Extraction of androgen–receptor complexes from regions of rat ventral prostate nuclei sensitive or resistant to nucleases

Davies, P.

doi:10.1677/joe.0.0990051

Cited by 9 publications

(11 citation statements)

References 30 publications

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“…3b). A similar effect was noted for the similarly treated rat prostate nuclease-resistant androgen-receptor complex (Davies, 1983).…”

Section: Resultssupporting

confidence: 74%

“…Pellets were lysed gently in EDTA (1 mmol/1; pH 7-4) and centrifuged at 2000 g for 10 min to yield the second supernatant (S2) and pellet (P) fractions. Sedi¬ mentation analyses of soluble fractions on linear and isokinetic gradients of sucrose (Davies et al 1980(Davies et al , 1982 and of androgen-receptor complexes released from the various fractions (Davies, 1983) have been described elsewhere. 'Free' androgen-receptor com¬ plexes were released from BPH epithelial cell nuclei by lysis before incubation with micrococcal nuclease ).…”

Section: Preparation Of Tissue Fractionsmentioning

confidence: 99%

“…No quantitative difference in receptors detected were observed using these procedures. Receptors associ¬ ated with oligonucleosomes were released using KC1 (0-6 mol/1) or DNAase I (Davies, 1983); those associ¬ ated with nuclease-resistant material were released with heparin at 10 g/1 (Davies, 1983) or with trypsin at 0-1 g/1 (Rennie, Bruchovsky & Cheng, 1983). …”

Section: Measurement Of Androgen-binding Sitesmentioning

confidence: 99%

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Intranuclear distribution of androgen receptors in human prostate carcinoma

Kyprianou¹,

Gingell²,

Davies³

1987

Journal of Endocrinology

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Androgen receptors in nuclei from human prostate carcinomas were characterized on the basis of their solubilization by, or resistance to, micrococcal nuclease. By this means, androgen receptors were assigned to three nuclear categories: those associated with nuclease-resistant structures, those associated with chromatin and those apparently uncommitted by association with either of these. Prostate carcinoma nuclei contained high concentrations (57-82% of total nuclear content) of nuclease-resistant androgen receptors. This was a different pattern from that observed previously for benign hypertrophic prostate epithelial nuclei which contained a variable high proportion of uncommitted androgen receptors. The differences could not be attributed to differential losses to cytosol, or to loss of functionality, as determined in vitro. The differences in distribution could reflect different responses of diseased cells to androgens, or the intervention of other factors more relevant to the disease process.

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“…3b). A similar effect was noted for the similarly treated rat prostate nuclease-resistant androgen-receptor complex (Davies, 1983).…”

Section: Resultssupporting

confidence: 74%

Section: Preparation Of Tissue Fractionsmentioning

confidence: 99%

Section: Measurement Of Androgen-binding Sitesmentioning

confidence: 99%

See 1 more Smart Citation

Intranuclear distribution of androgen receptors in human prostate carcinoma

Kyprianou¹,

Gingell²,

Davies³

1987

Journal of Endocrinology

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“…Preparation of nuclei and nuclear fractions Details of homogenization of tissue and the buffers employed have been given elsewhere (Davies, Thomas, Borthwick & Giles, 1980;Davies, Thomas & Giles, 1982;Davies, 1983;Davies & Thomas, 1984). These conditions of homogenization yield predominantly epithelial cells.…”

Section: Animals and Tissuesmentioning

confidence: 99%

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

Davies

Rushmere²

1990

Journal of Molecular Endocrinology

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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/l) 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.

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“…Apart from this structurally distinct diversity of binding, androgen receptors are heterogeneously distributed within chromatin, as revealed by nuclease digestion [22,24,35,36]. Micrococcal nuclease recognizes active chromatin structure and under some conditions may additionally detect chromatin features related to the actual rates of transcription of the associated genes [37-391, including features implicated in hormonal activation of genes [24,36,40,41].…”

Section: Introductionmentioning

confidence: 99%

Correlations between prostate chromatin structure and transcriptional activity and acceptor site distribution

1986

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Androgen-receptor complexes are intimately involved in the maintenance of rat ventral prostate chromatin in a transcriptionally active structure. The presence or absence of androgens influenced the quantity of transcriptionally active chromatin and the distribution of acceptor sites for androgen-receptor complexes as probed by endonucleolytic cleavage. After castration, changes in the sedimentation rates of nucleosome oligomers were consistent with the absence of androgen-receptor complexes and elongating polyribonucleotide chains. These changes were accompanied by decreases in the ability of chromatin released under conditions of minimal nuclease digestion to bind androgen-receptor complexes and to support incorporation of RNA precursors responsive to androgenic stimulation. Saturation analyses of chromatin and nuclear fractions with partially purified androgen-receptor complexes revealed two affinity classes of acceptor sites. After castration, alterations in the intrachromatin distribution of acceptor sites were consistent with their redeployment into areas of decreased nuclease sensitivity, as previously shown for androgen-responsive genes.

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Extraction of androgen–receptor complexes from regions of rat ventral prostate nuclei sensitive or resistant to nucleases

Cited by 9 publications

References 30 publications

Intranuclear distribution of androgen receptors in human prostate carcinoma

Intranuclear distribution of androgen receptors in human prostate carcinoma

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

Correlations between prostate chromatin structure and transcriptional activity and acceptor site distribution

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