• BMB Reports
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• v.39 no.3
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• pp.335-338
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• 2006

Methylglyoxal (MG) is an endogenous physiological metabolite which is present in increased concentrations in diabetics. MG reacts with the amino acids of proteins to form advanced glycation end products. In this in vitro study, we investigated the effect of MG on the structure and function of ceruloplasmin (CP) a serum oxidase carrier of copper ions in the human. When CP was incubated with MG, the protein showed increased electrophoretic mobility which represented the aggregates at a high concentration of MG (100 mM). MG-mediated CP aggregation led to the loss of enzymatic activity and the release of copper ions from the protein. Radical scavengers and copper ion chelators significantly prevented CP aggregation. CP is an important protein that circulates in plasma as a major copper transport protein. It is suggested that oxidative damage of CP by MG may induce perturbations of the copper transport system and subsequently lead to harmful intracellular condition. The proposed mechanism, in part, may provide an explanation for the deterioration of organs in the diabetic patient.

• BMB Reports
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• v.46 no.4
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• pp.225-229
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• 2013

Methylglyoxal (MG) is an endogenous metabolite which is present in increased concentrations in diabetics and reacts with amino acids to form advanced glycation end products. In this study, we investigated whether ferritin enhances DNA cleavage by the reaction of MG with lysine. When plasmid DNA was incubated with MG and lysine in the presence of ferritin, DNA strand breakage was increased in a dose-dependent manner. The ferritin/MG/lysine system-mediated DNA cleavage was significantly inhibited by reactive oxygen species (ROS) scavengers. These results indicated that ROS might participate in the ferritin/MG/lysine system-mediated DNA cleavage. Incubation of ferritin with MG and lysine resulted in a time-dependent release of iron ions from the protein molecules. Our data suggest that DNA cleavage caused by the ferritin/MG/lysine system via the generation of ROS by the Fenton-like reaction of free iron ions released from oxidatively damaged ferritin.

• Fisheries and Aquatic Sciences
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• v.25 no.10
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• pp.517-524
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• 2022

Over production of methylglyoxal (MGO) a highly reactive dicarbonyl compound, has been associated in progressive diabetes with vascular complication. Therefore, we investigated whether hot water extract of Loliolus beka meat (LBM-HWE) presents a preserve effect against MGO-induced cellular damage in human umbilical vein endothelial cells (HUVECs). The LBM-HWE extract showed to inhibit MGO-induced cytotoxicity. Additionally, the LBM-HWE reduced mRNA expression of pro-inflammatory cytokines, and reduced MGO-induced advanced glycation end product (AGEs) formation. Furthermore, LBM-HWE induced glyoxalase-1 mRNA expression and reduced MGO-induced carbonyl protein formation in HUVECs. The results implicate that LBM-HWE has protective ability against MGO-induced HUVECs toxicity by preventing AGEs formation. In conclusion, LBM-HWE could be used as a potential treatment material for the prevention of vascular complications of diabetes.

• Journal of Plant Biology
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• v.37 no.2
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• pp.195-201
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• 1994

In order to study the effects of polyamine inhibitors and polyamines on adventitious root formation, the correlation between adventitious root formation and carbohydrate metabolism was investigated in inoculated soybean (Glycine max L.) cotyledons at the concentration of $10^{-3}\;M$ methylglyoxal bis-(guanylhydrazone)[MGBG], and $10^{-3}\;M$ MGBG plus $10^{-5}\;M$ polyamines (putrescine, spermidine and spermine), respectively, for the adventitious root formation medium. The contents of starch, maltose and sucrose were lower in control and were higher in the treatments containing $10^{-3}\;M$ MGBG, and $10^{-3}\;M$ MGBG plus $10^{-5}\;M$ polyamines during culture. It was shown that the soluble sugar levels, except glucose, were higher than that of control in most of the treatments and the change in glucose contents tended to be similar to that control. The amylase activity increased in control and MGBG treatment, the maltase activity was higher in control and the invertase activity showed less substantial changes during culture.ulture.

• Journal of Plant Biology
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• v.34 no.1
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• pp.53-57
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• 1991

The effect of polyamines and methylglyoxal bis(guanylhydrazone)(MGBG) on the activity of diamine oxidase was studied in soybean (Glycine max) seedlings. $10^{-2}\;M$ of putrescine, spennidine, and spermine inhibited diamine oxidase activity, whereas $10^{-6}\;M$ putrescine increased enzyme activity. These results suggest that diamine oxidase can be induced by a specific substrate, putrescine. The content of putrescine was increased in response to the increase in concentratioin of MGBG. In vitro, 40% of the diamine oxidase activity was inhibited by $10^{-3}\;M$ MGBG. In vivo, the diamine oxidase activity was increased by a low concentrration of MGBG. It was suggested that MGBG inhibited the formation of spermidine and that the accumulated putrescine induced diamine oxidase, whereas the diamine oxidase acitivity was inhibited by a high concentration of MGBG. It is suggested that a high cocentration of MGBG increases the putrescine content by inhibiting diamine oxidase activity which is responsible for putrescine degradation.dation.

• The Korean Journal of Ecology
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• v.18 no.1
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• pp.17-30
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• 1995

The growth of Scenedesmus quadricauda (Trup.) Breb. is enhanced by methylyoxal (MG), a general inhibitor of cell division, at threshold concentration in conjunction with reatment timing relative to growth stage. The stimulatory effect of MG on algal cell growth was most significant with 2.27-fold of untreated algal culture in cell number when 0.5 mM of MG was added to the algal culture at the beginning of logarithmic phase with an initial MG concentration of 0.535 mg $MG/10^6cell$. A Specific growth rates (SGRs) of MG-treated cultures were rapidly increased at the beginning of logarithmic phase with 1.89-fold of untreated algal culture. Cultures inoculated with high cell numbers of 2.4 to 4.8 X $10^4$ cells/ml were less sensitive to 0.5 mM of MG treatment. The algal cell division was ranged from 0.392 to 0.924 mg MG/106 cell. If the cell number of an algal culture at the time of inoculation was low (0.6 X $10^4$ cells/ml) and MG was added before logarithmic phase, the cell number of 0.5 mM of MG-treated cultures were lower than those of controls. In algal cultures treated with high concentrations of MG (1.0 mM and 2.0 mM), the algal growth was inhibited. Photosynthetic rate of growth-enhanced algal by 0.5 mM of MG was significantly higher than that of untreated or 1.0 mM of MG-treated algal cell, while there was no significant difference among those groups in respiratory rate. Pyruvate concentration in 0.5 mM of MG-treated culture was incrcased agter methylglyoxal trcatment.

• Natural Product Sciences
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• v.27 no.4
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• pp.245-250
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• 2021

The methylglyoxal (MGO) trapping constituents from Malus baccata L. were investigated using incubation of MGO and crude extract under physiological conditions followed by HPLC analysis. The peak areas of MGO trapping compounds decreased, and their chemical structures were identified by HPLC-ESI/MS. Sieboldin was identified as a major active molecule representing MGO-trapping activity of the crude extract. After reaction of sieboldin and MGO, remaining MGO was calculated by microplate assay method using imine (Schiff base) formation of 2,4-dinitrophenylhydrazine (DNPH) and aldehyde group. After 4 h incubation, sieboldin trapped over 43.8% MGO at a concentration of 0.33 mM and showed MGO scavenging activity with an RC₅₀ value of 0.88 mM for the incubation of 30 min under physiological conditions. It was also confirmed that sieboldin inhibited the production of advanced glycation end products (AGE) produced by bovine serum albumins (BSA)/MGO. Additionally, MGO trapping mechanism of sieboldin was more specifically identified by ¹H-, ¹³C-, 2D NMR and, confirm to be attached to the position of C-3' (or 5').

• BMB Reports
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• v.45 no.3
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• pp.147-152
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• 2012

Methylglyoxal (MG) was identified as an intermediate in non-enzymatic glycation and increased levels were reported in patients with diabetes. In this study, we evaluated the effects of MG on the modification of ferritin. When ferritin was incubated with MG, covalent crosslinking of the protein increased in a time- and MG dose-dependent manner. Reactive oxygen species (ROS) scavengers, $N-acetyl-_L-cysteine$ and thiourea suppressed the MG-mediated ferritin modification. The formation of dityrosine was observed in MG-mediated ferritin aggregates and ROS scavengers inhibited the formation of dityrosine. During the reaction between ferritin and MG, the generation of ROS was increased as a function of incubation time. These results suggest that ROS may play a role in the modification of ferritin by MG. The reaction between ferritin and MG led to the release of iron ions from the protein. Ferritin exposure to MG resulted in a loss of arginine, histidine and lysine residues. It was assumed that oxidative damage to ferritin caused by MG may induce an increase in the iron content in cells, which is deleterious to cells. This mechanism, in part, may provide an explanation or the deterioration of organs under diabetic conditions.

• BMB Reports
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• v.28 no.3
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• pp.191-196
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• 1995

The role of polyamines in skeletal myoblast differentiation was investigated using the polyamine metabolic inhibitor methylglyoxal bis(guanylhydrazone)(MGBG). Concentrations of intracellular free spermidine and spermine increased 2 to 2.5-fold at the onset of myoblast fusion. The systhesis of actin, and creatine kinase activity both dramatically increased during myotube formation. However, MGBG at a concentration of 0.5 mM not only abolished the increase of intracellular free polyamines, but also reduced cell fusion to almost half the level of untreated cells, without noticeable morphological alteration. The production of actin, and creatine kinase activity were almost completely abolished by MGBG. The inhibition of myoblast fusion by MGBG was partially recovered with 0.1 mM of spermidine or spermine added externally. Results indicate that polyamines are necessary for normal myoblast differentiation. Since the first indication of myoblast differentiation is alignment of muscle cells and membrane fusion of adjacent cells, and since polyamine depletion completely inhibited the synthesis of actin, which might be associted with membranes, polyamine might be involved in myoblast differentiation through membrane reorganization events.

• BMB Reports
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• v.45 no.12
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• pp.748-753
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• 2012

A sequence of 10 amino acids at the C-terminus region of methylglyoxal synthase from Escherichia coli (EMGS) provides an arginine, which plays a crucial role in forming a salt bridge with a proximal aspartate residue in the neighboring subunit, consequently transferring the allosteric signal between subunits. In order to verify the role of arginine, the gene encoding MGS from a thermophile species, Thermus sp. GH5 (TMGS) lacking this arginine was cloned with an additional 30 bp sequence at the 3'-end and then expressed in form of a fusion TMGS with a 10 residual segment at the C-terminus ($TMGS^+$). The resulting recombinant enzyme showed a significant increase in cooperativity towards phosphate, reflected by a change in the Hill coefficient (nH) from 1.5 to 1.99. Experiments including site directed mutagenesis for Asp-10 in TMGS and $TMGS^+$, two dimentional structural survey, fluorescence and irreversible thermoinactivation were carried out to confirm this pathway.