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Biochem Soc Trans. 2008 Oct;36(Pt 5):1045-50. doi: 10.1042/BST0361045.

Dicarbonyls linked to damage in the powerhouse: glycation of mitochondrial proteins and oxidative stress.

Author information

1
Protein Damage and Systems Biology Research Group, Clinical Sciences Research Institute, Warwick Medical School, University of Warwick, University Hospital, Coventry CV2 2DX, UK.

Abstract

Protection of mitochondrial proteins from glycation by endogenous dicarbonyl compounds, methylglyoxal and glyoxal, was found recently to prevent increased formation of reactive oxygen species and oxidative and nitrosative damage to the proteome during aging and produce life extension in the nematode Caenorhabditis elegans. This suggests that dicarbonyl glycation damage to the mitochondrial proteome may be a preceding event to mitochondrial dysfunction leading to oxidative stress. Future research will address the functional charges in mitochondrial proteins that are the targets for dicarbonyl glycation.

PMID:
18793186
PMCID:
PMC2639773
DOI:
10.1042/BST0361045
[Indexed for MEDLINE]
Free PMC Article

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