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• W2088761454 abstract "We have demonstrated that when minces of epididymides from castrated rabbits are incubated with [3H]-testosterone radioactivity bound to a macromolecular component, it enters the nuclei. This entry is a temperature dependent phenomenon which is greater upon incubation at 23°C than at 0°C. In contrast, no macromolecular bound hormone could be detected in leg muscle cytosol or nuclei. The amount of radioactivity extractable from epididymal nuclei was a function of the molar concentration of KC1 in the extraction medium. However, even when 1.0 M KC1 was used, greater than 30% of the radioactivity bound to nuclei remained unextractable. Of the naturally occurring steroids that we used (testosterone, estradiol-17β, and cortisol) in competition studies, unlabeled testosterone was the most effective in preventing the nuclear accumulation of labeled androgen. Estradiol-17β also was effective in this regard, but was much less potent than testosterone under the conditions employed. Unlabeled cortisol was an ineffective inhibitor. The antiandrogens, cyproterone and SKF 7690, both of which inhibit binding to the epididymal cytoplasmic androgen receptor, completely inhibited nuclear accumulation of radioactivity, implying that nuclear accumulation is dependent on an initial binding to the cytoplasmic receptor. We have also demonstrated that the rabbit epididymis is capable of converting testosterone to 5α-dihydrotestosterone (5α-DHT). Although the tissues were incubated with [3H]-testosterone, 5α-DHT was selectively bound by the cytoplasmic receptor and concentrated in the nuclei." @default.
• W2088761454 created "2016-06-24" @default.
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• W2088761454 date "1976-10-01" @default.
• W2088761454 modified "2023-09-27" @default.
• W2088761454 title "Nuclear binding of [3H]-Androgens by the epididymis of sexually mature castrated rabbits" @default.
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• W2088761454 doi "https://doi.org/10.1016/0022-4731(76)90172-2" @default.
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