Mass spectrometry-based survey of age-associated protein carbonylation in rat brain mitochondria

Laszlo Prokai, Liang Jun Yan, José L. Vera-Serrano, Stanley M. Stevens, Michael J. Forster

Research output: Contribution to journalArticlepeer-review

40 Scopus citations


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.

Original languageEnglish
Pages (from-to)1583-1589
Number of pages7
JournalJournal of Mass Spectrometry
Issue number12
StatePublished - Dec 2007


  • Aging
  • Gel electrophoresis
  • Matrix-assisted laser desorption/ionization
  • Mitochondria
  • Oxidative stress
  • Protein carbonylation
  • Proteomics
  • Tandem mass spectrometry


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