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PubMedDate not supplied

Androgen receptor levels and androgen contents in the prostate lobes of intact and testosterone-treated Noble rats.

Plasma testosterone (T) levels were correlated with androgen receptors, tissue content of T, and 5 alpha-dihydrotestosterone (DHT) in the three anatomically-discrete prostate lobes of intact and castrated Noble (Nb) rats bearing T-filled silastic capsules. Differences in androgen receptor content and tissue androgen levels were observed among the three prostatic lobes of intact Nb rats. Total (cytosolic and nuclear) androgen receptor levels were highest in the ventral prostate followed by the dorsolateral and anterior prostate lobes. In the ventral and anterior prostate, androgen receptors were found to be equally distributed between cytosols and nuclear extracts, whereas in the dorsolateral prostate, androgen receptors were predominantly nuclear (cytosolic: nuclear = 1.5). The ventral prostate had the highest total androgen content and DHT was the major tissue androgen in all three lobes. The ratio of tissue DHT:T varied among the lobes; the highest value was observed in the dorsolateral prostate. The higher proportions of nuclear androgen receptor, as well as the elevated tissue DHT:T found in the dorsolateral prostate compared to other lobes, suggest that differences in the androgen activation process may exist between the dorsolateral prostate and other prostatic lobes. Despite lower plasma and tissue T levels, the DHT content, weight and cytodifferentiation in all lobes of T-treated castrated rats closely approximated the situation found in intact animals. Total androgen receptor levels were, however, elevated in all prostatic lobes of T-treated, castrated rats as compared to intact controls. These increases were primarily attributed to the augmented levels of androgen receptor in the nuclear extracts of the three prostate lobes. Exposure of the prostate to a constant level of T, produced by silastic implantation, might be responsible for the higher total androgen receptor levels and enhanced nuclear androgen receptor retention found in the prostates of T-treated, castrated rats.

Androgens↗
PubMedDate not supplied

Whole cell and nuclear androgen uptake in skin fibroblasts from infertile men.

In order to reexamine the hypothesis that a high percentage of infertile men with oligo/azoospermia have androgen resistance due to androgen receptor abnormalities, both whole cell and nuclear uptake of [3H]R1881 (a synthetic, nonmetabolizable androgen) were measured in intact, dispersed fibroblasts cultured from pubic skin biopsy specimens of 15 men selected because of infertility associated with varying degrees of oligozoospermia. Eight men had sperm densities less than or equal to 2 X 10(6)/ml; 7 were greater than 2 X 10(6)/ml. Serum levels of FSH and LH were elevated in the severely oligo/azoospermic group, but normal in the other infertile men; concentrations of testosterone, estradiol, and prolactin were normal in both groups. The controls were six normal, age-matched, fertile males. There was no difference in binding capacity or dissociation constant for androgen uptake either into whole cells (3940 +/- 940 [mean +/- SE] sites/cell vs. 4700 +/- 1120 sites/cell, P = NS) or into nuclei (1360 +/- 340 sites/cell vs. 1460 +/- 340 sites/cell, P = NS) of the fibroblasts from the patients vs. the controls, respectively. Furthermore, there was no correlation between patient sperm densities and fibroblast whole cell or nuclear uptake binding capacities. Finally, there was no difference in any androgen binding parameter when only the fibroblasts from the men with severe oligozoospermia or azoospermia were compared with the controls. The authors conclude that the infertility of men with severe testicular germ cell depletion cannot be accounted for by a quantitative androgen receptor abnormality in their pubic skin fibroblasts.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗
PubMedDate not supplied

Suppression of steroid receptor-chromatin interaction by inhibitors present in ammonium sulfate-fractionated rat testicular androgen receptor preparations.

Tritiated androgen receptor complex was partially purified by ammonium sulfate precipitation at 15 to 37% saturation from rat testicular or prostatic cytosols. A greater amount of prostatic tritiated androgen receptor complex bound to rat Sertoli cell chromatin than tritiated testicular androgen receptor complex. However, the testicular androgen receptor complex was more potent in competing for binding of either tritiated androgen receptor complex preparation to the Sertoli cell chromatin. Combining equal amounts of tritiated testicular and prostatic androgen receptor complexes resulted in lower binding than that observed with tritiated prostatic androgen receptor complex alone, while doubling the concentration of tritiated prostatic androgen receptor complex led to a 2-fold increase in binding. It is conceivable that the partially purified testicular androgen receptor complex preparations contain factor(s) that inhibit the binding interaction of tritiated androgen receptor complex with chromatin, while there is no evidence for the presence of such inhibitors in tritiated prostatic androgen receptor complex preparations. Fractionation of testicular cytosol on DEAE-cellulose yielded a flow-through fraction with inhibitory activity and a bound fraction containing tritiated androgen receptor complex that was eluted with 0.3 M KCl and also showed inhibitory activity. These factors also inhibited the binding of tritiated estradiol receptor complex to chromatin. They were non-dialyzable and their inhibitory effect was abolished after heating at 60 C for 30 minutes. It is concluded that ammonium sulfate-fractionated rat testicular androgen receptor complex preparations contain inhibitors of steroid receptor-chromatin interaction. The inhibitory factors can be fractionated into two distinct fractions by DEAE-cellulose column chromatography. They are nondialyzable and heat-labile. The precise chemical nature of the postulated inhibitor(s) remains to be determined.

Ammonium Sulfate↗
PubMedDate not supplied

Zinc and metallothionein levels and expression of zinc transporters in androgen-independent subline of LNCaP cells.

Zinc levels in the prostate have been reported to be associated with the development and progression of malignant prostate cells. To investigate the reason why the zinc content decreases during the progression of prostate cancer to an androgen-independent state, we compared the expression levels of metallothionein and zinc transporters between androgen-responsive LNCaP cells and its androgen-independent subline, AIDL cells. AIDL cells showed lower zinc levels than LNCaP cells and comparable levels of androgen receptor expression to LNCaP cells, consistent with some clinical aspects of androgen-independent prostatic cancer. AIDL cells exhibited a lower expression of zinc transporter 1 (ZnT1) and higher expression of ZnT3 than LNCaP cells. The content of metallothionein, which is a major zinc-binding protein, was significantly lower in AIDL cells than in LNCaP cells. Furthermore, the expression of ZnT3 mRNA was decreased by incubating LNCaP cells in medium containing hormone-stripped fetal calf serum and increased by addition of synthetic androgen R1881 to the medium, whereas the intracellular zinc levels were not affected under these conditions. These findings suggest that factors such as ZnT1 and metallothioneins other than ZnT3 are associated with the low intracellular zinc content in AIDL cells.

Androgens↗
PubMed2006

Quantifying effects of ligands on androgen receptor nuclear translocation, intranuclear dynamics, and solubility.

Using manual and automated high throughput microscopy (HTM), ligand-dependent trafficking of green fluorescent protein-androgen receptor (GFP-AR) was analyzed in fixed and living cells to determine its spatial distribution, solubility, mobility, and co-activator interactions. Within minutes, addition of the agonist R1881 resulted translocation of GFP-AR from the cytoplasm to the nucleus, where it displayed a hyperspeckled pattern and extraction resistance in low expressing cells. AR antagonists (Casodex, hydroxyflutamide) also caused nuclear translocation, however, the antagonist-bound GFP-AR had a more diffuse nuclear distribution, distinct from the agonist-bound GFP-AR, and was completely soluble; overexpressed GFP-AR in treated cells was extraction resistant, independent of ligand type. To more dramatically show the different effects of ligand on AR distribution, we utilized an AR with a mutation in the DNA binding domain (ARC619Y) that forms distinct foci upon exposure to agonists but retains a diffuse nuclear distribution in the presence of antagonists. Live-cell imaging of this mutant demonstrated that cytoplasmic foci formation occurs immediately upon agonist but not antagonist addition. Fluorescence recovery after photobleaching (FRAP) revealed that agonist-bound GFP-AR exhibited reduced mobility relative to unliganded or antagonist-bound GFP-AR. Importantly, agonist-bound GFP-AR mobility was strongly affected by protein expression levels in transiently transfected cells, and displayed reduced mobility even in slightly overexpressing cells. Cyan fluorescent protein-AR (CFP-AR) and yellow fluorescent protein-CREB binding protein (YFP-CBP) in the presence of agonists and antagonists were used to demonstrate that CFP-AR specifically co-localizes with YFP-CBP in an agonist dependent manner. Dual FRAP experiments demonstrated that CBP mobility mirrored AR mobility only in the presence of agonist. HTM enabled simultaneous studies of the sub-cellular distribution of GFP-AR and ARC619Y in response to a range of concentrations of agonists and antagonists (ranging from 10(-12) to 10(-5)) in thousands of cells. These results further support the notion that ligand specific interactions rapidly affect receptor and co-factor organization, solubility, and molecular dynamics, and each can be aberrantly affected by mutation and overexpression.

Active Transport, Cell Nucleus↗
PubMed2006

Genistein affects androgen-responsive genes through both androgen- and estrogen-induced signaling pathways.

This study examined the mechanisms by which the prostate cancer chemopreventive agent genistein modulates gene expression in LNCaP human prostate cancer cells. Expression of androgen- and estrogen-regulated genes was measured in LNCaP cells cultured in the presence or absence of hormonal stimulation and the presence or absence of genistein. Genistein strongly suppressed basal expression of androgen-responsive gene (ARG) mRNAs, including prostate-specific antigen (PSA) and Ste20-related proline-alanine-rich kinase (SPAK). However, genistein had little or no effect on basal expression of two other ARGs, beta2-microglobulin (B2M) or selenoprotein P (SEPP1). Culturing LNCaP cells in the presence of the synthetic androgen R1881-induced increases in PSA, SPAK, B2M, and SEPP1 mRNA levels. The R1881-induced expression of these genes was uniformly blocked by genistein. For PSA and SPAK, genistein also blocked or downregulated 17beta-estradiol-induced increases in mRNA expression. These results indicate that genistein selectively alters expression of ARG mRNAs in LNCaP cells through modulation of both androgen- and estrogen-induced signaling pathways.

Androgens↗
PubMed2004

The androgen receptor co-activator CBP is up-regulated following androgen withdrawal and is highly expressed in advanced prostate cancer.

The androgen receptor co-activator CREB (cAMP-response element binding protein)-binding protein (CBP) enhances androgen receptor activity after stimulation by androgenic hormones and androgen receptor antagonists. The aim of the present study was to investigate the regulation of CBP expression by steroid and peptide hormones in prostate cancer. For this purpose, LNCaP cells were treated with the synthetic androgen methyltrienolone (R1881), epidermal growth factor, insulin-like growth factor-I or interleukin-6 (IL-6). CBP protein and mRNA expression were studied by western blotting and real-time PCR, respectively. CBP expression was also investigated in tissue specimens obtained from 26 patients with therapy-resistant carcinoma of the prostate. In LNCaP cells, CBP protein was down-regulated by R1881 or IL-6. The non-steroidal anti-androgen bicalutamide antagonized the effects of R1881 and the Janus kinase inhibitor AG 490 reversed the effects of IL-6. In contrast, neither R1881 nor IL-6 caused any effect on CBP expression in the PC-3 cell line. In LNCaP cells, the inhibition of CBP expression by R1881 or IL-6 was also observed at the mRNA level. CBP protein was detected in all 26 specimens by immunohistochemistry. The results suggest that up-regulation of CBP during androgen ablation may be relevant to the failure of endocrine therapy in patients with prostate carcinoma.

Aged↗
PubMed2007

Evaluation of an in vitro model of androgen ablation and identification of the androgen responsive proteome in LNCaP cells.

Proteins responsive to androgen and anti-androgen may be involved in the development and progression of prostate cancer and the ultimate failure of androgen-ablation therapy. These proteins represent potential diagnostic and therapeutic targets for improved management of prostate cancer. We have investigated the effect of androgen (R1881) and anti-androgen (bicalutamide) on the androgen-responsive prostate cancer LNCaP cell line using a quantitative gel-based proteomic approach. Prior to analysis, the in vitro system was evaluated for reproducibility and validated by appropriate molecular responses to treatment. Six replicate samples were independently generated and analysed by 2-D DIGE. According to strict statistical criteria, 197 spots were differentially expressed, of which we have successfully identified 165 spots corresponding to 125 distinct proteins. Following androgen supplementation, 108 spots (68 proteins) were increased and 57 spots (39 proteins) were decreased. Essentially no difference was observed between control and anti-androgen-treated samples, confirming the absence of "off-target" effects of bicalutamide. Identified proteins were involved in diverse processes including the stress response and intracellular signalling. The potential contribution to disease of these processes and identified constituent proteins are discussed. This rigorous, statistically supported study of androgen responses has provided a number of potential candidates for development as diagnostic/prognostic markers and drug targets.

Androgens↗
PubMed2003

Growth inhibition and differentiation in human prostate carcinoma cells induced by the vitamin D analog 1alpha,24-dihydroxyvitamin D2.

BACKGROUND: Vitamin D has been suggested as a chemopreventive and therapeutic modality for prostate cancer. However, hypercalcemic toxicity has limited the use of 1alpha,25-dihydroxyvitamin D(3) (1,25-(OH)(2)D(3)) in clinical trials, prompting the search for analogs of vitamin D with less toxicity while retaining efficacy as a modality for cancer intervention. In this study, the less hypercalcemic vitamin D analog 1alpha,24-dihydroxyvitamin D(2) (1,24-(OH)(2)D(2)) was examined for its effects on cellular growth inhibition and differentiation induction in the LNCaP human prostate carcinoma cell line. METHODS: LNCaP cell growth was determined by quantifying DNA levels. Protein levels were determined using the ELISA method and immunoblotting. Levels of mRNA were determined using real-time quantitative reverse transcriptase PCR. RESULTS: LNCaP growth was decreased 50% by exposure to 0.01 nM 1,24-(OH)(2)D(2) after 96 hr in the presence of a growth stimulatory 0.1 nM dose of the androgen R1881. Prostate specific antigen (PSA) levels were increased 3.5-fold with 10 nM 1,24-(OH)(2)D(2) treatment compared to a 1.9-fold increase in PSA levels found with 10 nM 1,25-(OH)(2)D(3) under low androgen conditions. Neither 1,24-(OH)(2)D(2) nor 1,25-(OH)(2)D(3) affected the expression of cytokeratin 18 protein levels. Treatment with 10 nM 1,24-(OH)(2)D(2) alone produced a 1.3-fold increase in AR mRNA and a 2.2-fold increase in AR protein levels after 96 hr. Surprisingly, the addition of 1.0 nM R1881 alone or in combination with 10 nM 1,24-(OH)(2)D(2) produced an approximately 60% decrease in AR mRNA, whereas AR protein levels were increased 1.6-fold. CONCLUSIONS: Overall, 1,24-(OH)(2)D(2) was found to be at least as effective as 1,25-(OH)(2)D(3) at inhibiting growth and inducing differentiation markers in LNCaP prostate carcinoma cells and may thus prove useful in prostate cancer treatment.

Blotting, Western↗
PubMed2005

Expression of tumor-associated trypsinogens (TAT-1 and TAT-2) in prostate cancer.

BACKGROUND: Trypsinogens are pancreatic serine proteinases and expressed in several cancers as tumor-associated trypsinogens (TAT). Trypsin mediates activation of pro-uPA and pro-MMPs, thus promoting angiogenesis and tumor invasion. Recently, we described expression of TAT in the human male genital tract and now we studied TAT in relation to PSA in PCa. METHODS: TAT expression was studied by immunohistochemistry, in situ hybridization, RT-PCR, DNA-sequencing and IFMA. LNCaP cells were used to study secretion of TAT and PSA after androgen stimulation. RESULTS: Immunoreactive TAT was localized in all prostatic tumors (n = 109), lymph node (n = 16), and bone metastases (n = 17). Immunostaining intensity increased with higher Gleason's grade, whereas PSA immunostaining decreased significantly. PSA and TAT were not identically distributed in benign and malignant cells. Androgen stimulation of LNCaP cells decreased secretion of TAT and increased that of PSA. TAT mRNA was demonstrated in tissue sections and identified as TAT-1 and -2 by RT-PCR and DNA-sequencing. CONCLUSIONS: Expression of TAT is better preserved than PSA in high-grade PCa. Expression of TAT and PSA is regulated by different mechanisms as demonstrated in tissue sections and in vitro. Locally produced TAT may act in a paracrine mode to promote angiogenesis and tumor invasion in PCa by both activating and degrading of other proteinases. Further studies on the role of TAT in invasive PCa and on the mechanisms involved in the regulation of TAT expression are warranted.

Gene Expression Regulation, Enzymologic↗
PubMed2005

Role of androgen receptor in the progression of human prostate tumor cells to androgen independence and insensitivity.

BACKGROUND: Various studies have implicated the androgen receptor (AR) in the progression of androgen-dependent human prostate cancer cells to androgen-independent and androgen-insensitive phenotypes, but the exact role of AR in progression is unclear. METHODS: To mimic the clinical situation and test the role of AR in progression, we cultured androgen-dependent LNCaP 104-S prostate tumor cells in the presence of the antiandrogen Casodex (bicalutamide) to derive resistant (CDXR) clones. In a second step, we cultured CDXR cells in the presence of the androgen R1881, which generated androgen- and Casodex-insensitive (IS) cells. These cells were then characterized with regard to AR function and the effect of ectopic AR expression or AR knockdown on androgen sensitivity. RESULTS: CDXR cells showed increased AR expression and transcriptional activity. CDXR cell proliferation was unaffected by Casodex but was repressed by androgen in vitro and in vivo. IS cells, on the other hand, had greatly reduced AR expression and activity compared to CDXR cells. Knockdown of AR expression in CDXR cells produced cells that were insensitive to androgen. Conversely, re-expression of AR in IS cells regenerated cells that were repressed by androgen. Knockdown of AR expression in 104-S cells produced cells that remained stimulated by androgen, while overexpression of AR in 104-S cells generated an androgen-repressed phenotype but did not confer androgen-independent growth. CONCLUSIONS: Increased AR expression determines whether prostate cancer cells are repressed by androgen, but is not required for androgen independence. These results may have implications for anti-AR therapy for prostate cancer.

Androgen Antagonists↗
PubMed2006

Relaxin becomes upregulated during prostate cancer progression to androgen independence and is negatively regulated by androgens.

BACKGROUND: Relaxin is a potent peptide hormone normally secreted by the prostate. This study characterized relaxin expression during prostate cancer progression to androgen independence (AI), and in response to androgens. METHODS: The prostate cancer cell line, LNCaP, was assayed by microarrays and confirmatory Northern analysis to assess changes in relaxin levels due to androgen treatment and in LNCaP xenografts following castration. Relaxin protein levels were examined by immunohistochemistry (IHC) in tissue microarrays of human prostate cancer samples following androgen ablation. RESULTS: Relaxin levels decreased in a time and concentration-dependent manner due to androgens in vitro, and increased in xenografts post-castration. Relaxin increased in radical prostatectomy specimens after 6 months of androgen ablation and in AI tumors, was highest in bone metastases. CONCLUSIONS: Relaxin is negatively regulated by androgens in vitro and in vivo, which correlates to clinical prostate cancer specimens following androgen ablation. The role of relaxin in angiogenesis and tissue remodeling suggests it may contribute to prostate cancer progression.

Animals↗
PubMed1981

Influence of prostatic secretion protein on uptake of androgen-receptor complex in prostatic cell nuclei.

Prostatic secretion protein (PSP) is a major component of rat prostatic cytosol, and this protein is also found in the prostatic fluid. Purified PSP was found to inhibit the nuclear uptake of the [3H]methyltrienolone-receptor complex in vitro. Furthermore, purified PSP inhibited the binding of this androgen-receptor complex to DNA-cellulose. It is suggested that these effects of PSP may represent an intracellular control system regulating the concentration of PSP. Administration of estramustine, the dephosphorylated metabolite of the anti-cancer drug estramustine phosphate (Estracyt), to rats was found to decrease the weight of the prostate gland but to maintain the concentration of PSP, calculated as mg PSP/mg protein, at a constant level. In contrast, castration or administration of estradiol-17 beta valerate decreased the weight of the prostate gland as well as the concentration of PSP. These findings indicate that the mechanism of action of estramustine is at least partially different from that of estradiol-17 beta. Furthermore, it is suggested that estramustine may exert part of its action through its effects on the concentration of PSP.

Animals↗
PubMed1981

Androgen steroid-receptor binding in the canine epididymis.

The epididymis of the dog has been studied with regard to its ability to bind androgens with a high affinity and low capacity. A proteinaceous molecule was demonstrated in the high-speed supernatant fraction of disrupted cells that bound DHT and sedimented in a sucrose density gradient with a sedimentation coefficient of 8S with respect to bovine serum albumin. This binding protein was able to transport DHT to the nucleus at elevated temperatures where it sedimented as a 4S in a 5-20% sucrose density gradient. Even though this protein appears to be similar to other androgen receptors in other accessory sex organs in a variety of mammalian tissue, it is different from androgen-binding protein (ABP). The apparent specificity of the receptor protein for androgens was demonstrated using competition studies. The molecular configuration of the steroids was found to be instrumented in this selectivity. A reduced affinity of the androgen receptor was found when the steroid did not possess a hydroxyl group at the 17 beta-position and a 3-oxo-group irrespective of the degree of saturation of the A-ring. Studies concerning the physical properties of the androgen binder revealed a protein with a molecular weight of 220,000, a Stokes' radius of 54A, and a frictional ratio of 1.35.

Animals↗
PubMed1981

Androphilic proteins in the human prostate.

Dihydrotestosterone-binding protein in cytosols from human prostates was different from the R1881- and R5020-binding proteins. The R1881- and R5020-binding proteins in the cytosol were very similar and most of the binding sites for R1881 were capable of binding R5020. However, nuclear extracts showed equal binding to dihydrotestosterone and R1881, but not to R5020, suggesting that there might not be a progestin receptor in the human prostate. Maximum binding sites to dihydrotestosterone, R1881, and R5020 in cytosols were very similar among "normal" and pathological prostates except that dihydrotestosterone binding was higher in "normal" prostates than in the pathological ones. Histochemically, R1881-binding was observed in the epithelial cells and in malignant cells, but not in the stroma.

Androgen-Binding Protein↗
PubMed1984

Androgen receptor binding characteristics in the cytosol of the rat dorsolateral prostate gland and the Dunning R-3327 prostatic adenocarcinoma.

The incidence of prostatic cancer is highly correlated with advanced age, and it has been suggested that changes in androgen binding may be important in age-associated alterations in growth regulatory mechanisms of prostatic epithelial cells. In this study the effects of age on androgen binding characteristics in the dorsolateral prostate glands of young and aged Copenhagen rats were determined and the binding properties in the Dunning R3327/130 subline of rat prostatic adenocarcinoma were characterized. Tritium-labeled and nonlabeled methyltrienolone analogs (R1881) were used to study the binding properties of 5 alpha-dihydrotestosterone receptor in the cytosol of tumors and prostate glands. Binding of R1881 was low but specific for the androgen receptor as shown by competition studies in which nonlabeled R1881, 5 alpha-dihydrotestosterone, and testosterone competed successfully with 3H-R1881 for binding sites, but 17 beta-estradiol and low levels of progesterone did not. In Copenhagen dorsolateral prostate, Scatchard analysis suggested a single class of binding sites. In young animals (three to five months) the average binding capacity was 10.36 fmol/mg cytosol protein with a dissociation constant (Kd) of 2.28 nmol/L. The dorsolateral prostate of aged rats (11-16 months) showed no significant difference in specific binding characteristics as compared to the younger age group. Specific binding of 3H-R1881 in R3327/130 tumor was saturable with a single class of high-affinity binding sites having an average binding capacity of 64.77 fmol/mg cytosol protein and a Kd of 2.76 nmol/L. These data show that the tumor had approximately 6.5 times the number of binding sites as did the normal Copenhagen rat dorsolateral prostate gland. However, no age-related changes were detected through 11-16 months of age in the androgen binding characteristics of normal rat dorsolateral prostate gland that could be correlated with the higher concentration of androgen binding sites in the R3327/130 tumor subline.

Adenocarcinoma↗
PubMed1984

Clinical applications and value of receptor levels in treatment of prostate cancer.

Factors affecting the validity and interpretation of androgen receptor (AR) assays on prostatic carcinoma tissue are discussed, and attempts to relate AR concentration with response of the patient to hormonal manipulation are reviewed. It is concluded that nuclear AR content may be useful in evaluating prognosis and likely response to hormonal therapy, and that, owing to the heterogeneity of many prostatic carcinoma specimens, a reliable histochemical method for the assessment of androgen sensitivity would be a valuable supplement to the biochemical assay.

Androgens↗