Source:http://linkedlifedata.com/resource/pubmed/id/10400665
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
29
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pubmed:dateCreated |
1999-8-19
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pubmed:abstractText |
The objectives of this study were to estimate the structure of the lipid hydroperoxide-modified lysine residue and to prove the presence of the adducts in vivo. The reaction of lipid hydroperoxide toward the lysine moiety was investigated employing N-benzoyl-glycyl-L-lysine (Bz-Gly-Lys) as a model compound of Lys residues in protein and 13-hydroperoxyoctadecadienoic acid (13-HPODE) as a model of the lipid hydroperoxides. One of the products, compound X, was isolated from the reaction mixture of 13-HPODE and Bz-Gly-Lys and was then identified as N-benzoyl-glycyl-Nepsilon-(hexanonyl)lysine. To prove the formation of Nepsilon-(hexanonyl)lysine, named HEL, in protein exposed to the lipid hydroperoxide, the antibody to the synthetic hexanonyl protein was prepared and then characterized in detail. Using the anti-HEL antibody, the presence of HEL in the lipid hydroperoxide-modified proteins and oxidized LDL was confirmed. Furthermore, the positive staining by anti-HEL antibody was observed in human atherosclerotic lesions using an immunohistochemical technique. The amide-type adduct may be a useful marker for the lipid hydroperoxide-derived modification of biomolecules.
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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/13-hydroperoxy-9,11-octadecadienoic...,
http://linkedlifedata.com/resource/pubmed/chemical/Linoleic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Lipid Peroxides,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
20406-14
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:10400665-Humans,
pubmed-meshheading:10400665-Immunohistochemistry,
pubmed-meshheading:10400665-Linoleic Acids,
pubmed-meshheading:10400665-Lipid Peroxides,
pubmed-meshheading:10400665-Lysine,
pubmed-meshheading:10400665-Magnetic Resonance Spectroscopy,
pubmed-meshheading:10400665-Molecular Structure,
pubmed-meshheading:10400665-Oxidative Stress,
pubmed-meshheading:10400665-Proteins
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pubmed:year |
1999
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pubmed:articleTitle |
Formation of Nepsilon-(hexanonyl)lysine in protein exposed to lipid hydroperoxide. A plausible marker for lipid hydroperoxide-derived protein modification.
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pubmed:affiliation |
School of Humanities for Environmental Policy and Technology, Himeji Institute of Technology, Himeji 670-0092, USA. yojikato@hept.himeji-tech.ac.jp
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pubmed:publicationType |
Journal Article
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