Linked Life Data

12006176

Source:http://linkedlifedata.com/resource/pubmed/id/12006176

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2002-5-13
pubmed:abstractText
The mechanism of heme oxygenase-1 (ho-1) gene activation by 15-deoxy-Delta(12,14)-prostaglandin J(2) (15d-PGJ(2)) was examined. 15d-PGJ(2) stimulated expression of HO-1 mRNA and protein and of a mouse ho-1 gene promoter/luciferase fusion construct (HO15luc) in a dose-dependent manner in mouse hepatoma (Hepa) cells. HO15luc expression was not effected by troglitazone, a peroxisome proliferator-activated receptor-gamma (PPAR-gamma) ligand, but induction by 15d-PGJ(2) was abrogated by the antioxidant N-acetylcysteine. The primary 15d-PGJ(2) responsive sequences were localized to a 5' distal enhancer (E1) and identified as the stress-response element, previously shown to mediate ho-1 activation by several agents, including heme and heavy metals. Treatment of Hepa cells with 15d-PGJ(2) stimulated stress-response element-binding activity as judged by electrophoretic mobility shift assays. Antibody "supershift" experiments identified NF-E2 related factor 2 (Nrf2), but not Fos, Jun, or activating transcription factor/cyclic AMP response element binding protein transcription factors, within the 15d-PGJ(2)-induced complexes. Similarly, a dominant-negative mutant of Nrf2, but not of c-Jun or c-Fos, abrogated 15d-PGJ(2)-stimulated E1 transcription activity. Finally, prior induction of HO-1 in RAW264.7 mouse macrophages by 15d-PGJ(2) attenuated cell death caused by diesel exhaust particle extracts. These results demonstrate that induction of mouse HO-1 expression by 15d-PGJ(2) is independent of PPAR-gamma but dependent on oxidative stress, is regulated by the oxidative stress-activated transcription factor Nrf2, and provides cytoprotective activity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1523-0864
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
249-57
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:12006176-Animals, pubmed-meshheading:12006176-Cell Line, pubmed-meshheading:12006176-Enhancer Elements, Genetic, pubmed-meshheading:12006176-Enzyme Induction, pubmed-meshheading:12006176-Gene Expression Regulation, Enzymologic, pubmed-meshheading:12006176-Heme Oxygenase (Decyclizing), pubmed-meshheading:12006176-Heme Oxygenase-1, pubmed-meshheading:12006176-Immunologic Factors, pubmed-meshheading:12006176-Kinetics, pubmed-meshheading:12006176-Liver Neoplasms, Experimental, pubmed-meshheading:12006176-Macrophages, pubmed-meshheading:12006176-Membrane Proteins, pubmed-meshheading:12006176-Mice, pubmed-meshheading:12006176-Promoter Regions, Genetic, pubmed-meshheading:12006176-Prostaglandin D2, pubmed-meshheading:12006176-Prostaglandins E, pubmed-meshheading:12006176-Recombinant Fusion Proteins, pubmed-meshheading:12006176-Transcription, Genetic, pubmed-meshheading:12006176-Transcriptional Activation, pubmed-meshheading:12006176-Tumor Cells, Cultured
pubmed:year
2002
pubmed:articleTitle
Activation of the mouse heme oxygenase-1 gene by 15-deoxy-Delta(12,14)-prostaglandin J(2) is mediated by the stress response elements and transcription factor Nrf2.
pubmed:affiliation
Department of Molecular Genetics, Alton Ochsner Medical Foundation, New Orleans, LA 70121, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.