Linked Life Data

11306047

Source:http://linkedlifedata.com/resource/pubmed/id/11306047

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
2001-4-18
pubmed:abstractText
We have previously shown that expression of the Class 3 aldehyde dehydrogenase gene (ALDH3) is abrogated by hypoxia. This phenomenon occurs in rat hepatoma systems in which ALDH3 expression is xenobiotic-inducible as well as in rat primary corneal epithelial cells that exhibit high constitutive ALDH3 expression. We have begun to test various segments of the ALDH3 5' flanking region for elements that may mediate this effect using CAT reporter gene constructs. In addition, although the involvement of the Ah receptor nuclear translocator (ARNT) in xenobiotic induction of ALDH3 is well established, the role of ARNT in constitutive ALDH3 expression is not clear. Moreover, ARNT is also a component of the hypoxia inducible factor-1 (HIF-1) bipartite transcription factor complex that mediates hypoxic induction of a variety of genes. Concomitant activation of the xenobiotic and hypoxia pathways results in cross-talk and functional interference. It has been hypothesized that this interference is due to limiting levels of ARNT. To examine if ARNT levels are limiting during hypoxic and xenobiotic induction in the context of ALDH3 expression and to examine possible roles of ARNT in constitutive expression of ALDH3 in corneal epithelial cells we co-transfected rat corneal epithelial cells and H4-II-EC3 rat hepatoma cells with ALDH3 5' UTR-CAT reporter genes and expression vectors containing either wild type or dominant negative forms of ARNT. Our results indicate that during hypoxia and xenobiotic induction of ALDH3 in H4-II-EC3 cells ARNT is not the limiting transcription factor. Further, neither wild type nor dominant negative ARNT had effects on constitutive ALDH3 expression in corneal epithelial cells.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0009-2797
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
130-132
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
227-33
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11306047-Aldehyde Dehydrogenase, pubmed-meshheading:11306047-Animals, pubmed-meshheading:11306047-Anoxia, pubmed-meshheading:11306047-Aryl Hydrocarbon Receptor Nuclear Translocator, pubmed-meshheading:11306047-Cells, Cultured, pubmed-meshheading:11306047-Cornea, pubmed-meshheading:11306047-DNA-Binding Proteins, pubmed-meshheading:11306047-Down-Regulation, pubmed-meshheading:11306047-Epithelial Cells, pubmed-meshheading:11306047-Gene Expression Regulation, Enzymologic, pubmed-meshheading:11306047-Liver Neoplasms, Experimental, pubmed-meshheading:11306047-Oxidative Stress, pubmed-meshheading:11306047-Rats, pubmed-meshheading:11306047-Receptors, Aryl Hydrocarbon, pubmed-meshheading:11306047-Transcription Factors, pubmed-meshheading:11306047-Tumor Cells, Cultured, pubmed-meshheading:11306047-Xenobiotics
pubmed:year
2001
pubmed:articleTitle
Aldehyde dehydrogenase 3 gene regulation: studies on constitutive and hypoxia-modulated expression.
pubmed:affiliation
Cellular and Molecular Biology Research Group, The University of South Dakota School of Medicine, 57069, Vermillion, SD, USA. rindahl@usd.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.