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Related Experiment Videos

High-affinity dextromethorphan binding sites in guinea pig brain. I. Initial characterization.

G L Craviso, J M Musacchio

    Molecular Pharmacology
    |May 1, 1983
    PubMed
    Summary

    Tritiated dextromethorphan ([3H]DM) binds to two sites in guinea pig brain. High-affinity binding sites are protein-like, pH-dependent, and located in microsomes, suggesting they are not opiate receptors.

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    Brain research·1999

    Area of Science:

    • Neuropharmacology
    • Biochemistry

    Background:

    • Dextromethorphan (DM) is a widely used antitussive agent.
    • Understanding DM's binding characteristics is crucial for elucidating its pharmacological effects.

    Purpose of the Study:

    • To characterize the binding sites of tritiated dextromethorphan ([3H]DM) in guinea pig brain.
    • To determine the physicochemical properties and localization of these binding sites.

    Main Methods:

    • Radioligand binding assays using [3H]DM on guinea pig brain homogenates.
    • Investigating the effects of pH, temperature, ions, and enzymatic treatments on binding.
    • Subcellular fractionation to determine the localization of binding sites.

    Main Results:

    • Two distinct binding sites were identified: high-affinity (Kd = 13-20 nM) and low-affinity (Kd > 200 nM).

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  • High-affinity binding is rapid, reversible, saturable, pH-dependent, and reduced by heat and proteolytic enzymes, indicating a protein component.
  • Sites are concentrated in pons-medulla and cerebellum, primarily located in the microsomal fraction.
  • Certain ions affect binding, with micromolar calcium enhancing and millimolar concentrations of Li+, Ca2+, Mg2+, and Mn2+ decreasing binding.

    • Conclusions:

    • The characteristics of [3H]DM binding sites suggest they are not a subclass of opiate receptors.
    • The protein-like nature and microsomal localization point to specific molecular targets for DM in the brain.