Impairment of vascular endothelial nitric oxide synthase activity by advanced glycation end products
Abstract
Endothelial damage is believed to play a key role in the development of both micro‐ and macrovascular disease in diabetes, and advanced glycation end products (AGEs) may contribute importantly to this. To determine whether glucose‐derived AGEs can cause endothelial dysfunction, we examined the effects of albumin AGE‐modified by glucose (AGE‐Glu) both in vivo, after injection into rabbit femoral artery, and in vitro on rabbit aortic rings and cultured human umbilical vein endothelial cells (HUVEC). Exposure of blood vessels to AGE‐Glu, in vivo and in vitro, inhibited endothelium‐dependent vasorelaxation, whereas unmodified albumin did not. In isolated rabbit aorta, this effect was reversible after AGE‐Glu washout, and the response to the endothelium‐independent vasodilator sodium nitroprusside was unaffected by AGE‐Glu. In HUVEC, AGE‐Glu inhibited endothelial nitric oxide synthase activity, and this was associated with a decrease in serine phosphorylation of this enzyme. Longer term (72 h) incubation decreased HUVEC viability. Use of specific antibodies demonstrated that these effects were mediated by N ε ‐(carboxymethyl)lysine (CML), an important AGE found in vivo, and by the AGE‐R1 receptor. Furthermore, these effects all occurred at CML concentrations similar to those found in the plasma of diabetic patients. These results suggest an important role of AGE in the pathogenesis of diabetic vasculopathy.
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Superoxide can be generated by the oxygenase/heme domain, in a Ca2+/CaM-dependent way, or independently by the reductase domain from Ca2+/CaM.
“Superoxide can be generated by the oxygenase/heme domain, in a Ca2+/CaM-dependent way, or independently by the reductase domain from Ca2+/CaM (653, 1032).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [1032]
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- Authors
- Biao, X., Chibber, R., Ruggiero, D., Kohner, E., Ritter, J., & Ferro, A.
- Affiliations
- Center for Cardiovascular Biology & Medicine King's College London London UK
- King's College London (GB)
- Diabetic Microangiopathy Research Unit Villeurbanne France
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2003-05-08
- Volume
- 17
- Issue
- 10
- Pages
- 1289-1291
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W2159948606
- Cited by
- 195
- References
- 62
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 4 · 2023: 6 · 2022: 14 · 2021: 2 · 2020: 12 · 2019: 11 · 2018: 8 · 2017: 7 · 2016: 8 · 2015: 6 · 2014: 6 · 2013: 6 · 2012: 13
- FWCI
- 3.41
- Type
- journal article
- Language
- en
- Update notices
- erratum (2003-12-01)
- Open access
- closed
- Locations
- The FASEB Journal (publishedVersion)
- PubMed (publishedVersion)
- Research Portal (King's College London) (submittedVersion)
- Funders
- Wellcome Trust
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiovascular Health and Disease Prevention
- Keywords
- advanced glycation end products, endothelial nitric oxide synthase, endothelial dysfunction, diabetic vascular disease, carboxymethyllysine, serine phosphorylation, endothelium-dependent relaxation, human umbilical vein endothelial cells, albumin
- MeSH terms
- Receptor for Advanced Glycation End Products, Animals, Antibodies, Aorta, Arginine, Blood Pressure, Cells, Cultured, Citrulline, Diabetes Mellitus, Endothelium, Vascular, Enzyme Inhibitors, Female, Femoral Artery, Humans, Lysine, Male, Models, Biological, Nitric Oxide, Rabbits, Receptors, Immunologic, Vasodilation, Glycation End Products, Advanced, Nitric Oxide Synthase, NG-Nitroarginine Methyl Ester, Nitric Oxide Synthase Type III, In Vitro Techniques
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