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Peptide mapping of human serum albumin modified minimally by methylglyoxal in vitro and in vivo.
Ann N Y Acad Sci. 2005 Jun; 1043:260-6.AN

Abstract

Methylglyoxal is a potent glycating agent and important precursor of advanced glycation end products (AGEs) in physiological systems. Unlike glucose, methylglyoxal is predominantly an arginine-directed glycating agent. Methylglyoxal reacts with proteins to form mainly the arginine-derived hydroimidazolone AGE, Ndelta-(5-hydro-5-methyl-4-imidazolon-2-yl)-ornithine (MG-H1), argpyrimidine, the lysine-derived AGEs, N(epsilon)-(1-carboxyethyl)lysine (CEL), and methylglyoxal-derived lysine dimer (MOLD). Sites within proteins susceptible to modification by methylglyoxal have not been identified. Here we show that modification of human serum albumin by methylglyoxal forms mainly hydroimidazolone MG-H1 residues. The location of MG-H1 residues was identified by mass spectrometric peptide mapping. This method identified a hot spot of hydroimidazolone formation at Arg-410, with other minor MG-H1 modifications at Arg-114, Arg-186, Arg-218, and Arg-428. Other extracellular and intracellular proteins are modified by methylglyoxal in physiological systems. Modification of arginine residues by methylglyoxal may be particularly damaging because arginine residues have a high frequency of occurrence in ligand and substrate recognition sites in receptor and enzyme active sites.

Authors+Show Affiliations

Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, Essex CO4 3SQ, UK. thorp@essex.ac.ukNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

16037246

Citation

Ahmed, Naila, and Paul J. Thornalley. "Peptide Mapping of Human Serum Albumin Modified Minimally By Methylglyoxal in Vitro and in Vivo." Annals of the New York Academy of Sciences, vol. 1043, 2005, pp. 260-6.
Ahmed N, Thornalley PJ. Peptide mapping of human serum albumin modified minimally by methylglyoxal in vitro and in vivo. Ann N Y Acad Sci. 2005;1043:260-6.
Ahmed, N., & Thornalley, P. J. (2005). Peptide mapping of human serum albumin modified minimally by methylglyoxal in vitro and in vivo. Annals of the New York Academy of Sciences, 1043, 260-6.
Ahmed N, Thornalley PJ. Peptide Mapping of Human Serum Albumin Modified Minimally By Methylglyoxal in Vitro and in Vivo. Ann N Y Acad Sci. 2005;1043:260-6. PubMed PMID: 16037246.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Peptide mapping of human serum albumin modified minimally by methylglyoxal in vitro and in vivo. AU - Ahmed,Naila, AU - Thornalley,Paul J, PY - 2005/7/23/pubmed PY - 2005/10/28/medline PY - 2005/7/23/entrez SP - 260 EP - 6 JF - Annals of the New York Academy of Sciences JO - Ann. N. Y. Acad. Sci. VL - 1043 N2 - Methylglyoxal is a potent glycating agent and important precursor of advanced glycation end products (AGEs) in physiological systems. Unlike glucose, methylglyoxal is predominantly an arginine-directed glycating agent. Methylglyoxal reacts with proteins to form mainly the arginine-derived hydroimidazolone AGE, Ndelta-(5-hydro-5-methyl-4-imidazolon-2-yl)-ornithine (MG-H1), argpyrimidine, the lysine-derived AGEs, N(epsilon)-(1-carboxyethyl)lysine (CEL), and methylglyoxal-derived lysine dimer (MOLD). Sites within proteins susceptible to modification by methylglyoxal have not been identified. Here we show that modification of human serum albumin by methylglyoxal forms mainly hydroimidazolone MG-H1 residues. The location of MG-H1 residues was identified by mass spectrometric peptide mapping. This method identified a hot spot of hydroimidazolone formation at Arg-410, with other minor MG-H1 modifications at Arg-114, Arg-186, Arg-218, and Arg-428. Other extracellular and intracellular proteins are modified by methylglyoxal in physiological systems. Modification of arginine residues by methylglyoxal may be particularly damaging because arginine residues have a high frequency of occurrence in ligand and substrate recognition sites in receptor and enzyme active sites. SN - 0077-8923 UR - https://www.unboundmedicine.com/medline/citation/16037246/Peptide_mapping_of_human_serum_albumin_modified_minimally_by_methylglyoxal_in_vitro_and_in_vivo_ L2 - https://doi.org/10.1196/annals.1333.031 DB - PRIME DP - Unbound Medicine ER -