Methylglyoxal Modification of Protein
نویسندگان
چکیده
منابع مشابه
Methylglyoxal modification of protein. Chemical and immunochemical characterization of methylglyoxal-arginine adducts.
Methylglyoxal (MG), an endogenous metabolite that increases in diabetes and is a common intermediate in the Maillard reaction (glycation), reacts with proteins and forms advanced glycation end products. In the present study, we identify a novel MG-arginine adduct and also characterize the structure of a major fluorescent adduct. In addition, we describe the immunochemical study on the MG-argini...
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Objective. Here we tested the role of Glo I in the prevention of advanced glycation end product (AGE) formation in transgenic mouse lenses. Methods. A transgenic animal line that expressed high levels of human Glo I in the lens was developed from the C57B6 mouse strain. The role of Glo I in the inhibition of MGO-AGE formation was tested in organ-cultured lenses. Results. Organ culture of Wt and...
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Protein glycation by methylglyoxal is a nonenzymatic post-translational modification whereby arginine and lysine side chains form a chemically heterogeneous group of advanced glycation end-products. Methylglyoxal-derived advanced glycation end-products are involved in pathologies such as diabetes and neurodegenerative diseases of the amyloid type. As methylglyoxal is produced nonenzymatically f...
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Methylglyoxal is a highly reactive dicarbonyl degradation product formed from triose phosphates during glycolysis. Methylglyoxal forms stable adducts primarily with arginine residues of intracellular proteins. The biologic role of this covalent modification in regulating cell function is not known. Here, we report that in retinal Müller cells, increased glycolytic flux causes increased methylgl...
متن کاملBinding and Modification of Proteins by Methylglyoxal under Physiological Conditions
The physiological a-oxoaldehyde methylglyoxal binds and modifies arginine, lysine, and cysteine residues in proteins. The kinetics and mechanism of these reactions were investigated with Na-acetylamino acids and bovine serum albumin at pH 7.4 and 37 “C. The reaction of methylglyoxal with Na-acetylarginine involved the initial reversible formation of glycosylamine and 4,5-dihydroxy5-methylimidaz...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1999
ISSN: 0021-9258
DOI: 10.1074/jbc.274.26.18492