Source:http://linkedlifedata.com/resource/pubmed/id/17202378
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2007-1-4
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| pubmed:abstractText |
Triggering receptor expressed on myeloid cells-1 (TREM-1) is a recently identified cell surface molecule that is expressed by neutrophils and monocytes. TREM-1 expression is modulated by various ligands for TLRs in vitro and in vivo. However, the influence of PGE(2), a potential mediator of inflammation, on TREM-1 expression has not been elucidated. In this study, we examined the effects of PGE(2) on LPS-induced TREM-1 expression by resident murine peritoneal macrophages (RPM) and human PBMC. PGE(2) significantly induced murine TREM-1 (mTREM-1) expression by RPM. Up-regulation of TREM-1 expression was specific to PGE(2) among arachidonic acid metabolites, while ligands for chemoattractant receptor-homologous molecule expressed on Th2 cells and the thomboxane-like prostanoid receptor failed to induce mTREM-1 expression. PGE(2) also increased expression of the soluble form of TREM-1 by PBMC. LPS-induced TREM-1 expression was regulated by endogenous PGE(2) especially in late phase (>2 h after stimulation), because cyclooxygenase-1 and -2 inhibitors abolished this effect at that points. A synthetic EP4 agonist and 8-Br-cAMP also enhanced mTREM-1 expression by RPM. Furthermore, protein kinase A, PI3K, and p38 MAPK inhibitors prevented PGE(2)-induced mTREM-1 expression by RPM. Activation of TREM-1 expressed on PGE(2)-pretreated PBMC by an agonistic TREM-1 mAb significantly enhanced the production of IL-8 and TNF-alpha. These findings indicate that LPS-induced TREM-1 expression on macrophages is mediated, at least partly, by endogenous PGE(2) followed by EP4 and cAMP, protein kinase A, p38 MAPK, and PI3K-mediated signaling. Regulation of TREM-1 and the soluble form of TREM-1 expression by PGE(2) may modulate the inflammatory response to microbial pathogens.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
AIM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Dinoprostone,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/PTGER4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Ptger4 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Prostaglandin E,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Prostaglandin E, EP4...,
http://linkedlifedata.com/resource/pubmed/chemical/TREM1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/p38 Mitogen-Activated Protein...
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jan
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| pubmed:issn |
0022-1767
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
15
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| pubmed:volume |
178
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
1144-50
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| pubmed:dateRevised |
2010-11-18
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| pubmed:meshHeading |
pubmed-meshheading:17202378-Animals,
pubmed-meshheading:17202378-Cells, Cultured,
pubmed-meshheading:17202378-Cyclic AMP,
pubmed-meshheading:17202378-Cyclic AMP-Dependent Protein Kinases,
pubmed-meshheading:17202378-Dinoprostone,
pubmed-meshheading:17202378-Humans,
pubmed-meshheading:17202378-Lipopolysaccharides,
pubmed-meshheading:17202378-Macrophages, Peritoneal,
pubmed-meshheading:17202378-Membrane Glycoproteins,
pubmed-meshheading:17202378-Mice,
pubmed-meshheading:17202378-Mice, Inbred ICR,
pubmed-meshheading:17202378-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:17202378-Protein Kinase Inhibitors,
pubmed-meshheading:17202378-Receptors, Immunologic,
pubmed-meshheading:17202378-Receptors, Prostaglandin E,
pubmed-meshheading:17202378-Receptors, Prostaglandin E, EP4 Subtype,
pubmed-meshheading:17202378-Solubility,
pubmed-meshheading:17202378-Up-Regulation,
pubmed-meshheading:17202378-p38 Mitogen-Activated Protein Kinases
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| pubmed:year |
2007
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| pubmed:articleTitle |
Lipopolysaccharide-induced up-regulation of triggering receptor expressed on myeloid cells-1 expression on macrophages is regulated by endogenous prostaglandin E2.
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| pubmed:affiliation |
Research Unit for Clinical Immunology, RIKEN Research Center for Allergy and Immunology, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama City, Kanagawa 230-0045, Japan. y-mura@rcai.riken.jp
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| pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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