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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
50
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pubmed:dateCreated |
2001-1-8
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pubmed:abstractText |
Atherosclerotic lesions may progress due to a "failure to die" by vascular repair cells. Egr-1, a zinc finger transcription factor, is elevated more than 5-fold in human carotid lesions relative to the adjacent tunica media. Lesion cells in vitro also express 2-3-fold higher Egr-1 mRNA and protein levels but express much lower levels of the transforming growth factor-beta (TGF-beta) Type II receptor (TbetaR-2) and are functionally resistant to the antiproliferative effects of TGF-beta. Lesion cells fail to express a TbetaR-2 promoter/chloramphenicol acetyltransferase (CAT) construct but overexpress an Egr-1-inducible platelet-derived growth factor-A promoter/CAT construct. Transfection of Egr-1 cDNA represses TbetaR-2/CAT constructs but induces PDGF-A/CAT. Egr-1 transfection reduces the levels of TbetaR-2 and confers resistance to the antiproliferative effect of TGF-beta1. Egr-1 can interact directly with both the -143 Sp1 site and the positive regulatory element 2 (PRE2) (ERT/ets) region of the TbetaR-2 promoter. Thus, although activating a family of stress-responsive genes, Egr-1 also transcriptionally represses one of the major inhibitory pathways that restrains vascular repair.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chloramphenicol O-Acetyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/EGR1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Early Growth Response Protein 1,
http://linkedlifedata.com/resource/pubmed/chemical/Fibroblast Growth Factor 2,
http://linkedlifedata.com/resource/pubmed/chemical/Immediate-Early Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet-Derived Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Transforming Growth...,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/platelet-derived growth factor A,
http://linkedlifedata.com/resource/pubmed/chemical/transforming growth factor-beta...
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author |
pubmed-author:BushHHJr,
pubmed-author:CollinsTT,
pubmed-author:EYGG,
pubmed-author:FuCC,
pubmed-author:Ivison, Blakeman, Taylor, & Co,
pubmed-author:KreigerKK,
pubmed-author:McCaffreyT ATA,
pubmed-author:SchulickA HAH
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
275
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
39039-47
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:10982796-Arteries,
pubmed-meshheading:10982796-Arteriosclerosis,
pubmed-meshheading:10982796-Binding Sites,
pubmed-meshheading:10982796-Blotting, Western,
pubmed-meshheading:10982796-Cell Division,
pubmed-meshheading:10982796-Cell Nucleus,
pubmed-meshheading:10982796-Cells, Cultured,
pubmed-meshheading:10982796-Chloramphenicol O-Acetyltransferase,
pubmed-meshheading:10982796-Cloning, Molecular,
pubmed-meshheading:10982796-DNA, Complementary,
pubmed-meshheading:10982796-DNA-Binding Proteins,
pubmed-meshheading:10982796-Densitometry,
pubmed-meshheading:10982796-Dose-Response Relationship, Drug,
pubmed-meshheading:10982796-Early Growth Response Protein 1,
pubmed-meshheading:10982796-Fibroblast Growth Factor 2,
pubmed-meshheading:10982796-Genes, Reporter,
pubmed-meshheading:10982796-Humans,
pubmed-meshheading:10982796-Immediate-Early Proteins,
pubmed-meshheading:10982796-Nerve Growth Factor,
pubmed-meshheading:10982796-Platelet-Derived Growth Factor,
pubmed-meshheading:10982796-Promoter Regions, Genetic,
pubmed-meshheading:10982796-Protein-Serine-Threonine Kinases,
pubmed-meshheading:10982796-RNA,
pubmed-meshheading:10982796-RNA, Messenger,
pubmed-meshheading:10982796-Receptors, Transforming Growth Factor beta,
pubmed-meshheading:10982796-Recombinant Proteins,
pubmed-meshheading:10982796-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:10982796-Time Factors,
pubmed-meshheading:10982796-Transcription, Genetic,
pubmed-meshheading:10982796-Transcription Factors,
pubmed-meshheading:10982796-Transfection,
pubmed-meshheading:10982796-Veins,
pubmed-meshheading:10982796-Zinc Fingers
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pubmed:year |
2000
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pubmed:articleTitle |
Elevated Egr-1 in human atherosclerotic cells transcriptionally represses the transforming growth factor-beta type II receptor.
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pubmed:affiliation |
Department of Medicine, Division of Hematology/Oncology, Weill Medical College of Cornell University New York, New York 10021, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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