Further observations on the autoregulation of the prolactin receptor in rat ventral prostate explants

1987 ◽  
Vol 114 (3) ◽  
pp. 426-432
Author(s):  
H. Rui ◽  
I. Brekke ◽  
P. A. Torjesen ◽  
K. Purvis

Abstract. In confirmation and extension of an earlier preliminary communication, ovine prolactin was found to elevate prolactin binding by approximately 100% in rat ventral prostate explants incubated for 20 h in vitro. A stimulation was observed with low doses of ovine hormone (150 μg/l) which, from available data on the relative biological potencies, could be considered equivalent to the upper limit of the physiological range of endogenous rat prolactin. The response was associated with a lag period of 3–6 h. The effect could be obtained with other lactogenic hormones, including human and rat prolactin and human growth hormone, but not with non-lactogenic hormones such as insulin, hCG, corticosterone, testosterone or oestradiol. The prostaglandin synthesis inhibitor, indomethacin, and the Ca2+-antagonist, verapamil, could not counteract the increase in prolactin binding induced by prolactin treatment, nor could dibutyryl cyclic AMP alone mimic the response. These data suggest that prostaglandins, Ca2+ or cAMP do not mediate the alteration in receptor binding. Furthermore, inhibition of lysosome activity by chloroquine could not alone increase the prolactin binding in the control tissues, suggesting that up-regulation does not simply reflect a protective action of prolactin on receptor degradation.

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.


1970 ◽  
Vol 17 (6) ◽  
pp. 453-458 ◽  
Author(s):  
JUN SHIMAZAKI ◽  
JIN SATO ◽  
HISAKO NAGAI ◽  
KEIZO SHIDA

The Prostate ◽  
1985 ◽  
Vol 6 (3) ◽  
pp. 277-283 ◽  
Author(s):  
M. A. Blankenstein ◽  
J. -De Bolt Vries ◽  
A. Coert ◽  
H. Nievelstein ◽  
F. H. Schröder

In Vitro ◽  
1984 ◽  
Vol 20 (3) ◽  
pp. 216-228 ◽  
Author(s):  
Frederick B. Merk ◽  
Paul W. L. Kwan ◽  
Stanley Spilman ◽  
Louis Terracio ◽  
William H. J. Douglas

1992 ◽  
Vol 12 (4) ◽  
pp. 303-311 ◽  
Author(s):  
M. T. Gutierrez-Ocaña ◽  
S. Senar ◽  
M. A. Perez-Albarsanz ◽  
M. N. Recio

Chronic lindane intoxication by injecting subcutaneously the toxicant, resulted in an altered lipid pattern in rat ventral prostate membranes. An increase of membrane fluidity was also observed using a fluorescence polarization technique. When in vitro experiments were carried out with both treated and untreated rats, an interesting lack of parallelism was found, which could indicate the development of a resistance to membrane disordering by lindane. The observed changes in cholesterol and phospholipid composition are also consistent with the hypothesis that lindane perturbs the lipid matrix of membranes, possibly inducing complex compensatory changes in the membrane lipid composition.


1970 ◽  
Vol 63 (1) ◽  
pp. 69-78 ◽  
Author(s):  
Olav Unhjem

ABSTRACT Following incubation of rat ventral prostate slices with [1,2-3H]testosterone in vitro, radioactive material is found to be associated with the nuclei. Sodium chloride extraction of the nuclei removes macromolecules which might at least partially be responsible for this association. These macromolecules are probably components of the nuclear chromatin. Analyses of the radioactive material indicate that the major portion consists of dihydrotestosterone* and to a lesser extent of testosterone. All the radioactive material is linked non-covalently to the nuclear components responsible for the association.


2001 ◽  
Vol 26 (3) ◽  
pp. 175-184 ◽  
Author(s):  
D Marcantonio ◽  
LE Chalifour ◽  
MA Alaoui-Jamali And H T Huynh ◽  
MA Alaoui-Jamali ◽  
MA Alaoui-Jamali ◽  
...  

Steroid-sensitive gene-1 (SSG1) is a novel gene we cloned, found regulated by 17beta-estradiol in the rat uterus and mammary gland, and over-expressed in 7,12-dimethylbenz(a)anthracene-induced rat mammary tumors. We show here that SSG1 mRNA and protein expression are regulated by androgens in the rat ventral prostate. Increases in SSG1 mRNA levels were detected by Northern blotting after 24 h and reached a 27-fold peak 96 h following castration, relative to SSG1 mRNA expression in sham-operated rats. Dihydrotestosterone or testosterone supplementation of castrated rats prevented this rise in SSG1 mRNA. In contrast with SSG1 mRNA expression, SSG1 protein was decreased 16-fold 2 weeks following castration but was at control levels in the prostates of castrated rats receiving dihydrotestosterone or testosterone. Although SSG1 is regulated by androgens in vivo, treatment of LnCap cells with dihydrotestosterone, cyproterone acetate or flutamide did not result in the regulation of SSG1 protein levels in vitro. Immunofluorescence studies show that SSG1 is mainly expressed in prostatic smooth muscle cells. These results indicate that SSG1 is an androgen-regulated gene that is expressed in the smooth muscle component of the rat ventral prostate in vivo.


Sign in / Sign up

Export Citation Format

Share Document