Paper presented at the 25th Informal Meeting on Mass Spectrometry, Nyiregyháza-Sóstó, Hungary, 6–10 May, 2007.
Mass spectrometry-based survey of age-associated protein carbonylation in rat brain mitochondria†
Article first published online: 17 DEC 2007
Copyright © 2007 John Wiley & Sons, Ltd.
Journal of Mass Spectrometry
Volume 42, Issue 12, pages 1583–1589, December 2007
How to Cite
Prokai, L., Yan, L.-J., Vera-Serrano, J. L., Stevens, S. M. and Forster, M. J. (2007), Mass spectrometry-based survey of age-associated protein carbonylation in rat brain mitochondria. J. Mass Spectrom., 42: 1583–1589. doi: 10.1002/jms.1345
- Issue published online: 17 DEC 2007
- Article first published online: 17 DEC 2007
- Manuscript Accepted: 8 OCT 2007
- Manuscript Received: 17 JUN 2007
- National Institutes of Health
- Robert A. Welch Foundation. Grant Numbers: AG025384, AG022550, RR016780
- oxidative stress;
- protein carbonylation;
- gel electrophoresis;
- matrix-assisted laser desorption/ionization;
- tandem mass spectrometry
There is a body of evidence lending credence to the idea that oxidative stress may be responsible for age-related deleterious changes in brain function, and that protein carbonylation is a potential marker for such changes. An investigation of oxidative damage to mitochondrial proteins from aged rat brains was done using gel electrophoresis coupled with carbonylation-specific immunostaining. Six proteins that appeared to be susceptible to oxidative modification were identified by in-gel trypsin digestion followed by matrix-assisted laser desorption/ionization mass spectrometry and tandem mass spectrometry. Two subunits of the H+-transporting ATP synthase, adenine nucleotide translocator, voltage-dependent anion channel, glutamate oxaloacetate transaminase, and aconitase were identified as likely targets of age-associated carbonylation. Copyright © 2007 John Wiley & Sons, Ltd.