Linked Life Data

19460354

Source:http://linkedlifedata.com/resource/pubmed/id/19460354

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2009-6-9
pubmed:abstractText
We investigated the role of the activation function 1 (AF1) and AF2 domains of estrogen receptor alpha (ERalpha) in mediating dioxin-dependent recruitment of ERalpha to cytochrome P4501A1 (CYP1A1) and CYP1B1 in HuH-7 human hepatoma cells. Dioxin-induced recruitment of ERalpha wildtype (ERalpha-WT) and an ERalpha AF1 deletion mutant (ERalpha-DeltaAF1), but not a transcriptional inactive AF2 mutant (ERalpha-AF2mut) to CYP1A1 and CYP1B1. Direct interactions between AHR and the AF1 and AF2 domains of ERalpha were observed, and were independent of mutations in the AF2. Expression of ERalpha-WT increased dioxin-induced CYP1A1 and CYP1B1-regulated reporter activity, and CYP1A1 and CYP1B1 mRNA levels. However, no increases in gene expression above vector controls were observed in cells transfected with ERalpha-DeltaAF1 or ERalpha-AF2mut. Our data show that the AF2 domain contributes to dioxin-induced recruitment of ERalpha to AHR target genes, but that both the AF1 and AF2 domains are required for ERalpha-dependent increases in AHR activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1090-2104
pubmed:author
pubmed:issnType
Electronic
pubmed:day
24
pubmed:volume
385
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
263-8
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Activation function 2 mediates dioxin-induced recruitment of estrogen receptor alpha to CYP1A1 and CYP1B1.
pubmed:affiliation
Department of Pharmacology and Toxicology, University of Toronto, Toronto, Ont, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't