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Chemical modification of proteins by methylglyoxal.
Cell Mol Biol (Noisy-le-grand) 1998; 44(7):1139-45CM

Abstract

Methylglyoxal is formed in vivo by spontaneous decomposition of triose phosphate intermediates in aerobic glycolysis. It may also be formed during oxidative degradation of both carbohydrates (pentoses and ascorbate) and lipids (arachidonate). In addition to reaction with arginine residues to form imidazolone adducts, methylglyoxal reacts with lysine residues in protein to form N(epsilon)-(carboxyethyl)lysine (CEL) and the imidazolium crosslink, methylglyoxal-lysine dimer (MOLD). Like the glycoxidation products, N(epsilon)-(carboxymethyl)lysine (CML) and glyoxal-lysine dimer (GOLD) which are formed on reaction of glyoxal with protein, CEL and MOLD increase in lens proteins and skin collagen with age. CML and CEL also increase in skin collagen in diabetes, while all four compounds increase in plasma proteins in uremia. Overall, CML, CEL, GOLD and MOLD are quantitatively the major biomarkers of the Maillard reaction in tissue proteins. GOLD and MOLD, in particular, are present at 10-50 fold higher concentrations than the fluorescent crosslink, pentosidine. Together, these dicarbonyl-derived advanced glycation endproducts (AGEs) represent the major chemical modifications that accumulate in tissue proteins with age and in chronic diseases such as diabetes and atherosclerosis.

Authors+Show Affiliations

Department of Chemistry and Biochemistry, University of South Carolina, Columbia 29208, USA.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

9846896

Citation

Degenhardt, T P., et al. "Chemical Modification of Proteins By Methylglyoxal." Cellular and Molecular Biology (Noisy-le-Grand, France), vol. 44, no. 7, 1998, pp. 1139-45.
Degenhardt TP, Thorpe SR, Baynes JW. Chemical modification of proteins by methylglyoxal. Cell Mol Biol (Noisy-le-grand). 1998;44(7):1139-45.
Degenhardt, T. P., Thorpe, S. R., & Baynes, J. W. (1998). Chemical modification of proteins by methylglyoxal. Cellular and Molecular Biology (Noisy-le-Grand, France), 44(7), pp. 1139-45.
Degenhardt TP, Thorpe SR, Baynes JW. Chemical Modification of Proteins By Methylglyoxal. Cell Mol Biol (Noisy-le-grand). 1998;44(7):1139-45. PubMed PMID: 9846896.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Chemical modification of proteins by methylglyoxal. AU - Degenhardt,T P, AU - Thorpe,S R, AU - Baynes,J W, PY - 1998/12/10/pubmed PY - 1998/12/10/medline PY - 1998/12/10/entrez SP - 1139 EP - 45 JF - Cellular and molecular biology (Noisy-le-Grand, France) JO - Cell. Mol. Biol. (Noisy-le-grand) VL - 44 IS - 7 N2 - Methylglyoxal is formed in vivo by spontaneous decomposition of triose phosphate intermediates in aerobic glycolysis. It may also be formed during oxidative degradation of both carbohydrates (pentoses and ascorbate) and lipids (arachidonate). In addition to reaction with arginine residues to form imidazolone adducts, methylglyoxal reacts with lysine residues in protein to form N(epsilon)-(carboxyethyl)lysine (CEL) and the imidazolium crosslink, methylglyoxal-lysine dimer (MOLD). Like the glycoxidation products, N(epsilon)-(carboxymethyl)lysine (CML) and glyoxal-lysine dimer (GOLD) which are formed on reaction of glyoxal with protein, CEL and MOLD increase in lens proteins and skin collagen with age. CML and CEL also increase in skin collagen in diabetes, while all four compounds increase in plasma proteins in uremia. Overall, CML, CEL, GOLD and MOLD are quantitatively the major biomarkers of the Maillard reaction in tissue proteins. GOLD and MOLD, in particular, are present at 10-50 fold higher concentrations than the fluorescent crosslink, pentosidine. Together, these dicarbonyl-derived advanced glycation endproducts (AGEs) represent the major chemical modifications that accumulate in tissue proteins with age and in chronic diseases such as diabetes and atherosclerosis. SN - 0145-5680 UR - https://www.unboundmedicine.com/medline/citation/9846896/Chemical_modification_of_proteins_by_methylglyoxal_ L2 - https://www.lens.org/lens/search?q=citation_id:9846896 DB - PRIME DP - Unbound Medicine ER -