Mass spectrometry-based survey of age-associated protein carbonylation in rat brain mitochondria.
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.
Prokai
Laszlo
L
Department Molecular Biology and Immunology, University of North Texas Health Science Center, Fort Worth 76109-2699, USA. lprokai@hsc.unt.edu
Yan
Liang-Jun
LJ
Vera-Serrano
José L
JL
Stevens
Stanley M
SM
Forster
Michael J
MJ
D000375:Aging / Q000502:physiology; D000818:Animals; D001921:Brain / Q000254:growth & development*; D001923:Brain Chemistry / Q000502:physiology*; D004591:Electrophoresis, Polyacrylamide Gel; D006834:Hydrazines / Q000737:chemistry; D007120:Immunochemistry; D008297:Male; D008928:Mitochondria / Q000737:chemistry / Q000378:metabolism*; D051336:Mitochondrial Membranes / Q000737:chemistry / Q000378:metabolism; D008970:Molecular Weight; D050050:Protein Carbonylation / Q000502:physiology*; D051381:Rats; D017207:Rats, Sprague-Dawley; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D053719:Tandem Mass Spectrometry
D006834:Hydrazines; C446799:dinitrophenylhydrazine