Published in

Portland Press, Biochemical Society Transactions, 5(36), p. 1045-1050, 2008

DOI: 10.1042/bst0361045

Links

Tools

Export citation

Search in Google Scholar

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

Journal article published in 2008 by Naila Rabbani ORCID, Paul J. Thornalley
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

Full text: Download

Red circle
Preprint: archiving forbidden
Orange circle
Postprint: archiving restricted
Red circle
Published version: archiving forbidden
Data provided by SHERPA/RoMEO

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.