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J. Gen. Physiol.,
Volume 110, Number 6, December 1, 1997 749-762
From the * Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, Ohio 44106; The ryanodine receptor (RyR)/Ca2+ release channel is an essential component of excitation-contraction coupling in striated muscle cells. To study the function and regulation of the Ca2+ release channel, we
tested the effect of caffeine on the full-length and carboxyl-terminal portion of skeletal muscle RyR expressed in a
Chinese hamster ovary (CHO) cell line. Caffeine induced openings of the full length RyR channels in a concentration-dependent manner, but it had no effect on the carboxyl-terminal RyR channels. CHO cells expressing the
carboxyl-terminal RyR proteins displayed spontaneous changes of intracellular [Ca2+]. Unlike the native RyR
channels in muscle cells, which display localized Ca2+ release events (i.e., "Ca2+ sparks" in cardiac muscle and "local release events" in skeletal muscle), CHO cells expressing the full length RyR proteins did not exhibit detectable spontaneous or caffeine-induced local Ca2+ release events. Our data suggest that the binding site for caffeine is likely to reside within the amino-terminal portion of RyR, and the localized Ca2+ release events observed in muscle cells may involve gating of a group of Ca2+ release channels and/or interaction of RyR with muscle-specific proteins.
Department of
Physiology, University of Maryland, Baltimore, Maryland 21201; and § Department of Pharmacology, University of Tokyo, Tokyo 113, Japan
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