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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1999-2-22
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pubmed:abstractText |
CYP3A1 gene (P450/6betaB) encodes testosterone 6beta-hydroxylase (EC 1.14.14.1) in rats. The promoter region of CYP3A1 gene contains three binding sites for nuclear factors: 6betaB-A (-105 to -86), 6betaB-B (-139 to -118), and 6betaB-C (-164 to -145). The 6betaB-A site shows a high degree of similarity to a consensus sequence of the binding site of hepatocyte nuclear factor 4 (HNF-4) and also to the 6betaA-A site on the rat CYP3A2 gene promoter region. Our previous study suggested an involvement of the 6betaA-A site in the basal transactivation of CYP3A2 gene using HepG2 cells. In the present study, transactivation through the 6betaB-A and 6betaA-A sites of CYP3A1 and CYP3A2 genes has directly been shown by coexpression of HNF-4 and CYP3A1 or CYP3A2 promoter-reporter fused genes. Similar experiments further showed that nuclear factor binding at the 6betaB-B site hampered HNF-4-mediated transactivation of CYP3A1 gene. Recombinant apolipoprotein AI regulatory protein I (ARP-1) and v-ErbA-related protein 3 (EAR-3) are shown to suppress HNF-4-mediated activation at the 6betaB-B site without competition of HNF-4.
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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/Aryl Hydrocarbon Hydroxylases,
http://linkedlifedata.com/resource/pubmed/chemical/COUP Transcription Factor I,
http://linkedlifedata.com/resource/pubmed/chemical/COUP Transcription Factor II,
http://linkedlifedata.com/resource/pubmed/chemical/COUP Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/CYP3A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cyp3a1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 CYP3A,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 Enzyme System,
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/Mixed Function Oxygenases,
http://linkedlifedata.com/resource/pubmed/chemical/Nr2f1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Nr2f2 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Steroid,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Steroid Hydroxylases,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/steroid hormone 6-beta-hydroxylase
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0003-9861
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 1999 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
362
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
32-7
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:9917326-Animals,
pubmed-meshheading:9917326-Aryl Hydrocarbon Hydroxylases,
pubmed-meshheading:9917326-Base Sequence,
pubmed-meshheading:9917326-Binding, Competitive,
pubmed-meshheading:9917326-COS Cells,
pubmed-meshheading:9917326-COUP Transcription Factor I,
pubmed-meshheading:9917326-COUP Transcription Factor II,
pubmed-meshheading:9917326-COUP Transcription Factors,
pubmed-meshheading:9917326-Cytochrome P-450 CYP3A,
pubmed-meshheading:9917326-Cytochrome P-450 Enzyme System,
pubmed-meshheading:9917326-DNA-Binding Proteins,
pubmed-meshheading:9917326-Hepatocyte Nuclear Factor 4,
pubmed-meshheading:9917326-Mixed Function Oxygenases,
pubmed-meshheading:9917326-Molecular Sequence Data,
pubmed-meshheading:9917326-Phosphoproteins,
pubmed-meshheading:9917326-Rats,
pubmed-meshheading:9917326-Receptors, Steroid,
pubmed-meshheading:9917326-Repressor Proteins,
pubmed-meshheading:9917326-Sequence Deletion,
pubmed-meshheading:9917326-Steroid Hydroxylases,
pubmed-meshheading:9917326-Transcription Factors,
pubmed-meshheading:9917326-Transcriptional Activation
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pubmed:year |
1999
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pubmed:articleTitle |
Hepatocyte nuclear factor 4-mediated activation of rat CYP3A1 gene and its modes of modulation by apolipoprotein AI regulatory protein I and v-ErbA-related protein 3.
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pubmed:affiliation |
Division of Drug Metabolism and Molecular Toxicology, Faculty of Pharmaceutical Sciences, Tohoku University, Sendai, 980-8578, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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