2005
DOI: 10.1111/j.1748-1716.2005.01516.x
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Human skeletal muscle myosin function at physiological and non‐physiological temperatures

Abstract: The present results suggest a significantly reduced difference in shortening velocity between different human muscle fibre types at physiological temperature than previously reported at lower temperatures (12 or 15 degrees C) with implications for human in vivo muscle function.

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Cited by 16 publications
(11 citation statements)
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References 41 publications
(69 reference statements)
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“…In vitro motility studies after extraction of myosin from millimeter short muscle fiber segments from human percutaneous muscle biopsies have shown that the aging-related slowing at the single muscle fiber level is primarily caused by altered structural-functional properties of the motor protein myosin (33,34,42). Multiple slow MHC isoforms have been identified in skeletal muscle (14,18,35,47), and the possibility cannot be excluded that the slowing in old age is associated with an aging-related upregulation of an isoform not, or less, expressed in young individuals. However, there is to our knowledge no evidence of the expression of novel slow MHC isoforms in old age with migration properties similar to the ␤/slow (type I) MHC on SDS-PAGE.…”
Section: Discussionmentioning
confidence: 99%
“…In vitro motility studies after extraction of myosin from millimeter short muscle fiber segments from human percutaneous muscle biopsies have shown that the aging-related slowing at the single muscle fiber level is primarily caused by altered structural-functional properties of the motor protein myosin (33,34,42). Multiple slow MHC isoforms have been identified in skeletal muscle (14,18,35,47), and the possibility cannot be excluded that the slowing in old age is associated with an aging-related upregulation of an isoform not, or less, expressed in young individuals. However, there is to our knowledge no evidence of the expression of novel slow MHC isoforms in old age with migration properties similar to the ␤/slow (type I) MHC on SDS-PAGE.…”
Section: Discussionmentioning
confidence: 99%
“…Although alterations in contractile function at the whole muscle level are reflective of myofiber contractile behavior (41,45,48,51), it is difficult to directly compare values obtained in isolated muscle fibers with values obtained in vivo. In addition to the factors previously mentioned, isolated myofibers are examined in vitro at 15°C, which alters peak tension, V o , and power production (4,27,34). This approach provides information about the contractile mechanics intrinsic to the myofiber in a fiber type-specific manner that provides insights into the cellular factors that may influence whole muscle performance.…”
Section: Discussionmentioning
confidence: 99%
“…These data are results of experiments conducted at relatively low temperature (15–18 °C). While this is substantially below the temperature in the intact muscle, recent data conducted at 35 °C indicate that the fiber type difference at more physiological relevant temperature is much less and in the magnitude of 1:2 between MyHC I and MyHC II fibers (Lionikas et al, 2006).…”
mentioning
confidence: 94%