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Food Chem Toxicol. 2013 Oct;60:10-37. doi: 10.1016/j.fct.2013.06.052. Epub 2013 Jul 16.

Advanced glycation endproducts in food and their effects on health.

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Department of Nutrition, Exercise and Sports, Faculty of Science, University of Copenhagen, Rolighedsvej 30, 1958 Frederiksberg C, Denmark.


Advanced glycation endproducts (AGEs) form by Maillard-reactions after initial binding of aldehydes with amines or amides in heated foods or in living organisms. The mechanisms of formation may include ionic as well as oxidative and radical pathways. The reactions may proceed within proteins to form high-molecular weight (HMW) AGEs or among small molecules to form low-molecular weight (LMW) AGEs. All free amino acids form AGEs, but lysine or arginine side chains dominate AGE formation within proteins. The analysis of AGEs in foods and body fluids is most often performed by ELISA or LC-MS; however, none of the methodologies cover all HMW and LMW AGEs. Most research is, therefore, carried out using 'representative' AGE compounds, most often N(ε)-carboxymethyl-lysine (CML). Only LMW AGEs, including peptide-bound forms, and carbonyls may be absorbed from the gut and contribute to the body burden of AGEs. Some AGEs interact with specific pro- or anti-inflammatory receptors. Most studies on the biological effects of AGEs have been carried out by administering heated foods. The pro-inflammatory and deteriorating biological effects of AGEs in these studies, therefore, need further confirmation. The current review points out several research needs in order to address important questions on AGEs in foods and health.


1,4-bis(5-amino-5-carboxy-1-pentyl)pyrazinium radical cation; 1-DG; 1-deoxyglucosone; 3-DG; 3-deoxyglucosone; AGEAGE; AGER1; ALE; Advanced glycation endproducts; BSA; CEL; CML; CROSSPY; DAD; DODIC; DOLD; Diet; ELISA; Food preparation; GC; GO; GODIC; GOLD; HMW; HPLC; Insulin sensitivity; LDL; LMW; MAPK; MG; MG-H; MODIC; MOLD; MRP; MS; Maillard reaction; Maillard reaction product; N(ε)-carboxyethyllysine; N(ε)-carboxymethyl-lysine; NADPH; NF-κB; PBMC; RAGE; SIRT1; T1D; T2D; Type 2 diabetes; advanced glycation endproduct; advanced glycation endproduct receptor 1; advanced lipoxidation endproduct; apoE; apolipoprotein E; bovine serum albumin; diode array detector; enzyme-linked immunosorbent assay; gas chromatography; glyoxal; high molecular weight; high performance liquid chromatography; imidazolium cross-link derived from 3-deoxyglucosone and lysine-arginine; imidazolium cross-link derived from 3-deoxyglucosone and lysine-lysine; imidazolium cross-link derived from glyoxal and lysine-arginine; imidazolium cross-link derived from glyoxal and lysine-lysine; imidazolium cross-link derived from methylglyoxal and lysine-arginine; imidazolium cross-link derived from methylglyoxal and lysine-lysine; low molecular weight; low-density lipoprotein; mass spectrometry; methylglyoxal; methylglyoxal-derived hydroimidazolone; mitogen-activated protein kinases; nicotinamide adenine dinucleotide phosphate; nuclear factor kappa B; peripheral blood mononuclear cells; receptor for advanced glycation endproducts; sRAGE; sirtuin-1; soluble receptor for advanced glycation endproducts; type 1 diabetes; type 2 diabetes

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