The distribution of myosin heavy chain (MHC) isoforms, fiber type composition, and fiber size of the vastus lateralis muscle were analyzed by sodium dodecylsulfate polymerase gel electrophoresis (SDS-PAGE), ATPase histochemistry, and immunocytochemistry in a group of adult sedentary men before and a
Favourable associations between the myosin heavy-chain and light-chain isoforms in human skeletal muscle
โ Scribed by Masanobu Wada; Shigeru Katsuta; Tokuhide Doi; Shin -ya Kuno
- Publisher
- Springer
- Year
- 1990
- Tongue
- English
- Weight
- 638 KB
- Volume
- 416
- Category
- Article
- ISSN
- 0031-6768
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โฆ Synopsis
Histochemical and biochemical analyses were performed in order to examine the relationship between myosin light-chain (LC) isoforms and fibre-type distributions in whole human skeletal muscle. Muscle biopsies were obtained from the vastus lateralis muscle in six healthy men, and analysed for the relative area occupied by each fibre type (percentage of fibre type area) and the molar ratio of each LC isoform. The percentage of type I fibre area was positively correlated with the molar ratio of slow LC (LC1s and LC2s) to total LC. The regression line was located below the line of unity. Also, the ratio of percentage of type IIa fibre area to that of type II fibre area was positively correlated with the molar ratio of the fast alkali LC LC1f to fast alkali LCs LC1f and LC3f. These results support previous study, having shown that in human skeletal muscle some type I fibres express various amounts of fast LC in addition to slow LC and suggest that fast myosin heavy-chain HCIIa is favourably associated with LC1f, whereas HCIIb is favourably associated with LC3f.
๐ SIMILAR VOLUMES
The myosin heavy chain (MHC) composition of slng~ibres frc~nm, vastus lateralis was analysed by one-dimensional electrophoresis and immunoblottinq in three groups of young men with distinct difference in physical activity patterns. No major co-existence of MHC isoforms was found in the group with so