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Related Experiment Videos

Progestin-binding protein in human benign prostatic hypertrophy.

T Kodama, M Ito, R Sato

    Endocrinologia Japonica
    |April 1, 1981
    PubMed
    Summary
    This summary is machine-generated.

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    Benign prostatic hypertrophy cytosols contain progestin-binding components that bind R 5020 and other progestins. These components differ from dihydrotestosterone-binding proteins and may not represent the steroid receptor.

    Area of Science:

    • Endocrinology
    • Molecular Biology
    • Urology

    Background:

    • Benign prostatic hypertrophy (BPH) is a common condition in aging men.
    • The role of steroid hormones, including progestins, in BPH pathogenesis is not fully understood.
    • Identifying specific hormone-binding proteins in BPH tissues is crucial for understanding disease mechanisms.

    Purpose of the Study:

    • To characterize progestin-binding components in human benign prostatic hypertrophy cytosols.
    • To differentiate these components from known steroid-binding proteins.

    Main Methods:

    • Cytosol preparation from human BPH tissue.
    • High-affinity binding assays using radiolabeled progestins (R 5020, ORG 2058, progesterone).
    • Biochemical characterization including ammonium sulfate precipitation, sedimentation analysis, gel filtration (Sephadex G-200), heat stability, and delipidization.

    Related Experiment Videos

  • Competition binding assays with R 1881.
  • Analysis of nuclear extracts.

    • Main Results:

    • Cytosols from BPH contained high-affinity progestin-binding components for R 5020, ORG 2058, and progesterone.
    • The primary R 5020-binding protein was precipitated by 0-30% ammonium sulfate and exhibited sedimentation coefficients of 3.6S and 8.4S.
    • This protein eluted in the void volume of Sephadex G-200, indicating a large molecular size.
    • Key differences were observed compared to dihydrotestosterone-binding proteins, including precipitability, heat stability, and delipidization susceptibility.
    • R 1881 significantly inhibited binding of R 5020 and ORG 2058, suggesting these sites also bind R 1881.
    • Nuclear extracts showed R 1881 binding but lacked the R 5020-binding protein.

    Conclusions:

    • Human BPH cytosols possess distinct progestin-binding proteins.
    • These proteins differ significantly from dihydrotestosterone-binding proteins found in the same tissue.
    • The observed progestin-binding proteins in cytosols do not appear to be the classical steroid receptor, as evidenced by their properties and the lack of co-elution with R 1881 binding in nuclear extracts.