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rdf:type |
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lifeskim:mentions |
umls-concept:C0011847,
umls-concept:C0030012,
umls-concept:C0035820,
umls-concept:C0037083,
umls-concept:C0162574,
umls-concept:C0205263,
umls-concept:C0225336,
umls-concept:C1415619,
umls-concept:C1417701,
umls-concept:C1545588,
umls-concept:C1710082,
umls-concept:C1801960
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pubmed:issue |
4
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pubmed:dateCreated |
2011-3-22
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pubmed:abstractText |
Hyperglycemia and diabetes are associated with increased formation of advanced glycation end products and enhanced oxidative stress, leading to the progression of diabetic vascular disease. We have investigated the mechanisms by which AGE-modified bovine albumin (AGE-BSA) induces reactive oxygen species (ROS) generation, leading to nuclear factor-erythroid 2-related factor (Nrf2) dependent induction of the antioxidant genes heme oxygenase-1 (HO-1) and NADPH:quinone oxidoreductase 1 (NQO1) in bovine aortic endothelial cells.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Free Radical Scavengers,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosylation End Products, Advanced,
http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase-1,
http://linkedlifedata.com/resource/pubmed/chemical/NAD(P)H Dehydrogenase (Quinone),
http://linkedlifedata.com/resource/pubmed/chemical/NF-E2-Related Factor 2,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Reactive Oxygen Species,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin, Bovine,
http://linkedlifedata.com/resource/pubmed/chemical/advanced glycation end...
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1590-3729
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pubmed:author |
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pubmed:copyrightInfo |
Copyright © 2010 Elsevier B.V. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:volume |
21
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
277-85
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pubmed:meshHeading |
pubmed-meshheading:20227863-Animals,
pubmed-meshheading:20227863-Cattle,
pubmed-meshheading:20227863-Cell Nucleus,
pubmed-meshheading:20227863-Cells, Cultured,
pubmed-meshheading:20227863-Diabetes Mellitus,
pubmed-meshheading:20227863-Endothelium, Vascular,
pubmed-meshheading:20227863-Enzyme Induction,
pubmed-meshheading:20227863-Free Radical Scavengers,
pubmed-meshheading:20227863-Glycosylation End Products, Advanced,
pubmed-meshheading:20227863-Heme Oxygenase-1,
pubmed-meshheading:20227863-Hyperglycemia,
pubmed-meshheading:20227863-NAD(P)H Dehydrogenase (Quinone),
pubmed-meshheading:20227863-NF-E2-Related Factor 2,
pubmed-meshheading:20227863-Oxidative Stress,
pubmed-meshheading:20227863-Protein Transport,
pubmed-meshheading:20227863-RNA, Messenger,
pubmed-meshheading:20227863-Reactive Oxygen Species,
pubmed-meshheading:20227863-Serum Albumin, Bovine,
pubmed-meshheading:20227863-Signal Transduction,
pubmed-meshheading:20227863-Time Factors
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pubmed:year |
2011
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pubmed:articleTitle |
Induction of HO-1 and redox signaling in endothelial cells by advanced glycation end products: a role for Nrf2 in vascular protection in diabetes.
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pubmed:affiliation |
Cardiovascular Division, School of Medicine, King's College London, 150 Stamford Street, London SE1 9NH, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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