pubmed-article:16978838 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16978838 | lifeskim:mentions | umls-concept:C0287531 | lld:lifeskim |
pubmed-article:16978838 | lifeskim:mentions | umls-concept:C1705047 | lld:lifeskim |
pubmed-article:16978838 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:16978838 | lifeskim:mentions | umls-concept:C1333257 | lld:lifeskim |
pubmed-article:16978838 | lifeskim:mentions | umls-concept:C1366876 | lld:lifeskim |
pubmed-article:16978838 | lifeskim:mentions | umls-concept:C1833235 | lld:lifeskim |
pubmed-article:16978838 | lifeskim:mentions | umls-concept:C0015744 | lld:lifeskim |
pubmed-article:16978838 | lifeskim:mentions | umls-concept:C2911691 | lld:lifeskim |
pubmed-article:16978838 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
pubmed-article:16978838 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
pubmed-article:16978838 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
pubmed-article:16978838 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:16978838 | pubmed:dateCreated | 2007-1-1 | lld:pubmed |
pubmed-article:16978838 | pubmed:abstractText | Mitogen-activated protein (MAP) kinases play a critical role in innate immune responses to microbial infection through eliciting the biosynthesis of proinflammatory cytokines. MAP phosphatases (MKP)-1 is an archetypical member of the dual-specificity phosphatase family that deactivates MAP kinases. Induction of MKP-1 has been implicated in attenuating the lipopolysaccharide (LPS) and Peptidoglycan (PGN) responses, but how the expression of the MKP-1 is regulated is still not fully understood. Here, we show that inhibition of p38 MAP kinase by specific inhibitor SB 203580 or RNA interference (RNAi) markedly reduced the expression of MKP-1 in LPS or PGN-treated macrophages, which is correlated with prolonged activation of p38 and JNK. Depletion of MAPKAP kinase 2 (MK2), a downstream substrate of p38, by RNAi also inhibited the expression of MKP-1. The mRNA level of MKP-1 is not affected by inhibition of p38, but the expression of MKP-1 is inhibited by treatment of cycloheximide. Thus, p38 MAPK plays a critical role in mediating expression of MKP-1 at a post-transcriptional level. Furthermore, inhibition of p38 by SB 203580 prevented the expression of MKP-1 in LPS-tolerized macrophages, restored the activation of MAP kinases after LPS restimulation. These results indicate a critical role of p38-MK2-dependent induction of MKP-1 in innate immune responses. | lld:pubmed |
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pubmed-article:16978838 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16978838 | pubmed:language | eng | lld:pubmed |
pubmed-article:16978838 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16978838 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:16978838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16978838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16978838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16978838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16978838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16978838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16978838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16978838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:16978838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16978838 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16978838 | pubmed:month | Feb | lld:pubmed |
pubmed-article:16978838 | pubmed:issn | 0898-6568 | lld:pubmed |
pubmed-article:16978838 | pubmed:author | pubmed-author:LiuYusenY | lld:pubmed |
pubmed-article:16978838 | pubmed:author | pubmed-author:ChenTingT | lld:pubmed |
pubmed-article:16978838 | pubmed:author | pubmed-author:KongLingL | lld:pubmed |
pubmed-article:16978838 | pubmed:author | pubmed-author:ZhuangZi-Heng... | lld:pubmed |
pubmed-article:16978838 | pubmed:author | pubmed-author:YuMing-CanMC | lld:pubmed |
pubmed-article:16978838 | pubmed:author | pubmed-author:GeBao-XueBX | lld:pubmed |
pubmed-article:16978838 | pubmed:author | pubmed-author:HuJun-HaoJH | lld:pubmed |
pubmed-article:16978838 | pubmed:author | pubmed-author:ZangJing-WuJW | lld:pubmed |
pubmed-article:16978838 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16978838 | pubmed:volume | 19 | lld:pubmed |
pubmed-article:16978838 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16978838 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16978838 | pubmed:pagination | 393-400 | lld:pubmed |
pubmed-article:16978838 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:16978838 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:16978838 | pubmed:articleTitle | Feedback control of MKP-1 expression by p38. | lld:pubmed |
pubmed-article:16978838 | pubmed:affiliation | Signal Transduction Lab of Institute of Health Sciences, Shanghai Institutes for Biological Sciences [corrected] Chinese Academy of Sciences & [corrected] Shanghai Jiao-Tong University School of Medicine, China. | lld:pubmed |
pubmed-article:16978838 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:16978838 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:16978838 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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