Oxidative modification of ferritin induced by methylglyoxal.

Abstract:

: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.

journal_name

BMB Rep

journal_title

BMB reports

authors

An SH,Lee MS,Kang JH

doi

10.5483/BMBRep.2012.45.3.147

subject

Has Abstract

pub_date

2012-03-01 00:00:00

pages

147-52

issue

3

eissn

1976-6696

issn

1976-670X

journal_volume

45

pub_type

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