Journal of Applied Physiology
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J Appl Physiol 82: 1297-1304, 1997;
8750-7587/97 $5.00
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Journal of Applied Physiology
Vol. 82, No. 4, pp. 1297-1304, April 1997
EXERCISE AND MUSCLE

Response of compressed skinned skeletal muscle fibers to conditions that simulate fatigue

Kathryn H. Myburgh and Roger Cooke

Department of Biochemistry and Biophysics and Cardiovascular Research Institute, University of California, San Francisco, California 94143

Received 7 August 1996; accepted in final form 25 November 1996.

Myburgh, Kathryn H., and Roger Cooke. Response of compressed skinned skeletal muscle fibers to conditions that simulate fatigue. J. Appl. Physiol. 82(4): 1297-1304, 1997.---During fatigue, muscles become weaker, slower, and more economical at producing tension. Studies of skinned muscle fibers can explain some but not all of these effects, and, in particular, they are less economical in conditions that simulate fatigue. We investigated three factors that may contribute to the different behavior of skinned fibers. 1) Skinned fibers have increased myofilament lattice spacing, which is reversible by osmotic compression. 2) A myosin subunit becomes phosphorylated during fatigue. 3) Inosine 5'-monophosphate (IMP) accumulates during fatigue. We tested the response of phosphorylated and unphosphorylated single skinned fibers (isometric tension, contraction velocity, and adenosinetriphosphatase activity) to changes in lattice spacing (0-5% dextran) and IMP (0-5 mM) in the presence of altered concentrations of Pi (3-25 mM), H+ (pH 7-6.2), and ADP (0-5 mM). The response of maximally activated skinned fibers to the direct metabolites of ATP hydrolysis is not altered by osmotic compression, phosphorylating myosin subunits, or increasing IMP concentration. These factors, therefore, do not explain the discrepancy between intact and skinned fibers during fatigue.

pH; phosphate; force; velocity; mechanics; inosine 5'-monophosphate; phosphorylation; lattice compression

0161-7567/97 $5.00 Copyright © 1997 the American Physiological Society




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