| pubmed-article:11956198 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11956198 | lifeskim:mentions | umls-concept:C0025519 | lld:lifeskim |
| pubmed-article:11956198 | lifeskim:mentions | umls-concept:C0243192 | lld:lifeskim |
| pubmed-article:11956198 | lifeskim:mentions | umls-concept:C0003692 | lld:lifeskim |
| pubmed-article:11956198 | lifeskim:mentions | umls-concept:C0166415 | lld:lifeskim |
| pubmed-article:11956198 | lifeskim:mentions | umls-concept:C0079411 | lld:lifeskim |
| pubmed-article:11956198 | lifeskim:mentions | umls-concept:C0299477 | lld:lifeskim |
| pubmed-article:11956198 | pubmed:issue | 26 | lld:pubmed |
| pubmed-article:11956198 | pubmed:dateCreated | 2002-6-24 | lld:pubmed |
| pubmed-article:11956198 | pubmed:abstractText | The recent demonstrations that cyclooxygenase-2 and leukocyte-type 12-lipoxygenase (LOX) efficiently oxygenate 2-arachidonylglycerol (2-AG) prompted an investigation into related oxygenases capable of metabolizing this endogenous cannabinoid receptor ligand. We evaluated the ability of six LOXs to catalyze the hydroperoxidation of 2-AG. Soybean 15-LOX, rabbit reticulocyte 15-LOX, human 15-LOX-1, and human 15-LOX-2 oxygenate 2-AG, providing 15(S)-hydroperoxyeicosatetraenoic acid glyceryl ester. In contrast, potato and human 5-LOXs do not efficiently metabolize this endocannabinoid. Among a series of structurally related arachidonyl esters, arachidonylglycerols serve as the preferred substrates for 15-LOXs. Steady-state kinetic analysis demonstrates that both 15-LOX-1 and 15-LOX-2 oxygenate 2-AG comparably or preferably to arachidonic acid. Furthermore, 2-AG treatment of COS-7 cells transiently transfected with human 15-LOX expression vectors or normal human epidermal keratinocytes results in the production and extracellular release of 15-hydroxyeicosatetraenoic acid glyceryl ester (15-HETE-G), establishing that lipoxygenase metabolism of 2-AG occurs in an eukaryotic cellular environment. Investigations into the potential biological actions of 15-HETE-G indicate that this lipid, in contrast to its free-acid counterpart, acts as a peroxisome proliferator-activated receptor alpha agonist. The results demonstrate that 15-LOXs are capable of acting on 2-AG to provide 15-HETE-G and elucidate a potential role for endocannabinoid oxygenation in the generation of peroxisome proliferator-activated receptor alpha agonists. | lld:pubmed |
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| pubmed-article:11956198 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11956198 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11956198 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11956198 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11956198 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11956198 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:11956198 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11956198 | pubmed:author | pubmed-author:BoeglinWillia... | lld:pubmed |
| pubmed-article:11956198 | pubmed:author | pubmed-author:MarnettLawren... | lld:pubmed |
| pubmed-article:11956198 | pubmed:author | pubmed-author:BrashAlan RAR | lld:pubmed |
| pubmed-article:11956198 | pubmed:author | pubmed-author:DuBoisRaymond... | lld:pubmed |
| pubmed-article:11956198 | pubmed:author | pubmed-author:GuptaRajnish... | lld:pubmed |
| pubmed-article:11956198 | pubmed:author | pubmed-author:KozakKevin... | lld:pubmed |
| pubmed-article:11956198 | pubmed:author | pubmed-author:MoodyJohn SJS | lld:pubmed |
| pubmed-article:11956198 | pubmed:author | pubmed-author:JiChuanC | lld:pubmed |
| pubmed-article:11956198 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11956198 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:11956198 | pubmed:volume | 277 | lld:pubmed |
| pubmed-article:11956198 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11956198 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11956198 | pubmed:pagination | 23278-86 | lld:pubmed |
| pubmed-article:11956198 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:11956198 | pubmed:meshHeading | pubmed-meshheading:11956198... | lld:pubmed |
| pubmed-article:11956198 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11956198 | pubmed:articleTitle | 15-Lipoxygenase metabolism of 2-arachidonylglycerol. Generation of a peroxisome proliferator-activated receptor alpha agonist. | lld:pubmed |
| pubmed-article:11956198 | pubmed:affiliation | Department of Biochemistry, Vanderbilt-Ingram Cancer Center and Center in Molecular Toxicology, Nashville, Tennessee, USA. | lld:pubmed |
| pubmed-article:11956198 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11956198 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11956198 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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