Development of a conventional immunochemical detection system for determination of Nδ-(5-hydro-5-methyl-4-imidazolone-2-yl)-ornithine in methylglyoxal-modified proteins

Methylglyoxal (MGO) produced during glycolysis is known to react with arginine residues on proteins to generate advanced glycation end products, such as N δ -(5-hydro-5-methyl-4-imidazolone-2-yl)-ornithine (MG-H1). Since the production of MGO is increased during hyperglycemia or metabolic disorders...

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Bibliographic Details
Published in:Glycoconjugate journal 2021-06, Vol.38 (3), p.293-301
Main Authors: Yamaguchi, Hiroko, Nagai, Mime, Sugawa, Hikari, Yasuda, Hisataka, Nagai, Ryoji
Format: Article
Language:English
Subjects:
Advanced glycosylation end products
Advances in Glcation: from food to human health and disease
Amino acids
Antibodies
Biochemistry
Biomedical and Life Sciences
Carbohydrate metabolism
Enzyme-linked immunosorbent assay
Glycolysis
Glycosylation
Hyperglycemia
Imidazoles - chemistry
Immunochemistry
Ions
Life Sciences
Liquid chromatography
Mass spectroscopy
Metabolic disorders
Monoclonal antibodies
Oligopeptides - chemistry
Original Article
Ornithine
Ornithine - analogs & derivatives
Ornithine - chemistry
Pathology
Proteins
Pyruvaldehyde
Pyruvaldehyde - chemistry
Western blotting
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Summary:Methylglyoxal (MGO) produced during glycolysis is known to react with arginine residues on proteins to generate advanced glycation end products, such as N δ -(5-hydro-5-methyl-4-imidazolone-2-yl)-ornithine (MG-H1). Since the production of MGO is increased during hyperglycemia or metabolic disorders in vivo , it is considered that the measurement of MG-H1 is useful for evaluating abnormalities in carbohydrate metabolism. Thus, we prepared a monoclonal antibody against MG-H1 to develop a conventional measurement system for MG-H1. Reactivity and specificity of the antibody to MGO-modified protein were confirmed by enzyme-linked immunosorbent assay and western blotting, respectively. The measurement of MG-H1 content by the antibody was positively correlated with that by electrospray ionization-liquid chromatography-tandem mass spectrometry and the ratio of modified arginine residues by amino acid analysis. Our results demonstrated that immunochemical methods could be useful for the estimation of MG-H1 content in modified proteins.
ISSN:0282-0080
1573-4986
DOI:10.1007/s10719-020-09957-5