pubmed-article:18025233 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18025233 | lifeskim:mentions | umls-concept:C0919490 | lld:lifeskim |
pubmed-article:18025233 | lifeskim:mentions | umls-concept:C0024432 | lld:lifeskim |
pubmed-article:18025233 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
pubmed-article:18025233 | lifeskim:mentions | umls-concept:C0387583 | lld:lifeskim |
pubmed-article:18025233 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:18025233 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:18025233 | lifeskim:mentions | umls-concept:C0249854 | lld:lifeskim |
pubmed-article:18025233 | pubmed:issue | 11 | lld:pubmed |
pubmed-article:18025233 | pubmed:dateCreated | 2007-11-20 | lld:pubmed |
pubmed-article:18025233 | pubmed:abstractText | Selective expression of cyclooxygenase 2 (COX-2) by macrophages could have an important role in the pathobiology of inflammation. We reported a functional synergism between PU.1 and other transcription factors that contributes to COX-2 gene expression in macrophages. PU.1 resides in the nuclear compartment and is activated by phosphorylation to bind to cognate DNA elements containing a 5'-GGAA/T-3' motif, but the involved kinase has not been discovered. We tested the hypothesis that NF-kappaB-inducing kinase (NIK) regulates COX-2 gene expression in macrophages through inducible phosphorylation of PU.1. Our initial experiments showed an in vitro protein-protein binding interaction between myc-NIK and GST-PU.1. Purified myc-NIK had a strong in vitro kinase activity for purified GST-PU.1, and this activity and production of COX-2 protein is blocked by treatment with a nonspecific kinase inhibitor, 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole. We used short interfering RNA to develop a stable NIK knockdown macrophage cell line that had an approximately 50% decrease in COX-2 protein production and decreased generation of PGD(2), and this was correlated with decreased binding of activated PU.1 to the COX-2 promoter in response to treatment with endotoxin. These findings suggest a novel role for NIK in mediating COX-2 gene expression in endotoxin-treated macrophages by a mechanism that involves phosphorylation of PU.1. | lld:pubmed |
pubmed-article:18025233 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18025233 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18025233 | pubmed:language | eng | lld:pubmed |
pubmed-article:18025233 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18025233 | pubmed:citationSubset | AIM | lld:pubmed |
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pubmed-article:18025233 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18025233 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18025233 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18025233 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:18025233 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18025233 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18025233 | pubmed:month | Dec | lld:pubmed |
pubmed-article:18025233 | pubmed:issn | 0022-1767 | lld:pubmed |
pubmed-article:18025233 | pubmed:author | pubmed-author:van... | lld:pubmed |
pubmed-article:18025233 | pubmed:author | pubmed-author:ChristmanJohn... | lld:pubmed |
pubmed-article:18025233 | pubmed:author | pubmed-author:SadikotRuxana... | lld:pubmed |
pubmed-article:18025233 | pubmed:author | pubmed-author:AtchisonMicha... | lld:pubmed |
pubmed-article:18025233 | pubmed:author | pubmed-author:AzimAnser CAC | lld:pubmed |
pubmed-article:18025233 | pubmed:author | pubmed-author:JooMyungsooM | lld:pubmed |
pubmed-article:18025233 | pubmed:author | pubmed-author:ParkGye... | lld:pubmed |
pubmed-article:18025233 | pubmed:author | pubmed-author:WangXuerongX | lld:pubmed |
pubmed-article:18025233 | pubmed:author | pubmed-author:CaoHongmeiH | lld:pubmed |
pubmed-article:18025233 | pubmed:author | pubmed-author:MathewBijiB | lld:pubmed |
pubmed-article:18025233 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:18025233 | pubmed:day | 1 | lld:pubmed |
pubmed-article:18025233 | pubmed:volume | 179 | lld:pubmed |
pubmed-article:18025233 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18025233 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18025233 | pubmed:pagination | 7868-75 | lld:pubmed |
pubmed-article:18025233 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
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pubmed-article:18025233 | pubmed:meshHeading | pubmed-meshheading:18025233... | lld:pubmed |
pubmed-article:18025233 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:18025233 | pubmed:articleTitle | NF-kappaB-inducing kinase regulates cyclooxygenase 2 gene expression in macrophages by phosphorylation of PU.1. | lld:pubmed |
pubmed-article:18025233 | pubmed:affiliation | Department of Medicine, University of Illinois, Chicago, IL 60612, USA. | lld:pubmed |
pubmed-article:18025233 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:18025233 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:18025233 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
entrez-gene:19225 | entrezgene:pubmed | pubmed-article:18025233 | lld:entrezgene |
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