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Department of Anesthesiology and Department of Physiology and Biophysics, Mayo Clinic and Foundation, Rochester, Minnesota 55905
Received 12 August 1996; accepted in final form 22 May 1997.
Perkins, William J., Young-Soo Han, and Gary C. Sieck.
Skeletal muscle force and actomyosin ATPase activity reduced by
nitric oxide donor. J. Appl. Physiol.
83(4): 1326-1332, 1997.
Nitric oxide (NO) may exert direct
effects on actin-myosin cross-bridge cycling by modulating critical
thiols on the myosin head. In the present study, the effects of the NO
donor sodium nitroprusside (SNP; 100 µM to 10 mM) on mechanical
properties and actomyosin adenosinetriphosphatase (ATPase) activity of
single permeabilized muscle fibers from the rabbit psoas muscle were
determined. The effects of
N-ethylmaleimide (NEM; 5-250
µM), a thiol-specific alkylating reagent, on mechanical properties of
single fibers were also evaluated. Both NEM (
25 µM) and SNP (1
mM) significantly inhibited isometric force and actomyosin ATPase
activity. The unloaded shortening velocity of SNP-treated single fibers
was decreased, but to a lesser extent, suggesting that SNP effects on
isometric force and actomyosin ATPase were largely due to decreased cross-bridge recruitment. The calcium sensitivity of SNP-treated single
fibers was also decreased. The effects of SNP, but not NEM, on force
and actomyosin ATPase activity were reversed by treatment with 10 mM
DL-dithiothreitol, a
thiol-reducing agent. We conclude that the NO donor SNP inhibits
contractile function caused by reversible oxidation of contractile
protein thiols.
rabbit psoas; pharmacology; sodium nitroprusside; sulfhydryl reagents; ethylmaleimide; dithiothreitol; adenosinetriphosphatase
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