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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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

The levels of nuclear progesterone and estradiol receptors have been followed during the development and decline of deciduomata induced in the uteri of ovariectomised rats. There were broadly 2 phases of deciduomal growth, the first phase being associated with high estrogen nuclear receptor levels per unit DNA. Progesterone nuclear receptor levels did not greatly change (in relation to DNA content) during both phases of full deciduomal development but peak levels were observed on day 5 after decidualization. Alkaline phosphatase activity was maximal by day 3, before peak hormone receptor levels were reached in the nuclei.
Mol Cell Endocrinol 1980 Nov
PMID:Nuclear progesterone and estradiol receptors in deciduomata induced in ovariectomised rats. 743 24

We have used reverse transcription followed by polymerase chain reaction amplification to investigate changes in expression of nerve growth factor (NGF) mRNA in immortalized hippocampal neurons after treatment with the glucocorticoids dexamethasone and corticosterone, the glucocorticoid antagonist RU38486, and the gonadal steroids progesterone and 17-beta oestradiol. We found that NGF mRNA levels rise after application of either dexamethasone or corticosterone, and that this rise is prevented by the antagonist. Thus, neurotrophin expression is modulated by the physiological glucocorticoid and is mediated by type II glucocorticoid receptors. Progesterone has no effect, while 17-beta oestradiol suppresses NGF mRNA in a postnatally-derived cell line but does not change levels in an embryonic line. An increase in neurotrophin expression is therefore not a general response to steroid hormone application, and may be a specific defence against the presence of metabolically endangering glucocorticoids.
Brain Res Mol Brain Res 1995 Jul
PMID:Neurotrophin expression modulated by glucocorticoids and oestrogen in immortalized hippocampal neurons. 747 24

The ability of ovarian steroids to regulate the excitability of hippocampal neurons may be mediated by alterations in the inhibitory activity of GABA. We assessed the ability of estradiol, progesterone, and 3 alpha-OH-5 alpha-pregnan-20-one (3 alpha-OH-DHP; a metabolite of progesterone) to regulate gene expression of selected GABAA receptor subunits (alpha 1, alpha 2, beta 1, beta 2, and gamma 2). Using in situ hybridization, we found that progesterone, or 3 alpha-OH-DHP, suppressed mRNA levels for the alpha 1 subunit in the CA2, CA3, and the dentate gyrus subfields of the hippocampus in animals that were pretreated with estradiol. Progesterone had a more limited effect on the alpha 2 subunit, suppressing mRNA levels in estradiol-primed animals only in the CA3 region. In contrast, progesterone increased mRNA levels for the gamma 2 subunit in the CA1, CA2, and CA3 regions of the hippocampus, but only in animals that were not estradiol-primed. Estradiol alone had no significant effect on the expression of any subunit examined. Beta 1 and beta 2 subunit mRNA levels were not altered by any of the hormones tested. These data support the conclusion that progesterone and its metabolites may regulate excitability of the hippocampus by modulating the GABAA receptor gene expression; these effects of progesterone are dependent upon the circulating levels of estradiol. Alterations in the gene expression of selective subunits may lead to changes in the density of GABAA receptor protein or to changes in receptor subunit composition which might alter receptor sensitivity to activation by GABA or modulators such as the benzodiazepines and convulsants.
Brain Res Mol Brain Res 1995 Sep
PMID:Specific subunit mRNAs of the GABAA receptor are regulated by progesterone in subfields of the hippocampus. 750 Aug 38

Yeast cells can respond and adapt to osmotic stress. In our attempt to clarify the molecular mechanisms of cellular responses to osmotic stress, we cloned seven cDNAs for hyperosmolarity-responsive (HOR) genes from Saccharomyces cerevisiae by a differential screening method. Structural analysis of the clones revealed that those designated HOR1, HOR3, HOR4, HOR5 and HOR6 encoded glycerol-3-phosphate dehydrogenase (Gpd1p), glucokinase (Glk1p), hexose transporter (Hxt1p), heat-shock protein 12 (Hsp12p) and Na+, K+, Li(+)-ATPase (Ena1p), respectively. HOR2 and HOR7 corresponded to novel genes. Gpd1p is a key enzyme in the synthesis of glycerol, which is a major osmoprotectant in S. cerevisiae. Cloning of HOR1/GPD1 as a HOR gene indicates that the accumulation of glycerol in yeast cells under hyperosmotic stress is, at least in part, caused by an increase in the level of GPDH protein. We performed a series of Northern blot analyses using HOR cDNAs as probes and RNAs prepared from cells grown under various conditions and from various mutant cells. The results suggested that all the HOR genes are regulated by common signal transduction pathways. However, the fact that they exhibited certain distinct responses indicated that they might also be regulated by specific pathways in addition to the common pathways. Ca2+ seemed to be involved in the signaling systems. In addition, Hog1p, one of the MAP kinases in yeast, appeared to be involved in the regulation of expression of HOR genes, although its function seemed to be insufficient for the overall regulation of expression of these genes.
Mol Gen Genet 1995 Nov 15
PMID:Cloning and characterization of seven cDNAs for hyperosmolarity-responsive (HOR) genes of Saccharomyces cerevisiae. 750 Sep 33

The present study tested the hypothesis that hydrogen peroxide (H2O2) inhibits low-density lipoprotein (LDL) uptake and LDL-supported steroidogenesis by luteal cells. LDL uptake: dispersed porcine luteal cells from mid-cycle (days 6-11, estrus = day 0) were incubated for 0-120 min at 37 degrees C in F-10 medium + 0.1% BSA containing various concentrations of H2O2 (0-1000 microM). Cells were washed with catalase (2800 U/ml), and then with fresh medium. Cell viability based on trypan blue exclusion was unaltered by H2O2 exposure through 60 min. H2O2-exposed cells were incubated with fluorescent-tagged-LDL (Dil-LDL; 1 microgram/ml) for 10 min at 37 degrees C. Fluorescence of small (SLC) and large (LLC) luteal cells was analyzed by flow cytometry (n = 6 experiments). H2O2 (> or = 10 microM) caused a progressive reduction (P < 0.01) in mean fluorescence intensity (MFI) of SLC and LLC indicative of up to a 30-35% decline in LDL uptake. Progesterone (P) production: dispersed luteal cells (4 x 10(4)/0.2 ml) were pre-cultured in DMEM/F-12 medium overnight (approximately 18 h) in 96-well culture plates. Wells were rinsed and fresh media (0.2 ml) containing H2O2 (0-500 microM) was added. After 30 min, the following treatments were added: human(h)LDL (0 or 50 micrograms/ml), human chorionic gonadotropin (hCG; 0 or 100 ng/ml), hCG + LDL, or 22R-hydroxycholesterol (22[OH]-C; 0 or 25 micrograms/ml). Cells were incubated for an additional 4 h, and P concentrations in final media samples were measured by RIA.(ABSTRACT TRUNCATED AT 250 WORDS)
Mol Cell Endocrinol 1995 Jun
PMID:Hydrogen peroxide suppresses low-density lipoprotein (LDL) uptake and LDL-supported steroidogenesis by porcine luteal cells. 755 84

The protein kinase domains of mouse A-Raf and B-Raf were expressed as fusion proteins with the hormone binding domain of the human estrogen receptor in mammalian cells. In the absence of estradiol, 3T3 and rat1a cells expressing delta A-Raf:ER and delta B-Raf:ER were nontransformed, but upon the addition of estradiol the cells became oncogenically transformed. Morphological oncogenic transformation was more rapid and distinctive in cells expressing delta B-Raf:ER compared with cells expressing delta A-Raf:ER. Biochemical analysis of cells transformed by delta A-Raf:ER and delta B-Raf:ER revealed several interesting differences. The activation of delta B-Raf:ER consistently led to the rapid and robust activation of both MEK and p42/p44 MAP kinases. By contrast, the activation of delta A-Raf:ER led to a weak activation of MEK and the p42/p44 MAP kinases. The extent of activation of MEK in cells correlated with the ability of the different Raf kinases to phosphorylate and activate MEK1 in vitro. delta B-Raf:ER phosphorylated MEK1 approximately 10 times more efficiently than delta Raf-1:ER and at least 500 times more efficiently than delta A-Raf:ER under the conditions of the immune-complex kinase assays. These results were confirmed with epitope-tagged versions of the Raf kinase domains expressed in insect cells. The activation of all three delta Raf:ER proteins in 3T3 cells led to the hyperphosphorylation of the resident p74raf-1 and mSOS1 proteins, suggesting the possibility of "cross-talk" between the different Raf kinases and feedback regulation of intracellular signaling pathways. The activation of either delta B-Raf:ER or delta Raf-1:ER in quiescent 3T3 cells was insufficient to promote the entry of the cells into DNA synthesis. By contrast, the activation of delta A-Raf:ER in quiescent 3T3 cells was sufficient to promote the entry of the cells into S phase after prolonged exposure to beta-estradiol. The delta Raf:ER system has allowed us to reveal significant differences between the biological and biochemical properties of oncogenic forms of the Raf family of protein kinases. We anticipate that cells expressing these proteins and other estradiol-regulated protein kinases will be useful tools in future attempts to unravel the complex web of interactions involved in intracellular signal transduction pathways.
Mol Cell Biol 1995 Nov
PMID:Conditionally oncogenic forms of the A-Raf and B-Raf protein kinases display different biological and biochemical properties in NIH 3T3 cells. 756 95

Endometrial fibroblasts derived from uterine endometrium as controls and endometrial cancer cells (Ishikawa and HHUA cells) were used to analyze the manner of induction of c-Ha-ras transcripts in endometrial cancers, some of which are estrogen-dependent in growth. Estrogen increased c-Ha-ras expression and tyrosine kinase (TK) activity in fibroblast and Ishikawa cells, but not in HHUA cells. Progesterone diminished c-Ha-ras expression and tyrosine kinase (TK) activity induced by estradiol in the fibroblasts, but not in Ishikawa cells, which persistently overexpressed c-Ha-ras. In these cells, epidermal growth factor (EGF) increased c-Ha-ras expression as did estradiol. Pretreatment with tyrphostin, an inhibitor of TK, abolished estrogen-inducible overexpression of c-Ha-ras. The combination of both estradiol and EGF at maximum effective concentration exerted no additive or synergistic effect on induction of c-Ha-ras expression. In conclusion, persistent activation of TK might lead to overexpression of c-Ha-ras in some endometrial cancer cells under estrogen predominant milieu, which might be associated with the transformation or growth potential.
J Steroid Biochem Mol Biol 1995 Oct
PMID:Estrogen induces c-Ha-ras expression via activation of tyrosine kinase in uterine endometrial fibroblasts and cancer cells. 757 18


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