| pubmed-article:19906641 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19906641 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:19906641 | lifeskim:mentions | umls-concept:C0031308 | lld:lifeskim |
| pubmed-article:19906641 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:19906641 | lifeskim:mentions | umls-concept:C1514758 | lld:lifeskim |
| pubmed-article:19906641 | lifeskim:mentions | umls-concept:C1568094 | lld:lifeskim |
| pubmed-article:19906641 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:19906641 | pubmed:dateCreated | 2010-1-25 | lld:pubmed |
| pubmed-article:19906641 | pubmed:abstractText | Resolvins are endogenous lipid mediators that actively regulate the resolution of acute inflammation. Resolvin E1 (RvE1; (5S,12R,18R)-trihydroxy-6Z,8E,10E,14Z,16E-eicosapentaenoic acid) is an endogenous anti-inflammatory and pro-resolving mediator derived from eicosapentaenoic acid that regulates leukocyte migration and enhances macrophage phagocytosis of apoptotic neutrophils to resolve inflammation. In the inflammatory milieu, RvE1 mediates counter-regulatory actions initiated via specific G protein-coupled receptors. Here, we have identified RvE1-specific signaling pathways initiated by the RvE1 receptor ChemR23. RvE1 stimulated phosphorylation of Akt that was both ligand- and receptor-dependent. RvE1 regulated Akt phosphorylation in a time (0-15 min)- and dose-dependent (0.01-100 nm) manner in human ChemR23-transfected Chinese hamster ovary cells. RvE1 stimulated phosphorylation of both Akt and a 30-kDa protein, a downstream target of Akt, identified using a phospho-Akt substrate antibody. The 30-kDa protein was identified as ribosomal protein S6, a translational regulator, and its phosphorylation was inhibited by a phosphatidylinositol 3-kinase (PI3K) inhibitor (wortmannin) and an ERK inhibitor (PD98059) but not by a p38-MAPK inhibitor (SB203580). Ribosomal protein S6 is a downstream target of the PI3K/Akt signaling pathway as well as the Raf/ERK pathway. In ChemR23-expressing differentiated HL60 cells, RvE1 also stimulated the phosphorylation of ribosomal protein S6. In addition, RvE1 enhanced phagocytosis of zymosan A by human macrophages, which are inhibited by PD98059 and rapamycin (mTOR inhibitor). These results indicate that RvE1 initiates direct activation of ChemR23 and signals receptor-dependent phosphorylation. These phosphorylation-signaling pathways identified for RvE1 receptor-ligand interactions underscore the importance of endogenous pro-resolving agonists in resolving acute inflammation. | lld:pubmed |
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| pubmed-article:19906641 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:19906641 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19906641 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19906641 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:19906641 | pubmed:issn | 1083-351X | lld:pubmed |
| pubmed-article:19906641 | pubmed:author | pubmed-author:SerhanCharles... | lld:pubmed |
| pubmed-article:19906641 | pubmed:author | pubmed-author:AritaMakotoM | lld:pubmed |
| pubmed-article:19906641 | pubmed:author | pubmed-author:Van... | lld:pubmed |
| pubmed-article:19906641 | pubmed:author | pubmed-author:OhiraTaisukeT | lld:pubmed |
| pubmed-article:19906641 | pubmed:author | pubmed-author:OmoriKazuhiro... | lld:pubmed |
| pubmed-article:19906641 | pubmed:author | pubmed-author:RecchiutiAnto... | lld:pubmed |
| pubmed-article:19906641 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19906641 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:19906641 | pubmed:volume | 285 | lld:pubmed |
| pubmed-article:19906641 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19906641 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19906641 | pubmed:pagination | 3451-61 | lld:pubmed |
| pubmed-article:19906641 | pubmed:dateRevised | 2011-7-20 | lld:pubmed |
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| pubmed-article:19906641 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:19906641 | pubmed:articleTitle | Resolvin E1 receptor activation signals phosphorylation and phagocytosis. | lld:pubmed |
| pubmed-article:19906641 | pubmed:affiliation | Department of Anesthesiology, Perioperative and Pain Medicine, Brigham and Women's Hospital and Harvard Medical School, Center for Experimental Therapeutics and Reperfusion Injury, Boston, Massachusetts 02115, USA. | lld:pubmed |
| pubmed-article:19906641 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19906641 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:19906641 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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