Studies on the mechanism of the antiandrogenic effect of a putative 5α -reductase inhibitor
The mechanism of the antiandrogenic effect of 5,10-seco-19-norpregnane-4,5-diene-3,10,20-trione (secosteroid), reputedly an irreversible inhibitor of 5α -reductase, was investigated. Its addition (10 μM) to culture media effectively suppressed the synthesis of rat epididymal proteins specifically in...
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1987
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00224731_v28_n2_p227_Vazquez http://hdl.handle.net/20.500.12110/paper_00224731_v28_n2_p227_Vazquez |
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paper:paper_00224731_v28_n2_p227_Vazquez2023-06-08T14:51:03Z Studies on the mechanism of the antiandrogenic effect of a putative 5α -reductase inhibitor antiandrogen enzyme inhibitor steroid 5alpha reductase animal cell biological model cell culture endocrine system epididymis in vitro study male genital system nonhuman rat Androgen Antagonists Animal Binding, Competitive Cytosol Depression, Chemical Epididymis Gene Expression Regulation Male Microsomes Norpregnadienes Proteins Rats Rats, Inbred Strains Receptors, Androgen Stanolone Support, Non-U.S. Gov't Testosterone Testosterone 5-alpha-Reductase The mechanism of the antiandrogenic effect of 5,10-seco-19-norpregnane-4,5-diene-3,10,20-trione (secosteroid), reputedly an irreversible inhibitor of 5α -reductase, was investigated. Its addition (10 μM) to culture media effectively suppressed the synthesis of rat epididymal proteins specifically induced by 0.1 μM testosterone (T) or dihydrotestosterone (DHT). Under the same conditions, secosteroid did not change the rate at which labeled T was metabolized to 5α -reduced compounds. In a comparative study, secosteroid inhibited 5α -reductase in an isolated microsomal fraction while not affecting the enzyme activity in minced tissue. Secosteroid was shown to be a competitor of the binding of [3H]T and [3H]DHT (both at 4nM) to the epididymal cytosol androgen receptor, with ID50 of 1 μM for the former and 4μM for the latter, thus explaining the mechanism involved in its antiandrogenic properties. © 1987. 1987 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00224731_v28_n2_p227_Vazquez http://hdl.handle.net/20.500.12110/paper_00224731_v28_n2_p227_Vazquez |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
antiandrogen enzyme inhibitor steroid 5alpha reductase animal cell biological model cell culture endocrine system epididymis in vitro study male genital system nonhuman rat Androgen Antagonists Animal Binding, Competitive Cytosol Depression, Chemical Epididymis Gene Expression Regulation Male Microsomes Norpregnadienes Proteins Rats Rats, Inbred Strains Receptors, Androgen Stanolone Support, Non-U.S. Gov't Testosterone Testosterone 5-alpha-Reductase |
| spellingShingle |
antiandrogen enzyme inhibitor steroid 5alpha reductase animal cell biological model cell culture endocrine system epididymis in vitro study male genital system nonhuman rat Androgen Antagonists Animal Binding, Competitive Cytosol Depression, Chemical Epididymis Gene Expression Regulation Male Microsomes Norpregnadienes Proteins Rats Rats, Inbred Strains Receptors, Androgen Stanolone Support, Non-U.S. Gov't Testosterone Testosterone 5-alpha-Reductase Studies on the mechanism of the antiandrogenic effect of a putative 5α -reductase inhibitor |
| topic_facet |
antiandrogen enzyme inhibitor steroid 5alpha reductase animal cell biological model cell culture endocrine system epididymis in vitro study male genital system nonhuman rat Androgen Antagonists Animal Binding, Competitive Cytosol Depression, Chemical Epididymis Gene Expression Regulation Male Microsomes Norpregnadienes Proteins Rats Rats, Inbred Strains Receptors, Androgen Stanolone Support, Non-U.S. Gov't Testosterone Testosterone 5-alpha-Reductase |
| description |
The mechanism of the antiandrogenic effect of 5,10-seco-19-norpregnane-4,5-diene-3,10,20-trione (secosteroid), reputedly an irreversible inhibitor of 5α -reductase, was investigated. Its addition (10 μM) to culture media effectively suppressed the synthesis of rat epididymal proteins specifically induced by 0.1 μM testosterone (T) or dihydrotestosterone (DHT). Under the same conditions, secosteroid did not change the rate at which labeled T was metabolized to 5α -reduced compounds. In a comparative study, secosteroid inhibited 5α -reductase in an isolated microsomal fraction while not affecting the enzyme activity in minced tissue. Secosteroid was shown to be a competitor of the binding of [3H]T and [3H]DHT (both at 4nM) to the epididymal cytosol androgen receptor, with ID50 of 1 μM for the former and 4μM for the latter, thus explaining the mechanism involved in its antiandrogenic properties. © 1987. |
| title |
Studies on the mechanism of the antiandrogenic effect of a putative 5α -reductase inhibitor |
| title_short |
Studies on the mechanism of the antiandrogenic effect of a putative 5α -reductase inhibitor |
| title_full |
Studies on the mechanism of the antiandrogenic effect of a putative 5α -reductase inhibitor |
| title_fullStr |
Studies on the mechanism of the antiandrogenic effect of a putative 5α -reductase inhibitor |
| title_full_unstemmed |
Studies on the mechanism of the antiandrogenic effect of a putative 5α -reductase inhibitor |
| title_sort |
studies on the mechanism of the antiandrogenic effect of a putative 5α -reductase inhibitor |
| publishDate |
1987 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00224731_v28_n2_p227_Vazquez http://hdl.handle.net/20.500.12110/paper_00224731_v28_n2_p227_Vazquez |
| _version_ |
1768541693185884160 |