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rdf:type |
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lifeskim:mentions |
umls-concept:C0012591,
umls-concept:C0020792,
umls-concept:C0034987,
umls-concept:C0040135,
umls-concept:C0086418,
umls-concept:C0242299,
umls-concept:C0597357,
umls-concept:C1332838,
umls-concept:C1417830,
umls-concept:C1446409,
umls-concept:C1709060
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pubmed:issue |
18
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pubmed:dateCreated |
1997-6-2
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pubmed:abstractText |
While the TR4 orphan receptor (TR4) is able to repress the expression of its target genes via its interaction with the direct repeat 1-hormone response element (DR1-HRE) and DR2-HRE, we now report that TR4 can also induce the transcriptional activity of the reporter gene containing a DR4-HRE via chloramphenicol acetyltransferase assay. Electrophoretic mobility shift assay and Scatchard analysis reveal a strong binding affinity (dissociation constant = 2 nM) between TR4 and DR4-HRE. The induction mediated by TR4 was detected not only in the synthetic DR4-HRE but also in some genes, such as rat alpha-myosin heavy-chain and S14 genes, containing the DR4 or DR4-like motif, which have been suggested to be the response elements for a thyroid hormone receptor. Our data also demonstrate this TR4-mediated gene induction is TR4 dose- and DR4 sequence-dependent. Together, our data suggest that DR4-HRE can be a positive regulatory element for TR4, which may be able to induce the transcriptional activity of the genes containing such positive HREs.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin Heavy Chains,
http://linkedlifedata.com/resource/pubmed/chemical/NR2C2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Steroid,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Thyroid Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tr4 protein, rat
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12215-20
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9115296-Animals,
pubmed-meshheading:9115296-Base Sequence,
pubmed-meshheading:9115296-Binding Sites,
pubmed-meshheading:9115296-DNA-Binding Proteins,
pubmed-meshheading:9115296-Genes, Reporter,
pubmed-meshheading:9115296-HIV Long Terminal Repeat,
pubmed-meshheading:9115296-Humans,
pubmed-meshheading:9115296-Kinetics,
pubmed-meshheading:9115296-Mutagenesis, Site-Directed,
pubmed-meshheading:9115296-Myosin Heavy Chains,
pubmed-meshheading:9115296-Nerve Tissue Proteins,
pubmed-meshheading:9115296-Protein Biosynthesis,
pubmed-meshheading:9115296-Rats,
pubmed-meshheading:9115296-Receptors, Steroid,
pubmed-meshheading:9115296-Receptors, Thyroid Hormone,
pubmed-meshheading:9115296-Recombinant Fusion Proteins,
pubmed-meshheading:9115296-Regulatory Sequences, Nucleic Acid,
pubmed-meshheading:9115296-Repetitive Sequences, Nucleic Acid,
pubmed-meshheading:9115296-Transcription, Genetic,
pubmed-meshheading:9115296-Transfection,
pubmed-meshheading:9115296-Tumor Cells, Cultured
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pubmed:year |
1997
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pubmed:articleTitle |
Identification of direct repeat 4 as a positive regulatory element for the human TR4 orphan receptor. A modulator for the thyroid hormone target genes.
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pubmed:affiliation |
Comprehensive Cancer Center, University of Wisconsin, Madison, Wisconsin 53792, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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