Lactate inhibits Ca21-activated Ca21-channel activity from skeletal muscle sarcoplasmic reticulum
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چکیده
Favero, Terence G., Anthony C. Zable, David Colter, and Jonathan J. Abramson. Lactate inhibits Ca21-activated Ca21-channel activity from skeletal muscle sarcoplasmic reticulum. J. Appl. Physiol. 82(2): 447–452, 1997.— Sarcoplasmic reticulum (SR) Ca21-release channel function is modified by ligands that are generated during about of exercise. We have examined the effects of lactate on Ca21and caffeine-stimulated Ca21 release, [3H]ryanodine binding, and single Ca21-release channel activity of SR isolated from rabbit white skeletal muscle. Lactate, at concentrations from 10 to 30mM, inhibited Ca21and caffeine-stimulated [3H]ryanodine binding to and inhibited Ca21and caffeine-stimulated Ca21 release from SR vesicles. Lactate also inhibited caffeine activation of single-channel activity in bilayer reconstitution experiments. These findings suggest that intense muscle activity, which generates high concentrations of lactate, will disrupt excitation-contraction coupling. This may lead to decreases in Ca21 transients promoting a decline in tension development and contribute to muscle fatigue.
منابع مشابه
Effect of lactate on depolarization-induced Ca21 release in mechanically skinned skeletal muscle fibers
Dutka, T. L., and G. D. Lamb. Effect of lactate on depolarization-induced Ca21 release in mechanically skinned skeletal muscle fibers. Am. J. Physiol. Cell Physiol. 278: C517–C525, 2000.—It is unclear whether accumulation of lactate in skeletal muscle fibers during intense activity contributes to muscle fatigue. Using mechanically skinned fibers from rat and toad muscle, we were able to examine...
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