Formation of plasma advanced glycosylation end products (AGEs) has no influence on plasma viscosity

Mellinghoff, Achim C.; Reininger, Armin J.; Wuerth, Jean-Paul; Founds, Hank; Landgraf, R.; Hepp, K. D.

doi:10.1002/(sici)1096-9136(199710)14:10<832::aid-dia492>3.0.co;2-9

Cited by 23 publications

(11 citation statements)

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“…Of note, unlike most other "diabetogenic" factors, AGEs are known to contribute to other diabetic organ toxicity (15,(25)(26)(27)(28)(29)(30)(31)(32)(33). Of interest, CML and MG-related derivatives were negligible in L-AGE diet, relative to the H-AGE diet; otherwise, these two preparations were identical (37). While no class of heat-enhanced compounds has been implicated in the etiology of type 1 diabetes thus far, AGEs are known to manifest an intriguing array of cellular effects, namely oxidant stress, nuclear factor (NF)-B activation, or apoptosis and death (15,17,34,36), and may constitute such a class.…”

Section: Discussionmentioning

confidence: 99%

“…CML-BSA and methylglyoxal-BSA derivatives (MG) in rodent food were assessed by enzyme-linked immunosorbent assay (ELISA) using monoclonal antibodies anti-CML-KLH (4G9) (Alteon, Northvale, NJ) (ELISA-1) or anti-MG-ovalbumin (MG3D11) (ELISA-2), as described (36,37).…”

Section: Methodsmentioning

confidence: 99%

“…Serum and urine AGE levels were determined by ELISA-1, as described (36,37). Urinary albumin (UA) levels were measured with an anti-mouse albumin-based ELISA kit (Bethyl Laboratories, Montgomery, TX); urinary creatinine was assessed by a standard colorimetric method (Stanbio Laboratory, San Antonio, TX).…”

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confidence: 99%

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Fetal or Neonatal Low-Glycotoxin Environment Prevents Autoimmune Diabetes in NOD Mice

et al. 2003

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Advanced glycation end products (AGEs) are implicated in ␤-cell oxidant stress. Diet-derived AGE (dAGE) are shown to contribute to end-organ toxicity attributed to diabetes. To assess the role of dAGE on type 1 diabetes, NOD mice were exposed to a high-AGE diet (H-AGE) and to a nutritionally similar diet with approximate fivefold-lower levels of N ⑀ -carboxymethyllysine (CML) and methylglyoxal-derivatives (MG) (L-AGE). Suppression of serum CML and MG in L-AGE-fed mice was marked by suppression of diabetes (H-AGE mice >94% vs. L-AGE mice 33% in founder [F] 0 , 14% in F 1 , and 13% in F 2 offspring, P < 0.006) and by a delay in disease onset (4-month lag). Survival for L-AGE mice was 76 vs. 0% after 44 weeks of H-AGE mice. Reduced insulitis in L-AGE versus H-AGE mice (P < 0.01) was marked by GAD-and insulin-unresponsive pancreatic interleukin (IL)-4 -positive CD4؉ cells compared with the GADand insulin-responsive interferon (IFN)-␥-positive Tcells from H-AGE mice (P

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Fetal or Neonatal Low-Glycotoxin Environment Prevents Autoimmune Diabetes in NOD Mice

et al. 2003

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“…The presence of amyloid was demonstrated by the appearance of green birefringence from alkaline alcoholic Congo red staining under polarized light. 26 Immunostaining was performed with antibodies directed against AGE (polyclonal, anti-AGE, dilution 1:20), CML (monoclonal, clone 4G9, dilution 1:1000; Roche Diagnostics GmbH, Penzberg, Germany), 27 human RAGE (monoclonal, dilution 1:20), 28 and human AA amyloid (monoclonal, clone mc 1 , dilution 1:500; DAKO, Hamburg, Germany). Before immunostaining with anti-AGE the specimens were pretreated with 10 mmol/L of ethylenediaminetetraacetic acid (2 ϫ 10 minutes, 450 W microwave oven).…”

Section: Histochemistry and Immunohistochemistrymentioning

confidence: 99%

Advanced Glycation End Products and Receptor for Advanced Glycation End Products in AA Amyloidosis

Röcken

Kientsch-Engel

Mansfeld

et al. 2003

The American Journal of Pathology

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Advanced glycation end products (AGEs) may be involved in either amyloidogenesis or complications related to amyloid. We hypothesized that AGEs may influence the pathogenesis of AA amyloidosis, and investigated the spatial and temporal relationship between AGEs, carboxy methyl lysine (CML), the AGE receptor (RAGE), and AA amyloid in humans and mice. Specimens from patients with AL and ATTR amyloidosis served as a control. Using immunohistochemistry, AGEs, CML, and RAGE were found within amyloid deposits, more commonly in AA amyloid than in AL amyloid and not in ATTR amyloid. Western blotting showed that multiple proteins (between 12 and >60 kd) are modified, but not the AA amyloid fibril protein itself. In the murine model of AA amyloidosis, we found a marked interindividual variability with respect to local and systemic CML levels, as well as to splenic RAGE transcription. Serum levels of CML correlated with the duration of the inflammatory response but not with amounts of splenic RAGE mRNA. Other as yet unidentified variables, especially of the heterogeneous group of AGEs, probably modulate transcription of RAGE and influence amyloidogenesis. CML serum levels, in turn, may prove useful in predicting patients at risk. Advanced glycation end products (AGEs) formed by nonenzymatic glycoxidation of proteins and lipids have been implicated in complications contributing to the increased morbidity and mortality of patients suffering from diabetes and uremia. Hyperglycemia in diabetic patients, and oxidative stress and carbonyl stress in uremic patients, contribute to the formation of AGEs, which are a chemically heterogeneous group of stable covalently bound and cross-linked adducts.

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“…20 and by competitive ELISA (Penzberg, Germany) with the monoclonal antibody 4G-9 directed against N e -(carboxymethyl)-lysine (CML) as described previously. 21,22 Advanced oxidation protein products were determined in plasma spectrophotometrically on a microplate reader (MRX, Dynatech, USA) according to Witko-Sarsat et al, 13 malondialdehyde (MDA) levels by HPLC after derivatization with thiobarbituric acid, 23 lipofuscin levels turbidimetrically, 23 Hcy concentrations by employing HPLC, 24 and those of plasma neopterin by ELISA (Immunotech, Marseille, France).…”

Section: Patientsmentioning

confidence: 99%

Effects of ramipril in nondiabetic nephropathy: improved parameters of oxidatives stress and potential modulation of advanced glycation end products

Šebeková

Gazdíková

Syrova³

et al. 2003

J Hum Hypertens

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Formation of plasma advanced glycosylation end products (AGEs) has no influence on plasma viscosity

Cited by 23 publications

References 0 publications

Fetal or Neonatal Low-Glycotoxin Environment Prevents Autoimmune Diabetes in NOD Mice

Fetal or Neonatal Low-Glycotoxin Environment Prevents Autoimmune Diabetes in NOD Mice

Advanced Glycation End Products and Receptor for Advanced Glycation End Products in AA Amyloidosis

Effects of ramipril in nondiabetic nephropathy: improved parameters of oxidatives stress and potential modulation of advanced glycation end products

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