Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/11554
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dc.contributor.author | Pouliot, M. | - |
dc.contributor.author | Gilbert, C. | - |
dc.contributor.author | Borgeat, P. | - |
dc.contributor.author | Poubelle, P. | - |
dc.contributor.author | Bourgoin, S. | - |
dc.contributor.author | McColl, S. | - |
dc.contributor.author | Naccache, P. | - |
dc.date.issued | 1998 | - |
dc.identifier.citation | The FASEB Journal, 1998; 12(12):1109-1123 | - |
dc.identifier.issn | 0892-6638 | - |
dc.identifier.issn | 1530-6860 | - |
dc.identifier.uri | http://hdl.handle.net/2440/11554 | - |
dc.description.abstract | Proinflammatory agents were assessed for their capacity to stimulate the expression of the inducible cyclooxygenase isoform (COX-2) in human neutrophils. A number of agents, including PMA, opsonized bacteria and zymosan, LPS, GM-CSF, TNF-alpha, and fMLP, induced COX-2 protein expression through signaling pathways involving transcription and protein synthesis events. Northern blots showed that freshly isolated neutrophils expressed low levels of COX-2 mRNA, which rapidly increased after incubation with inflammatory agents. A characterization of the signal transduction pathways leading to COX-2 protein expression was initiated. In LPS-treated neutrophils, efficient induction of COX-2 required the presence of serum and involved ligand binding to the CD14 surface antigen. The specific inhibitor of p38 mitogen-activated protein kinase (p38 MAPK), SB 203580, had little effect on the induction of COX-2 expression in neutrophils, in contrast to what had been previously observed with other inflammatory cell types. Depending on the agonist present, ethanol differentially blocked the stimulated expression of COX-2, raising the possibility that phospholipase D activation might take part in the process of COX-2 induction. Major COX-2-derived prostanoids synthesized by inflammatory neutrophils were identified by liquid-chromatography and tandem mass-spectrometry as TXA2 and PGE2. The agonist-induced synthesis of TXA2 and PGE2 was effectively blocked by cycloheximide and by the specific COX-2 inhibitor NS-398. These results show that COX-2 can be induced in an active state by different classes of inflammatory mediators in the neutrophil. They support the concept that, in these cells, the COX-2 isoform is preeminent over COX-1 for the stimulated-production of prostanoids, and also suggest that neutrophil COX-2 displays a distinct profile of expression among circulatory cells. | - |
dc.language.iso | en | - |
dc.publisher | FEDERATION AMER SOC EXP BIOL | - |
dc.source.uri | http://www.fasebj.org/content/12/12/1109.abstract | - |
dc.subject | Neutrophils | - |
dc.subject | Humans | - |
dc.subject | Escherichia coli | - |
dc.subject | Tetradecanoylphorbol Acetate | - |
dc.subject | Isoenzymes | - |
dc.subject | Lipopolysaccharides | - |
dc.subject | Zymosan | - |
dc.subject | N-Formylmethionine Leucyl-Phenylalanine | - |
dc.subject | Tumor Necrosis Factor-alpha | - |
dc.subject | Granulocyte-Macrophage Colony-Stimulating Factor | - |
dc.subject | Membrane Proteins | - |
dc.subject | Antibodies | - |
dc.subject | Epitopes | - |
dc.subject | Blotting, Western | - |
dc.subject | Signal Transduction | - |
dc.subject | Phagocytosis | - |
dc.subject | Transcription, Genetic | - |
dc.subject | Gene Expression Regulation, Enzymologic | - |
dc.subject | Amino Acid Sequence | - |
dc.subject | Molecular Sequence Data | - |
dc.subject | Prostaglandin-Endoperoxide Synthases | - |
dc.subject | Cyclooxygenase 2 | - |
dc.subject | In Vitro Techniques | - |
dc.title | Expression and activity of prostoglandin endoperoxide synthase-2 in inflammatory human neutrophils | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1096/fasebj.12.12.1109 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | McColl, S. [0000-0003-0949-4660] | - |
Appears in Collections: | Aurora harvest 2 Microbiology and Immunology publications |
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