17β-estradiol-stimulated eNOS gene transcriptional activation is regulated through the estrogen-responsive element in eNOS promoter

2007 ◽  
Vol 12 (4) ◽  
pp. 446-449 ◽  
Author(s):  
Jiho Min
Keyword(s):  
Transcriptional Activation ◽  
Enos Gene ◽  
Estrogen Responsive Element ◽  
17Β Estradiol ◽  
Responsive Element

scholarly journals Neuropeptide B mediates female sexual receptivity in medaka fish, acting in a female-specific but reversible manner

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Towako Hiraki-Kajiyama ◽  
Junpei Yamashita ◽  
Keiko Yokoyama ◽  
Yukiko Kikuchi ◽  
Mikoto Nakajo ◽  
...  
Keyword(s):  
Mating Behavior ◽  
Transcriptional Activation ◽  
Sex Steroid ◽  
Critical Element ◽  
Specific Expression ◽  
Behavioral Studies ◽  
Estrogen Responsive Element ◽  
Mating Behaviors ◽  
Responsive Element ◽  
Female Specific

Male and female animals display innate sex-specific mating behaviors. In teleost fish, altering the adult sex steroid milieu can effectively reverse sex-typical mating behaviors, suggesting remarkable sexual lability of their brains as adults. In the teleost medaka, neuropeptide B (NPB) is expressed female-specifically in the brain nuclei implicated in mating behavior. Here, we demonstrate that NPB is a direct mediator of estrogen action on female mating behavior, acting in a female-specific but reversible manner. Analysis of regulatory mechanisms revealed that the female-specific expression of NPB is dependent on direct transcriptional activation by estrogen via an estrogen-responsive element and is reversed in response to changes in the adult sex steroid milieu. Behavioral studies of NPB knockouts revealed that female-specific NBP mediates female receptivity to male courtship. The female-specific NPB signaling identified herein is presumably a critical element of the neural circuitry underlying sexual dimorphism and lability of mating behaviors in teleosts.

scholarly journals Neuropeptide B mediates female sexual receptivity in medaka fish, acting in a female-specific but reversible manner

2019 ◽  
Author(s):  
Towako Hiraki-Kajiyama ◽  
Junpei Yamashita ◽  
Keiko Yokoyama ◽  
Kohei Hosono ◽  
Yukika Kawabata-Sakata ◽  
...  
Keyword(s):  
Mating Behavior ◽  
Transcriptional Activation ◽  
Sex Steroid ◽  
Critical Element ◽  
Specific Expression ◽  
Behavioral Studies ◽  
Estrogen Responsive Element ◽  
Mating Behaviors ◽  
Responsive Element ◽  
Female Specific

AbstractMale and female animals display innate sex-specific mating behaviors. Among vertebrates, teleosts are unique in that altering the adult sex steroid milieu can reverse sex-typical mating behaviors, suggesting sexual lability of their brains. In the teleost medaka, neuropeptide B (NPB) is expressed female-specifically in the brain nuclei implicated in mating behavior. Here, we demonstrate that NPB is a direct mediator of estrogen action on female mating behavior, acting in a female-specific but reversible manner. Analysis of regulatory mechanisms revealed that the female-specific expression of NPB is dependent on direct transcriptional activation by estrogen via an estrogen-responsive element and is reversed in response to changes in the adult sex steroid milieu. Behavioral studies of NPB knockouts revealed that female-specific NBP mediates female receptivity to male courtship. The female-specific NPB signaling identified herein is presumably a critical element of the neural circuitry underlying sexual dimorphism and lability of mating behaviors in teleosts.

scholarly journals Estrogen Induces Selective Transcription of Caveolin1 Variants in Human Breast Cancer through Estrogen Responsive Element-Dependent Mechanisms

2020 ◽  
Vol 21 (17) ◽  
pp. 5989
Author(s):  
Antonella Romano ◽  
Antonia Feola ◽  
Antonio Porcellini ◽  
Vincenzo Gigantino ◽  
Maurizio Di Bonito ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Transcriptional Activation ◽  
Protein Isoforms ◽  
Regulatory Control ◽  
Physiological Processes ◽  
Regulatory Circuit ◽  
Estrogen Responsive Element ◽  
Histone H3 Methylation ◽  
Responsive Element ◽  
H3 Acetylation

The estrogen receptor (ER) signaling regulates numerous physiological processes mainly through activation of gene transcription (genomic pathways). Caveolin1 (CAV1) is a membrane-resident protein that behaves as platform to enable different signaling molecules and receptors for membrane-initiated pathways. CAV1 directly interacts with ERs and allows their localization on membrane with consequent activation of ER-non-genomic pathways. Loss of CAV1 function is a common feature of different types of cancers, including breast cancer. Two protein isoforms, CAV1α and CAV1β, derived from two alternative translation initiation sites, are commonly described for this gene. However, the exact transcriptional regulation underlying CAV1 expression pattern is poorly elucidated. In this study, we dissect the molecular mechanism involved in selective expression of CAV1β isoform, induced by estrogens and downregulated in breast cancer. Luciferase assays and Chromatin immunoprecipitation demonstrate that transcriptional activation is triggered by estrogen-responsive elements embedded in CAV1 intragenic regions and DNA-binding of estrogen-ER complexes. This regulatory control is dynamically established by local chromatin changes, as proved by the occurrence of histone H3 methylation/demethylation events and association of modifier proteins as well as modification of H3 acetylation status. Thus, we demonstrate for the first time, an estrogen-ERs-dependent regulatory circuit sustaining selective CAV1β expression.

scholarly journals 17β-Estradiol Inhibits Iron Hormone Hepcidin Through an Estrogen Responsive Element Half-Site

Endocrinology ◽  
2012 ◽  
Vol 153 (7) ◽  
pp. 3170-3178 ◽  
Author(s):  
Qing Yang ◽  
Jinlong Jian ◽  
Stuart Katz ◽  
Steven B. Abramson ◽  
Xi Huang
Keyword(s):  
Hepg2 Cells ◽  
Gene Knockout ◽  
Negative Regulator ◽  
Estrogen Responsive Element ◽  
Gene Knockout Mice ◽  
17Β Estradiol ◽  
Responsive Element ◽  
Hepcidin Gene ◽  
Hepcidin Mrna ◽  
Half Site

Interaction of estrogen with iron at the systemic level is long suspected, but direct evidence linking the two is limited. In the present study, we examined the effects of 17β-estradiol (E2) on hepcidin, a key negative regulator of iron absorption from the liver. We found that transcription of hepcidin was suppressed by E2 treatment in human liver HuH7 and HepG2 cells, and this down-regulation was blocked by E2 antagonist ICI 182780. Chromatin immunoprecipitation, deletion, and EMSA detected a functional estrogen responsive element half-site that is located between −2474 and −2462 upstream from the start of transcription of the hepcidin gene. After cloning the human hepcidin promoter into the pGL3Luc-Reporter vector, luciferase activity was also down-regulated by E2 treatment in HepG2 cells. E2 reduced hepcidin mRNA in wild-type mice as well as in hemochromatosis Fe gene knockout mice. In summary, our data suggest that hepcidin inhibition by E2 is to increase iron uptake, a mechanism to compensate iron loss during menstruation. This mechanism may also contribute to increased iron stores in oral contraceptive users.

scholarly journals Estrogenic Activities of Fatty Acids and a Sterol Isolated from Royal Jelly

2008 ◽  
Vol 5 (3) ◽  
pp. 295-302 ◽  
Author(s):  
Kazu-Michi Suzuki ◽  
Yoichiro Isohama ◽  
Hiroe Maruyama ◽  
Yayoi Yamada ◽  
Yukio Narita ◽  
...  
Keyword(s):  
Royal Jelly ◽  
Binding Assay ◽  
Estrogenic Activity ◽  
Luminal Epithelium ◽  
Concomitant Treatment ◽  
Decenoic Acid ◽  
Estrogen Responsive Element ◽  
17Β Estradiol ◽  
Responsive Element ◽  
Mcf 7

We have previously reported that royal jelly (RJ) from honeybees (Apis mellifera) has weak estrogenic activity mediated by interaction with estrogen receptors that leads to changes in gene expression and cell proliferation. In this study, we isolated four compounds from RJ that exhibit estrogenic activity as evaluated by a ligand-binding assay for the estrogen receptor (ER) β. These compounds were identified as 10-hydroxy-trans-2-decenoic acid, 10-hydroxydecanoic acid,trans-2-decenoic acid and 24-methylenecholesterol. All these compounds inhibited binding of 17β-estradiol to ERβ, although more weakly than diethylstilbestrol or phytoestrogens. However, these compounds had little or no effect on the binding of 17β-estradiol to ERα. Expression assays suggested that these compounds activated ER, as evidenced by enhanced transcription of a reporter gene containing an estrogen-responsive element. Treatment of MCF-7 cells with these compounds enhanced their proliferation, but concomitant treatment with tamoxifen blocked this effect. Exposure of immature rats to these compounds by subcutaneous injection induced mild hypertrophy of the luminal epithelium of the uterus, but was not associated with an increase in uterine weight. These findings provide evidence that these compounds contribute to the estrogenic effect of RJ.

scholarly journals Single-Chain Estrogen Receptors (ERs) Reveal that the ERα/β Heterodimer Emulates Functions of the ERα Dimer in Genomic Estrogen Signaling Pathways

2004 ◽  
Vol 24 (17) ◽  
pp. 7681-7694 ◽  
Author(s):  
Xiaodong Li ◽  
Jing Huang ◽  
Ping Yi ◽  
Robert A. Bambara ◽  
Russell Hilf ◽  
...  
Keyword(s):  
Signaling Pathways ◽  
Mammalian Cells ◽  
Target Genes ◽  
Estrogen Receptor Α ◽  
Estrogen Signaling ◽  
Single Chain ◽  
Estrogen Responsive Element ◽  
17Β Estradiol ◽  
Responsive Element

ABSTRACT The effects of estrogens, particularly 17β-estradiol (E2), are mediated by estrogen receptor α (ERα) and ERβ. Upon binding to E2, ERs homo- and heterodimerize when coexpressed. The ER dimer then regulates the transcription of target genes through estrogen responsive element (ERE)-dependent and -independent pathways that constitute genomic estrogen signaling. Although ERα and ERβ have similar ERE and E2 binding properties, they display different transregulatory capacities in both ERE-dependent and -independent signaling pathways. It is therefore likely that the heterodimerization provides novel functions to ERs by combining distinct properties of the contributing partners. The elucidation of the role of the ER heterodimer is critical for the understanding of physiology and pathophysiology of E2 signaling. However, differentially determining target gene responses during cosynthesis of ER subtypes is difficult, since dimers formed are a heterogeneous population of homo- and heterodimers. To circumvent the pivotal dimerization step in ER action and hence produce a homogeneous ER heterodimer population, we utilized a genetic fusion strategy. We joined the cDNAs of ERα and/or ERβ to produce single-chain ERs to simulate the ER homo- and heterodimers. The fusion ERs interacted with ERE and E2 in a manner similar to that observed with the ER dimers. The homofusion receptors mimicked the functions of the parent ER dimers in the ERE-dependent and -independent pathways in transfected mammalian cells, whereas heterofusion receptors emulated the transregulatory properties of the ERα dimer. These results suggest that ERα is the functionally dominant partner in the ERα/β heterodimer.

scholarly journals 17β-estradiol binding to ERα promotes the progression of prolactinoma through estrogen-response element-induced CaBP-9k up-regulation

2020 ◽  
Vol 40 (1) ◽  
Author(s):  
Jun Liu ◽  
Hao Han ◽  
Wenpeng Lu ◽  
Gaoyang Fan
Keyword(s):  
Cell Apoptosis ◽  
Cell Counting ◽  
Transcriptional Level ◽  
Calbindin D9k ◽  
Estrogen Response ◽  
Estrogen Responsive Element ◽  
Gene Reporter Assay ◽  
17Β Estradiol ◽  
Responsive Element ◽  
Luciferase Gene Reporter Assay

Abstract 17β-estradiol (E2) is considered to be an important instigator of prolactinoma, and can positively regulate the expression of calbindin-D9k (CaBP-9k) which contains an estrogen responsive element (ERE) via estrogen receptors (ERs). However, the detailed mechanism of E2 in promoting CaBP-9k expression and their roles in prolactinoma progression remain unclear. Here, we aimed to characterize it. The luciferase gene reporter assay with luc-ERE transfection showed that E2 treatment significantly enhanced the transcriptional level of CaBP-9k, whereas CaBP-9k activity was reduced when GH3 and MMQ cells were treated with AZD9496, an antagonist of ERα. E2 treatment increased the protein expressions of CaBP-9k and ERα but not ERβ, whereas this effect was also abolished when cells were treated with AZD9496. Besides, immunoprecipitation (IP) and immunofluorescence assays demonstrated that CaBP-9k could directly interact with ERα not ERβ, and Chromatin IP (ChIP) assay showed that ERα could bind to ERE of the CaBP-9k promoter. Moreover, cell counting kit-8 (CCK-8) and flow cytometry assays showed that E2 treatment significantly enhanced cell viability and inhibited cell apoptosis, but these effects were all abolished when ERα was down-regulated by short hairpin RNA (shRNA) or inhibited by AZD9496, as well as CaBP-9K suppression in both GH3 and MMQ cell lines. Taken together, these findings indicated that E2 stimulation promoted prolactin cell proliferation and inhibited cell apoptosis through ERα-induced CaBP-9k up-regulation, which then accelerated the advanced progression of prolactinoma.

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