rdf:type |
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lifeskim:mentions |
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pubmed:issue |
25
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pubmed:dateCreated |
1995-2-27
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pubmed:abstractText |
Hepatocyte Nuclear Factor 4 (HNF-4), a liver-enriched orphan receptor of the nuclear receptor superfamily, is required for the expression of a wide variety of liver-specific genes including apoAI. To explore the possibility that site A of the apoAI gene enhancer might also be the target for HNF-4 without the interference of endogenous mammalian cell proteins that also bind to site A, we tested the ability of HNF-4 to activate transcription from site A in yeast cells. Electrophoretic mobility shift assays (EMSA) and Scatchard plot analysis demonstrated that yeast produced HNF-4 binds to site A with an affinity two times higher than that of yeast produced RXR alpha. Mapping analysis indicated that the 5' portion of site A containing two imperfect direct repeats (TGAACCCTTGACC) and the sequence of the trinucleotide spacer (CCT) between these imperfect repeats are critical determinants for selective binding and transactivation by HNF-4. Similar observations were obtained when these mutated versions of site A were evaluated by transient cotransfection assays in CV1 cells. We conclude that the unique structural determinants of site A in conjunction with the differential binding affinity of HNF-4 for site A may play a fundamental role in apoAI gene regulation.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-1312668,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-1321332,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-1323763,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-1646397,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-1648450,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-1648451,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-1846669,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-1899293,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-2279702,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-2566384,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-2677733,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-2689442,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-2895420,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-3020028,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-3043665,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-3121329,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-3283939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-3290686,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-3549451,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-8045412,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-8146430,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-8167573,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-8344962,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-8387213,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-8440243,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7838720-8464705
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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/Apolipoprotein A-I,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hepatocyte Nuclear Factor 4,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
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 |
Dec
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pubmed:issn |
0305-1048
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
22
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5665-71
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7838720-Animals,
pubmed-meshheading:7838720-Apolipoprotein A-I,
pubmed-meshheading:7838720-Base Sequence,
pubmed-meshheading:7838720-Binding Sites,
pubmed-meshheading:7838720-Cell Line,
pubmed-meshheading:7838720-Cercopithecus aethiops,
pubmed-meshheading:7838720-DNA-Binding Proteins,
pubmed-meshheading:7838720-Enhancer Elements, Genetic,
pubmed-meshheading:7838720-Gene Expression Regulation,
pubmed-meshheading:7838720-Hepatocyte Nuclear Factor 4,
pubmed-meshheading:7838720-Molecular Sequence Data,
pubmed-meshheading:7838720-Oligodeoxyribonucleotides,
pubmed-meshheading:7838720-Phosphoproteins,
pubmed-meshheading:7838720-Promoter Regions, Genetic,
pubmed-meshheading:7838720-Protein Binding,
pubmed-meshheading:7838720-RNA, Messenger,
pubmed-meshheading:7838720-Receptors, Retinoic Acid,
pubmed-meshheading:7838720-Retinoid X Receptors,
pubmed-meshheading:7838720-Saccharomyces cerevisiae,
pubmed-meshheading:7838720-Transcription, Genetic,
pubmed-meshheading:7838720-Transcription Factors,
pubmed-meshheading:7838720-Transfection
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pubmed:year |
1994
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pubmed:articleTitle |
Transcriptional regulation of the apoAI gene by hepatic nuclear factor 4 in yeast.
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pubmed:affiliation |
Department of Cardiovascular Molecular Biology, Lederle Laboratories, American Cyanamid Co., Pearl River, NY 10965.
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pubmed:publicationType |
Journal Article
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