The DOI matches its Crossref record; 57 of the 57 references it cites were found in a registry or an index.
Activation of NADPH oxidase by AGE links oxidant stress to altered gene expression via RAGE
Abstract
Engagement of the receptor for advanced glycation end products (RAGE) by products of nonenzymatic glycation/oxidation triggers the generation of reactive oxygen species (ROS), thereby altering gene expression. Because dissection of the precise events by which ROS are generated via RAGE is relevant to the pathogenesis of complications in AGE-related disorders, such as diabetes and renal failure, we tested the hypothesis that activation of NADPH oxidase contributed, at least in part, to enhancing oxidant stress via RAGE. Here we show that incubation of human endothelial cells with AGEs on the surface of diabetic red blood cells, or specific AGEs, (carboxymethyl)lysine (CML)-modified adducts, prompted intracellular generation of hydrogen peroxide, cell surface expression of vascular cell adhesion molecule-1, and generation of tissue factor in a manner suppressed by treatment with diphenyliodonium, but not by inhibitors of nitric oxide. Consistent with an important role for NADPH oxidase, although macrophages derived from wild-type mice expressed enhanced levels of tissue factor upon stimulation with AGE, macrophages derived from mice deficient in a central subunit of NADPH oxidase, gp91phox, failed to display enhanced tissue factor in the presence of AGE. These findings underscore a central role of NADPH oxidase in AGE-RAGE-mediated generation of ROS and provide a mechanism for altered gene expression in AGE-related disorders.
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Cites
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RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease
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Self-citationVitamin E Supplementation and Cardiovascular Events in High-Risk Patients
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RAGE Mediates a Novel Proinflammatory Axis
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Self-citationAdvanced protein glycosylation in diabetes and aging
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Self-citationBlockade of RAGE-amphoterin signalling suppresses tumour growth and metastases
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The Receptor for Advanced Glycation End Products (RAGE) Is a Cellular Binding Site for Amphoterin
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Cited by
Mechanisms of Diabetic Complications
Forbes, J. M., & Cooper, M. E. (2013) · Physiological Reviews · doi:10.1152/physrev.00045.2011 · Cited by 2,890
Advanced Glycation End Products: Sparking the Development of Diabetic Vascular Injury
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Self-citationReactive Oxygen Species in Metabolic and Inflammatory Signaling
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Diabetes and Vascular Disease: Pathophysiology, Clinical Consequences, and Medical Therapy: Part I
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Metadata
- Authors
- Wautier, M.-P., Chappey, O., Corda, S., Stern, D. M., Schmidt, A. M., & Wautier, J.-L.
- Venue
- American Journal of Physiology-Endocrinology and Metabolism
- Publisher
- American Physiological Society
- Published
- 2001-05-01
- Volume
- 280
- Issue
- 5
- Pages
- E685-E694
- ISSN
- 0193-1849 (ISSN-L)
- 1522-1555
- OpenAlex
- W2121527030
- Cited by
- 1,072
- References
- 57
- FWCI
- 15.65
- Type
- journal article
- Language
- en
- Open access
- closed
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- Wautier, M.-P., Chappey, O., Corda, S., Stern, D. M., Schmidt, A. M., & Wautier, J.-L. (2001). Activation of NADPH oxidase by AGE links oxidant stress to altered gene expression via RAGE. American Journal of Physiology-Endocrinology and Metabolism. https://doi.org/10.1152/ajpendo.2001.280.5.e685
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