Print Email Facebook Twitter Advanced glycation end product ligands for the receptor for advanced glycation end products: Biochemical characterization and formation kinetics Title Advanced glycation end product ligands for the receptor for advanced glycation end products: Biochemical characterization and formation kinetics Author Valencia, J.V. Weldon, S.C. Quinn, D. Kiers, G.H. de Groot, J. TeKoppele, J.M. Hughes, T.E. Gaubius instituut TNO Publication year 2004 Abstract Advanced glycation end products (AGEs) accumulate with age and at an accelerated rate in diabetes. AGEs bind cell-surface receptors including the receptor for advanced glycation end products (RAGE). The dependence of RAGE binding on specific biochemical characteristics of AGEs is currently unknown. Using standardized procedures and a variety of AGE measures, the present study aimed to characterize the AGEs that bind to RAGE and their formation kinetics in vitro. To produce AGEs with varying RAGE binding affinity, bovine serum albumin (BSA) AGEs were prepared with 0.5M glucose, fructose, or ribose at times of incubation from 0 to 12 weeks or for up to 3 days with glycolaldehyde or glyoxylic acid. The AGE-BSAs were characterized for RAGE binding affinity, fluorescence, absorbance, carbonyl content, reactive free amine content, molecular weight, pentosidine content, and N-ε-carboxymethyl lysine content. Ribose-AGEs bound RAGE with high affinity within 1 week of incubation in contrast to glucose- and fructose-AGE, which required 12 and 6 weeks, respectively, to generate equivalent RAGE ligands (IC50=0.66, 0.93, and 1.7μM, respectively). Over time, all of the measured AGE characteristics increased. However, only free amine content robustly correlated with RAGE binding affinity. In addition, detailed protocols for the generation of AGEs that reproducibly bind RAGE with high affinity were developed, which will allow for further study of the RAGE-AGE interaction. © 2003 Elsevier Inc. All rights reserved. Chemicals / CAS: advanced glycation end product receptor, 198785-73-8, 247590-69-8; fructose, 30237-26-4, 57-48-7, 7660-25-5, 77907-44-9; glucose, 50-99-7, 84778-64-3; glyoxylic acid, 298-12-4; pentosidine, 124505-87-9; ribose, 34466-20-1, 50-69-1, 93781-19-2; Acetaldehyde, 75-07-0; advanced glycosylation end-product receptor; Amines; Arginine, 74-79-3; Fructose, 30237-26-4; Glucose, 50-99-7; glycolaldehyde, 141-46-8; Glycosylation End Products, Advanced; Glyoxylates; glyoxylic acid, 298-12-4; Ligands; Lysine, 56-87-1; Membrane Proteins; N(6)-carboxymethyllysine, 5746-04-3; pentosidine, 124505-87-9; Receptors, Immunologic; Recombinant Proteins; Ribose, 50-69-1; Serum Albumin, Bovine Molecular Sequence Numbers: GENBANK: CAA76847; Subject Health BiologyBiomedical ResearchAdvanced glycation end productsAgeFormation kineticsGlycationMaillard reactionRAGEReceptor for advanced glycation end productsSerum albumin6 n carboxymethyllysineAdvanced glycation end productAdvanced glycation end product receptorAldehyde derivativeBovine serum albuminCarbonyl derivativeGlyoxylic acidLigandPentosidineRiboseBinding affinityChemical reaction kineticsCorrelation analysisFluorescenceGlycationHuman cellIncubation timeMolecular interactionMolecular mechanicsNucleotide sequencePriority journalReceptor affinityReceptor bindingAcetaldehydeAminesArginineDiabetes MellitusFructoseGlucoseGlycosylation End Products, AdvancedGlyoxylatesHumansLigandsLysineMembrane ProteinsMolecular WeightReceptors, ImmunologicRecombinant ProteinsRegression AnalysisRiboseSerum Albumin, BovineSpectrometry, FluorescenceBovinae To reference this document use: http://resolver.tudelft.nl/uuid:870320c1-23e3-425b-82b3-fc3269838bb0 DOI https://doi.org/10.1016/j.ab.2003.09.013 TNO identifier 237573 ISSN 0003-2697 Source Analytical Biochemistry, 324 (1), 68-78 Document type article Files To receive the publication files, please send an e-mail request to TNO Library.