Lactoylglutathione lyase

About: Lactoylglutathione lyase is a research topic. Over the lifetime, 771 publications have been published within this topic receiving 35158 citations. The topic is also known as: GLOD1 & GLYI.

DJ-1 glyoxalase activity makes a modest contribution to cellular defense against methylglyoxal damage in neurons

Abstract: Human DJ-1 is a cytoprotective protein whose absence causes Parkinson’s disease and is also associated with other diseases. DJ-1 has an established role as a redox-regulated protein that defends against oxidative stress and mitochondrial dysfunction. Multiple studies have suggested that DJ-1 is also a protein/nucleic acid deglycase that plays a key role in the repair of glycation damage caused by methylglyoxal (MG), a reactive α-keto aldehyde formed by central metabolism. Contradictory reports suggest that DJ-1 is a glyoxalase but not a deglycase and does not play a major role in glycation defense. Resolving this issue is important for understanding how DJ-1 protects cells against insults that can cause disease. We find that DJ-1 reduces levels of reversible adducts of MG with guanine and cysteine in vitro. The steady-state kinetics of DJ-1 acting on reversible hemithioacetal substrates are fitted adequately with a computational kinetic model that requires only a DJ-1 glyoxalase activity, supporting the conclusion that deglycation is an apparent rather than a true activity of DJ-1. Sensitive and quantitative isotope-dilution mass spectrometry shows that DJ-1 modestly reduces the levels of some irreversible guanine and lysine glycation products in primary and cultured neuronal cell lines and whole mouse brain, consistent with a small but measurable effect on total neuronal glycation burden. However, DJ-1 does not improve cultured cell viability in exogenous MG. In total, our results suggest that DJ-1 is not a deglycase and has only a minor role in protecting neurons against methylglyoxal toxicity.

Glyoxalase I Polymorphism in Belgium

Abstract: The phenotypes of red cell glyoxalase I (EC 4.4.1.5) were determined by cellogel electrophoresis in 750 Belgian persons. The gene frequencies found were 0.432 for GLO1 and 0.568 for GLO2.

S‐(nitrocarbobenzoxy)glutathiones: potent competitive inhibitors of mammalian glyoxalase ii

Abstract: Three potent competitive inhibitors of mammalian liver glyoxalase II, the S-(o-, m-, and p-nitrocarbobenzoxy)-glutathiones, have been synthesized and studied. The Ki values of the ortho, meta, and para isomers, as inhibitors of rat liver glyoxalase II, were 15, 9, and 6.5 microM, respectively. While showing marked competitive inhibition of glyoxalase II, the glutathione derivatives were almost inactive as inhibitors of glyoxalase I. For example, with the para isomer, [I]0.5 values for rat liver glyoxalase I and II were 925 and 12 microM, respectively. This is in marked contrast to other glyoxalase II competitive inhibitors, which in general are even more effective against glyoxalase I. The S-(o-, m-, and p-nitrocarbobenzoxy)glutathiones have found utility as affinity ligands for the purification of rat liver glyoxalase II and may well have use in the study of the glyoxalase enzymes in vivo.

Apoptosis-inducing agent inhibiting glyoxsalase i activity

Abstract: PROBLEM TO BE SOLVED: To provide a glyoxalase I activity-inhibiting agent and an apoptosis-inducing agent, having a new skeleton without having GSH (glutathione) as a base skeleton. SOLUTION: This glyoxalase I activity-inhibiting agent including compounds having a specific pharmacophore and the apoptosis-inducing agent based on the glyoxalase I-inhibiting activity are provided. COPYRIGHT: (C)2006,JPO&NCIPI

Inhibition of yeast glyoxalase I by biologically active peptides.

Abstract: The antiglyoxylase activity of biologically active peptides f-Met-Leu-Phe-OCH3 and Boc-Phe-Leu-Phe-OCH3 has been evaluated and compared with those of standard inhibitors s-octylglutathione and squaric acid. The inhibitory properties of these peptides are discussed in terms of biological and pharmacological aspects.