-1). 5. The relative proportion of alkali MLC isoforms (MLC3f, MLC1f) was determined by means of electrophoretic separation and densitometric quantification and was expressed as MLC3f/MLC2f with reference to the dithio-nitrobenzoic acid (DTNB) light chain (MLC2f). The mean value of the MLC3f/MLC2f ratio was significantly lower in IIA than in IIX and IIB fibres. 6. Vo was found to be proportional to the relative content of MLC3f in IIA, IIX and IIB fibres.(ABSTRACT TRUNCATED AT 250 WORDS)Keywords
This publication has 27 references indexed in Scilit:
- Three myosin heavy chain isoforms in type 2 skeletal muscle fibresJournal of Muscle Research and Cell Motility, 1989
- Three fast myosin heavy chains in adult rat skeletal muscleFEBS Letters, 1988
- Type 1, 2A, and 2B myosin heavy chain electrophoretic analysis of rat muscle fibersBiochemical and Biophysical Research Communications, 1986
- Differential binding of rabbit fast muscle myosin light chain isoenzymes to regulated actinFEBS Letters, 1985
- A sensitive SDS-page method separating myosin heavy chain isoforms of rat skeletal muscles reveals the heterogeneous nature of the embryonic myosinBiochemical and Biophysical Research Communications, 1983
- Assembly and kinetic properties of myosin light chain isozymes from fast skeletal muscleJournal of Molecular Biology, 1983
- Hydrolysis of ATP and reversible binding to F-actin by myosin heavy chains free of all light chainsNature, 1981
- Fast-white and fast-red isomyosins in guinea pig musclesBiochemical and Biophysical Research Communications, 1980
- Fast and slow myosin within single skeletal muscle fibres of adult rabbitsNature, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970