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Journal ArticleDOI

Identification of Nε-(carboxyethyl)lysine, one of the methylglyoxal-derived AGE structures, in glucose-modified protein: mechanism for protein modification by reactive aldehydes

TLDR
In this article, a separation system for N e -(carboxyethyl)lysine (CEL) was developed by HPLC equipped with a styrene-divinylbenzene copolymer resin coupled with sulfonic group cation-exchange column and examined whether CEL is formed from proteins modified by glucose via the Maillard reaction.
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This article is published in Journal of Chromatography B.The article was published on 2003-05-05. It has received 34 citations till now. The article focuses on the topics: Methylglyoxal & Acetyllysine.

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Citations
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Journal ArticleDOI

Methylglyoxal in food and living organisms.

TL;DR: Methylglyoxal in biological samples can be quantified by HPLC or GC methods with preliminary derivatization into more stable chromophores and/or fluorophores, or derivatives suitable for determination by MS by use of diamino derivatives of benzene and naphthalene, 6-hydroxy-2,4,5-triaminopyrimidine, cysteamine, and o-(2,3, 4,5,6-pentafluorobenzyl
Journal ArticleDOI

Melanoidins from coffee infusions. Fractionation, chemical characterization, and effect of the degree of roast.

TL;DR: The results obtained suggest that the chelating ability of these coffee melanoidins is modulated by their carbohydrates, and that the 75% ethanol soluble fractions were almost devoid of carbohydrates.
Journal ArticleDOI

Vascular methylglyoxal metabolism and the development of hypertension

TL;DR: Investigation in spontaneously hypertensive rats found increased aortic MG, AGE formation and oxidative stress were associated with blood pressure increase in SHR, which may cause endothelial dysfunction and altered vascular reactivity.
Journal ArticleDOI

Measurement of Nε-(Carboxymethyl)lysine and Nε-(Carboxyethyl)lysine in Human Plasma Protein by Stable-Isotope-Dilution Tandem Mass Spectrometry

TL;DR: This stable-isotope-dilution tandem mass spectrometry method is suitable for simultaneous analysis of CML and CEL in hydrolysates of plasma proteins and its robustness makes it suitable for assessing the value of these compounds as biomarkers of oxidative stress resulting from sugar and lipid oxidation.
Journal ArticleDOI

Increased methylglyoxal and advanced glycation end products in kidney from spontaneously hypertensive rats

TL;DR: MG and AGEs formation was significantly elevated in kidney from SHR, which may cause local vascular and tubular damage, contributing to the development and complications of hypertension.
References
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Journal ArticleDOI

Aminoguanidine prevents diabetes-induced arterial wall protein cross-linking

TL;DR: The identification of aminoguanidine as an inhibitor of advanced nonenzymatic glycosylation product formation makes possible precise experimental definition of the pathogenetic significance of this process and suggests a potential clinical role for aminogsuanidine in the future treatment of chronic diabetic complications.
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Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose.

TL;DR: Alpha-Oxoaldehydes were formed in early glycation from the degradation of glucose and Schiff's base adduct, which suggests that short periods of hyperglycaemia, as occur in impaired glucose tolerance, may be sufficient to increase the concentrations of alpha-oxoaldeHydes in vivo.
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Identification of N epsilon-carboxymethyllysine as a degradation product of fructoselysine in glycated protein.

TL;DR: The browning of fFL incubation mixtures proceeded to a greater extent under a nitrogen versus an air atmosphere, suggesting that oxidative degradation of Amadori adducts to form CML may limit the browning reactions of glycated proteins.
Journal ArticleDOI

Effect of collagen turnover on the accumulation of advanced glycation end products.

TL;DR: First experimental evidence that protein turnover is a major determinant in AGE accumulation in different collagen types is provided, thereby providing the first reasonable estimates of the half-lives of these collagens.
Journal ArticleDOI

The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life.

TL;DR: Investigation has brought new developments in the involvement of the glyoxalase in cell growth and vesicle mobilization, with increasing evidence of changes in the gly oxalase system during tumor growth and diabete mellitus, particularly relating to the development of associated clinical complications.
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