Methylglyoxal-induced glycation affects protein topography

Seidler, Norbert W.; Kowalewski, Catherine

doi:10.1016/s0003-9861(02)00662-8

Cited by 30 publications

(19 citation statements)

References 32 publications

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“…As reported previously (34), aspartate aminotransferase (10 M) activity was decreased by 20 -90% by 1-5 mM methylglyoxal at 37°C (Fig. 3E).…”

Section: Dj-1 Deglycates Fbp Aldolase and Aspartate Transaminasesupporting

confidence: 89%

“…BSA arginines were measured using phenanthrenequinone (32). Glycation/deglycation of fructose bisphosphate aldolase A (from rabbit muscle; EC 4.1.2.13; Sigma) and aspartate aminotransferase (from pig heart, cytoplasmic; EC 2.6.1.1; Sigma) were followed by measuring enzymatic activities (33,34), by detecting the glycated forms with anti-AGE antibodies (Cell Biolabs Inc.), and by mass spectrometry. Deglycation experiments were performed at least three times, and representative results are shown.…”

Section: Methodsmentioning

confidence: 99%

“…BSA contains a single exposed cysteine (Cys 34 , titratable by DTNB) involved in oxidative stress protection. DJ-1 can repair this cysteine from sulfenylation (6).…”

Section: Dj-1 Deglycates Glutathione and Protein Cysteinesmentioning

confidence: 99%

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Parkinsonism-associated Protein DJ-1/Park7 Is a Major Protein Deglycase That Repairs Methylglyoxal- and Glyoxal-glycated Cysteine, Arginine, and Lysine Residues

Richarme

Mihoub

Dairou

et al. 2015

Journal of Biological Chemistry

237

233

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Background: Protein glycation is a nonenzymatic covalent reaction between proteins and carbonyl groups resulting in protein denaturation. Results: DJ-1 is the first protein deglycase that repairs proteins from glycation by glyoxals, which constitutes most glycation damage. Conclusion: DJ-1 is a novel protein repair enzyme that protects proteins against glycation. Significance: DJ-1 deglycase activity changes our view on glycation/deglycation and DJ-1-associated Parkinsonism.

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“…As reported previously (34), aspartate aminotransferase (10 M) activity was decreased by 20 -90% by 1-5 mM methylglyoxal at 37°C (Fig. 3E).…”

Section: Dj-1 Deglycates Fbp Aldolase and Aspartate Transaminasesupporting

confidence: 89%

Section: Methodsmentioning

confidence: 99%

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Parkinsonism-associated Protein DJ-1/Park7 Is a Major Protein Deglycase That Repairs Methylglyoxal- and Glyoxal-glycated Cysteine, Arginine, and Lysine Residues

Richarme

Mihoub

Dairou

et al. 2015

Journal of Biological Chemistry

237

233

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“…The same dependence concerned the activity of the other enzymes, including the glycolytic ones [26,27,30,31]. The loss of enzymatic activity is most likely caused by the binding of MG to the lysine and arginine present in the active center and other regions of the enzyme.…”

Section: Discussionmentioning

confidence: 87%

“…The level of cellular AGE depends on the intracellular mechanisms of enzymatic MG detoxification in the glyoxalase or aldose reductase system, as well as on the activity of fructosamine-3-kinase and fructoselysine-3-phosphate hydrolase, the enzymes which releases free hexose from proteins glycated at early steps of the Maillard reaction [23,24]. Numerous reports on the glycation of intercellular proteins indicate the susceptibility of many enzymes to modification with methylglyoxal [25][26][27]. Despite extensive studies on the role of glycolysis in the generation of MG as a glycating factor, data are scarce on such a modification of just glycolytic enzymes.…”

Section: Introductionmentioning

confidence: 99%

Inhibition of human muscle-specific enolase by methylglyoxal and irreversible formation of advanced glycation end products

Gamian

Staniszewska

Danielewicz

2009

Journal of Enzyme Inhibition and Medicinal Chemistry

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Methylglyoxal (MG) was studied as an inhibitor and effective glycating factor of human muscle-specific enolase. The inhibition was carried out by the use of a preincubation procedure in the absence of substrate. Experiments were performed in anionic and cationic buffers and showed that inhibition of enolase by methylglyoxal and formation of enolasederived glycation products arose more effectively in slight alkaline conditions and in the presence of inorganic phosphate. Incubation of 15 micromolar solutions of the enzyme with 2 mM, 3.1 mM and 4.34 mM MG in 100 mM phosphate buffer pH 7.4 for 3 h caused the loss a 32%, 55% and 82% of initial specific activity, respectively. The effect of MG on catalytic properties of enolase was investigated. The enzyme changed the K M value for glycolytic substrate 2-phospho-D-glycerate (2-PGA) from 0.2 mM for native enzyme to 0.66 mM in the presence of MG. The affinity of enolase for gluconeogenic substrate phosphoenolpyruvate altered after preincubation with MG in the same manner, but less intensively. MG has no effect on V max and optimal pH values. Incubation of enolase with MG for 0-48 h generated high molecular weight protein derivatives. Advanced glycation end products (AGEs) were resistant to proteolytic degradation by trypsin. Magnesium ions enhanced the enzyme inactivation by MG and facilitated AGEs formation. However, the protection for this inhibition in the presence of 2-PGA as glycolytic substrate was observed and AGEs were less effectively formed under these conditions.

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Acrolein scavengers: Reactivity, mechanism and impact on health

Zhu

Sun

Jiang

et al. 2011

Molecular Nutrition Food Res

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Acrolein (ACR) is an α,β-unsaturated aldehyde that exists extensively in the environment and (thermally processed) foods. It can also be generated through endogenous metabolism. Its high electrophilicity makes this aldehyde notorious for its facile reaction with biological nucleophiles, leading to the modification of proteins/DNA and depletion of glutathione. Recent studies also have revealed its roles in disturbing various cell signing pathways in biological systems. With growing evidences of ACR's implication in human diseases, strategies to eliminate its hazardous impacts are of great importance. One of the intervention strategies is the application of reactive scavengers to directly trap ACR. Some known ACR scavengers include sulfur (thiol)-containing and nitrogen (amino)-containing compounds as well as the newly emerging natural polyphenols. In this review, the interactions between ACR and its scavengers are highlighted. The discussion about ACR scavengers is mainly focused on their chemical reactivity, trapping mechanisms as well as their roles extended to biological relevance. In addition to their direct trapping effect on ACR, these scavengers might possess multiple functions and offer additional benefits against ACR-induced toxicity. A comprehensive understanding of the mechanism involved may help to establish ACR scavenging as a novel therapeutic intervention against human diseases that are associated with ACR and/or oxidative stress.

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Methylglyoxal-induced glycation affects protein topography

Cited by 30 publications

References 32 publications

Parkinsonism-associated Protein DJ-1/Park7 Is a Major Protein Deglycase That Repairs Methylglyoxal- and Glyoxal-glycated Cysteine, Arginine, and Lysine Residues

Parkinsonism-associated Protein DJ-1/Park7 Is a Major Protein Deglycase That Repairs Methylglyoxal- and Glyoxal-glycated Cysteine, Arginine, and Lysine Residues

Inhibition of human muscle-specific enolase by methylglyoxal and irreversible formation of advanced glycation end products

Acrolein scavengers: Reactivity, mechanism and impact on health

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