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Korean J Physiol Pharmacol. 2011 Aug;15(4):245-9. doi: 10.4196/kjpp.2011.15.4.245. Epub 2011 Aug 31.

Amphetamine-induced ERM Proteins Phosphorylation Is through PKCβ Activation in PC12 Cells.

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  • 1Dongguk University Research Institute of Biotechnology, Seoul 100-715, Korea.

Abstract

Amphetamine, a synthetic psychostimulant, is transported by the dopamine transporter (DAT) to the cytosol and increases the exchange of extracellular amphetamine by intracellular dopamine. Recently, we reported that the phosphorylation levels of ezrin-radixin-moesin (ERM) proteins are regulated by psychostimulant drugs in the nucleus accumbens, a brain area important for drug addiction. However, the significance of ERM proteins phosphorylation in response to drugs of abuse has not been fully investigated. In this study, using PC12 cells as an in vitro cell model, we showed that amphetamine increases ERM proteins phosphorylation and protein kinase C (PKC) β inhibitor, but not extracellular signal-regulated kinase (ERK) or phosphatidylinositol 3-kinases (PI3K) inhibitors, abolished this effect. Further, we observed that DAT inhibitor suppressed amphetamine-induced ERM proteins phosphorylation in PC12 cells. These results suggest that PKCβ-induced DAT regulation may be involved in amphetmaine-induced ERM proteins phosphorylation.

KEYWORDS:

Amphetamine; Dopamine transporter; ERM proteins (ezrin, radixin, moesin); PC12 cells; PKCβ

PMID:
21994482
PMCID:
PMC3186925
DOI:
10.4196/kjpp.2011.15.4.245
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