| pubmed-article:8407937 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8407937 | lifeskim:mentions | umls-concept:C0052441 | lld:lifeskim |
| pubmed-article:8407937 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8407937 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
| pubmed-article:8407937 | lifeskim:mentions | umls-concept:C0043335 | lld:lifeskim |
| pubmed-article:8407937 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:8407937 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:8407937 | lifeskim:mentions | umls-concept:C0013879 | lld:lifeskim |
| pubmed-article:8407937 | pubmed:issue | 28 | lld:pubmed |
| pubmed-article:8407937 | pubmed:dateCreated | 1993-11-24 | lld:pubmed |
| pubmed-article:8407937 | pubmed:abstractText | Xenobiotic responsive element (XRE) is an inducible enhancer element that drives inducible expression of P-4501A1 gene in response to xenobiotic inducers. The XRE-binding factor appears in the nuclei of Hepa-1 cells treated with 3-methylcholanthrene (3-MC). Association of the Ah receptor and Arnt (Ah receptor nuclear translocator) in an XRE-binding complex was examined by anti-Ah receptor and Arnt antibodies. Both antibodies inhibited the sequence-specific XRE-binding activity of nuclear extracts from 3-MC-treated Hepa-1 cells and of the cytosolic fraction which was prepared from the nontreated cells and treated in vitro with 3-MC. These results indicate that Ah receptor and Arnt proteins are components of the XRE-binding factor and suggest that Arnt as well as the Ah receptor are localized in the cytosol of nontreated cells. The Ah receptor present in C4 cells, a mutant of Hepa-1 cells defective in the Arnt function, showed an inducer-dependent association with Arnt synthesized in an in vitro translation system. Co-transfection of the expression plasmids of the Ah receptor and Arnt exhibited synergistically more activated transcription from a reporter gene pMC6.3k consisting of the P-4501A1 gene promoter and enhancer than transfection with either of the two plasmids alone. These findings indicate that the Ah receptor and Arnt proteins form a complex that activates transcription in an inducer-dependent manner. | lld:pubmed |
| pubmed-article:8407937 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8407937 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8407937 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8407937 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:8407937 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8407937 | pubmed:author | pubmed-author:YoshidaAA | lld:pubmed |
| pubmed-article:8407937 | pubmed:author | pubmed-author:SogawaKK | lld:pubmed |
| pubmed-article:8407937 | pubmed:author | pubmed-author:FOGJJ | lld:pubmed |
| pubmed-article:8407937 | pubmed:author | pubmed-author:Fujii-Kuriyam... | lld:pubmed |
| pubmed-article:8407937 | pubmed:author | pubmed-author:MatsushitaNN | lld:pubmed |
| pubmed-article:8407937 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8407937 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:8407937 | pubmed:volume | 268 | lld:pubmed |
| pubmed-article:8407937 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8407937 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8407937 | pubmed:pagination | 21002-6 | lld:pubmed |
| pubmed-article:8407937 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:8407937 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8407937 | pubmed:articleTitle | A factor binding to the xenobiotic responsive element (XRE) of P-4501A1 gene consists of at least two helix-loop-helix proteins, Ah receptor and Arnt. | lld:pubmed |
| pubmed-article:8407937 | pubmed:affiliation | Department of Chemistry, Faculty of Science, Tohoku University, Sendai, Japan. | lld:pubmed |
| pubmed-article:8407937 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8407937 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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