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Protein kinase C activators decrease dopamine uptake into striatal synaptosomes

B J Copeland1, V Vogelsberg, N H Neff

  • 1Neuroscience Program, Ohio State University, College of Medicine, Columbus, USA.

The Journal of Pharmacology and Experimental Therapeutics
|June 1, 1996
PubMed
Summary
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Protein kinase C activators, phorbol 12-myristate 13-acetate (PMA) and sn-1,2 dioctanoylglycerol (DiC8), reduce dopamine uptake in brain synaptosomes. This modulation of dopamine transporter activity is mediated by protein kinase C signaling pathways.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Pharmacology

Background:

  • Dopamine transporter (DAT) function is crucial for regulating dopaminergic neurotransmission.
  • Protein kinase C (PKC) is implicated in various cellular signaling pathways, including those affecting neurotransmitter transporters.

Purpose of the Study:

  • To investigate the role of protein kinase C (PKC) in modulating dopamine uptake into striatal synaptosomes.
  • To elucidate the specific mechanisms by which PKC activation impacts DAT activity.

Main Methods:

  • Primary cultures of rat striatal synaptosomes were used to measure dopamine uptake.
  • Synaptosomes were incubated with PKC activators (PMA, DiC8) and inhibitors (staurosporine, okadaic acid).
  • Kinetic analysis and ligand binding assays (mazindol) were employed to characterize changes in DAT function.

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Main Results:

  • PKC activators PMA and DiC8 significantly decreased dopamine uptake, with no effect from inactive 4 alpha-PMA.
  • The observed decrease in uptake was irreversible upon washout of the activators.
  • Kinetic studies revealed a reduction in the apparent V(max) of DAT, without altering its K(m).
  • Mazindol binding to DAT remained unaffected, suggesting no change in transporter number or direct ligand interaction.
  • The protein kinase inhibitor staurosporine blocked the DiC8-induced decrease in uptake.
  • Okadaic acid, a protein phosphatase inhibitor, reduced uptake independently and potentiated the effect of DiC8.

Conclusions:

  • Protein kinase C activation plays a significant role in the regulation of dopamine transporter activity.
  • PKC-mediated phosphorylation events likely underlie the observed decrease in dopamine uptake.
  • These findings highlight a novel regulatory mechanism for dopaminergic neurotransmission involving PKC signaling.