Cloning of the human oestrogen receptor cDNA

Green, Stephen; Walter, P.; Greene, Geoffrey L.; Krust, Andrée; Goffin, Colette; Jensen, Elwood V.; Scrace, Geoffrey T.; Waterfield, Mike; Chambon, Pierre

doi:10.1016/0022-4731(86)90035-x

Cited by 258 publications

(148 citation statements)

References 21 publications

Supporting

Mentioning

143

Contrasting

Unclassified

Order By: Relevance

“…Two ERs have been identified: α and β, which are distinct proteins encoded by separate genes located on different chromosomes. ERα consists of 595 amino acid residues with a molecular mass of 66 kDa [33], while ERβ consists of 485 amino acid residues with a molecular mass of 54 kDa [34], both of which have shown high homology of the amino acid sequence. Braidman et al reported that ERα among these receptors was expressed in human osteoblasts, and resultant ERα protein was detected in osteocytes, indicating that ER is a major receptor in osteocytes [35].…”

Section: Introductionmentioning

confidence: 99%

Immunolocalization of sclerostin synthesized by osteocytes in relation to bone remodeling in the interradicular septa of ovariectomized rats

Guo

Liu

et al. 2012

Journal of Electron Microscopy

View full text Add to dashboard Cite

This study aimed to elucidate whether estrogen deficiency would affect the synthesis of an osteocyte-derived factor, sclerostin, in the mesial region of alveolar bone. Eight 9-week-old Wister female rats were ovariectomized (OVX), and the other eight rats were Sham-operated (Sham). After 4 weeks, the interradicular septa of mandibular first molar were embedded in paraffin, and then, were histochemically examined. Sclerostin-positive osteocytes were located in a superficial layer of the mesial region of Sham bone, while the OVX mesial region showed a lesser presence of the sclerostin-reactive osteocytes. There was no significant difference in the distribution of estrogen receptor  and TUNEL-positive cells in either Sham or OVX groups. Meanwhile, the Sham mesial region demonstrated many osteoclasts, but the OVX specimens showed numerous osteoclasts in association with intense immunolabeling of the receptor activator of the nuclear factor kB ligand. Complex meshwork of cement lines was seen consistent with irregularly-distributed osteocytic lacunar-canalicular system in the OVX mesial region, compared with those of the Sham specimens. In conclusion, estrogen deficiency appears to inhibit osteocytes for sclerostin synthesis in the mesial region of the interradicular septum, mediated by accelerated bone remodeling, rather than by directly effecting osteocytes. words

show abstract

Section: Introductionmentioning

confidence: 99%

Immunolocalization of sclerostin synthesized by osteocytes in relation to bone remodeling in the interradicular septa of ovariectomized rats

Guo

Liu

et al. 2012

Journal of Electron Microscopy

View full text Add to dashboard Cite

show abstract

“…The vectors encoding the wild-type eNOS and mutant eNOS of serine 1179 to alanine (S1179A eNOS) was a kind gift from Dr. W. C. Sessa (Yale University, New Haven, CT) (31). The human estrogen receptor ␣ (ER␣) expression vector, pSG5-HEGO, was a kind gift from Dr. P. Chambon (Institut de Chimie Biologique, Strasbourg, France) (48). The plasmid pSG5-mER␤ encoding nucleotides 12-1469 of ER␤ (35) was kindly provided Dr. E. R. Levin (University of California, Irvine, CA) via Dr. K. S. Korach (National Institutes of Health, Research Triangle Park, NC).…”

Section: Methodsmentioning

confidence: 99%

Estrogen Induces the Akt-dependent Activation of Endothelial Nitric-oxide Synthase in Vascular Endothelial Cells

Hisamoto¹,

Ohmichi²,

Kurachi³

et al. 2001

Journal of Biological Chemistry

350

249

View full text Add to dashboard Cite

Although estrogen is known to activate endothelial nitric oxide synthase (eNOS) in the vascular endothelium, the molecular mechanism responsible for this effect remains to be elucidated. In studies of both human umbilical vein endothelial cells ( The inhibitory effect of estrogen on the development of atherosclerosis has been suggested by abundant human epidemiological and animal experimental data (1-9). The incidence of atherosclerotic diseases is lower in premenopausal women than in men, steeply rises in postmenopausal women, and is reduced to premenopausal levels in postmenopausal women who receive estrogen therapy (10 -12). Until recently, the atheroprotective effects of estrogen were attributed principally to the effects on serum lipid concentrations. However, estrogeninduced alterations in serum lipids account for only approximately one-third of the observed clinical benefits of estrogen (12)(13)(14). Recent evidence suggests that the direct actions of estrogen on blood vessels contribute to the cardioprotective effects of estrogen (13, 15). There are many kinds of direct effects of estrogen on blood vessels, such as estrogen-induced increases of vasodilatation and inhibition of the response of blood vessels to injury and the development of atherosclerosis. However, the molecular mechanism underlying the estrogeninduced vasodilatation has not yet been determined. Several studies suggest that a key mediator of this vasodilator response could be the endothelium-derived relaxing factor nitric oxide (NO), and that brief treatment with estrogen increases basal NO release in endothelial cells without elevation of eNOS mRNA or protein (16). Estrogen activates endothelial nitric oxide synthase (eNOS) without altering expression of the eNOS gene in vascular endothelium (17)(18)(19)(20). However, the details of the mechanism of the estrogen-induced eNOS activation are not yet well understood.The serine/threonine kinase termed Akt or protein kinase B (PKB) 1 is an important regulator of various cellular processes, including glucose metabolism and cell survival (21, 22). Activation of receptor tyrosine kinases and G-protein-coupled receptors, and stimulation of cells by mechanical force, can lead to the phosphorylation and activation of . Akt was identified as a downstream component of survival signaling through phosphatidylinositol 3-kinase (PI3K) (26 -30). Akt may be regulated by both phosphorylation and the direct binding of PI3K lipid products to the Akt pleckstrin homology domain. Akt can then phosphorylate substrates such as glycogen synthase kinase-3, 6-phosphofructo-2-kinase, and BAD. More recently, it was found that eNOS is also an Akt substrate and is activated by Akt-dependent phosphorylation to release NO in endothelial cells (31-34).The actions of estrogen can be mediated by the classical nuclear receptors, ER␣ and ER␤ (35,36) or through other putative membrane receptors. By definition, rapid effects of estrogen that involve nongenomic mechanisms are independent of transcriptional activation by the nuclea...

show abstract

“…Studies suggest that changes in follicular or periovulatory estradiol secretion may be critical to the onset of symptoms of PMS [9,10] . It has been widely accepted that the action of E 2 is mediated by the nuclear estrogen receptors (ER), ERα and ERβ [11,12] , which function as ligand-dependent transcription factors and regulate the transcription of target genes. ERα plays the major role in estrogen responsiveness in the female rat pituitary [13] due it having a higher affinity to estrogen than ERβ does.…”

Section: Introductionmentioning

confidence: 99%

Casticin, a flavonoid isolated from Vitex rotundifolia, inhibits prolactin release in vivo and in vitro

Zhang

Zheng

et al. 2010

Acta Pharmacol Sin

View full text Add to dashboard Cite

Aim: To investigate the anti-hyperprolactinemia activity of casticin, a flavonoid isolated from Vitex rotundifolia, and elucidate its molecular mechanism. Methods: Hyperprolactinemia (MIHP) was induced by administration of metoclopramide dihydrochloride (50 mg/kg, tid, ip, for 10 d) in SD rats and the primary pituitary cells were prepared from the pituitary glands of the SD rats. Prolactin concentrations were measured using a radioimmunoassay. Cell viability was measured using an MTT assay. The mRNA expression of estrogen receptor alpha and beta in rat pituitary cells was measured using semi-quantitative RT-PCR analysis. Results: The level of serum prolactin in the MIHP model group was 2.1 fold higher than that in the untreated control group (P<0.01). Casticin (10, 20, and 40 mg/kg, ip, for 7 d) reduced serum prolactin levels by 33.9%, 54.3%, and 64.7%, respectively (P<0.01). The positive control drug bromocriptine 1 mg/kg decreased the serum prolactin concentration in MIHP rats by 44.9%. 17β-Estradiol (E2) significantly increased the proliferation of pituitary cells and casticin (1 and 10 μmol/L) markedly inhibited E2-induced pituitary cell proliferation by 27.7% and 42.1%, respectively. Stimulation of pituitary cells with E2 increased prolactin secretion into the cell culture supernatants, and casticin (0.1, 1, and 10 μmol/L) significantly inhibited the prolactin release stimulated by E2 in a concentration-dependent manner. Casticin (1 and 10 μmol/L) significantly inhibited ERα mRNA expression in pituitary cells stimulated with E2 (P<0.01) but increased ERβ mRNA expression at a concentration of 10 μmol/L (P<0.01). However, casticin had no effects on proliferation and prolectin release of the unstimulated primary pituitary cells in vitro. Conclusion: Casticin inhibited the release of prolactin from pituitary cells of SD rats stimulated with E2 in vivo and in vitro. These effects might be related with inhibiting the ERα mRNA expression and increasing the ERβ mRNA expression.

show abstract

Cloning of the human oestrogen receptor cDNA

Cited by 258 publications

References 21 publications

Immunolocalization of sclerostin synthesized by osteocytes in relation to bone remodeling in the interradicular septa of ovariectomized rats

Immunolocalization of sclerostin synthesized by osteocytes in relation to bone remodeling in the interradicular septa of ovariectomized rats

Estrogen Induces the Akt-dependent Activation of Endothelial Nitric-oxide Synthase in Vascular Endothelial Cells

Casticin, a flavonoid isolated from Vitex rotundifolia, inhibits prolactin release in vivo and in vitro

Contact Info

Product

Resources

About