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Published on: March 5, 2019
Amphetamine-induced ERM Proteins Phosphorylation Is through PKCβ Activation in PC12 Cells
Ha Jin Jeong1, Jeong-Hoon Kim, Songhee Jeon
1Dongguk University Research Institute of Biotechnology, Seoul 100-715, Korea.
Summary
Amphetamine increases ezrin-radixin-moesin (ERM) protein phosphorylation via dopamine transporter (DAT) regulation. Protein kinase C beta (PKCβ) is involved in this amphetamine-induced effect.
Area of Science:
- Neuroscience
- Molecular Biology
- Pharmacology
Background:
- Psychostimulant drugs, like amphetamine, impact brain regions crucial for addiction.
- The role of ezrin-radixin-moesin (ERM) protein phosphorylation in response to drugs of abuse requires further investigation.
- Amphetamine is transported by the dopamine transporter (DAT), influencing dopamine exchange.
Purpose of the Study:
- To investigate the involvement of ERM protein phosphorylation in amphetamine's effects.
- To identify the specific signaling pathways, such as protein kinase C (PKC) and extracellular signal-regulated kinase (ERK), involved in amphetamine-induced ERM phosphorylation.
- To explore the relationship between the dopamine transporter (DAT) and ERM protein phosphorylation in response to amphetamine.
Main Methods:
- Utilized PC12 cells as an in vitro model system.
- Administered amphetamine and specific inhibitors (PKCβ, ERK, PI3K, DAT) to cell cultures.
- Monitored and analyzed ERM protein phosphorylation levels.
Main Results:
- Amphetamine significantly increased ERM protein phosphorylation in PC12 cells.
- Inhibition of Protein Kinase C beta (PKCβ) abolished the amphetamine-induced ERM phosphorylation.
- Inhibitors for Extracellular Signal-Regulated Kinase (ERK) and Phosphatidylinositol 3-Kinases (PI3K) did not affect this phosphorylation.
- A dopamine transporter (DAT) inhibitor suppressed amphetamine-induced ERM protein phosphorylation.
Conclusions:
- Protein Kinase C beta (PKCβ) plays a critical role in mediating amphetamine-induced ERM protein phosphorylation.
- Dopamine transporter (DAT) regulation is implicated in the mechanism of amphetamine's effect on ERM proteins.
- These findings suggest a novel pathway involving PKCβ and DAT in the cellular response to amphetamine.
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