| pubmed-article:18270204 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18270204 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:18270204 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:18270204 | lifeskim:mentions | umls-concept:C0072301 | lld:lifeskim |
| pubmed-article:18270204 | lifeskim:mentions | umls-concept:C0024426 | lld:lifeskim |
| pubmed-article:18270204 | lifeskim:mentions | umls-concept:C0599946 | lld:lifeskim |
| pubmed-article:18270204 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:18270204 | pubmed:dateCreated | 2008-4-8 | lld:pubmed |
| pubmed-article:18270204 | pubmed:abstractText | Macrophage activation participates pivotally in the pathophysiology of chronic inflammatory diseases, including atherosclerosis. Through the receptor EP4, prostaglandin E(2) (PGE(2)) exerts an anti-inflammatory action in macrophages, suppressing stimulus-induced expression of certain proinflammatory genes, including chemokines. We recently identified a novel EP4 receptor-associated protein (EPRAP), whose function in PGE(2)-mediated anti-inflammation remains undefined. Here we demonstrate that PGE(2) pretreatment selectively inhibits lipopolysaccharide (LPS)-induced nuclear factor kappaB1 (NF-kappaB1) p105 phosphorylation and degradation in mouse bone marrow-derived macrophages through EP4-dependent mechanisms. Similarly, directed EPRAP expression in RAW264.7 cells suppresses LPS-induced p105 phosphorylation and degradation, and subsequent activation of mitogen-activated protein kinase kinase 1/2. Forced expression of EPRAP also inhibits NF-kappaB activation induced by various proinflammatory stimuli in a concentration-dependent manner. In co-transfected cells, EPRAP, which contains multiple ankyrin repeat motifs, directly interacts with NF-kappaB1 p105/p50 and forms a complex with EP4. In EP4-overexpressing cells, PGE(2) enhances the protective action of EPRAP against stimulus-induced p105 phosphorylation, whereas EPRAP silencing in RAW264.7 cells impairs the inhibitory effect of PGE(2)-EP4 signaling on LPS-induced p105 phosphorylation. Additionally, EPRAP knockdown as well as deficiency of NF-kappaB1 in macrophages attenuates the inhibitory effect of PGE(2) on LPS-induced MIP-1beta production. Thus, PGE(2)-EP4 signaling augments NF-kappaB1 p105 protein stability through EPRAP after proinflammatory stimulation, limiting macrophage activation. | lld:pubmed |
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| pubmed-article:18270204 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18270204 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18270204 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18270204 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18270204 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18270204 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:18270204 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:18270204 | pubmed:author | pubmed-author:LibbyPeterP | lld:pubmed |
| pubmed-article:18270204 | pubmed:author | pubmed-author:MinamiManabuM | lld:pubmed |
| pubmed-article:18270204 | pubmed:author | pubmed-author:AikawaMasanor... | lld:pubmed |
