| pubmed-article:7642610 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7642610 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:7642610 | lifeskim:mentions | umls-concept:C0015684 | lld:lifeskim |
| pubmed-article:7642610 | lifeskim:mentions | umls-concept:C0051405 | lld:lifeskim |
| pubmed-article:7642610 | lifeskim:mentions | umls-concept:C0125903 | lld:lifeskim |
| pubmed-article:7642610 | lifeskim:mentions | umls-concept:C0038592 | lld:lifeskim |
| pubmed-article:7642610 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:7642610 | pubmed:issue | 33 | lld:pubmed |
| pubmed-article:7642610 | pubmed:dateCreated | 1995-9-18 | lld:pubmed |
| pubmed-article:7642610 | pubmed:abstractText | Human prostaglandin-endoperoxide H synthase-1 and -2 (hPGHS-1 and hPGHS-2) were expressed by transient transfection of COS-1 cells. Microsomes prepared from the transfected cells were used to measure the rates of oxygenation of several 18- and 20-carbon polyunsaturated fatty acid substrates including eicosapentaenoic, arachidonic, dihomo-gamma-linolenic > alpha-linolenic (delta 9, 12, 15), gamma-linolenic, and linoleic acids. Comparisons of kcat/Km values indicate that the order of efficiency of oxygenation is arachidonate > dihomo-gamma-linolenate > linoleate > alpha-linolenate for both isozymes; while the order of efficiency was the same for hPGHS-1 and hPGHS-2, alpha-linolenate was a particularly poor substrate for hPGHS-1. Gamma-Linolenate and eicosapentaenoate were poor substrates for both isozymes, but in each case, these two fatty acids were better substrates for hPGHS-2 than hPGHS-1. These studies of substrate specificities are consistent with previous studies of the interactions of PGHS isozymes with nonsteroidal anti-inflammatory drugs that have indicated that the cyclooxygenase active site of PGHS-2 is somewhat larger and more accommodating than that of PGHS-1. The major products formed from linoleate and alpha-linolenate were characterized. 13-Hydroxy-(9Z,11E)-octadecadienoic acid was found to be the main product formed from alpha-linoleate by both isozymes. The major products of oxygenation of alpha-linolenate were determined by mass spectrometry to be 12-hydroxy-(9Z,13E/Z,15Z)-octadecatrienoic acids. This result suggests that alpha-linolenate is positioned in the cyclooxygenase active site with a kink in the carbon chain such that hydrogen abstraction occurs from the omega 5-position in contrast to abstraction of the omega 8-hydrogen from other substrates. | lld:pubmed |
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| pubmed-article:7642610 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7642610 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7642610 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7642610 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:7642610 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:7642610 | pubmed:author | pubmed-author:WatsonJ TJT | lld:pubmed |
| pubmed-article:7642610 | pubmed:author | pubmed-author:SmithW LWL | lld:pubmed |
| pubmed-article:7642610 | pubmed:author | pubmed-author:LagardeMM | lld:pubmed |
| pubmed-article:7642610 | pubmed:author | pubmed-author:XuNN | lld:pubmed |
| pubmed-article:7642610 | pubmed:author | pubmed-author:HuangZ HZH | lld:pubmed |
| pubmed-article:7642610 | pubmed:author | pubmed-author:LaneuvilleOO | lld:pubmed |
| pubmed-article:7642610 | pubmed:author | pubmed-author:DeWittD LDL | lld:pubmed |
| pubmed-article:7642610 | pubmed:author | pubmed-author:GageD ADA | lld:pubmed |
| pubmed-article:7642610 | pubmed:author | pubmed-author:BreuerD KDK | lld:pubmed |
| pubmed-article:7642610 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7642610 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:7642610 | pubmed:volume | 270 | lld:pubmed |
| pubmed-article:7642610 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7642610 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7642610 | pubmed:pagination | 19330-6 | lld:pubmed |
| pubmed-article:7642610 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:7642610 | pubmed:meshHeading | pubmed-meshheading:7642610-... | lld:pubmed |
| pubmed-article:7642610 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7642610 | pubmed:articleTitle | Fatty acid substrate specificities of human prostaglandin-endoperoxide H synthase-1 and -2. Formation of 12-hydroxy-(9Z, 13E/Z, 15Z)- octadecatrienoic acids from alpha-linolenic acid. | lld:pubmed |
| pubmed-article:7642610 | pubmed:affiliation | Department of Biochemistry, Michigan State University, East Lansing 48824, USA. | lld:pubmed |
| pubmed-article:7642610 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7642610 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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