pubmed-article:7507507 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7507507 | lifeskim:mentions | umls-concept:C0126732 | lld:lifeskim |
pubmed-article:7507507 | lifeskim:mentions | umls-concept:C0014257 | lld:lifeskim |
pubmed-article:7507507 | lifeskim:mentions | umls-concept:C0079904 | lld:lifeskim |
pubmed-article:7507507 | lifeskim:mentions | umls-concept:C0220905 | lld:lifeskim |
pubmed-article:7507507 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
pubmed-article:7507507 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:7507507 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:7507507 | pubmed:dateCreated | 1994-3-3 | lld:pubmed |
pubmed-article:7507507 | pubmed:abstractText | Structural analysis of the promoters of several endothelial genes induced at sites of inflammatory or immune responses reveals binding sites for the transcription factor nuclear factor kappa B (NF-kappa B). Endothelial cells express transcripts encoding the p50/p105 and p65 components of NF-kappa B and the rel-related proto-oncogene c-rel; steady state levels of these transcripts are transiently increased by tumor necrosis factor alpha (TNF-alpha). Western blotting revealed that stimulation of endothelial cells with TNF-alpha resulted in nuclear accumulation of the p50 and p65 components of NF-kappa B. Ultraviolet crosslinking and immunoprecipitation demonstrated binding of the p50 and p65 components of NF-kappa B to the E-selectin kappa B site. Endothelial cells express an inhibitor of NF-kappa B activation, I kappa B-alpha (MAD-3). Protein levels of this inhibitor fall rapidly after TNF-alpha stimulation. In parallel, p50 and p65 accumulate in the nucleus and RNA transcript levels for I kappa B-alpha are dramatically upregulated. Recombinant p65 stimulates expression of E-selectin promoter-reporter constructs. I kappa B-alpha inhibits p65 or TNF-alpha-stimulated E-selectin promoter-reporter gene expression in transfected endothelial cells. The NF-kappa B and I kappa B-alpha system may be an inducible regulatory mechanism in endothelial activation. | lld:pubmed |
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pubmed-article:7507507 | pubmed:language | eng | lld:pubmed |
pubmed-article:7507507 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7507507 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:7507507 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:7507507 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7507507 | pubmed:month | Feb | lld:pubmed |
pubmed-article:7507507 | pubmed:issn | 0022-1007 | lld:pubmed |
pubmed-article:7507507 | pubmed:author | pubmed-author:WilliamsA JAJ | lld:pubmed |
pubmed-article:7507507 | pubmed:author | pubmed-author:CollinsTT | lld:pubmed |
pubmed-article:7507507 | pubmed:author | pubmed-author:ReadM AMA | lld:pubmed |
pubmed-article:7507507 | pubmed:author | pubmed-author:WhitleyM ZMZ | lld:pubmed |
pubmed-article:7507507 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7507507 | pubmed:day | 1 | lld:pubmed |
pubmed-article:7507507 | pubmed:volume | 179 | lld:pubmed |
pubmed-article:7507507 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7507507 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7507507 | pubmed:pagination | 503-12 | lld:pubmed |
pubmed-article:7507507 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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