scholarly journals Solubilization of Testosterone 5α-Reductase from Nuclear Fraction of Rat Ventral Prostate

1973 ◽  
Vol 20 (5) ◽  
pp. 489-495 ◽  
Author(s):  
JUN SHIMAZAKI ◽  
YUMIKO OHKI ◽  
HIROSHI KURIHARA ◽  
NOBUO FURUYA ◽  
KEIZO SHIDA
1976 ◽  
Vol 81 (4) ◽  
pp. 854-864 ◽  
Author(s):  
Risto Johansson

ABSTRACT The effects of prolactin, growth hormone and insulin on the total uptake and specific binding of tritiated dihydrotestosterone in the cultured rat ventral prostate were examined. In similar conditions prolactin and insulin act synergistically with testosterone on the macromolecule synthesis of the prostate, but have no effect on the conversion of testosterone to dihydrotestosterone. The total uptake of tritiated dihydrotestosterone to the tissues was slightly, but not statistically significantly, increased by prolactin, insulin and growth hormone. The majority of the radioactive dihydrotestosterone in the tissue was in free form or very loosely bound. None of these three hormones altered the binding of tritiated dihydrotestosterone to the cytoplasmic receptors. Non-radioactive dihydrotestosterone, cyproterone and cyproterone acetate in 1000 foid excess strongly decreased the binding of tritiated dihydrotestosterone to the cytoplasmic reseptors and to the nuclei. That part of the binding, which was inhibited by the hormones was considered to represent the specific binding to the receptors. Insulin stimulated both the specific and the unspecific uptake of dihydrotestosterone to the nuclei. Prolactin only stimulated the specific uptake to the nuclei while growth hormone had no effect. Autoradiography of the nuclear fraction indicated a firm binding of tritiated dihydrotestosterone to the nuclei. The radioactivity of the other contaminating cell components in this fraction appeared to be negligible.


1971 ◽  
Vol 66 (2) ◽  
pp. 352-356 ◽  
Author(s):  
Kjell J. Tveter

ABSTRACT Slices from prostate glands of castrated male rats were incubated with [3H] 5α-dihydrotestosterone in Eagle's tissue culture medium. The labelled androgen was associated with androphilic macromolecules both in the prostatic cytosol and the nuclei. The addition of the anti-androgenic compound, 17α-methyl-β-nortestosterone (SK & F 7690) to the incubation medium inhibited the formation of the nuclear 5α-dihydrotestosterone-protein complex, and markedly reduced the cytosol 5α-dihydrotestosterone-protein complex. Likewise, the uptake of [3H] 5α-dihydrotestosterone by the prostatic nuclear fraction was reduced by about 40%.


1987 ◽  
Vol 147 (1) ◽  
pp. 196-203 ◽  
Author(s):  
Jocelyne G. Léger ◽  
Michael L. Montpetit ◽  
Martin P. Tenniswood

1970 ◽  
Vol 65 (3) ◽  
pp. 517-524 ◽  
Author(s):  
Olav Unhjem

ABSTRACT The ability of various steroids and metabolic inhibitors to influence the binding of androgen to soluble macromolecules in the rat ventral prostate was evaluated in vitro. The results obtained revealed some structural requirements of steroids for binding to the macromolecules. An androstane skeleton with the α-configuration of the hydrogen atom at position 5 seemed to be essential for binding as well as a keto group at position 3. N-ethylmaleimide, Na-iodoacetate and p-hydroxymercuribenzoate inhibited the binding of androgen to macromolecules. The androgen-macromolecular complexes appeared to be rather stable at temperatures below 5°C.


The Prostate ◽  
2003 ◽  
Vol 55 (2) ◽  
pp. 118-127 ◽  
Author(s):  
Sung Joon Kim ◽  
Sun Young Shin ◽  
Ji Eun Lee ◽  
Jun Hee Kim ◽  
Dae-Yong Uhm

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