Mass spectrometry-based survey of age-associated protein carbonylation in rat brain mitochondria |
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Authors: | Prokai Laszlo Yan Liang-Jun Vera-Serrano José L Stevens Stanley M Forster Michael J |
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Institution: | Department Molecular Biology and Immunology, University of North Texas Health Science Center, Fort Worth 76109-2699, USA. lprokai@hsc.unt.edu |
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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. |
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Keywords: | proteomics mitochondria aging oxidative stress protein carbonylation gel electrophoresis matrix‐assisted laser desorption/ionization tandem mass spectrometry |
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