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Vol. 273, Issue 1, 242-247, January 2, 1998

Sphingosine Inhibits Voltage-operated Calcium Channels in GH4C1 Cells

Alexey TitievskyDagger , Ira TitievskayaDagger , Michael PasternackDagger , Kai KailaDagger , and Kid TörnquistDagger §

From the Dagger  Department of Biosciences, Division of Animal Physiology, University of Helsinki, Helsinki, the § Minerva Foundation Institute for Medical Research, Helsinki, and the Department of Biology, Åbo Akademi University, Turku, Finland

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 GDPbeta 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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