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A brain synaptic dopamine-binding protein: isolation and partial characterization.

K Moroi, L L Hsu

    Journal of Neuroscience Research
    |January 1, 1984
    PubMed
    Summary
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    Researchers purified a dopamine-binding protein (DABP) from rat brain cortex. This protein shows high affinity for dopamine agonists, suggesting it may be related to D2 or D3 dopamine receptors.

    Area of Science:

    • Neuroscience
    • Biochemistry
    • Molecular Biology

    Background:

    • Dopamine receptors are crucial for neurotransmission in the brain.
    • Identifying specific dopamine-binding proteins aids in understanding receptor function.
    • Previous research has focused on receptor subtypes, but specific binding proteins remain elusive.

    Purpose of the Study:

    • To purify and characterize a dopamine-binding protein (DABP) from rat brain cortex.
    • To investigate the binding properties and potential receptor association of the purified DABP.

    Main Methods:

    • Purification of DABP from synaptosomal membranes using cholic acid solubilization, agarose gel filtration, and dopamine affinity chromatography.
    • Characterization of the purified DABP using native and SDS polyacrylamide gel electrophoresis.

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  • Assessment of binding affinity for dopamine agonists and antagonists using affinity chromatography and photoaffinity labeling.

    • Main Results:

    • A homogeneous DABP was successfully purified with a yield of 0.006% protein and 0.03% binding.
    • The purified DABP exhibited specific [3H]-DA binding of 117 fmol/mg protein/10 min, a 4.6-fold purification.
    • The protein consists of a single 34.5 kDa subunit and shows higher affinity for dopamine agonists, suggesting a link to D2 or D3 receptors.

    Conclusions:

    • A novel dopamine-binding protein has been isolated and characterized from the rat brain cortex.
    • The purified DABP displays characteristics consistent with dopamine D2 or D3 receptors.
    • This purified protein serves as a valuable tool for further investigating dopamine receptor mechanisms.