Korean J Physiol Pharmacol.  2011 Aug;15(4):245-249. 10.4196/kjpp.2011.15.4.245.

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

• Jeong HJ
• Kim JH
• Jeon S

• KMID: 1448929
• DOI: http://doi.org/10.4196/kjpp.2011.15.4.245

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) beta 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 PKCbeta-induced DAT regulation may be involved in amphetmaine-induced ERM proteins phosphorylation.

Keyword

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

MeSH Terms

Amphetamine
Animals
Brain
Cytosol
Dopamine
Dopamine Plasma Membrane Transport Proteins
Nucleus Accumbens
PC12 Cells
Phosphatidylinositol 3-Kinases
Phosphorylation
Phosphotransferases
Protein Kinase C
Proteins
Street Drugs
Substance-Related Disorders
Amphetamine
Dopamine
Dopamine Plasma Membrane Transport Proteins
Phosphatidylinositol 3-Kinases
Phosphotransferases
Protein Kinase C
Proteins
Street Drugs