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

Authors
 Ha Jin Jeong ; Jeong-Hoon Kim ; Songhee Jeon 
Citation
 Korean Journal of Physiology & Pharmacology, Vol.15(4) : 245~249, 2011 
Journal Title
 Korean Journal of Physiology & Pharmacology 
ISSN
 1226-4512 
Issue Date
2011
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.
URI
http://ir.ymlib.yonsei.ac.kr/handle/22282913/94341
DOI
10.4196/kjpp.2011.15.4.245
Appears in Collections:
1. 연구논문 > 1. College of Medicine > Dept. of Physiology
Yonsei Authors
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