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Related Experiment Videos

Species differences in dopamine transporters: postmortem changes and glycosylation differences

A Patel1, G Uhl, M J Kuhar

  • 1Molecular Pharmacology Section, NIDA Addiction Research Center, Baltimore, Maryland 21224.

Journal of Neurochemistry
|August 1, 1993
PubMed
Summary

Species differences in dopamine transporter (DAT) molecular mass may stem from posttranslational modifications and postmortem degradation. These factors influence DAT function and cocaine analogue binding, impacting transporter research.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Dopamine transporters (DATs) exhibit varying molecular masses across species.
  • Differences in N-linked glycosylation sites between rat and human DAT are predicted by cDNA sequences.

Purpose of the Study:

  • To investigate the reasons behind species-specific differences in dopamine transporter (DAT) molecular mass.
  • To explore the roles of posttranslational modifications and postmortem changes in DAT molecular mass variation.

Main Methods:

  • Photoaffinity labeling of DATs from various species and cell lines.
  • Analysis of DAT molecular mass after postmortem delay and neuraminidase treatment.
  • Comparison of cocaine analogue binding affinities.

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Main Results:

  • Apparent molecular masses of DATs differ significantly across species (rat, human, dog, primate).
  • Postmortem delay in rat DAT led to decreased molecular mass and cocaine analogue binding.
  • Neuraminidase treatment affected native rat DAT but not expressed DAT, indicating differential glycosylation.

Conclusions:

  • Postmortem degradation and cell-type-specific posttranslational processing, particularly N-linked glycosylation, contribute to species differences in DAT molecular mass.
  • Observed differences in DAT molecular mass and glycosylation impact transporter function and ligand binding, relevant for transporter research.