Androgen receptors in benign and malignant prostatic tissue.
A new procedure has been developed to purify prostatic cell nuclei and to achieve a high yield of nuclear material for study. This technique allowed the investigation of the enzyme 5-alpha-reductase and its relationship to the translocation of dihydrotestosterone and androgen receptors into the nucleus of the prostatic cell. The studies revealed that 5-alpha-reductase was localized chiefly to the stromal components of all types of prostatic tissue. Although there is a higher concentration of dihydrotestosterone in carcinoma tissue the 5-alpha-reductase activity is low. Studies on the effect of androgens and antiandrogens on nuclear uptake of androgen revealed that androgens are potent stimulants of receptor translocation, while antiandrogens stimulate little or no translocation.
D013741:3-Oxo-5-alpha-Steroid 4-Dehydrogenase / Q000378:metabolism; D000726:Androgen Antagonists / Q000494:pharmacology; D000818:Animals; D003534:Cyproterone / Q000494:pharmacology; D013196:Dihydrotestosterone / Q000378:metabolism; D004963:Estrenes / Q000494:pharmacology; D005485:Flutamide / Q000494:pharmacology; D006801:Humans; D008297:Male; D011470:Prostatic Hyperplasia / Q000378:metabolism*; D011471:Prostatic Neoplasms / Q000378:metabolism*; D051381:Rats; D011944:Receptors, Androgen / Q000378:metabolism*; D011987:Receptors, Steroid / Q000378:metabolism*
D000726:Androgen Antagonists; D004963:Estrenes; D011944:Receptors, Androgen; D011987:Receptors, Steroid; D013196:Dihydrotestosterone; C005672:R 2956; D005485:Flutamide; D003534:Cyproterone; D013741:3-Oxo-5-alpha-Steroid 4-Dehydrogenase