Oxidative modification of ferritin induced by methylglyoxal

An, Sung Ho; Lee, Myeong Seon; Kang, Jung Hoon

doi:10.5483/bmbrep.2012.45.3.147

Cited by 11 publications

(8 citation statements)

References 55 publications

(47 reference statements)

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“…Studies have shown that ferritin can act as an acute phase reactant; also, ferritin has been linked to certain metabolic diseases and their components [2,3,20]. The latter assumption has been derived only from statistical correlations, with the mechanisms through which ferritin participates in such disorders remaining unclear [3,21]. On the other hand, it has been shown that ferritin can undergo oxidative damage by carbonyl compounds, such as methylglyoxal or ROS, which have been related to the increase in the iron content of cells that can be deleterious to cells [21,22].…”

Section: Discussionmentioning

confidence: 99%

“…The latter assumption has been derived only from statistical correlations, with the mechanisms through which ferritin participates in such disorders remaining unclear [3,21]. On the other hand, it has been shown that ferritin can undergo oxidative damage by carbonyl compounds, such as methylglyoxal or ROS, which have been related to the increase in the iron content of cells that can be deleterious to cells [21,22]. Advanced glycation end-products (AGEs) are a diverse group of highly oxidant compounds with pathogenic significance in diabetes as well as in several other chronic diseases.…”

Section: Discussionmentioning

confidence: 99%

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Glycoxidated ferritin induces the release of microparticles positive for Toll-like receptors derived from peripheral blood CD14+ cells

Soto

Moroyoqui

Martínez-Soto

et al. 2017

ARCH BIOL SCI BELGRA

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Both increased serum ferritin levels and Toll-like receptor (TLR) activation show independent association with the inflammatory processes. During inflammation, cell activation and apoptosis are accompanied by the release of membranederived microparticles (MPs), which are considered to be mediators of intercellular communication as they induce specific responses in target cells. The aim of this study was to determine whether glycated and glycoxidated ferritin induce in vitro release TLR microparticles from CD14+ peripheral blood mononuclear cells. Peripheral blood mononuclear cells were stimulated with glycated, glycoxidated and native ferritin. The release of microparticles from CD14+ cells, the presence of TLR2+ and TLR4+ on the microparticles surface and the presence of interleukins-6 and -8 (IL-6 and IL-8) inside the microparticles after stimulation were determined by flow cytometry. The role of nuclear factor κB (NF-κB) was evaluated by pretreatment of the cells with the Bay 11-7085 inhibitor. Glycated and glycoxidated ferritin induced the release of microparticles from CD14+ cells, the majority of which expressed TLR2+ and TLR4+ on their surface and contained IL-6 and IL-8. These effects were dependent on NF-κB activation. Our findings show that glycated and glycoxidated ferritin might be involved in the release of microparticles and stimulation of inflammatory responses.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Glycoxidated ferritin induces the release of microparticles positive for Toll-like receptors derived from peripheral blood CD14+ cells

Soto

Moroyoqui

Martínez-Soto

et al. 2017

ARCH BIOL SCI BELGRA

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“…In addition, we have also reported that the modification of ferritin, iron containing protein, was induced by MG (16). To further examine whether the modification of ferritin causes DNA damage, we exposed the plasmid pUC19 to the ferritin/MG/lysine system.…”

Section: Resultsmentioning

confidence: 99%

Oxidative damage of DNA induced by the reaction of methylglyoxal with lysine in the presence of ferritin

Kang

2013

BMB Reports

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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. [BMB Reports 2013; 46(4): 225-229]

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“…Since acid hydrolysis destroys tryptophan, the tryptophan content of oxidized and native Cu,Zn-SOD preparations was determined by means of alkaline hydrolysis as described previously (43). The amino acid content of acid and alkaline hydrolysates was determined by HPLC separation of their phenylisothiocyanate derivatives by using a Pico-tag free amino acid analysis column and a 996 photodiode array detector (Waters, USA).…”

Section: Methodsmentioning

confidence: 99%

Modification and inactivation of Cu,Zn-superoxide dismutase by the lipid peroxidation product, acrolein

Kang

2013

BMB Reports

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Acrolein is the most reactive aldehydic product of lipid peroxidation and is found to be elevated in the brain when oxidative stress is high. The effects of acrolein on the structure and function of human Cu,Zn-superoxide dismutase (SOD) were examined. When Cu,Zn-SOD was incubated with acrolein, the covalent crosslinking of the protein was increased, and the loss of enzymatic activity was increased in a dose-dependent manner. Reactive oxygen species (ROS) scavengers and copper chelators inhibited the acrolein-mediated Cu,Zn-SOD modification and the formation of carbonyl compound. The present study shows that ROS may play a critical role in acrolein-induced Cu,Zn-SOD modification and inactivation. When Cu,Zn-SOD that has been exposed to acrolein was subsequently analyzed by amino acid analysis, serine, histidine, arginine, threonine and lysine residues were particularly sensitive. It is suggested that the modification and inactivation of Cu,Zn-SOD by acrolein could be produced by more oxidative cell environments. [BMB Reports 2013; 46(11): 555-560]

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Oxidative modification of ferritin induced by methylglyoxal

Abstract: Methylglyoxal (MG) was identified as an intermediate in

Cited by 11 publications

References 55 publications

Glycoxidated ferritin induces the release of microparticles positive for Toll-like receptors derived from peripheral blood CD14+ cells

Glycoxidated ferritin induces the release of microparticles positive for Toll-like receptors derived from peripheral blood CD14+ cells

Oxidative damage of DNA induced by the reaction of methylglyoxal with lysine in the presence of ferritin

Modification and inactivation of Cu,Zn-superoxide dismutase by the lipid peroxidation product, acrolein

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