Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The objective of this study was to determine whether progesterone-induced estrogen receptor regulatory factor (ReRF) is a component of hamster uterine nuclei or a cytoplasmic contaminant of the nuclear fraction. Crude uterine nuclei were prepared in low salt buffer and were purified by either the hexylene glycol method or an isotonic sucrose-Triton X-100 procedure. ReRF activity was measured as a net percentage increase in estrogen receptor inactivation after incubation of a 0.5 M KCl nuclear extract at 36 degrees C for 30 min. Progesterone treatment (5 mg/kg, s.c. in oil, 2 h) increased net receptor inactivation to the same extent (9-12% net increase) in extract made from each nuclear preparation. Extensive washing of nuclei caused a progressive decline in recovery of ReRF activity, in parallel with the behavior of KCl-extractable nuclear protein and estrogen receptor. These results demonstrate that ReRF is a loosely bound component of the uterine nucleus.
Mol Cell Endocrinol 1983 Oct
PMID:Localization of estrogen receptor regulatory factor in the uterine nucleus. 664 77

Multiple molecular forms of plasminogen activator were detected in normal human mammary epithelial cells in culture. Cells derived from (normal) breast mammoplasty specimens and grown on the surface of collagen gels exhibited three major classes of plasminogen activator isozymes (Mr = 100,000 [100K], 75,000 [75K], and 55,000 [55K]). The activity of the 100K and 75K isozymes was greatly reduced when the cells were grown on conventional tissue-culture-grade plastic surfaces. MCF-7, a human mammary carcinoma cell line, exhibited predominantly or exclusively the 55K isozyme, irrespective of the cell growth substratum. The activity of the 55K isozyme was more than twofold higher for MCF-7 cells grown on collagen gels than for cells grown on plastic. Progesterone, diethylstilbestrol, and estrogen stimulated the activity of the 55K isozyme of MCF-7 cells, but only when the cells were grown on a plastic surface. The plasminogen activator activities of the normal human mammary epithelial cells were not stimulated by these hormones, irrespective of the growth substratum. These results show that the expression of plasminogen activator isozymes by human mammary epithelial cells is subject to modulation by the extracellular matrix. Normal and malignant cells may differ in their responsiveness to these effects.
Mol Cell Biol 1983 Jun
PMID:Effect of the extracellular matrix on plasminogen activator isozyme activities of human mammary epithelial cells in culture. 668 79

Granulosa and theca cells obtained from patients were isolated and cultivated in a chemically defined medium containing gonadotropins and/or testosterone. Progesterone secretion by granulosa cells was consistently stimulated (2-40-fold) in all 5 patients by the addition of follicle-stimulating hormone (FSH, 0.25 micrograms/ml). In the presence of testosterone (0.5 micro M) alone, progesterone production was stimulated (2-8-fold) in 4 out of the 5 patients and cells of one patient showed a greater response to testosterone than to FSH alone. In 2 of the 5 patients, it was also noted that FSH and testosterone acted in a synergistic manner to stimulate the production of progesterone by granulosa cells. On the other hand, human chorionic gonadotropin (hCG, 1.0 IU/ml) alone failed to exert any significant effect. None of the treatments examined altered the production of progesterone by theca cells. These results suggest a role for FSH and testosterone in regulating progesterone biosynthesis by granulosa cells of the human ovary during follicular development.
Mol Cell Endocrinol 1981 Jul
PMID:The role of gonadotropins and testosterone in progesterone production by human ovarian granulosa cells. 679 Mar 15

MCF-7 cells contain progesterone, estradiol and glucocorticoid receptors. Following addition of these hormones to the growth medium of the cells, hormone-receptor complexes were found to sediment with chromatin fragments produced by trace digestion with micrococcal nuclease. The binding in all cases could be competed by excess unlabeled hormone. In each case the fragments with which the hormone-receptor complexes were associated tended to be smaller than the bulk chromatin fragments, indicating a greater sensitivity of those chromatin regions to the nuclease. The mononucleosomes released by more extensive digestion with micrococcal nuclease contained different amounts of each of the three hormone-receptor complexes. Progesterone could usually be detected on mononucleosomes only after very brief sedimentation analyses, whereas glucocorticoid- and estradiol-labeled mononucleosomes were stable during long centrifugations. Comparison of glucocorticoid- and estradiol-labeled mononucleosomes indicated that their sedimentation rates differed from one another and from bulk nucleosomes. Estradiol nucleosomes from MCF-7 cells and rat uterus (Senior and Frankel, 1978) sediment significantly faster than bulk nucleosomes, while glucocorticoid nucleosomes from MCF-7 cells and rat hepatoma cells sediment with, or even fractionally slower than, bulk nucleosomes.
Mol Cell Endocrinol 1983 Jun
PMID:Progesterone, glucocorticoid and estradiol receptors in MCF-7 cells bind to chromatin. 686 95

Progesterone binds to specific high-affinity and limited-capacity binding sites of chick-oviduct microsomes of estrogen-primed chicks. The dissociation constant is 2 x 10(-9) M (range 1.6--3.0) and the number of binding sites 500 femtomoles/mg microsomal protein (range 464--551). Treatment of the estrogen-primed chicks by progesterone had no apparent effect on the progesterone-binding capacity or affinity. Competition studies showed that testosterone, R-5020, Org-2058, D-norgestrel, 5 alpha-dihydrotestosterone and R-2323 were effective competitors of progesterone, in that order, whereas cortisol, estradiol and estrone exhibited only minimal displacement. No displacement of microsome-bound [3H]progesterone was found with fenoterol or prostaglandin F2 alpha. No high-affinity progesterone-binding sites were found in the microsomal fractions of liver, muscle, intestine or brain. On the basis of steroid-binding affinity and steroid-specificity determinations, the microsomal progesterone-binding components seem to be different from the progesterone receptor previously described in chick oviduct cytosol.
Mol Cell Endocrinol 1980 Aug
PMID:Progesterone-binding properties of the microsomal fraction from chick oviduct. 690 88

Epithelial cell-rich fractions of rat mammary gland were prepared using percoll gradients after collagenase dispersion. Their insulin-binding characteristics were similar to those of crude acini but superior to unfractionated isolated cells. Optimal binding was obtained after 60 min at 20 degrees C or 16 h at 4 degree C at pH 7.8 Binding at 37 degrees C was lower due probably to an enhanced rate of insulin degradation. 48 h after ovariectomy of 18-day pregnant rats insulin binding to acini doubled due to an increase in the number of insulin receptors. Progesterone but not bromocriptine (which prevented the rise in serum prolactin which occurred after ovariectomy) prevented this increase in insulin binding. These results illustrate that the change in serum progesterone rather than prolactin increases insulin binding to the mammary cell at parturition whilst insulin binding decreases in adipose tissue at the same time (Flint et al., Mol. Cell Endocrinol, 20, 101-111, 1981) enabling coordinated changes in the metabolism of these 2 tissues to take place during the perinatal period.
Mol Cell Endocrinol 1982 May
PMID:Insulin binding to rat mammary gland at various stages of cell isolation and purification. 704 14

The in vitro effects of progesterone, testosterone and estradiol-17 beta on steroid accumulation by isolated rabbit follicles were examined. Progesterone had no effect on LH-stimulated androgen accumulation but inhibited LH-stimulated estrogen accumulation at 10(-7) M and 10(-6) M. Testosterone at 10(-5) M but not at 10(-6) M or 10(-7) M, inhibited LH-stimulated progesterone accumulation. LH-stimulated estrogen accumulation was inhibited at all dose levels of testosterone. Estradiol (10(-5) M) inhibited LH-stimulated androgen accumulation and had no effects on progesterone accumulation. It is concluded that the steroidal milieu of follicles can influence their response to LH.
Mol Cell Endocrinol 1982 Apr
PMID:In vitro effects of sex steroids on LH-stimulated steroid accumulation by isolated rabbit ovarian follicles. 708 61

The effect of oestrogen and progesterone on prostaglandin synthesis and on DNA synthesis by rat decidual cells was studied in a culture system. The cells were explanted from deciduoma either during the proliferation phase (namely on the 5th day of leukocytic smear, Day L5:"L5 cells") or during the maintenance phase ("L8 cells") and examined on the second day of culture. Oestradiol-17 beta (7 X 10(-11) M) and progesterone (6 X 10(-8) M) significantly inhibited accumulation of PGE by cells explanted on Day L5: L8-cell cultures showed no significant response to oestradiol and the progesterone effect was markedly reduced. Progesterone stimulated [3H]thymidine incorporation into cells explanted on Day L5, but had no effect on L8-cultures. Other inhibitors of PG synthesis, namely cortisol, flufenamic acid and indomethacin, also had a stimulatory effect on DNA synthesis by L5 cells. PGE2 (5-10 micrograms/ml) inhibited DNA synthesis in control, indomethacin-treated and progesterone-treated L5-cell cultures, suggesting that the progesterone-induced stimulation of DNA synthesis may be in part be due to its inhibitory effect on PGE accumulation by decidual cells. The possibility is discussed that during the proliferation phase of decidual development in vivo, the rate of DNA synthesis may be influenced by steroid-induced changes in PGE content of the tissue.
Mol Cell Endocrinol 1980 Dec
PMID:Role of steroid hormones and prostaglandins in the regulation of DNA synthesis by decidual cells in culture. 720 33

The hormonal regulation of uterine and oviductal cytoplasmic estrogen and progesterone receptors was studied in immature beagles that were untreated, treated with estradiol-17 beta, or treated sequentially with estradiol and progesterone. Estradiol treatment increased the concentration of estrogen receptors in both tissues. Progesterone receptors were not detectable in the reproductive tract of untreated animals, but increased dramatically under the influence of estradiol. Estrogen withdrawal following estrogen stimulation concomitant estrogen plus progesterone administration, and estrogen withdrawal plus progesterone administration all caused significant reductions in both estrogen and progesterone receptors in uterine oviductal cytosols when compared to estrogen treatment alone. Estrogen withdrawal resembled estrogen plus progesterone administration in reducing both estrogen and progesterone receptor levels, although estrogen withdrawal plus progesterone administration resulted in a further reduction in both receptor concentrations. The same positive and negative relationships between estrogen and progesterone receptor content were observed in uterine cytosols from cycling and ovariectomized adults. These data suggest that estrogen and progesterone regulate their respective receptors and that tissue sensitivity to both steroids may be controlled by mechanisms involving fluctuations in receptor concentration in the reproductive tract of the beagle.
Mol Cell Endocrinol 1981 Feb
PMID:Hormonal regulation of cytoplasmic estrogen and progesterone receptors in the beagle uterus and oviduct. 721 1

Progestin(norethindrone and norethindrone acetate)-binding protein, exhibiting characteristics similar to uterine progesterone receptor, has been identified in human uterine cytosol. The progestin receptor was characterized by sedimentation coefficient, 4.2 S; Stokes radius, 39 A; frictional ratio, 1.29; isoelectric pH, 4.6; molecular radius, 2.7 nm; and molecular weight in the range 67 000--74 000. The ammonium-sulfate-precipitated progestin-receptor complex was eluted from a DEAE-cellulose column at 0.18 M KCl. The progestin binding was saturable and stereospecific. The sequential variation in receptor concentration (early proliferative, 3800--4300 sites/cell; late proliferative, 9500--11 200 sites/cell; early secretory, 4900--6200 sites/cell; late secretory, 1800--2300 sites/cell) was in conformity for progesterone and the progestins, when concurrently measured. Oral administration of norethindrone significantly reduced the cytoplasmic and nuclear receptor concentration for estradiol and progesterone. A significant observation was that the progestins stabilized the receptor by forming a slowly dissociating complex with a t 1/2 approximately 110--130 min as compared with the progesterone-receptor complex dissociating with t 1/2 approximately 41 min. Thus, the uterine progestin receptor recognizes progestins in general, although with a varying degree of affinity, and the altered rate constants could be of putative importance in determining the biological potency of the progestins.
Mol Cell Endocrinol 1980 Aug
PMID:Progestin receptors in human uterine cytosol. 740 3


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