Methylglyoxal scavenging capacity of fiber-bound polyphenols from highland barley during colonic fermentation and its modulation on methylglyoxal-interfered gut microbiota
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Ingredient
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Lactoylglutathione lyase
Collagen VI
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Extracellular methylglyoxal toxicity in Saccharomyces cerevisiae: role of glucose and phosphate ions
Aim: The purpose of this study was to investigate the behaviour of Saccharomyces cerevisiae in response to extracellular methylglyoxal. Methods and Results: Cell survival to methylglyoxal and the importance of phosphates was investigated. The role of methylglyoxal detoxification systems and methylglyoxal‐derived protein glycation were studied and the relation to cell survival or death was evaluated. Extracellular methylglyoxal decreased cell viability, and the presence of phosphate enhanced this effect. d‐glucose seems to exert a protective effect towards this toxicity. Methylglyoxal‐induced cell death was not apoptotic and was not related to intracellular glycation processes. The glyoxalases and aldose reductase were important in methylglyoxal detoxification. Mutants lacking glyoxalase I and II showed increased sensitivity to methylglyoxal, while strains overexpressing these genes had increased resistance. Conclusions: Extracellular methylglyoxal induced non‐apoptotic cell death, being unrelated to glycation. Inactivation of methylglyoxal‐detoxifying enzymes by phosphate is one probable cause. Phosphate and d‐glucose may also act through their complex involvement in stress response mechanisms. Significance and Impact of the Study: These findings contribute to elucidate the mechanisms of cell toxicity by methylglyoxal. This information could be useful to on‐going studies using yeast as a eukaryotic cell model to investigate methylglyoxal‐derived glycation and its role in neurodegenerative diseases.
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Lactoylglutathione lyase
Aldehyde Reductase
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Transient or chronic hyperglycaemia increases the formation of intracellular reactive oxygen species and aldehydes. The accumulation of reactive aldehydes is implicated in the development of diabetic complications. Methylglyoxal, a glucose dependent α-dicarbonyl might be the most important reactive aldehyde in diabetes and its complications. Diabetes was the first disease in which evidence emerged for the increased formation of methylglyoxal in the cells and in the serum. Methylglyoxal has a toxic effect on insulin secretion from pancreatic beta-cells, and on modifications of proteins and nucleic acids. Moreover, methylglyoxal is one of the major precursors of advanced glycation end-products. The glyoxalase enzyme system that exists in all mammalian cells is catalyzing the detoxification of methylglyoxal. This review summarizes the methylglyoxal metabolism in normoglycaemic and hyperglycamic conditions and the role of methylglyoxal in the development of late diabetic microvascular complications. Orv. Hetil., 2012, 153, 574–585.
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Major carbonyl compounds from a extract of ground roasted coffee beans were identified as 5-hydroxymethylfurfural, acetol, glyoxal, methylglyoxal and diacetyl. Among these carbonyl compounds, methylglyoxal showed considerable mutagenic activity toward Salmonella typhimurium TA100 without S9 mix (around 100,000 revertants/mg). More than 50% of the total mutagenic activity of coffee can be accounted for by the activity of methylglyoxal.
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The formation of methylglyoxal is increased during hyperglycemia associated with diabetes mellitus. Enhanced methylglyoxal concentration in biological systems is associated with increased reversible and irreversible modification of protein. The chronic exposure to high methylglyoxal concentrations appears to be linked to the development of diabetic complications. Intervention with aldose reductase inhibitors or aminoguanidine, which is an efficient scavenger of methylglyoxal, in diabetes mellitus may prevent increased methylglyoxal concentration.
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Lactoylglutathione lyase
Carbohydrate Metabolism
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To determine whether the Maillard reaction of methylglyoxal is associated with human lens aging and cataractogenesis and to investigate how glutathione depletion affects methylglyoxal-derived modifications in organ-cultured lenses.Antibodies against methylglyoxal-derived modifications were developed in rabbits and purified by immunoaffinity chromatography. A competitive enzyme-linked immunosorbent assay (ELISA) measured methylglyoxal-derived products in human lens proteins. Lenses of galactosemic rats grown in organ culture were used to assess the role of glutathione-dependent pathways in methylglyoxal metabolism and Maillard reactions.Methylglyoxal-derived modifications in the human lens were age dependent, and brunescent lenses had the highest levels of these modifications. Immunofluorescence staining identified antigens distributed throughout the lens, with higher levels in old lenses than in younger ones. Experiments with normal or galactosemic rat lenses grown in organ culture showed that lens proteins do not have an increase in methylglyoxal-modified proteins when cultured in medium containing 500 microM methylglyoxal alone, but they accumulate modified proteins when cultured with DL-glyceraldehyde. Inclusion of 30 mM glucose in the medium marginally increased methylglyoxal-derived products, but there was no correlation between lens glutathione content and methylglyoxal-derived modifications.Methylglyoxal-mediated Maillard reactions that occur in the human lens may play a role in lens aging and cataract formation. Methylglyoxal is probably derived from metabolic pathways within the lens. Decreased glutathione in organ-cultured rat lenses does not significantly influence methylglyoxal-mediated Maillard reactions.
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