IMMS Article

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

  1. Laszlo Prokai1,*,
  2. Liang-Jun Yan2,
  3. José L. Vera-Serrano1,
  4. Stanley M. Stevens Jr1,3,
  5. Michael J. Forster2

Article first published online: 17 DEC 2007

DOI: 10.1002/jms.1345

Issue

Journal of Mass Spectrometry

Journal of Mass Spectrometry

Volume 42, Issue 12, pages 1583–1589, December 2007

Additional Information

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

Author Information

  1. 1

    Department Molecular Biology and Immunology, University of North Texas Health Science Center, Fort Worth, USA

  2. 2

    Department of Pharmacology and Neuroscience, University of North Texas Health Science Center, Fort Worth, USA

  3. 3

    Proteomics Facility, Interdisciplinary Center for Biotechnology Research, University of Florida, Gainesville, USA

*Department of Molecular Biology and Immunology, University of North Texas Health Science Center, 3500 Camp Bowie Boulevard, Fort Worth, TX 76107-2699, USA.

  1. †

    Paper presented at the 25th Informal Meeting on Mass Spectrometry, Nyiregyháza-Sóstó, Hungary, 6–10 May, 2007.

Publication History

  1. Issue published online: 17 DEC 2007
  2. Article first published online: 17 DEC 2007
  3. Manuscript Accepted: 8 OCT 2007
  4. Manuscript Received: 17 JUN 2007

Funded by

  • National Institutes of Health
  • Robert A. Welch Foundation. Grant Numbers: AG025384, AG022550, RR016780

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Keywords:

  • proteomics;
  • mitochondria;
  • aging;
  • oxidative stress;
  • protein carbonylation;
  • gel electrophoresis;
  • matrix-assisted laser desorption/ionization;
  • tandem mass spectrometry

Abstract

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.

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