TY - JOUR

T1 - Advanced glycation endproducts in food and their effects on health

AU - Poulsen, Malene Wibe

AU - Hedegaard, Rikke Susanne Vingborg

AU - Andersen, Jeanette Marker

AU - de Courten, Barbora

AU - Bügel, Susanne Gjedsted

AU - Nielsen, John

AU - Skibsted, Leif Horsfelt

AU - Dragsted, Lars Ove

N1 - CURIS 2013 NEXS 042

PY - 2013

Y1 - 2013

N2 - 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-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.

AB - 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-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.

UR - http://www.scopus.com/inward/record.url?scp=84881522629&partnerID=8YFLogxK

U2 - 10.1016/j.fct.2013.06.052

DO - 10.1016/j.fct.2013.06.052

M3 - Review

C2 - 23867544

AN - SCOPUS:84881522629

VL - 60

SP - 10

EP - 37

JO - Food and Chemical Toxicology

JF - Food and Chemical Toxicology

SN - 0278-6915

IS - 1

ER -