Protein nitration with aging in the rat semimembranosus and soleus muscles.
On the basis of the accelerated age-related effects in type II muscle, we hypothesized that with aging the semimembranosus (type II) muscle would accumulate a greater amount of oxidized proteins compared to proteins in the soleus (type I) muscle. In this study, 3-nitrotyrosine (3-NT) was used as a stable marker of protein oxidative damage. The presence of 3-NT was evaluated in muscles from young adult, old, and very old Fischer 344 rats to provide an indication of the time course of muscle protein oxidative damage. A significant age-associated increase in nitrotyrosine-modified proteins was observed. The modified proteins identified by matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry include the sarcoplasmic reticulum Ca(+2)-ATPase, aconitase, beta-enolase, triosephosphate isomerase, and carbonic anhydrase III. These proteins, involved in metabolism and calcium homeostasis, exhibited an age-dependent increase in 3-NT content in both muscles. However, significant levels of 3-NT modification were present at an earlier age in the semimembranosus muscle.
Fugere
Nicole A
NA
University of Minnesota, 420 Delaware Street S.E., Minneapolis, MN 55455, USA.
Ferrington
Deborah A
DA
Thompson
LaDora V
LV
D000375:Aging / Q000502:physiology*; D000818:Animals; D008297:Male; D018656:Muscle Fibers, Fast-Twitch / Q000378:metabolism*; D018657:Muscle Fibers, Slow-Twitch / Q000378:metabolism*; D009124:Muscle Proteins / Q000378:metabolism*; D018482:Muscle, Skeletal / Q000378:metabolism*; D018384:Oxidative Stress / Q000502:physiology; D051381:Rats; D011916:Rats, Inbred F344; D014443:Tyrosine / Q000031:analogs & derivatives* / Q000378:metabolism
D009124:Muscle Proteins; C002744:3-nitrotyrosine; D014443:Tyrosine