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(Received for publication, April 22, 1996)
From the Department of Molecular and Cell Biology, University of
California at Berkeley, Berkeley, California, 94720
Calcium stores from cultured skeletal muscle
cells were depleted using cyclopiazonic acid (CPA), a reversible
inhibitor of Ca2+-ATPases at the sarcoplasmic reticulum.
Store depletion led to activation of the calcium-specific leak channel,
as assayed using single-channel patch clamp analysis and rates of
manganese influx and quenching of fura-2 fluorescence. Two novel
dihydropyridine compounds inhibited this single-channel leak channel
activity, the resting and depletion-induced manganese influx, and
refilling of the CPA-depleted intracellular calcium store. These
compounds represent the first antagonists for a calcium leak channel
and for a channel that mediates a capacitative current. The development
of the skeletal muscle capacitative current was inhibited by genistein,
a tyrosine kinase inhibitor, but was not affected by okadaic acid, a
phosphatase inhibitor, or econazole. Thus, the capacitative current in
cultured skeletal muscle cells was mediated by the calcium leak channel
and was inhibited by pharmacological antagonists and may provide a
model system for uncovering the complete set of signals leading from
store depletion to channel activation.
Volume 271, Number 37,
Issue of September 13, 1996
pp. 22358-22367
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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