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1 Department of Biology, University of Portland, Portland, Oregon 97203; and 2 Department of Physics, Portland State University, Portland, Oregon 97207
Received 6 June 1996; accepted in final form 3 October 1996.
Favero, Terence G., Anthony C. Zable, David Colter, and
Jonathan J. Abramson. Lactate inhibits Ca2+-activated
Ca2+-channel activity from skeletal muscle sarcoplasmic
reticulum. J. Appl. Physiol. 82(2): 447-452, 1997.
Sarcoplasmic reticulum (SR) Ca2+-release channel
function is modified by ligands that are generated during about of
exercise. We have examined the effects of lactate on Ca2+-
and caffeine-stimulated Ca2+ release,
[3H]ryanodine binding, and single
Ca2+-release channel activity of SR isolated from rabbit
white skeletal muscle. Lactate, at concentrations from 10 to 30 mM,
inhibited Ca2+- and caffeine-stimulated
[3H]ryanodine binding to and inhibited Ca2+-
and caffeine-stimulated Ca2+ 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 Ca2+ transients promoting a decline in tension
development and contribute to muscle fatigue.
calcium; muscle fatigue; caffeine; lactate; skeletal muscle
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