Proteomic identification of age-dependent protein nitration in rat skeletal muscle.
Age-related protein nitration was studied in skeletal muscle of Fisher 344 and Fisher 344/Brown Norway (BN) F1 rats by a proteomic approach. Proteins from young (4 months) and old (24 months) Fisher 344 rats and young (6 months) and old (34 months) Fisher 344/BN F1 animals were separated by 2-D gel electrophoresis. Western blot showed an age-related increase in the nitration of a few specific proteins, which were identified by MALDI-TOF MS and ESI-MS/MS. We identified age-dependent apparent nitration of beta-enolase, alpha-fructose aldolase, and creatine kinase, which perform important functions in muscle energy metabolism, suggesting that the nitration of such key proteins can be, in part, responsible for the decline of muscle motor function of the muscle. Furthermore, we have identified the apparent nitration of succinate dehydrogenase, rab GDP dissociation inhibitor beta (GdI-2), triosephosphate isomerase, troponin I, alpha-crystallin, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH).
Kanski
Jaroslaw
J
Department of Pharmaceutical Chemistry, University of Kansas, Lawrence, KS, USA.
Alterman
Michail A
MA
Schöneich
Christian
C
D017677:Age Distribution; D000818:Animals; D015153:Blotting, Western; D003402:Creatine Kinase / Q000378:metabolism*; D015180:Electrophoresis, Gel, Two-Dimensional; D004734:Energy Metabolism; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism*; D009043:Motor Activity / Q000502:physiology; D018482:Muscle, Skeletal / Q000201:enzymology; D030421:Peroxynitrous Acid / Q000378:metabolism*; D010751:Phosphopyruvate Hydratase / Q000378:metabolism*; D040901:Proteomics; D051381:Rats; D011916:Rats, Inbred F344; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014443:Tyrosine / Q000378:metabolism*
D030421:Peroxynitrous Acid; D014443:Tyrosine; D003402:Creatine Kinase; D005634:Fructose-Bisphosphate Aldolase; D010751:Phosphopyruvate Hydratase