Dicarbonyls linked to damage in the powerhouse: glycation of mitochondrial proteins and oxidative stress.
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.
Rabbani
Naila
N
Protein Damage and Systems Biology Research Group, Clinical Sciences Research Institute, Warwick Medical School, University of Warwick, University Hospital, Coventry CV2 2DX, UK.
Thornalley
Paul J
PJ
D000375:Aging / Q000502:physiology; D000818:Animals; D017173:Caenorhabditis elegans / Q000502:physiology; D006031:Glycosylation; D006037:Glyoxal / Q000737:chemistry; D008136:Longevity / Q000502:physiology; D008928:Mitochondria / Q000737:chemistry / Q000378:metabolism; D024101:Mitochondrial Proteins / Q000737:chemistry* / Q000378:metabolism; D015394:Molecular Structure; D018384:Oxidative Stress; D050050:Protein Carbonylation; D011765:Pyruvaldehyde / Q000737:chemistry; D017382:Reactive Oxygen Species / Q000737:chemistry
D024101:Mitochondrial Proteins; D017382:Reactive Oxygen Species; D006037:Glyoxal; D011765:Pyruvaldehyde
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