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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
17
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pubmed:dateCreated |
2000-6-2
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pubmed:abstractText |
In this study we examined the effect of oxidized low density lipoprotein (ox-LDL) on the intracellular production of reactive oxygen species (ROS) in bovine aortic endothelial cells (BAECs) and whether this increase occurs through its binding to the endothelial receptor lectin-like ox-LDL receptor-1 (LOX-1). Furthermore, this study also aimed to ascertain whether the binding of ox-LDL to LOX-1 is associated with NF-kappaB activation. ox-LDL induced a significant dose-dependent increase in ROS production after a 30-s incubation with BAECs (p < 0.01). ROS formation was markedly reduced in BAECs incubated with anti-LOX-1 monoclonal antibody (p < 0.001), while control nonimmune IgG produced no effect. ox-LDL induced a time- and dose-dependent significant increase in ROS formation only in CHO-K1 cells stably expressing bovine LOX-1 (p < 0.001), while no increase was present in CHO-K1 cells. The activation of the transcription factor NF-kappaB in BAECs was evident after a 5-min incubation with ox-LDL and was attenuated by anti-LOX-1 monoclonal antibody. The conclusion is that one of the pathophysiological consequences of ox-LDL binding to LOX-1 may be the activation of NF-kappaB through an increased ROS production.
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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/6-hydroxy-2,5,7,8-tetramethylchroman...,
http://linkedlifedata.com/resource/pubmed/chemical/Anticholesteremic Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Antioxidants,
http://linkedlifedata.com/resource/pubmed/chemical/Ascorbic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Chromans,
http://linkedlifedata.com/resource/pubmed/chemical/Fluoresceins,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/OLR1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Probucol,
http://linkedlifedata.com/resource/pubmed/chemical/Reactive Oxygen Species,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Oxidized LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Scavenger Receptors, Class E,
http://linkedlifedata.com/resource/pubmed/chemical/diacetyldichlorofluorescein,
http://linkedlifedata.com/resource/pubmed/chemical/oxidized low density lipoprotein
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
275
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12633-8
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:10777555-Animals,
pubmed-meshheading:10777555-Anticholesteremic Agents,
pubmed-meshheading:10777555-Antioxidants,
pubmed-meshheading:10777555-Ascorbic Acid,
pubmed-meshheading:10777555-CHO Cells,
pubmed-meshheading:10777555-Cattle,
pubmed-meshheading:10777555-Cells, Cultured,
pubmed-meshheading:10777555-Chromans,
pubmed-meshheading:10777555-Cricetinae,
pubmed-meshheading:10777555-Endothelium, Vascular,
pubmed-meshheading:10777555-Fluoresceins,
pubmed-meshheading:10777555-Humans,
pubmed-meshheading:10777555-Hydrogen Peroxide,
pubmed-meshheading:10777555-Lipoproteins, LDL,
pubmed-meshheading:10777555-NF-kappa B,
pubmed-meshheading:10777555-Probucol,
pubmed-meshheading:10777555-Protein Binding,
pubmed-meshheading:10777555-Reactive Oxygen Species,
pubmed-meshheading:10777555-Receptors, LDL,
pubmed-meshheading:10777555-Receptors, Oxidized LDL,
pubmed-meshheading:10777555-Scavenger Receptors, Class E,
pubmed-meshheading:10777555-Time Factors
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pubmed:year |
2000
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pubmed:articleTitle |
Oxidized low density lipoprotein (ox-LDL) binding to ox-LDL receptor-1 in endothelial cells induces the activation of NF-kappaB through an increased production of intracellular reactive oxygen species.
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pubmed:affiliation |
Department of Biomedical and Surgical Sciences, Verona University, 37134 Verona, Italy. comina@medicinad.univr.it
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pubmed:publicationType |
Journal Article
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