The age-related decrease in contractile speed observed in slow muscle fibers may be due to intrinsic changes in the properties of myosin with age.
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The effect of age on the motor protein myosin was examined in a novel in vitro motility assay. Myosin was extracted from soleus fibres of young (3–6 month) and old (20–24 month) rats. All fibres expressed the type I myosin heavy chain (MyHC) and the slow isoforms of the myosin light chains (MyLCs). In vitro motility speed was significantly (P < 0.001) faster in the young adult (1.43 ± 0.23 μm s–1) than in the aged group (1.27 ± 0.23 μm s–1). The result indicates that the age‐related decrease in contractile speed observed in slow fibres may be the effect of a change in the properties of myosin with age.
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No clinical implications; hypothesis-generating for myosin changes underlying age-related slowing in rodent slow fibers.
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Höök et al. (1999) studied this question.
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