Linked Life Data

9743233

Source:http://linkedlifedata.com/resource/pubmed/id/9743233

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:9743233rdf:typepubmed:Citationlld:pubmed
pubmed-article:9743233lifeskim:mentionsumls-concept:C0086418lld:lifeskim
pubmed-article:9743233lifeskim:mentionsumls-concept:C0085828lld:lifeskim
pubmed-article:9743233lifeskim:mentionsumls-concept:C0162508lld:lifeskim
pubmed-article:9743233lifeskim:mentionsumls-concept:C1135918lld:lifeskim
pubmed-article:9743233lifeskim:mentionsumls-concept:C0242606lld:lifeskim
pubmed-article:9743233lifeskim:mentionsumls-concept:C0074129lld:lifeskim
pubmed-article:9743233lifeskim:mentionsumls-concept:C0162493lld:lifeskim
pubmed-article:9743233lifeskim:mentionsumls-concept:C1367731lld:lifeskim
pubmed-article:9743233lifeskim:mentionsumls-concept:C1150587lld:lifeskim
pubmed-article:9743233lifeskim:mentionsumls-concept:C1705632lld:lifeskim
pubmed-article:9743233lifeskim:mentionsumls-concept:C1167622lld:lifeskim
pubmed-article:9743233lifeskim:mentionsumls-concept:C0597360lld:lifeskim
pubmed-article:9743233lifeskim:mentionsumls-concept:C0031586lld:lifeskim
pubmed-article:9743233lifeskim:mentionsumls-concept:C0205263lld:lifeskim
pubmed-article:9743233lifeskim:mentionsumls-concept:C1546857lld:lifeskim
pubmed-article:9743233lifeskim:mentionsumls-concept:C1879547lld:lifeskim
pubmed-article:9743233pubmed:issue9lld:pubmed
pubmed-article:9743233pubmed:dateCreated1998-10-1lld:pubmed
pubmed-article:9743233pubmed:abstractTextReactive oxygen species generated by treatment of smooth muscle cells (SMCs) with either phorbol 12-myristate 13-acetate or with the combination of H2O2 and vanadate strongly induce expression of the class A scavenger receptor (SR-A) gene. In the current studies, cis-acting elements in the proximal 245 bp of the SR-A promoter were shown to direct luciferase reporter expression in response to oxidative stress in both SMCs and macrophages. A composite activating protein-1 (AP-1)/ets binding element located between -67 and -50 bp relative to the transcriptional start site is critical for macrophage SR-A activity. Mutation of either the AP-1 or the ets component of this site also prevented promoter activity in SMCs. Mutation of a second site located between -44 and -21 bp, which we have identified as a CCAAT/enhancer binding protein (C/EBP) element, reduced the inducible activity of the promoter in SMCs by 50%, suggesting that combinatorial interactions between these sites are necessary for optimal gene induction. Interactions between SMC nuclear extracts and the SR-A promoter were analyzed by electrophoretic mobility shift assay. c-Jun/AP-1 binding activity, specific for the -67- to -50-bp site, was induced in SMCs by the same conditions that increased SR-A expression. Moreover, phorbol 12-myristate 13-acetate, H2O2, or the combination of H2O2 and sodium orthovanadate (vanadate) activated c-Jun-activating kinase. The binding activity within SMC extracts specific for the C/EBP site was shown to be C/EBPbeta in SMCs. Taken together, these findings demonstrate that reactive oxygen species regulate the interactions between c-Jun/AP-1 and C/EBPbeta in the SR-A promoter. Furthermore, induction of oxidative stress in THP-1 cells, with a combination of 10 micromol/L vanadate and 100 micromol/L H2O2, induced macrophage differentiation, adhesion, and SR activity. These data suggest that vascular oxidative stress may contribute to the induction of SR-A expression and thereby promote the uptake of oxidatively modified low density lipoprotein by both macrophage and SMCs to produce foam cells in atherosclerotic lesions.lld:pubmed
pubmed-article:9743233pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9743233pubmed:languageenglld:pubmed
pubmed-article:9743233pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9743233pubmed:citationSubsetIMlld:pubmed
pubmed-article:9743233pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9743233pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9743233pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9743233pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9743233pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9743233pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9743233pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9743233pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9743233pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9743233pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9743233pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9743233pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9743233pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9743233pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9743233pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9743233pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9743233pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9743233pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9743233pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9743233pubmed:statusMEDLINElld:pubmed
pubmed-article:9743233pubmed:monthSeplld:pubmed
pubmed-article:9743233pubmed:issn1079-5642lld:pubmed
pubmed-article:9743233pubmed:authorpubmed-author:PitasR ERElld:pubmed
pubmed-article:9743233pubmed:authorpubmed-author:GlassC KCKlld:pubmed
pubmed-article:9743233pubmed:authorpubmed-author:Mietus-Snyder...lld:pubmed
pubmed-article:9743233pubmed:issnTypePrintlld:pubmed
pubmed-article:9743233pubmed:volume18lld:pubmed
pubmed-article:9743233pubmed:ownerNLMlld:pubmed
pubmed-article:9743233pubmed:authorsCompleteYlld:pubmed
pubmed-article:9743233pubmed:pagination1440-9lld:pubmed
pubmed-article:9743233pubmed:dateRevised2009-11-19lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:meshHeadingpubmed-meshheading:9743233-...lld:pubmed
pubmed-article:9743233pubmed:year1998lld:pubmed
pubmed-article:9743233pubmed:articleTitleTranscriptional activation of scavenger receptor expression in human smooth muscle cells requires AP-1/c-Jun and C/EBPbeta: both AP-1 binding and JNK activation are induced by phorbol esters and oxidative stress.lld:pubmed
pubmed-article:9743233pubmed:affiliationGladstone Institute of Cardiovascular Disease, and Department of Pediatrics, University of California, San Francisco 94141-9100, USA.lld:pubmed
pubmed-article:9743233pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9743233pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9743233lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9743233lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9743233lld:pubmed