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Vol. 284, Issue 2, 592-598, February 1998
Department of Pharmacology, University of Michigan Medical School,
Ann Arbor, Michigan
The stimulant drug amphetamine is postulated to enhance dopamine
release through the plasmalemmal dopamine transporter by an exchange
diffusion with synaptosomal dopamine. Because protein kinase C has been
shown to have an effect on dopamine transporter activity, we examined
the effect of protein kinase C inhibitors on endogenous dopamine
release stimulated by amphetamine in perfused rat striatal slices. At
concentrations of 1 µM, the selective protein kinase C inhibitors
chelerythrine, Ro31-8220 and calphostin C nearly completely inhibited
endogenous dopamine release elicited by 1 µM amphetamine. The
inactive analog bisindoylmaleimide V had no effect. Extracellular
Ca++ was not required for the effect of the inhibitors. The
importance of vesicular dopamine release was examined by determining
inhibitor activity in reserpine-treated rats. Dopamine release elicited by 1 µM amphetamine was not significantly altered in
reserpine-treated rats compared with control animals. Ro31-8220 at 1 µM completely blocked amphetamine-induced dopamine release in
reserpine-treated rats. Activation of protein kinase C with 250 nM of
the phorbol ester 12-O-tetradecanoylphorbol 13-acetate increased
dopamine release, and the release was not additive with 1 µM
amphetamine. Both chelerythrine and Ro31-8220 at 1 µM increased
[3H]dopamine uptake by 17% and 30%, respectively,
whereas a brief exposure to 12-O-tetradecanoylphorbol 13-acetate
slightly inhibited [3H]dopamine uptake. Our results
suggest that amphetamine-mediated dopamine release through the
plasmalemmal transporter is highly dependent on protein kinase C
activity.
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