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Related Experiment Videos

Androgen-binding proteins in human benign prostatic hypertrophy.

V Rosen, I Jung, E E Baulieu

    The Journal of Clinical Endocrinology and Metabolism
    |October 1, 1975
    PubMed
    Summary
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    This study identified two high-affinity binding components in benign prostatic hypertrophy (BPH) cytosol: the androgen receptor and a sex steroid-binding protein (SBP). The androgen receptor was largely occupied by endogenous androgens, suggesting significant hormonal activity within the prostate.

    Area of Science:

    • Endocrinology
    • Molecular Biology
    • Urology

    Background:

    • Benign prostatic hypertrophy (BPH) involves complex hormonal regulation within the prostate.
    • Understanding androgen binding in prostate tissue is crucial for BPH research.

    Purpose of the Study:

    • To characterize high-affinity steroid binding components in human benign prostatic hypertrophy (BPH) cytosol.
    • To investigate the presence and characteristics of the androgen receptor and sex steroid-binding protein (SBP) in BPH tissue.

    Main Methods:

    • Glycerol gradient ultracentrifugation of BPH cytosol labeled with radiolabeled androgens.
    • Radioimmunoassay to measure endogenous androgens.
    • Equilibrium dialysis and Sephadex G-150 column chromatography to analyze binding proteins.

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    Main Results:

    • Two high-affinity binding components were identified: the androgen receptor (8 S) and an SBP-like protein (4 S).
    • The androgen receptor showed high affinity for androgens and was significantly occupied by endogenous androgens (>90%).
    • The SBP-like protein was present in cytosol at a lower concentration than in plasma and showed characteristics suggesting intracellular localization or exposure to the intracellular environment.

    Conclusions:

    • BPH cytosol contains a functional androgen receptor largely occupied by endogenous androgens.
    • An SBP-like protein is present in BPH cytosol, potentially originating from plasma but exhibiting characteristics suggesting interaction with the intracellular milieu.
    • These findings contribute to understanding the hormonal environment within BPH tissue.