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Androgen binding in human testis.

W R Burke, R F Aten, A J Eisenfeld

    The Journal of Urology
    |July 1, 1977
    PubMed
    Summary
    This summary is machine-generated.

    Human testes cytosol contains molecules that bind dihydrotestosterone (DHT), similar to serum binding proteins. This binding is intrinsic to the testes and not solely due to blood contamination.

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    Area of Science:

    • Endocrinology
    • Molecular Biology
    • Andrology

    Background:

    • Testosterone and its metabolites are crucial for male reproductive functions.
    • The transport and availability of androgens are regulated by specific binding proteins.
    • Understanding androgen-binding mechanisms in testicular tissue is vital.

    Purpose of the Study:

    • To investigate the presence and characteristics of dihydrotestosterone-binding macromolecules in human testicular cytosol.
    • To determine if these binding macromolecules are similar to known serum binding proteins.

    Main Methods:

    • Preparation of human testis cytosol.
    • Binding assays using tritiated dihydrotestosterone.
    • Steroid competition studies.
    • Analysis of heat sensitivity and dissociation rate constants.

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    Main Results:

    • Human testis cytosol contains macromolecules that bind tritiated dihydrotestosterone.
    • Binding characteristics (steroid competition, heat sensitivity, dissociation rates) resemble serum testosterone-estradiol-binding globulin (SHBG).
    • The quantity of DHT binding in testicular cytosol exceeds levels attributable to serum contamination.

    Conclusions:

    • Human testicular cytosol possesses intrinsic dihydrotestosterone-binding macromolecules.
    • These testicular binding macromolecules share properties with serum SHBG.
    • The presence of these binding proteins suggests a role in local androgen regulation within the testis.