Advanced glycation end products quench nitric oxide in vitro

Uhlmann, Susann; Rezzoug, Karen; Friedrichs, Ulrike; Stephan, Holger; Wiedemann, Peter

doi:10.1007/s00417-002-0548-x

Cited by 12 publications

(8 citation statements)

References 43 publications

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“…AGEs-related decrease of eNOS mRNA expression associated with low NOS activity and NO avaibility, by quenching NO [39], reduces endothelial cells' antiplatelet activity and increases expression of adhesion molecules [40], as well as PMN-endothelial cell adhesion [41]. This fits well with the recent data, which have shown that AGEs enhance the expression of endothelial cell adhesion molecules [10,11].…”

Section: Discussionsupporting

confidence: 87%

Effect of advanced glycation end-products on gene expression and synthesis of TNF-α and endothelial nitric oxide synthase by endothelial cells

Rashid

Benchetrit

Fishman

et al. 2004

Kidney International

106

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Section: Discussionsupporting

confidence: 87%

Effect of advanced glycation end-products on gene expression and synthesis of TNF-α and endothelial nitric oxide synthase by endothelial cells

Rashid

Benchetrit

Fishman

et al. 2004

Kidney International

106

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“…AGE cross-linking in vessel wall collagen increases the area of the extracellular matrix, resulting in increased stiffness of the vessel wall. AGEs have also been shown to interact with NO, reducing its bioavailability and activity (22), and to increase the adhesion of macromolecules, such as macrophages and LDL, to the vessel wall (23), and the adhesion of leukocytes to coronary fibroblasts (24). AGEs have been observed in atherosclerotic plaques, foam cells, and fatty streaks (25).…”

Section: Discussionmentioning

confidence: 99%

Skin Intrinsic Fluorescence Is Associated With Coronary Artery Disease in Individuals With Long Duration of Type 1 Diabetes

et al. 2012

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OBJECTIVESkin intrinsic fluorescence (SIF) reflects many factors, including the presence of certain advanced glycation end products. We investigated whether SIF was associated with coronary artery disease (CAD) in type 1 diabetes and whether this relationship was independent of renal disease.RESEARCH DESIGN AND METHODSSIF was measured in 112 subjects from the Pittsburgh Epidemiology of Diabetes Complications (EDC) study and 60 from MedStar Health Research Institute when mean age and diabetes duration were 48 and 36 years, respectively. Cumulative glycemic exposure (updated mean A1C) represented a mean of 18 years’ follow-up in EDC and 10.3 in MedStar.RESULTSOf the 172 participants, 30 had CAD (15 male and 15 female). SIF levels were higher in those with CAD (P < 0.0001). SIF was strongly associated with CAD (odds ratio [OR] 3.5 [95% CI 2.1–6.1]). After age, duration, and updated mean A1C were controlled for, SIF remained associated with CAD (2.4 [1.3–4.4]), more strongly in men (5.6 [2.1–14.6]) than in women (1.4 [0.61–3.3]). As there was no significant sex interaction, further analyses were conducted combining the sexes. Further accounting for sex and nephropathy status did not improve the model fit, though with nephropathy in the model, the OR for SIF was reduced to 1.7 (95% CI 0.89–3.4).CONCLUSIONSSIF has a significant cross-sectional association with CAD. This association is strongly linked to age and duration and, to a lesser degree, to mean A1C and renal disease. SIF therefore may be a useful overall marker of CAD risk in type 1 diabetes.

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“…Thus, the AGE‐RAGE system is theoretically able to account for most of the observed spectrum of changes in nitrergic neurones in diabetes. The interaction between NO and AGEs may be even more complex: AGEs can also quench NO; 42 in turn NO can reduce the formation of AGEs 43 . The formation of AGEs in diabetes can therefore lead to suppression of NO in many ways; this in turn can further enhance AGE production, amplifying the original insult.…”

Section: Discussionmentioning

confidence: 99%

Suppression of nNOS expression in rat enteric neurones by the receptor for advanced glycation end‐products

Korenaga

Micci

Taglialatela

et al. 2006

Neurogastroenterology Motil

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Diabetes mellitus results in a loss of neuronal nitric oxide synthase (nNOS) expression in the myenteric plexus but the underlying mechanisms remain unknown. We hypothesized that this may be mediated by advanced glycation end-products (AGEs), a class of modified protein adducts formed by non-enzymatic glycation that interact with the receptor for AGE (RAGE) and which are important in the pathogenesis of other diabetic complications. Whole mount preparations of longitudinal muscles with adherent myenteric plexus (LM-MPs) from the duodenum of adult male rats were exposed to glycated bovines serum albumin (AGE-BSA) or BSA for 24 h. Western blotting, immunohistochemistry and real-time reverse transcriptase polymerase chain reaction (RT-PCR) for mRNA showed a significant reduction in nNOS expression in LM-MPs after exposure to AGE-BSA. NO release, as measured by the Griess reaction, was also significantly reduced by AGE-BSA. A neutralizing antibody against RAGE attenuated the reduction of nNOS protein caused by AGE-BSA. Immunohistochemistry revealed co-localization of RAGE expression with Hu, a marker for neuronal cells but not for S-100, a glial marker. Advanced glycation end-products reduce nNOS expression in the rat myenteric neurones acting via the receptor RAGE. Our results suggest novel pathways for disruption of the nitrergic phenotype in diabetes.

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Advanced glycation end products quench nitric oxide in vitro

Cited by 12 publications

References 43 publications

Effect of advanced glycation end-products on gene expression and synthesis of TNF-α and endothelial nitric oxide synthase by endothelial cells

Effect of advanced glycation end-products on gene expression and synthesis of TNF-α and endothelial nitric oxide synthase by endothelial cells

Skin Intrinsic Fluorescence Is Associated With Coronary Artery Disease in Individuals With Long Duration of Type 1 Diabetes

Suppression of nNOS expression in rat enteric neurones by the receptor for advanced glycation end‐products

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