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Articles in PresS, published online ahead of print February 27, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00008.2002
Submitted on January 8, 2002
Accepted on February 21, 2002
1 Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN, USA; Center on Aging, University of Minnesota, Minneapolis, MN, USA
2 Physical Medicine and Rehabilitation, University of Minnesota, Minneapolis, MN, USA; Center on Aging, University of Minnesota, Minneapolis, MN, USA
* To whom correspondence should be addressed. E-mail: dl{at}ddt.biochem.umn.edu.
We tested the hypothesis that age-associated decline in muscle function is related to a change in myosin ATPase activity. Single, glycerinated semimembranosus fibers from young (8-12 mo) and aged (32-37 mo) F344xBN male rats were analyzed simultaneously for force and myosin ATPase activity over a range of [Ca2+]. Maximal force generation was ~20% lower in fibers from aged animals (P = 0.02), but myosin ATPase activity was not different between fibers from young and aged rats (686 ±46 µM/s, n = 30; 697±46 µM/s, n = 33; P = 0.89). The apparent rate constant for the dissociation of strong-binding myosin from actin (gapp) was calculated to be ~30% greater in fibers from aged animals (P = 0.03) indicating that the lower force produced by fibers from aged animals is due to a greater flux of myosin heads from the strong-binding state to the weak-binding state during contraction. This is in agreement with our previous electron paramagnetic resonance experiments, which showed that fibers from older rats have a reduced fraction of myosin heads in the strong-binding state during a maximal isometric contraction.
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