Effects of aging on mitochondrial function in skeletal muscle of American American Quarter Horses.
Skeletal muscle function, aerobic capacity, and mitochondrial (Mt) function have been found to decline with age in humans and rodents. However, not much is known about age-related changes in Mt function in equine skeletal muscle. Here, we compared fiber-type composition and Mt function in gluteus medius and triceps brachii muscle between young (age 1.8 ± 0.1 yr, n = 24) and aged (age 17-25 yr, n = 10) American Quarter Horses. The percentage of myosin heavy chain (MHC) IIX was lower in aged compared with young muscles (gluteus, P = 0.092; triceps, P = 0.012), while the percentages of MHC I (gluteus; P < 0.001) and MHC IIA (triceps; P = 0.023) were increased. Mass-specific Mt density, indicated by citrate synthase activity, was unaffected by age in gluteus, but decreased in aged triceps (P = 0.023). Cytochrome-c oxidase (COX) activity per milligram tissue and per Mt unit decreased with age in gluteus (P < 0.001 for both) and triceps (P < 0.001 and P = 0.003, respectively). Activity of 3-hydroxyacyl-CoA dehydrogenase per milligram tissue was unaffected by age, but increased per Mt unit in aged gluteus and triceps (P = 0.023 and P < 0.001, respectively). Mt respiration of permeabilized muscle fibers per milligram tissue was unaffected by age in both muscles. Main effects of age appeared when respiration was normalized to Mt content, with increases in LEAK, oxidative phosphorylation capacity, and electron transport system capacity (P = 0.038, P = 0.045, and P = 0.007, respectively), independent of muscle. In conclusion, equine skeletal muscle aging was accompanied by a shift in fiber-type composition, decrease in Mt density and COX activity, but preserved Mt respiratory function.
Department of Animal Sciences, University of Florida, Gainesville, Florida.
Chengcheng
C
Li
Department of Animal Sciences, University of Florida, Gainesville, Florida.
Sarah H
SH
White
Department of Animal Sciences, University of Florida, Gainesville, Florida.
Lori K
LK
Warren
Department of Animal Sciences, University of Florida, Gainesville, Florida steffiw@ufl.edu.
Stephanie E
SE
Wohlgemuth
D015094:3-Hydroxyacyl CoA Dehydrogenases / Q000378:metabolism; D000375:Aging / Q000378:metabolism / Q000502:physiology*; D000818:Animals; D002950:Citrate (si)-Synthase / Q000378:metabolism; D004579:Electron Transport / Q000502:physiology; D003576:Electron Transport Complex IV / Q000378:metabolism; D005260:Female; D006736:Horses; D008297:Male; D008928:Mitochondria / Q000378:metabolism / Q000502:physiology*; D018485:Muscle Fibers, Skeletal / Q000378:metabolism / Q000502:physiology*; D018995:Myosin Heavy Chains / Q000378:metabolism; D010084:Oxidation-Reduction
D015094:3-Hydroxyacyl CoA Dehydrogenases; D003576:Electron Transport Complex IV; D002950:Citrate (si)-Synthase; D018995:Myosin Heavy Chains
3-hydroxyacyl-CoA dehydrogenase; citrate synthase; cytochrome-c oxidase; high-resolution respirometry; myosin heavy chain isoform