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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1997-4-16
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pubmed:abstractText |
To determine whether lipid peroxidation is required for apolipoprotein B (apoB) carbonyl formation of human low-density lipoproteins (LDL) during copper-mediated oxidation, we investigated oxidation of native and probucol-preloaded LDL by measuring thiobarbituric acid-reactive substances (TBARS) and apoB carbonyls. Probucol was used because it is known to inhibit lipid peroxidation, but not protein modification. During copper-mediated oxidation, apoB carbonyls formed in a time-dependent manner; high copper concentrations (> or = 30 microM) resulted in saturation of apoB carbonyl content. ApoB carbonyl formation and lipid peroxidation were linearly related during incubation of LDL with copper for 3 h. During Cu(2+)-mediated LDL oxidation of probucol-LDL, TBARS production was very low, nonetheless apoB carbonyls increased significantly, and vitamin E was depleted. Bovine serum albumin (fatty acid free; BSA) oxidation in the presence of trace amounts of LDL, linoleic acid, or tert-butyl hydroperoxide was used to further understand the role of lipid peroxidation in apoB carbonyl formation. Protein carbonyl formation during BSA incubation with copper (either Cu+ or Cu2+) was trivial; however, further addition of linoleic acid (1:1, m/m), trace amounts of LDL (10 micrograms/ml), or tert-butyl hydroperoxide (1:1, m/m) markedly increased protein carbonyl formation. These results demonstrate that lipid peroxidation enhances copper-mediated carbonyl formation and suggest that copper ions react with LDL lipid hydroperoxides producing the necessary reactive species.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anticholesteremic Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins B,
http://linkedlifedata.com/resource/pubmed/chemical/Copper,
http://linkedlifedata.com/resource/pubmed/chemical/Free Radicals,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Probucol,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin, Bovine
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0003-9861
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
339
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
165-71
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9056246-Animals,
pubmed-meshheading:9056246-Anticholesteremic Agents,
pubmed-meshheading:9056246-Apolipoproteins B,
pubmed-meshheading:9056246-Cattle,
pubmed-meshheading:9056246-Copper,
pubmed-meshheading:9056246-Free Radicals,
pubmed-meshheading:9056246-Humans,
pubmed-meshheading:9056246-Hydrogen Peroxide,
pubmed-meshheading:9056246-Lipoproteins, LDL,
pubmed-meshheading:9056246-Oxidation-Reduction,
pubmed-meshheading:9056246-Probucol,
pubmed-meshheading:9056246-Serum Albumin, Bovine
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pubmed:year |
1997
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pubmed:articleTitle |
Apolipoprotein B carbonyl formation is enhanced by lipid peroxidation during copper-mediated oxidation of human low-density lipoproteins.
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pubmed:affiliation |
Department of Molecular and Cell Biology, University of California at Berkeley 94720-3200, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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