Delineation of sites mediating estrogen regulation of the rat creatine kinase B gene.

Wu-Peng, X. Sharon; Pugliese, Thomas; Dickerman, Herbert W.; Pentecost, Brian T.

doi:10.1210/mend.6.2.1569966

Cited by 32 publications

(33 citation statements)

References 25 publications

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“…Results of previous studies suggest that formation of ERSp1 complexes regulates E2-induced transactivation of the cmyc, creatine kinase B, and cathepsin D genes (18,41,84). An ER-Sp1 complex, GGGCGGn 23 ACGGG, was previously identified (Ϫ199 to Ϫ165) in the cathepsin D promoter (41), and further analysis of this sequence has identified an XRE, namely FIG.…”

Section: Discussionmentioning

confidence: 96%

Molecular Mechanism of Inhibition of Estrogen-Induced Cathepsin D Gene Expression by 2,3,7,8-Tetrachlorodibenzo-p-Dioxin (TCDD) in MCF-7 Cells

Krishnan

Porter

Santostefano

et al. 1995

Molecular and Cellular Biology

190

121

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17␤-Estradiol (E2) induces cathepsinThe aryl hydrocarbon (Ah) receptor protein is expressed in laboratory animals and humans and in mammalian cells in culture (54,65). Although the endogenous ligand(s) for this receptor has not been identified, several different classes of compounds reversibly bind the Ah receptor, and these include the polynuclear and polyhalogenated aromatic hydrocarbons (42,54,57,59,65,67). 3-Methylcholanthrene and 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) are prototypical aromatic hydrocarbons which exhibit high-affinity binding (K d Յ 1 nM) for the Ah receptor (44, 58) and have been utilized for characterizing Ah receptor-mediated responses.TCDD induces a broad spectrum of biochemical and toxic responses including a wasting syndrome, immune suppression, hepatotoxicity, developmental and reproductive toxicity, carcinogenicity, dermal toxicity, alteration of endocrine response pathways, and modulation of diverse enzyme activities (26,29,59,73,82). The induction of CYP1A1 gene expression by TCDD and 3-methylcholanthrene has been extensively investigated, and the results indicate that the Ah receptor acts as a nuclear ligand-induced transcription factor (13,29,73,82).After treatment of animals or cells with TCDD, there is a rapid formation of a heterodimeric nuclear Ah receptor complex (19) which consists of the ligand-binding protein (7) and the Ah receptor nuclear translocator (Arnt) protein (31). The unbound Ah receptor is associated with heat shock protein 90 (48,55,60,61), and the subcellular distribution of these proteins in the absence of ligand is currently being investigated (60, 61). The nuclear Ah receptor complex interacts with cognate genomic sequences (dioxin or xenobiotic responsive elements [DREs and XREs, respectively]) in the 5Ј-promoter region of the CYP1A1 gene and transactivates CYP1A1 gene expression (15-17, 27, 34, 70, 83). There is evidence that this transactivation process is comparable for induction of CYP1A1 gene expression and induction of the expression of other members of the Ah gene battery, namely CYP1A2, glucuronosyl transferase, aldehyde-3-dehydrogenase, glutathione S-transferase Ya gene, and NAD(P)H:menadione oxidoreductase (1,35,53,56,62,64). Other studies also report that enhanced expression of other genes by TCDD is due to posttranscriptional processes (20).TCDD also decreases gene expression and/or the respective activities of the encoded proteins. Phosphoenolpyruvate carboxy kinase, glucose-6-phosphatase, and tryptophan 2,3-dioxygenase activities and mRNA levels are decreased in rats treated with an acutely toxic dose (125 g/kg of body weight) of TCDD (72). Rat uterine c-fos and epidermal growth factor * Corresponding author. Mailing address: Department of Veterinary Physiology and Pharmacology, Texas A&M University, College Station, TX 77843-4466.

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Section: Discussionmentioning

confidence: 96%

Molecular Mechanism of Inhibition of Estrogen-Induced Cathepsin D Gene Expression by 2,3,7,8-Tetrachlorodibenzo-p-Dioxin (TCDD) in MCF-7 Cells

Krishnan

Porter

Santostefano

et al. 1995

Molecular and Cellular Biology

190

121

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“…This finding acquired relevance when we became aware of how the functional synergism between Sp1 and ER , through the formation of the ER /Sp1 complex, was responsible of the activation of other E 2 -responsive genes. For instance, in the promoter region of such genes the half palindromic ERE sequence and Sp1 were separated by a number of nucleotides ranging from 10 to 23 nt, such as cyclin D1, bcl2, retinoic acid receptor 1, IGF-binding protein 4, adenosine deaminase, DNA polymerase , c-fos, cathepsin D, transcription factor-E2F1, creatine kinase B, human progesterone receptor A promoter and, recently, cad gene (Dubik & Shiu 1992, Wu-Peng et al 1992, Krishnan et al 1994, Rishi et al 1995, Porter et al 1996, Scholz et al 1998, Wang et al 1998, Petz & Nardulli 2000, Salvatori et al 2000, Saville et al 2000, Tanaka et al 2000, Vyhlidal et al 2000, Li et al 2001, Khan et al 2003.…”

Section: Discussionmentioning

confidence: 99%

“…Both electrophoretic mobility shift assay (EMSA) and chromatin immunoprecipitation (ChIP) assay confirmed that the above-mentioned sequence is functionally involved in mediating the up-regulatory effect induced by E 2 on IRS-1 expression. The effect, as documented for other E 2 -responsive genes, occurs through the interaction between ER and Sp1 proteins, bound separately to the ERE half sequence and Sp1 responsive element respectively and present in the ERE/Sp1 region of the IRS-1 promoter (Dubik & Shiu 1992, Wu-Peng et al 1992, Krishnan et al 1994, Rishi et al 1995, Porter et al 1996, Scholz et al 1998, Petz & Nardulli 2000, Saville et al 2000, Khan et al 2003.…”

Section: Introductionmentioning

confidence: 97%

Evidence that the mouse insulin receptor substrate-1 belongs to the gene family on which the promoter is activated by estrogen receptor α through its interaction with Sp1

Panno¹,

Mauro²,

Marsico³

et al. 2006

Journal of Molecular Endocrinology

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In the present study, the molecular mechanism underlying the up-regulatory effect of estradiol (E 2 ) on mouse insulin receptor substrate-1 (IRS-1) promoter was investigated in CHO cells on which the same promoter had first been functionally characterized. The mouse IRS-1 promoter bears four consensus half Estrogen Responsive Elements (ERE) sequences and thirteen AP-1-and ten Sp1-binding elements. We performed molecular dissection of this promoter gene providing 38 different deleted constructs, containing the same AP-1 rich region with a progressively increased number of ERE half sites located downstream. None of these constructs was responsive to E 2 , while a downstream region (nt -1420 to -160) rich in GC elements was induced by E 2 . However, the latter region lost its intrinsic E 2 responsiveness when the whole IRS-1 promoter was mutated for deletion in all four ERE half sites. Deletion analysis of the ERE half sites demonstrated that only ERE located at the position -1500 to -1495, close to the GC-rich region, was able to maintain the induced activatory effect of E 2 on the IRS-1 gene. Electrophoretic mobility shift and chromatin immunoprecipitation assays identified the region containing the half ERE/Sp1 (nt -1500 to -1477) as the one conferring E 2 responsiveness to the whole promoter. This effect occurs through the functional interaction between E 2 /ER and Sp1.

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“…However, among them, only a small number have been shown to possess functional EREs within the transcription regulatory region. In mammals, these genes include transcription factors, such as JUN [32] , FOS [33] , PGR [34] , and TP53 [35] , intracellular signaling molecules, such as HRAS [36] , BCL2 [37] , and BRCA1 [38] , enzymes, such as CHAT [39] , NQO1 [40] , and CKB [41] , secreted proteins, such as LTF [42] , SCGB1A1 [43] , OVGP1 [44] , C3 [45] , and AGT [46] , hormones, such as LHB [47] , OXT [48] , PRL [49] , and AVP [50] , membrane proteins, such as SNAT2 [51] and VEGFA [52] , the motogen TFF1 [53] , and the protease CTSD [54] . These genes are assumed to directly mediate various estrogen actions in normal tissues, as well as in cancer and other diseases.…”

Section: Steroid Hormone Target Genes and The Transcription Cascadementioning

confidence: 99%

Identification of estrogen-responsive genes based on the DNA binding properties of estrogen receptors using high-throughput sequencing technology

2014

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Estrogens are important endocrine hormones that control physiological functions in reproductive organs, and play a pivotal role in the generation and progression of breast cancer. Therapeutic drugs including anti-estrogen and aromatase inhibitors are used to treat patients with breast cancer. The estrogen receptors, ERα and ERβ, function as hormone-dependent transcription factors that directly regulate the expression of their target genes. Therefore, a better understanding of the function and regulation of estrogen-responsive genes provides insight into the gene regulation network associated with breast cancer. Recent technological developments in highthroughput sequencing have enabled the genome-wide identification of estrogen-responsive genes. Further elucidating the estrogen gene cascade is critical for advancements in the diagnosis and treatment of breast cancer.

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Delineation of sites mediating estrogen regulation of the rat creatine kinase B gene.

Cited by 32 publications

References 25 publications

Molecular Mechanism of Inhibition of Estrogen-Induced Cathepsin D Gene Expression by 2,3,7,8-Tetrachlorodibenzo-p-Dioxin (TCDD) in MCF-7 Cells

Molecular Mechanism of Inhibition of Estrogen-Induced Cathepsin D Gene Expression by 2,3,7,8-Tetrachlorodibenzo-p-Dioxin (TCDD) in MCF-7 Cells

Evidence that the mouse insulin receptor substrate-1 belongs to the gene family on which the promoter is activated by estrogen receptor α through its interaction with Sp1

Identification of estrogen-responsive genes based on the DNA binding properties of estrogen receptors using high-throughput sequencing technology

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