Linked Life Data

1340765

Source:http://linkedlifedata.com/resource/pubmed/id/1340765

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
1992-8-26
pubmed:databankReference
pubmed:abstractText
Deletion mutagenesis and transfection studies into hepatic (mouse hepatoma (Hepa-1) and human hepatoblastoma (Hep-G2)) and nonhepatic (HeLa) cells indicated that high levels of expression of the human NAD(P)H:quinone oxidoreductase gene in tumor cells and its induction by beta-naphthoflavone and 3-(2)-tert-butyl-4-hydroxyanisole are mediated by human antioxidant response element (hARE) located in the region between -470 and -445. The hARE, when attached to the thymidine kinase promoter and transfected into several mammalian cells, expressed high levels of the chloramphenicol acetyltransferase gene that was inducible by beta-naphthoflavone and 3-(2)-tert-butyl-4-hydroxyanisole. Nucleotide sequence analysis of the hARE revealed the presence of a recognition site for binding to the AP1 protein. Mutation of the AP1 binding site located within the hARE resulted in the loss of expression and induction upon transfection into various cell types. Band shift and competition assays with hARE and nuclear extracts from control and beta-naphthoflavone-treated Hepa-1, Hep-G2 and HeLa cells indicated specific interaction of regulatory protein(s) to the hARE. The supershift assays using antibodies against specific proteins of the AP1 family identified Jun-D and c-Fos as two members in the hARE-protein complex observed in band shift assays.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
267
pubmed:geneSymbol
NQO<down>1</down>
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15097-104
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:1340765-Amino Acid Sequence, pubmed-meshheading:1340765-Animals, pubmed-meshheading:1340765-Antioxidants, pubmed-meshheading:1340765-Benzoflavones, pubmed-meshheading:1340765-Binding Sites, pubmed-meshheading:1340765-Butylated Hydroxyanisole, pubmed-meshheading:1340765-Chloramphenicol O-Acetyltransferase, pubmed-meshheading:1340765-Enzyme Induction, pubmed-meshheading:1340765-Gene Expression Regulation, Enzymologic, pubmed-meshheading:1340765-Glutathione Transferase, pubmed-meshheading:1340765-HeLa Cells, pubmed-meshheading:1340765-Humans, pubmed-meshheading:1340765-Mice, pubmed-meshheading:1340765-Molecular Sequence Data, pubmed-meshheading:1340765-Mutagenesis, pubmed-meshheading:1340765-NAD(P)H Dehydrogenase (Quinone), pubmed-meshheading:1340765-Plasmids, pubmed-meshheading:1340765-Proto-Oncogene Proteins c-fos, pubmed-meshheading:1340765-Proto-Oncogene Proteins c-jun, pubmed-meshheading:1340765-Sequence Homology, Nucleic Acid, pubmed-meshheading:1340765-Transfection, pubmed-meshheading:1340765-Tumor Cells, Cultured, pubmed-meshheading:1340765-beta-Naphthoflavone
pubmed:year
1992
pubmed:articleTitle
Regulation of human NAD(P)H:quinone oxidoreductase gene. Role of AP1 binding site contained within human antioxidant response element.
pubmed:affiliation
Department of Pharmacology, Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.