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Muscle fiber types of women after resistance training — Quantitative ultrastructure and enzyme activity

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Abstract

Muscle biopsies of the vastus lateralis muscle taken before and after 18 weeks of resistance training were compared by preparing frozen cross sections for electron microscopy and using adjacent sections for fiber typing by myosin ATPase activity. Quantitative ultrastructural changes were observed in histochemically-identified muscle fiber types of twelve young women who underwent the training. The percentage of type IIB fibers decreased and IIA fibers increased. The cross-sectional area of all major fiber types increased with training. The absolute volume of myofibrils, intermyofibrillar space, and mitochondria increased with training for most major fiber types (type I, IIA and IIAB), but the relative volume percentages were not significantly changed because of corresponding fiber hypertrophy. Mean mitochondrial size for types I and IIA and myofibril size for types IIC and IIB increased significantly with training. The capillary number per fiber and density did not change with training. Activity levels were measured for selected glycolytic and oxidative enzymes. Cytochrome oxidase and hexokinase increased significantly with training, while creatine kinase, citrate synthase, phosphofructokinase, glyceraldehyde phosphate dehydrogenase and hydroxyacyl CoA dehydrogenase enzymes were not significantly altered. The results suggest that this type of high-repetition resistance training causes the intracellular components of all fiber types to increase proportionally with an increase in fiber size. In addition, the enzyme analysis indicates the muscle as a whole may increase its oxidative phosphorylation capacity in conjunction with the decreased percentage of type IIB fibers.

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Present address: Department of Medicine, University of California at San Diego, School of Medicine, San Diego, CA, 92103, USA

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Wang, N., Hikida, R.S., Staron, R.S. et al. Muscle fiber types of women after resistance training — Quantitative ultrastructure and enzyme activity. Pflügers Arch. 424, 494–502 (1993). https://doi.org/10.1007/BF00374913

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  • DOI: https://doi.org/10.1007/BF00374913

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