Lactate inhibits Ca2+-activated Ca2+-channel activity from skeletal muscle sarcoplasmic reticulum |
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Authors: | Favero Terence G; Zable Anthony C; Colter David; Abramson Jonathan J |
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Institution: | Favero, Terence G.; Zable, , Anthony C.; Colter, , David; Abramson, Jonathan J. |
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Abstract: | Favero, Terence G., Anthony C. Zable, David Colter, andJonathan J. Abramson. Lactate inhibits Ca2+-activatedCa2+-channel activity from skeletal muscle sarcoplasmicreticulum. J. Appl. Physiol. 82(2): 447-452, 1997. Sarcoplasmic reticulum (SR) Ca2+-release channelfunction is modified by ligands that are generated during about ofexercise. We have examined the effects of lactate on Ca2+-and caffeine-stimulated Ca2+ release,3H]ryanodine binding, and singleCa2+-release channel activity of SR isolated from rabbitwhite skeletal muscle. Lactate, at concentrations from 10 to 30 mM,inhibited Ca2+- and caffeine-stimulated3H]ryanodine binding to and inhibited Ca2+-and caffeine-stimulated Ca2+ release from SR vesicles.Lactate also inhibited caffeine activation of single-channel activityin bilayer reconstitution experiments. These findings suggest thatintense muscle activity, which generates high concentrations oflactate, will disrupt excitation-contraction coupling. This may lead todecreases in Ca2+ transients promoting a decline in tensiondevelopment and contribute to muscle fatigue. |
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