Source:http://linkedlifedata.com/resource/pubmed/id/16945374
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2007-5-18
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pubmed:abstractText |
Apolipoprotein A-IV (apoA-IV) inhibits lipid peroxidation, thus demonstrating potential anti-atherogenic properties. The aim of this study was to investigate how the inhibition of low density lipoprotein (LDL) oxidation was influenced by common apoA-IV isoforms. Recombinant wild type apoA-IV (100 microg/ml) significantly inhibited the oxidation of LDL (50 microg protein/ml) by 5 microM CuSO(4) (P<0.005), but not by 100 microM CuSO(4), suggesting that it may act by binding copper ions. ApoA-IV also inhibited the oxidation of LDL by the water-soluble free-radical generator 2,2'-azobis(amidinopropane) dihydrochloride (AAPH; 1 mM), as shown by the two-fold increase in the time for half maximal conjugated diene formation (T(1/2); P<0.05) suggesting it can also scavenge free radicals in the aqueous phase. Compared to wild type apoA-IV, apoA-IV-S347 decreased T(1/2) by 15% (P=0.036) and apoA-IV-H360 increased T(1/2) by 18% (P=0.046). All apoA-IV isoforms increased the relative electrophoretic mobility of native LDL, suggesting apoA-IV can bind to LDL and acts as a site-specific antioxidant. The reduced inhibition of LDL oxidation by apoA-IV-S347 compared to wild type apoA-IV may account for the previous association of the APOA4 S347 variant with increased CHD risk and oxidative stress.
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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/2,2'-azobis(2-amidinopropane),
http://linkedlifedata.com/resource/pubmed/chemical/APOA5 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Amidines,
http://linkedlifedata.com/resource/pubmed/chemical/Antioxidants,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins A,
http://linkedlifedata.com/resource/pubmed/chemical/Copper Sulfate,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9150
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
192
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
266-74
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pubmed:dateRevised |
2011-9-22
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pubmed:meshHeading |
pubmed-meshheading:16945374-Amidines,
pubmed-meshheading:16945374-Antioxidants,
pubmed-meshheading:16945374-Apolipoproteins A,
pubmed-meshheading:16945374-Copper Sulfate,
pubmed-meshheading:16945374-Humans,
pubmed-meshheading:16945374-Lipid Peroxidation,
pubmed-meshheading:16945374-Lipoproteins, LDL,
pubmed-meshheading:16945374-Mutagenesis, Site-Directed,
pubmed-meshheading:16945374-Oxidation-Reduction,
pubmed-meshheading:16945374-Protein Isoforms
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pubmed:year |
2007
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pubmed:articleTitle |
Common variants of apolipoprotein A-IV differ in their ability to inhibit low density lipoprotein oxidation.
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pubmed:affiliation |
Centre for Cardiovascular Genetics, British Heart Foundation Laboratories, Royal Free and University College London Medical School, London, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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