Similarities between 5alpha-dihydrotestosterone-receptor complexes from human and rat prostatic tissue: effects on RNA polymerase activity.
Protein macromolecules specifically binding [3H]5alpha-dihydrotestosterone ([3H]DHT) have been identified in cytosol and in nuclei prepared from human benign hypertrophic prostate. These macromolecules have similar properties to receptor proteins from other androgen-dependent tissues, as regards sedimentation coefficients on sucrose gradients and steroid specificity. Cytosol preparations from androgen-dependent tissues were able to transfer [3H]DHT in a recoverable protein-bound form to nuclei of other androgen-dependent tissues but not to nuclei of androgen-independent tissues. No transfer of radioactive steroid from cytosol of these latter tissues to any nuclei could be achieved. Labelled cytosol preparations from androgen-dependent tissues could stimulate the RNA polymerase activity of nuclei from androgen-dependent tissues but not that of nuclei from androgen-independent tissues. Cytosol preparations from these latter tissues could not affect RNA polymerase activity. Under suitable ionic conditions, human cytosol preparations containing DHT could stimulate both alpha-amanitin-sensitive and -insensitive RNA polymerase activities of human prostatic nuclei. However, rat ventral prostatic DHT-cytosol protein complexes were equally as efficient in performing this function, suggesting the possible involvement of specific DHT-receptor complexes in this process. It is therfore suggested that receptor molecules from androgen-dependent tissues may not be species specific but may share properties which would facilitate research into the understanding and aetiology of pathological conditions.
D000818:Animals; D001665:Binding Sites; D002467:Cell Nucleus / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism*; D013196:Dihydrotestosterone / Q000378:metabolism* / Q000494:pharmacology; D006801:Humans; D008297:Male; D011467:Prostate / Q000378:metabolism*; D011485:Protein Binding; D011506:Proteins / Q000502:physiology*; D051381:Rats; D011956:Receptors, Cell Surface; D013347:Subcellular Fractions / Q000378:metabolism
D011506:Proteins; D011956:Receptors, Cell Surface; D013196:Dihydrotestosterone; D012321:DNA-Directed RNA Polymerases