Molecular cloning of human and rat complementary DNA encoding androgen receptors

Science ◽  
1988 ◽  
Vol 240 (4850) ◽  
pp. 324-326 ◽  
Author(s):  
CS Chang ◽  
J Kokontis ◽  
ST Liao
Keyword(s):  
Androgen Receptors ◽  
Steroid Receptors ◽  
Ventral Prostate ◽  
Cdna Libraries ◽  
Human Testis ◽  
Dna Binding Domain ◽  
Dna Encoding ◽  
High Affinity ◽  
Autoimmune Antibodies ◽  
Rat Ventral Prostate

Complementary DNAs (cDNAs) encoding androgen receptors were obtained from human testis and rat ventral prostate cDNA libraries. The amino acid sequence deduced from the nucleotide sequences of the cDNAs indicated the presence of a cysteine-rich DNA-binding domain that is highly conserved in all steroid receptors. The human cDNA was transcribed and the RNA product was translated in cell-free systems to yield a 76-kilodalton protein. The protein was immunoprecipitable by human autoimmune antibodies to the androgen receptor. The protein bound androgens specifically and with high affinity.

Association of glucocorticoid receptors with prostate nuclear sites for androgen receptors and with androgen response elements

1990 ◽  
Vol 5 (2) ◽  
pp. 117-127 ◽  
Author(s):  
P. Davies ◽  
N. K. Rushmere
Keyword(s):  
Glucocorticoid Receptors ◽  
Androgen Receptors ◽  
Steroid Receptors ◽  
Normal Population ◽  
Ventral Prostate ◽  
Response Elements ◽  
High Affinity ◽  
Glucocorticoid Response ◽  
Nuclear Structures

ABSTRACT Ventral prostate glands of intact normal rats contained low levels (2500 molecules/cell) of high-affinity (dissociation constant (Kd) 0·57 nmol/l) glucocorticoid receptors (GR). Levels of GR increased 2·8-fold 1 day after castration, and 4·3-fold 3 days after castration. Nuclear GR increased from a normal value of 1150 molecules/nucleus to 5200 molecules/nucleus 3 days after castration. The greater increase in intranuclear GR was in that associated with oligomeric chromatin. Although nuclear GR never approached the normal population of nuclear androgen receptors (AR; approximately 16000 molecules/nucleus), the selective rise in chromatin-associated receptors ensured that almost 60% of chromatin sites remained occupied. GR associated with prostate nuclear structures in a similar manner to AR, and exogenous GR bound saturably and with high affinity (Kd 100 pmol/1) to a similar number of sites as did AR. Both steroid receptors apparently competed for the same sites. In DNA—cellulose competition analyses, synthetic oligonucleotides containing glucocorticoid response elements or putative androgen response elements competed similarly against immobilized non-specific DNA for both AR and GR. In view of these data and information from other sources, it is probable that the role of GR in the prostate should be assessed with a view to understanding its action under conditions of androgen deprivation.

Expression of androgen receptors and prostatic steroid-binding protein during development of the rat ventral prostate

1988 ◽  
Vol 117 (3) ◽  
pp. 361-NP ◽  
Author(s):  
Y. L. Zhang ◽  
Z. X. Zhou ◽  
Y. D. Zhang ◽  
M. G. Parker
Keyword(s):  
Gene Expression ◽  
Androgen Receptors ◽  
Binding Protein ◽  
Transient Increase ◽  
Neonatal Rat ◽  
Ventral Prostate ◽  
Rat Ventral Prostate ◽  
Old Rats ◽  
Steroid Binding ◽  
Steroid Binding Protein

ABSTRACT Prostatic steroid-binding protein (PSBP) mRNAs transcribed from the three genes C1, C2 and C3 were quantitated in neonatal rat ventral prostate by Northern blot analysis. Transcription was initiated at day 14 for C1 and C2 and day 10 for C3, and reached mature levels by day 21 for C1 and C2 and day 28 for C3. The changes of both cytoplasmic and nuclear prostatic androgen receptors in 10- to 150-day-old rats were investigated by radioligand assay and showed a fivefold transient increase between days 10 and 28. Thus there was a good correlation between the onset of PSBP gene expression and the transient increase in androgen receptors; increases in receptor concentration may be a prerequisite for changes in gene expression. J. Endocr. (1988) 117, 361–366

Androgen receptors in rat ventral prostate microsomes

1974 ◽  
Vol 373 (1) ◽  
pp. 1-9 ◽  
Author(s):  
Paul Robel ◽  
Jean-Paul Blondeau ◽  
Etienne-Emile Baulieu
Keyword(s):  
Androgen Receptors ◽  
Ventral Prostate ◽  
Rat Ventral Prostate

SPECIFIC HIGH-AFFINITY OESTRADIOL BINDING IN RAT VENTRAL PROSTATE

1980 ◽  
Vol 87 (2) ◽  
pp. 285-292 ◽  
Author(s):  
M. GINSBURG ◽  
I. JUNG-TESTAS ◽  
E. E. BAULIEU
Keyword(s):  
Binding Sites ◽  
Ventral Prostate ◽  
Scatchard Analysis ◽  
Endocrine Control ◽  
High Affinity ◽  
Rat Ventral Prostate ◽  
Low Salt ◽  
Equilibrium Dissociation ◽  
Intact Rats ◽  
Binding Component

The presence of a specific saturable oestradiol-binding component was demonstrated in cytosol from rat ventral prostate. Centrifugation of cytosol, previously incubated with [3H]oestradiol at 0 °C, on low salt glycerol—Tris gradients revealed two oestradiol-binding systems with sedimentation coefficients of 8S and 4S. Excess unlabelled dihydrotestosterone (17β-hydroxy-5α-androstan-3-one) did not compete with the oestradiol binding, whereas excess unlabelled oestradiol or diethylstilboestrol abolished the 8S and 4S peaks. The oestradiol binding to these components could not be detected after proteolytic treatment. Scatchard analysis of saturable oestradiol binding in cytosol of prostates from intact rats and from rats 14 days after orchidectomy indicated that the equilibrium dissociation constant (KDeq) was about 10−10 mol/l at 0 °C, and the concentrations of high-affinity binding sites were approximately 10 fmol oestradiol bound/mg protein. Lower concentrations of oestradiol binding (approximately 2 fmol/mg protein) were found in cytosols from prostates obtained 2 and 4 days after castration. The transient decrease of oestradiol binding was not due to the presence in prostate cytosol of a factor that inactivated the oestradiol receptor. It is proposed that the oestradiol receptor in the cytosol from ventral prostate tissue of the rat is under endocrine control.

ANDROGEN RECEPTORS IN PROLACTIN PRODUCING PITUITARY TUMOURS IN RATS

1977 ◽  
Vol 86 (2) ◽  
pp. 288-298 ◽  
Author(s):  
Arne Attramadal ◽  
Oddvar Naess ◽  
Egil Haug ◽  
Vidar Hansson ◽  
Ken Purvis
Keyword(s):  
Androgen Receptor ◽  
Binding Sites ◽  
Androgen Receptors ◽  
Sedimentation Coefficient ◽  
Ventral Prostate ◽  
Scatchard Analysis ◽  
Receptor Complex ◽  
Pituitary Tumours ◽  
High Affinity ◽  
Androgen Binding

ABSTRACT The androgen receptor system in prolactin secreting oestrogen induced pituitary tumours has been studied. The tumour cytosol was found to contain specific androgen receptors binding [3H]5α-dihydrotestosterone (DHT) and [3H] testosterone (T) with high affinity and low capacity. Scatchard analysis of the saturation data for T revealed one class of high affinity binding sites. The equilibrium constant of dissociation (Kd) was ∼ 4 × 10−10 m and the number of binding sites was calculated to be 12.8 femtomoles/mg protein. The sedimentation coefficient of the androgen receptor complex in low salt sucrose gradients was ∼ 7 S, the electrophoretic mobility (RF) in 3.25 % polyacrylamide gels ∼ 0.5 and the isoelectric point 5.8. The protein nature of the receptor was indicated by the finding that protease, but not DNase and RNase, eliminated androgen binding. Furthermore, the receptor was thermolabile and functionally dependent on free SH-groups since androgen binding was eliminated by heating 45°C for 30 min) and treatment with p-chloromercuriphenyl sulphonate (1 mm). Steroid specificity was tested in vitro by examining the competing efficiency of different unlabelled steroids for the binding of [3H]T. The affinity of DHT for the receptor was approximately twice that of testosterone while the binding affinity of oestradiol-17β and progesterone was very low. Cortisol had no affinity for the androgen receptor. The dissociation of the androgen receptor complex was very slow at 0°C (t ½ > 48 h). Thus, the characteristics of the cytoplasmic androgen receptors of the prolactin producing pituitary tumours are very similar to those of the androgen receptors earlier demonstrated in the anterior pituitary, hypothalamus, ventral prostate, epididymis and testis. The presence of specific androgen receptors in prolactin producing pituitary tumours indicates that androgen is involved in the regulation of synthesis and release of prolactin.

Phosphorylation status of nuclear and cytosolic androgen receptors in the rat ventral prostate

The Prostate ◽  
1989 ◽  
Vol 14 (2) ◽  
pp. 91-101 ◽  
Author(s):  
E. J. Golsteyn ◽  
J. S. Graham ◽  
H. J. Goren ◽  
Y. A. Lefebvre
Keyword(s):  
Androgen Receptors ◽  
Ventral Prostate ◽  
Rat Ventral Prostate
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