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Related Experiment Videos

Dopamine transporter: solubilization from dog caudate nucleus.

R Lew1, D E Grigoriadis, J Sharkey

  • 1Neuroscience Branch, National Institute on Drug Abuse, Baltimore, Maryland 21224.

Synapse (New York, N.Y.)
|January 1, 1989
PubMed
Summary

Researchers characterized the dopamine transporter in dog caudate nucleus using 3H-GBR 12935. This radioligand demonstrated specific, saturable, and high-affinity binding, confirming its utility for dopamine transporter studies.

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Area of Science:

  • Neuroscience
  • Pharmacology
  • Biochemistry

Background:

  • The dopamine transporter (DAT) plays a crucial role in regulating dopaminergic neurotransmission.
  • Radioligand binding assays are essential for characterizing transporter properties and for drug discovery.
  • Investigating DAT in non-rodent species can provide comparative insights into its function and pharmacology.

Purpose of the Study:

  • To characterize the binding properties of the digitonin-solubilized dopamine transporter from dog caudate nucleus using the radioligand 3H-GBR 12935.
  • To confirm the specificity of 3H-GBR 12935 binding to the dopamine transporter.

Main Methods:

  • Digitonin-solubilization of dopamine transporter from dog caudate nucleus.
  • Radioligand binding assays using 3H-GBR 12935.

Related Experiment Videos

  • Competition binding studies with known dopamine transporter ligands and inhibitors of other monoamine transporters.

    • Main Results:

    • Specific binding of 3H-GBR 12935 was observed in dog caudate soluble fractions but not in rat cerebellum.
    • Binding was saturable and exhibited high affinity (KD = 23.42 nM, Bmax = 2.57 pmol/mg protein).
    • Binding was abolished by heating or trypsin treatment and was competed by known dopamine transporter inhibitors, but not by norepinephrine or serotonin reuptake inhibitors.

    Conclusions:

    • 3H-GBR 12935 is a suitable radioligand for labeling and characterizing the solubilized dopamine transporter from dog caudate nucleus.
    • The binding characteristics are consistent with those of the dopamine transporter, validating its use in pharmacological studies.