pubmed-article:16614756 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16614756 | lifeskim:mentions | umls-concept:C0007227 | lld:lifeskim |
pubmed-article:16614756 | lifeskim:mentions | umls-concept:C0033551 | lld:lifeskim |
pubmed-article:16614756 | lifeskim:mentions | umls-concept:C1419067 | lld:lifeskim |
pubmed-article:16614756 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:16614756 | pubmed:dateCreated | 2006-5-3 | lld:pubmed |
pubmed-article:16614756 | pubmed:abstractText | We investigated the mechanisms by which inhibitors of prostaglandin G/H synthase-2 (PGHS-2; known colloquially as COX-2) increase the incidence of myocardial infarction and stroke. These inhibitors are believed to exert both their beneficial and their adverse effects by suppression of PGHS-2-derived prostacyclin (PGI(2)) and PGE(2). Therefore, the challenge remains to identify a mechanism whereby PGI(2) and PGE(2) expression can be suppressed while avoiding adverse cardiovascular events. Here, selective inhibition, knockout, or mutation of PGHS-2, or deletion of the receptor for PGHS-2-derived PGI(2), was shown to accelerate thrombogenesis and elevate blood pressure in mice. These responses were attenuated by COX-1 knock down, which mimics the beneficial effects of low-dose aspirin. PGE(2) biosynthesis is catalyzed by the coordinate actions of COX enzymes and microsomal PGE synthase-1 (mPGES-1). We show that deletion of mPGES-1 depressed PGE(2) expression, augmented PGI(2) expression, and had no effect on thromboxane biosynthesis in vivo. Most importantly, mPGES-1 deletion affected neither thrombogenesis nor blood pressure. These results suggest that inhibitors of mPGES-1 may retain their antiinflammatory efficacy by depressing PGE(2), while avoiding the adverse cardiovascular consequences associated with PGHS-2-mediated PGI(2) suppression. | lld:pubmed |
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pubmed-article:16614756 | pubmed:language | eng | lld:pubmed |
pubmed-article:16614756 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16614756 | pubmed:citationSubset | AIM | lld:pubmed |
pubmed-article:16614756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16614756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:16614756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16614756 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16614756 | pubmed:month | May | lld:pubmed |
pubmed-article:16614756 | pubmed:issn | 0021-9738 | lld:pubmed |
pubmed-article:16614756 | pubmed:author | pubmed-author:FunkColin DCD | lld:pubmed |
pubmed-article:16614756 | pubmed:author | pubmed-author:YuYingY | lld:pubmed |
pubmed-article:16614756 | pubmed:author | pubmed-author:WangMiaoM | lld:pubmed |
pubmed-article:16614756 | pubmed:author | pubmed-author:ChengYanY | lld:pubmed |
pubmed-article:16614756 | pubmed:author | pubmed-author:FitzgeraldGar... | lld:pubmed |
pubmed-article:16614756 | pubmed:author | pubmed-author:LawsonJohnJ | lld:pubmed |
pubmed-article:16614756 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16614756 | pubmed:volume | 116 | lld:pubmed |
pubmed-article:16614756 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16614756 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16614756 | pubmed:pagination | 1391-9 | lld:pubmed |
pubmed-article:16614756 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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