The Korean Journal of Physiology and Pharmacology

  • 제15권4호
  • /
  • Pages.245-249
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  • 2011
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  • 1226-4512(pISSN)
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  • 2093-3827(eISSN)
대한약리학회 (The Korean Society of Pharmacology)
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Amphetamine-induced ERM Proteins Phosphorylation Is through $PKC{\beta}$ Activation in PC12 Cells

  • Jeong, Ha-Jin (Dongguk University Research Institute of Biotechnology) ;
  • Kim, Jeong-Hoon (Department of Physiology, Brain Korea 21 Project for Medical Science, Yonsei University College of Medicine) ;
  • Jeon, Song-Hee (Dongguk University Research Institute of Biotechnology)
  • 투고 : 2011.07.18
  • 심사 : 2011.08.23
  • 발행 : 2011.08.30
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초록

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 $PKC{\beta}$-induced DAT regulation may be involved in amphetmaine-induced ERM proteins phosphorylation.

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참고문헌

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피인용 문헌

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