We are analyzing https://link.springer.com/article/10.1007/s00125-004-1392-9.

Title:
Binding of receptor for advanced glycation end products (RAGE) ligands is not sufficient to induce inflammatory signals: lack of activity of endotoxin-free albumin-derived advanced glycation end products | Diabetologia
Description:
Aims/hypothesis Activation of the receptor for advanced glycation end products (RAGE) reportedly triggers cellular responses implicated in the pathogenesis of diabetes, such as increasing vascular cell adhesion molecule-1 (VCAM-1) expression on vascular endothelial cells and inducing TNF-α secretion by mononuclear cells. The objective of this study was to evaluate whether RAGE binding affinity of AGE-BSAs and cellular activation correlate. Methods To produce AGEs with varying glycation, bovine albumin AGEs were prepared with 500 mmol/l of glucose, fructose or ribose at times of incubation from 1 to 12 weeks. In addition, AGE-BSA was generated using either glyoxylic acid or glycolaldehyde. Cellular binding of the AGE-BSAs and the effect on endothelial cell VCAM-1 expression were studied in RAGE-expressing human microvascular endothelial cell line-4 cells. Induction of TNF-α secretion was assessed using RAGE-expressing human peripheral blood mononuclear cells (PBMCs). Results Cellular binding of the different AGE preparations correlated well with RAGE affinity. Interestingly, we found that the AGE preparations, which were essentially endotoxin free (≤0.2 ng/mg protein), were incapable of inducing VCAM-1 or TNF-α secretion regardless of RAGE binding affinity, AGE concentration or incubation time. In contrast, the reported RAGE ligand S100b was confirmed to induce VCAM-1 expression on endothelial cells and TNF-α secretion by PBMCs after 24 h of treatment. Conclusions/interpretation The results of this study suggest that AGE modification and high RAGE binding affinity are not sufficient to generate pro-inflammatory signalling molecules. Thus, RAGE binding affinity of AGE-BSAs does not seem to correlate with cellular activation. Our findings using AGEs with strong RAGE-binding properties indicate that AGEs may not uniformly play a role in cellular activation.
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Keywords {🔍}

cells, bsa, rage, binding, cell, vcam, tnfα, age, google, scholar, hmec, cellular, pubmed, cas, ages, advanced, endothelial, agebsas, glycation, end, agebsa, human, usa, assay, article, products, activation, expression, fig, diabetes, receptor, lps, media, affinity, hsrage, incubated, secretion, preparations, found, ngml, control, µgml, incubation, pbmcs, plates, values, inflammatory, vascular, mmoll, antibody,

Topics {✒️}

sp-sepharose fast-flow resin cyanogen-bromide-activated sepharose 4b rabbit polyclonal anti-iκbα goat anti-rabbit conjugated 20 ng/ml human tnf-α cell-based bsa-binding elisa polyclonal anti-rage antibody anti-human rage antibody gibco brl/life technologies 2-isopropylidenehydrazono-4-oxo-thiazolidin-5-ylacetanilide endotoxin-free distilled h2o maillard reaction products platelet-derived growth factor full size image 125i-rib500 bsa wk6 protein g-sepharose chromatography cell-free binding assay radioligand-based binding assay age-responsive cellular models induce tnf-α secretion strong rage-binding properties tnf-α production assay keyhole limpet haemocyanin cell-free assay observed 100 ng/ml lipopolysaccharide/endotoxin radioligand-based assay provided inducing tnf-α secretion ice-cold extraction buffer tbs-casein blocking solution tbs-casein-blocking solution bsa-based binding assay inducing tnf-α production iron activates nf-kappab 20 ng/ml tnf-α ga-bsa-immunised animals lipopolysaccharide/endotoxin nf-κb signal-transduction receptor rage sugar-derived age-bsas significant tnf-α response 1000 anti-iκbα antibody bovine albumin ages show iκb-α degradation advanced glycation endproducts low-grade inflammatory state characterised age-binding protein measured tnf-α secretion endothelial cell line anti-bsa antibody glyoxylic-acid-derived ages anti-rage igg

Questions {❓}

Pradhan AD, Ridker PM (2002) Do atherosclerosis and type 2 diabetes share a common inflammatory basis?

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         description:Activation of the receptor for advanced glycation end products (RAGE) reportedly triggers cellular responses implicated in the pathogenesis of diabetes, such as increasing vascular cell adhesion molecule-1 (VCAM-1) expression on vascular endothelial cells and inducing TNF-α secretion by mononuclear cells. The objective of this study was to evaluate whether RAGE binding affinity of AGE-BSAs and cellular activation correlate. To produce AGEs with varying glycation, bovine albumin AGEs were prepared with 500 mmol/l of glucose, fructose or ribose at times of incubation from 1 to 12 weeks. In addition, AGE-BSA was generated using either glyoxylic acid or glycolaldehyde. Cellular binding of the AGE-BSAs and the effect on endothelial cell VCAM-1 expression were studied in RAGE-expressing human microvascular endothelial cell line-4 cells. Induction of TNF-α secretion was assessed using RAGE-expressing human peripheral blood mononuclear cells (PBMCs). Cellular binding of the different AGE preparations correlated well with RAGE affinity. Interestingly, we found that the AGE preparations, which were essentially endotoxin free (≤0.2 ng/mg protein), were incapable of inducing VCAM-1 or TNF-α secretion regardless of RAGE binding affinity, AGE concentration or incubation time. In contrast, the reported RAGE ligand S100b was confirmed to induce VCAM-1 expression on endothelial cells and TNF-α secretion by PBMCs after 24 h of treatment. The results of this study suggest that AGE modification and high RAGE binding affinity are not sufficient to generate pro-inflammatory signalling molecules. Thus, RAGE binding affinity of AGE-BSAs does not seem to correlate with cellular activation. Our findings using AGEs with strong RAGE-binding properties indicate that AGEs may not uniformly play a role in cellular activation.
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         Metabolic Diseases
         Human Physiology
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