Linked Life Data

10965913

Source:http://linkedlifedata.com/resource/pubmed/id/10965913

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2000-9-21
pubmed:abstractText
Functional interactions or cross-talk between ligand-activated nuclear receptors and the proinflammatory transcription factor nuclear factor-kappaB (NF-kappaB) may play a major role in ligand-mediated modification of diseases processes. In particular, the cardioprotective effects of estrogen replacement therapy are thought to be due in part to the ability of ligand-bound estrogen receptor (ER) to inhibit NF-kappaB function. In the current study 17beta-estradiol-bound ERalpha interfered with cytokine-induced activation of a NF-kappaB reporter in HepG2 cells. The estrogen metabolite, 17alpha-ethinyl estradiol, and the phytoestrogen, genistein, were also effective inhibitors of NF-kappaB activation, whereas tamoxifen, 4-hydroxytamoxifen, and raloxifene were inactive. This inhibition was reciprocal, as NF-kappaB interfered with the trans-activation properties of ERalpha. Ligand-bound ERalpha did not inhibit NF-kappaB binding to DNA, but it did decrease the histone acetyltransferase activity required for NF-kappaB transcriptional activity. Coexpression of the transcription coactivator CREB binding protein (CBP), but not steroid receptor coactivator 1a, reversed the ERalpha-mediated inhibition of NF-kappaB activity. Mammalian two-hybrid experiments also revealed that ligand-bound ERalpha can interact functionally with CBP-NF-kappaB complexes. We suggest that CBP targeting by ERalpha results in the inhibition of NF-kappaB and may occur through formation of transcriptionally inert multimeric complexes that are dependent upon the nature of the ERalpha ligand.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0013-7227
pubmed:author
pubmed:issnType
Print
pubmed:volume
141
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3403-11
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10965913-Adenoviridae, pubmed-meshheading:10965913-Anticholesteremic Agents, pubmed-meshheading:10965913-Blotting, Western, pubmed-meshheading:10965913-CREB-Binding Protein, pubmed-meshheading:10965913-Cell Line, pubmed-meshheading:10965913-Electrophoresis, pubmed-meshheading:10965913-Estrogens, pubmed-meshheading:10965913-Genetic Vectors, pubmed-meshheading:10965913-Histone Deacetylase Inhibitors, pubmed-meshheading:10965913-Humans, pubmed-meshheading:10965913-Interleukin-1, pubmed-meshheading:10965913-Luciferases, pubmed-meshheading:10965913-NF-kappa B, pubmed-meshheading:10965913-Nuclear Proteins, pubmed-meshheading:10965913-Plasmids, pubmed-meshheading:10965913-Receptor Cross-Talk, pubmed-meshheading:10965913-Receptors, Estrogen, pubmed-meshheading:10965913-Trans-Activators, pubmed-meshheading:10965913-Transfection
pubmed:year
2000
pubmed:articleTitle
The role of CBP in estrogen receptor cross-talk with nuclear factor-kappaB in HepG2 cells.
pubmed:affiliation
Women's Health Research Institute, Wyeth-Ayerst Laboratories, Inc, Radnor, Pennsylvania 19087, USA. harnisd@war.wyeth.com
pubmed:publicationType
Journal Article