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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
34
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pubmed:dateCreated |
1995-9-28
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pubmed:abstractText |
We have previously demonstrated that an everted repeat of the hexamer PuGGTCA located within the gamma F-crystallin promoter mediates activation of the murine gamma F-crystallin gene by retinoic acid and thyroid hormone receptors. Here, we show that the recently identified retinoic acid receptor-related orphan nuclear receptor (ROR alpha) is expressed in the murine lens and activates the gamma F-crystallin promoter. In contrast to the retinoic acid and thyroid hormone receptors, activation of the gamma F-crystallin promoter by ROR alpha requires binding to the single 3' half-site and spacer sequences of gamma F-crystallin hormone response element (gamma F-HRE). We further demonstrate that ROR alpha-dependent activation is repressed by the competitive binding of retinoic acid receptor/retinoid X receptor heterodimers to the gamma F-HRE in the absence of all-trans-retinoic acid. These studies suggest that the interplay of retinoid receptors and ROR alpha on the gamma F-HRE may constitute an important mechanism regulating gamma F-crystallin gene expression in the murine lens.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Crystallins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Ribosomal,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Retinoic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Retinoid X Receptors,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
20156-61
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:7650034-Animals,
pubmed-meshheading:7650034-Base Sequence,
pubmed-meshheading:7650034-Binding, Competitive,
pubmed-meshheading:7650034-Binding Sites,
pubmed-meshheading:7650034-Crystallins,
pubmed-meshheading:7650034-DNA, Ribosomal,
pubmed-meshheading:7650034-DNA Primers,
pubmed-meshheading:7650034-Gene Expression Regulation,
pubmed-meshheading:7650034-Lens, Crystalline,
pubmed-meshheading:7650034-Mice,
pubmed-meshheading:7650034-Molecular Sequence Data,
pubmed-meshheading:7650034-Promoter Regions, Genetic,
pubmed-meshheading:7650034-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:7650034-Receptors, Retinoic Acid,
pubmed-meshheading:7650034-Retinoid X Receptors,
pubmed-meshheading:7650034-Transcription Factors
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pubmed:year |
1995
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pubmed:articleTitle |
Functional interactions between retinoic acid receptor-related orphan nuclear receptor (ROR alpha) and the retinoic acid receptors in the regulation of the gamma F-crystallin promoter.
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pubmed:affiliation |
Royal Victoria Hospital, Department of Biochemistry, McGill University, Montréal, Québec, Canada.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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