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1 Departments of Anesthesiology and Physiology & Biophysics, Mayo Medical School, Rochester, MN, USA
* To whom correspondence should be addressed. E-mail: sieck.gary{at}mayo.edu.
Early postnatal development of rat diaphragm muscle (DIAm) is marked by dramatic transitions in myosin heavy chain (MHC) isoform expression. We hypothesized that the transition from MHCNeo to adult fast MHC isoform expression in DIAm fibers is accompanied by an increase in both the maximum velocity of the actomyosin ATPase reaction (Vmax ATPase) and the ATP consumption rate during maximum isometric activation (ATPiso). Rat DIAm fibers were evaluated at postnatal day 0, 14 and 28 (D-0, D-14 and D-28) and in adults (D-84). Across all ages, Vmax ATPase of fibers was significantly higher than ATPiso. The reserve capacity for ATP consumption [1- (ratio of ATPiso to Vmax ATPase)] was remarkably constant (~55-60%) across age groups, although at D-28 and in adults the reserve capacity for ATP consumption was slightly higher for fibers expressing MHCSlow compare to fast MHC isoforms. At D-28 and in adults, both Vmax ATPase and ATPiso were lower in fibers expressing MHCSlow followed in rank order by fibers expressing MHC2A, MHC2X and MHC2B. For fibers expressing MHCNeo, Vmax ATPase and ATPiso were comparable to values for adult fibers expressing MHCSlow, but significantly lower than values for fibers expressing fast MHC isoforms. We conclude that postnatal transitions from MHCNeo to adult fast MHC isoform expression in DIAm fibers are associated with corresponding but disproportionate changes in Vmax ATPase and ATPiso.
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