Amphetamine-induced ERM Proteins Phosphorylation Is through PKCbeta Activation in PC12 Cells.
10.4196/kjpp.2011.15.4.245
- Author:
Ha Jin JEONG
1
;
Jeong Hoon KIM
;
Songhee JEON
Author Information
1. Dongguk University Research Institute of Biotechnology, Seoul 100-715, Korea. jsong0304@dongguk.edu
- Publication Type:In Vitro ; Original Article
- Keywords:
Amphetamine;
ERM proteins (ezrin, radixin, moesin);
PKCbeta;
PC12 cells;
Dopamine transporter
- MeSH:
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
- From:The Korean Journal of Physiology and Pharmacology
2011;15(4):245-249
- CountryRepublic of Korea
- Language:English
-
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.
