Characterization of 7–8S progestin binding protein in human prostate using vertical tube rotor

Schneider, Sara L.; Pontes, J. Edson; Gréco, J; Murphy, Gerald P.; Sandberg, Avery A.

doi:10.1016/0022-4731(84)90075-x

Cited by 12 publications

(3 citation statements)

References 42 publications

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“…In recent studies in which incubations were performed in the presence of molybdate, Kd's for the progesterone binder in cytosols were in the range of 0.2-1.0nM and Bmax's were in 20-90fmol/mg protein (Ekman et al, 1982, Sirett and Grant, 1982, Bashirelahi et al, 1983b, Schneider et al, 1984. In the present experiment, it is revealed that binding parameters for 3H-R 5020 in cytosols are almost identical to those of other reports.…”

Section: Binding Of 3h-ru 27987 In Nucler Extractsupporting

confidence: 78%

“…In the results reported by these authors, the amount of steroid attached to nuclei was relatively small and this does not seem to exclude the possibility of contamination of the nuclei with the labeled cytosol. On the other hand, Schneider et al (1984) reported that after a brief heat treatment, the cytosol bound with 3H-R 5020 becomes capable of being retained in a DNA cellulose column, and suggested the presence of progesterone receptor in the human prostate. In the present study, on the contrary, no retention of the cytosol combined with 3H-RU 27987 in a DNA Sepharose column was observed even after activation in a conventional way.…”

Section: Binding Of 3h-ru 27987 In Nucler Extractmentioning

confidence: 99%

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Properties of progestin-binding protein in benign hypertrophic human prostate.

et al. 1986

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RU 27987 is a new ligand for progesterone receptor and binds in high affinity to nuclei of target tissues of progesterone.Using this compound, progestin-binding components in the benign hypertrophic human prostate were studied, and compared with those examined with R 5020, a conventional ligand, in the study of progesterone receptor.In cytosols, the binding affinity of RU 27987 was higher than that of R 5020, and the number of maximum binding sites for RU 27987 seemed to be large but correlated well with those of R 5020. The binder for RU 27987 sedimented at 8.6 S, and the binding was specific to progestational steroids, indicating that binding properties of this binder in the cytosols are identical to those for R 5020.Although there was no binding with R 5020 in the nuclear extract, a small amount of specific binding with RU 27987 was detected.However, the cytosol bound with RU 27987 was not retained in DNA Sepharose and no specific binder for RU 27987 in the nuclear extract was observed in a sucrose density gradient centrifugation.From these observations, it was assumed that the nuclear binding observed was attributable to contamination of the cytosolic binder.The results obtained in the present study suggest that the progestinbinding component in the benign prostatic hypertrophy is not the progesterone receptor but a high affinity binder for progestins whose physiological role is not clear at present.

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Section: Binding Of 3h-ru 27987 In Nucler Extractsupporting

confidence: 78%

Section: Binding Of 3h-ru 27987 In Nucler Extractmentioning

confidence: 99%

Properties of progestin-binding protein in benign hypertrophic human prostate.

et al. 1986

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“…The R5020 K d reported here for the T47D progestin receptor is similar to the binding constant for the progestin receptor in human uterus, prostate and breast (Namkung & Petra 1981, Schneider et al 1984, Van der Walt et al 1986). These binding affinities and receptor concentrations for the TE85 and MC3T3-E1 cells are similar to those reported for other human osteosarcoma lines (Etienne et al 1990, Slootweg al.…”

Section: Saturation Analyses With [ 3 H]r5020supporting

confidence: 49%

Characterization of the progestin receptors in the human TE85 and murine MC3T3-E1 osteoblast-like cell lines

Gunnet¹,

Granger²,

Cryan³

et al. 1999

Journal of Endocrinology

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Progestins are believed to exert positive effects on bone density through receptors located in osteoblasts. In the present studies, the binding characteristics and regulation of the progestin receptors in two osteoblast-like cell lines were compared with those in human breast lines. Human TE85 and murine MC3T3-E1 osteoblast-like cells contain a single, high-affinity progestin binding site whose affinity and concentration are lower than in human breast cells. The osteoblastic progestin binding sites showed the expected steroid specificity and associated with the cell nuclei when occupied by ligand. The progestin receptors in osteoblastic cells also had sedimentation coefficients similar to those receptors in breast cells. The regulation of the progestin receptor in the osteoblast-like cells was explored by treating them with estradiol. In contrast to the large, rapid change seen in the breast cells, the progestin receptor levels in the MC3T3-E1 cells showed only a small, delayed up-regulation with estradiol treatment. The progestin receptor number in the TE85 cells was unaffected by estradiol. Down-regulation of the progestin receptors was explored by treating the cells with the progestin, norethindrone (NET). NET administration produced a rapid drop in progestin binding sites in the breast cells and a smaller, more gradual decline in MC3T3-E1 progestin binding. While the maximal decrease in receptor number occurred within 24 h in the breast cells, the receptor number was still continuing to fall after 72 h in the MC3T3-E1 cells. The data presented here demonstrate that both human and murine osteoblastlike cells contain a functional progestin receptor whose binding characteristics and regulation are similar, but not identical, to those receptors in other progestin target tissues such as the breast.

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Estrogen and progestin receptors in human prostatic carcinoma

Wolf

Schneider

Pontes

et al. 1985

Cancer

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Cytosol receptors for estrogens (ER) and progestins (PR) were assayed in human prostatic carcinoma (CaP) and benign prostatic hyperplasia (BPH). Specimens were obtained from either the peripheral or the periurethral zone of the prostate. Stringent criteria were used to identify and measure 7‐8S specific receptor using sucrose gradient analysis in a vertical tube rotor. Progesterone receptor was found in 14 BPH samples assayed and in 12 of 13 prostate cancers. In contrast, the 7‐8S estrogen receptor was found in none of the nine benign samples assayed and in all prostate cancers. BPH samples were taken from either peripheral or periurethral zones and gave similar results. The histology of individual specimens did not correlate with either the ER or PR present, and, in the cancers, there was no correlation between the pathologic stage or the Gleason score and receptor content.

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Characterization of 7–8S progestin binding protein in human prostate using vertical tube rotor

Cited by 12 publications

References 42 publications

Properties of progestin-binding protein in benign hypertrophic human prostate.

Properties of progestin-binding protein in benign hypertrophic human prostate.

Characterization of the progestin receptors in the human TE85 and murine MC3T3-E1 osteoblast-like cell lines

Estrogen and progestin receptors in human prostatic carcinoma

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