Journal of Applied Physiology AJP: Renal Physiology
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J Appl Physiol 94: 923-929, 2003; doi:10.1152/japplphysiol.00549.2002
8750-7587/03 $5.00
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Vol. 94, Issue 3, 923-929, March 2003

Endurance training-induced changes in alkali light chain patterns in type IIB fibers of the rat

Masanobu Wada1, Shuichiro Inashima1, Takashi Yamada2, and Satoshi Matsunaga3

1 Faculty of Integrated Arts and Sciences, 2 Faculty of Medicine, Hiroshima University, Higashihiroshima, 739-8521; and 3 Institute of Health Sciences and Physical Education, Osaka City University, Osaka, Japan 558-8585

The effects of endurance training on the expression of myosin were electrophoretically analyzed in the deep portion of vastus lateralis muscle from the rat. A 10-wk running program led to increases (P < 0.01) in myosin heavy chain (MHC) 2a and 2d with a decrease (P < 0.01) in MHC2b. Training also evoked a rearrangement of the isomyosin pattern with decreases in fast isomyosin (FM) 1 (P < 0.01) and FM2 (P < 0.05) and a rise in intermediate isomyosin (P < 0.01). These changes were accompanied by a 61% decrease (P < 0.01) in myosin light chain (MLC) 3F (11.8 ± 2.7 vs. 4.6 ± 4.2%). Two-dimensional electrophoresis made it possible to separate the triplet of isomyosins (FMb) consisting of MHC2b. Training elicited a 26% decrease (P < 0.05) in the FM1b fraction within FMb, i.e., FM1b/(FM1b + FM2b + FM3b) (24.2 ± 5.5 vs. 18.0 ± 4.3%). These changes resulted in a 10% decrease (P < 0.05) in the MLC3F fraction, i.e., MLC3F/(MLC1F + MLC3F), in FMb (44.9 ± 4.5 vs. 40.3 ± 3.2%). These results suggest that endurance training may exert the depressive effect on the contractile velocity of type IIB fibers and that a training-induced decrease in the contractile velocity of whole muscle may be caused by alterations in fast alkali MLC complements within a given fiber type as well as by transitions in MHC-based fiber populations.

myosin heavy chain; myosin light chain; isomyosin; isoform; electrophoresis


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