| http://purl.uniprot.org/citations/16303757 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16303757 | http://www.w3.org/2000/01/rdf-schema#comment | "The aromatase gene encodes the key enzyme for estrogen formation. Aromatase enzyme inhibitors eliminate total body estrogen production and are highly effective therapeutics for postmenopausal breast cancer. A distal promoter (I.4) regulates low levels of aromatase expression in tumor-free breast adipose tissue. Two proximal promoters (I.3/II) strikingly induce in vivo aromatase expression in breast fibroblasts surrounding malignant cells. Treatment of breast fibroblasts with medium conditioned with malignant breast epithelial cells (MCM) or a surrogate hormonal mixture (dibutyryl (Bt2)cAMP plus phorbol diacetate (PDA)) induces promoters I.3/II. The mechanism of promoter-selective expression, however, is not clear. Here we reported that sodium butyrate profoundly decreased MCM- or Bt2cAMP + PDA-induced promoter I.3/II-specific aromatase mRNA. MCM, Bt2cAMP + PDA, or sodium butyrate regulated aromatase mRNA or activity only via promoters I.3/II but not promoters I.1 or I.4 in breast, ovarian, placental, and hepatic cells. Mechanistically, recruitment of phosphorylated ATF-2 by a CRE (-211/-199, promoter I.3/II) conferred inductions by MCM or Bt2cAMP + PDA. Chromatin immunoprecipitation-PCR and immunoprecipitation-immunoblotting assays indicated that MCM or Bt2cAMP + PDA stabilized a complex composed of phosphorylated ATF-2, C/EBPbeta, and cAMP-response element-binding protein (CREB)-binding protein in the common regulatory region of promoters I.3/II. Overall, histone acetylation patterns of promoters I.3/II did not correlate with sodium butyrate-dependent silencing of promoters I.3/II. Sodium butyrate, however, consistently disrupted the activating complex composed of phosphorylated ATF-2, C/EBPbeta, and CREB-binding protein. This was mediated, in part, by decreased ATF-2 phosphorylation. Together, these findings represent a novel mechanism of sodium butyrate action and provide evidence that aromatase activity can be ablated in a signaling pathway- and cell-specific fashion."xsd:string |
| http://purl.uniprot.org/citations/16303757 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m508498200"xsd:string |
| http://purl.uniprot.org/citations/16303757 | http://purl.uniprot.org/core/author | "Lin Z."xsd:string |
| http://purl.uniprot.org/citations/16303757 | http://purl.uniprot.org/core/author | "Zhou J."xsd:string |
| http://purl.uniprot.org/citations/16303757 | http://purl.uniprot.org/core/author | "Deb S."xsd:string |
| http://purl.uniprot.org/citations/16303757 | http://purl.uniprot.org/core/author | "Bulun S.E."xsd:string |
| http://purl.uniprot.org/citations/16303757 | http://purl.uniprot.org/core/author | "Yilmaz M.B."xsd:string |
| http://purl.uniprot.org/citations/16303757 | http://purl.uniprot.org/core/author | "Amin S.A."xsd:string |
| http://purl.uniprot.org/citations/16303757 | http://purl.uniprot.org/core/author | "Bertan Y.M."xsd:string |
| http://purl.uniprot.org/citations/16303757 | http://purl.uniprot.org/core/author | "Gonca I.A."xsd:string |
| http://purl.uniprot.org/citations/16303757 | http://purl.uniprot.org/core/author | "Imir A.G."xsd:string |
| http://purl.uniprot.org/citations/16303757 | http://purl.uniprot.org/core/author | "Jianfeng Z."xsd:string |
| http://purl.uniprot.org/citations/16303757 | http://purl.uniprot.org/core/author | "Zihong L."xsd:string |
| http://purl.uniprot.org/citations/16303757 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16303757 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/16303757 | http://purl.uniprot.org/core/pages | "2585-2597"xsd:string |
| http://purl.uniprot.org/citations/16303757 | http://purl.uniprot.org/core/title | "A novel role of sodium butyrate in the regulation of cancer-associated aromatase promoters I.3 and II by disrupting a transcriptional complex in breast adipose fibroblasts."xsd:string |
| http://purl.uniprot.org/citations/16303757 | http://purl.uniprot.org/core/volume | "281"xsd:string |
| http://purl.uniprot.org/citations/16303757 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16303757 |
| http://purl.uniprot.org/citations/16303757 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16303757 |
| http://purl.uniprot.org/uniprot/#_A8K6W3-mappedCitation-16303757 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/16303757 |
| http://purl.uniprot.org/uniprot/#_Q16449-mappedCitation-16303757 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/16303757 |
| http://purl.uniprot.org/uniprot/#_Q16481-mappedCitation-16303757 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/16303757 |
| http://purl.uniprot.org/uniprot/#_P11511-mappedCitation-16303757 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/16303757 |