Binding of progesterone receptor by nuclear preparations of rabbit and guinea pig uterus.

Saffran, Judith; Loeser, Bonnie K.; Bohnett, S A; Faber, Lee E.

doi:10.1016/s0021-9258(17)33102-2

Cited by 29 publications

(1 citation statement)

References 30 publications

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“…The increase in rate of activation upon dilution which we have observed is clearly inconsistent with their findings. Furthermore, the progesterone-receptor complexes from rabbit and guinea pig uterus are activated by dilution and gel filtration (Saffran et al, 1976) in a manner comparable to the results which we have presented. The presence of an inhibitor of activation became apparent (Simons et al, 1976) when the dexamethasone-receptor complex of HTC cells was diluted with homologous cytosol.…”

Section: Discussionsupporting

confidence: 85%

Activation of the rat liver glucocorticoid-receptor complex

Ja¹,

Mh²,

Kp³

et al. 1977

Biochemistry

128

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The rat liver glucorcorticoid receptor has been activated using three procedures: heat, gel filtration, and dilution. With time after heat activation the steroid--receptor complex loses its capacity to bind to DNA--cellulose, while receptor activated by Sephadex G-25 and by dilution maintains DNA--cellulose binding capacity. The rates of steroid dissociation from nonactivated and activated receptor and essentially identical. However, nonactivated receptor is capable of rebinding steroid, while activated receptor has a reduced capacity to rebind steroid. The results of the gel filtration and dilution studies suggest that a low-molecular-weight factor(s) exists in rat liver cytosol which is involved in the process of activation.

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Section: Discussionsupporting

confidence: 85%

Activation of the rat liver glucocorticoid-receptor complex

Ja¹,

Mh²,

Kp³

et al. 1977

Biochemistry

128

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Characterization and Partial Purification of the 8–9S Androgen Receptor from Benign Prostatic Hyperplasia Tissues

KOUTSILIERIS,

GRONDIN,

BOUTHILLIER

et al. 1990

Journal of Andrology

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The present study reports a 3,800‐fold purification of the 8‐9S androgen‐receptor complex from benign prostate hyperplasia (BPH) tissues using differential chromatography. In addition, the BPH androgen receptor complexes have been characterized using sucrose density gradient (SDG) ultracentrifugation, gel permeation, and anion exchange high performance liquid chromatography (HPLC). Results indicate that a) under nontransforming conditions, BPH cytosols contained both 8‐9S (40–78%) and 4S (22–60%) androgen‐receptor forms, b) apparent molecular weights of these androgen‐receptor complexes, as analyzed by gel permeation HPLC, were estimated to correspond at 270 kDa, and 90 kDa respectively, c) 8‐9S androgen‐receptor complexes were retained on an anion exchange HPLC column and could be eluted at 0.22 M KCl at a linear gradient, whereas 4S complexes were not retained on anion exchange columns under identical experimental conditions, d) 10X dilution of BPH cytosols containing only the 4S (0.6 M KCl) form and subsequent chromatography on anion exchange HPLC system was indicative of fragmentation (these fragments were retained on anion exchange columns and could be eluted by 0.33 M KCl on a linear gradient HPLC), and e) increased temperature (22 C) was permissive of proteolytic fragmentation (fragments were estimated to correspond at 30, 15, and 5 kDa). The results are discussed in relationship with the composition of the nontransformed androgen‐receptor molecules.

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Application of octadecylsilyl‐silica in purification studies related to the nontransformed rat ventral prostate androgen receptor

et al. 1988

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We investigated the application of octadecylsilyl (ODS)-silica in studies related to characterization and purification of the nontransformed rat ventral prostate androgen receptor. The results indicated that ODS-silica successfully separates the free [3H]R1881 from the labeled [3H]R1881 transformed (4-5S) and nontransformed (8-9S) rat ventral prostate androgen receptors. Partial purification of the 8-9S receptor form was performed by the fractionation of rat cytosol using cartridges of the ODS-silica and fast-flow-rate phosphocellulose chromatography. Further purification was accomplished by differential chromatography (DEAE-cellulose and slow-flow-rate phosphocellulose chromatography). This partially purified 8-9S receptor, when analyzed on a gel permeation high-performance liquid chromatography column, resulted in a three-peak pattern of UV absorbance. One of these peaks corresponded to a 59-kD non[3H]R1881-binding protein and the remaining two corresponded to 270-kD and 190-kD[3H]R1881-binding proteins. These results demonstrate the usefulness of ODS-silica in androgen receptor studies. The association of a 59-kD nonsteroid binding protein with the nontransformed rat ventral prostate androgen receptor is discussed.

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Binding of progesterone receptor by nuclear preparations of rabbit and guinea pig uterus.

Cited by 29 publications

References 30 publications

Activation of the rat liver glucocorticoid-receptor complex

Activation of the rat liver glucocorticoid-receptor complex

Characterization and Partial Purification of the 8–9S Androgen Receptor from Benign Prostatic Hyperplasia Tissues

Application of octadecylsilyl‐silica in purification studies related to the nontransformed rat ventral prostate androgen receptor

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