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Androgen-binding proteins from human hyperplastic prostate as evaluated by electrophoresis
Archives of Andrology
|January 1, 1986
Summary
This study analyzed androgen-binding proteins in human prostate tissue using methyltrienolone (MT). Researchers identified distinct electrophoretic patterns, aiding in understanding androgen action and receptor identification.
Area of Science:
- Andrology
- Molecular Endocrinology
- Biochemistry
Background:
- Androgen action in prostatic tissue is mediated by receptor proteins.
- The synthesis of methyltrienolone (MT) in 1975 enabled specific searching for receptor proteins.
- MT distinguishes androgen receptors from other proteins like TeBG and albumin.
Purpose of the Study:
- To determine the electrophoretic patterns of human prostatic androgen-binding proteins.
- To compare these patterns with those from other male genital tract tissues (testes, epididymis).
- To use blood serum patterns as a reference.
Main Methods:
- Cytosol and nuclear fractions were isolated from homogenized prostatic tissue.
- Fractions were incubated with tritiated steroids (3H-dihydrotestosterone [3H-DHT] and 3H-MT).
- Dextran-coated charcoal treatment followed by polyacrylamide gel electrophoresis (PAGE) at pH 8.3.
Main Results:
- Prostatic cytosol incubated with 3H-DHT showed mobilities (Rf) at 0.195, 0.285, 0.815, 0.910.
- Incubation with 3H-MT revealed peaks at Rf 0.280, 0.570, and 0.969.
- Nuclear fractions bound 3H-DHT at various Rf values and 3H-MT at Rf 1.01.
Conclusions:
- Prostatic androgen-binding protein patterns share similarities with TeBG and albumin but exhibit lower binding capacity.
- Additional protein peaks with distinct mobilities are undergoing further identification.
- These findings contribute to understanding androgen receptor heterogeneity in the prostate.