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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
1996-2-27
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pubmed:abstractText |
Oxidative modification of LDL plays an important role in early atherogenesis but the mechanisms, nonenzymatic and/or enzymatic, by which LDL is oxidized in vivo remain to be established. Several lines of evidence suggest that cellular 15-lipoxygenase (arachidonate 15-oxidoreductase, EC.1.13.11.13) (15-LO) may contribute to oxidative modification of LDL, including recent studies demonstrating that murine fibroblasts overexpressing 15-LO have an enhanced capacity to oxidize LDL in the medium. The present studies were undertaken to better understand the mechanisms by which cells expressing 15-LO bring about oxidative modification of LDL. LDL incubated 1-2 h with the 15-LO-enriched cells showed a much higher lipoperoxide (LOOH) content than did LDL incubated with control cells. By far the largest absolute increase occurred in cholesteryl ester hydroperoxide (CE-OOH), a much lesser increase in free fatty acid hydroperoxides (FFA-OOH), and only a very small increase in phospholipid hydroperoxides (PL-OOH). Addition of EDTA to the medium abolished these increases in LDL lipid hydroperoxides. Enrichment of LDL with probucol or vitamin E also prevented CE-OOH accumulation. Incubation of LDL with linoleic acid hydroperoxide in the absence of cells also caused a significant increase in CE-OOH and this was markedly inhibited by EDTA. These findings provide further evidence for the potential of 15-LO to participate in LDL oxidation by way of a mechanism involving introduction of LOOH into the LDL particle followed by metal-catalyzed propagation.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arachidonate 15-Lipoxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/Copper,
http://linkedlifedata.com/resource/pubmed/chemical/Edetic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Lipid Peroxides,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0022-2275
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
36
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1996-2004
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:8558087-Animals,
pubmed-meshheading:8558087-Arachidonate 15-Lipoxygenase,
pubmed-meshheading:8558087-Cells, Cultured,
pubmed-meshheading:8558087-Chromatography, High Pressure Liquid,
pubmed-meshheading:8558087-Copper,
pubmed-meshheading:8558087-Edetic Acid,
pubmed-meshheading:8558087-Fibroblasts,
pubmed-meshheading:8558087-Gene Expression,
pubmed-meshheading:8558087-Gene Transfer Techniques,
pubmed-meshheading:8558087-Humans,
pubmed-meshheading:8558087-Kinetics,
pubmed-meshheading:8558087-Lipid Peroxidation,
pubmed-meshheading:8558087-Lipid Peroxides,
pubmed-meshheading:8558087-Lipoproteins, LDL,
pubmed-meshheading:8558087-Luminescent Measurements,
pubmed-meshheading:8558087-Mice,
pubmed-meshheading:8558087-Recombinant Proteins
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pubmed:year |
1995
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pubmed:articleTitle |
Lipoperoxides in LDL incubated with fibroblasts that overexpress 15-lipoxygenase.
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pubmed:affiliation |
Department of Medicine, University of California, San Diego, La Jolla 92093-0682, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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