title: Non-enzymatic glycosylation of the dipeptide L-carnosine, a potential anti-protein-cross-linking agent.
abstract: The dipeptide carnosine (beta-alanyl-L-histidine) was readily glycosylated non-enzymatically upon incubation with the sugars glucose, galactose, deoxyribose and the triose dihydroxyacetone. Carnosine inhibited glycation of actyl-Lys-His-amide by dihydroxyacetone and it protected alpha-crystallin, superoxide dismutase and catalise against glycation and cross-linking mediated by ribose, deoxyribose, dihydroxyacetone, dihydroxyacetone phosphate and fructose. Unlike certain glycated amino acids, glycated carnosine was non-mutagenic. The potential biological and therapeutic significance of these observations are discussed.
authors.affiliation: Division of Biomolecular Engineering, CSIRO, North Ryde, NSW, Australia.
authors.forename: A R
authors.initials: AR
authors.lastname: Hipkiss
authors.forename: J
authors.initials: J
authors.lastname: Michaelis
authors.forename: P
authors.initials: P
authors.lastname: Syrris
mesh_terms: D000409:Alanine / Q000633:toxicity; D002336:Carnosine / Q000737:chemistry* / Q000494:pharmacology* / Q000633:toxicity; D003432:Cross-Linking Reagents; D003855:Deoxyribose / Q000737:chemistry; D004099:Dihydroxyacetone Phosphate / Q000737:chemistry; D006031:Glycosylation / Q000187:drug effects; D008239:Lysine / Q000737:chemistry / Q000633:toxicity; D009005:Monosaccharides / Q000737:chemistry; D009152:Mutagenicity Tests; D009153:Mutagens / Q000633:toxicity; D011506:Proteins / Q000737:chemistry*
chemical_list: D003432:Cross-Linking Reagents; D009005:Monosaccharides; D009153:Mutagens; D011506:Proteins; D003855:Deoxyribose; D004099:Dihydroxyacetone Phosphate; D002336:Carnosine; D008239:Lysine; D000409:Alanine