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Vol. 273, Issue 1, 242-247, January 2, 1998
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From the In the present study we investigated the
mechanism of inhibitory action of sphingosine (SP) on voltage-activated
calcium channels (VOCCs) in pituitary
GH4C1 cells. Using the patch-clamp
technique in the whole-cell mode, we show that SP inhibits
Ba2+ currents (IBa) when 0.1 mM BAPTA is included in the patch pipette. However, when
the BAPTA concentration was raised to 1-10 mM, SP was
without a significant effect. The effect of SP was apparently not
mediated via a kinase, as it was not inhibited by staurosporine. By
using the double-pulse protocol (to release possible functional inhibition of the VOCCs by G proteins), we observed that G proteins apparently evoked very little functional inhibition of the VOCCs. Furthermore, including GDP Department of Biosciences,
S (guanyl-5
-yl thiophosphate) in the patch pipette did not alter the inhibitory effect of SP on the Ba2+ current, suggesting that SP did not modulate the VOCCs
via a G protein-dependent pathway. Single-channel
experiments with SP in the pipette, and experiments with excised
outside-out patches, suggested that SP directly inhibited VOCCs. The
main mechanism of action was a dose-dependent prolongation
of the closed time of the channels. The results thus show that SP is a
potent inhibitor of VOCCs in GH4C1 cells, and
that calcium may be a cofactor in this inhibition.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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