title: Fiber-type differences in muscle mitochondrial profiles.
abstract: Although striated muscles differ in mitochondrial content, the extent of fiber-type specific mitochondrial specializations is not well known. To address this issue, we compared mitochondrial structural and functional properties in red muscle (RM), white muscle (WM), and cardiac muscle of rainbow trout. Overall preservation of the basic relationships between oxidative phosphorylation complexes among fiber types was confirmed by kinetic analyses, immunoblotting of native holoproteins, and spectroscopic measurements of cytochrome content. Fiber-type differences in mitochondrial properties were apparent when parameters were expressed per milligram mitochondrial protein. However, the differences diminished when expressed relative to cytochrome oxidase (COX), possibly a more meaningful denominator than mitochondrial protein. Expressed relative to COX, there were no differences in oxidative phosphorylation enzyme activities, pyruvate-based respiratory rates, H2O2 production, or state 4 proton leak respiration. These data suggest most mitochondrial qualitative properties are conserved across fiber types. However, there remained modest differences ( approximately 50%) in stoichiometries of selected enzymes of the Krebs cycle, beta-oxidation, and antioxidant enzymes. There were clear differences in membrane fluidity (RM > cardiac, WM) and proton conductance (H+/min/mV/U COX: WM > RM > cardiac). The pronounced differences in mitochondrial content between fiber types could be attributed to a combination of differences in myonuclear domain and modest effects on the expression of nuclear- and mitochondrially encoded respiratory genes. Collectively, these studies suggest constitutive pathways that transcend fiber types are primarily responsible for determining most quantitative and qualitative properties of mitochondria.
authors.affiliation: Department of Biology, Queen's University, Kingston, Ontario, Canada K7L 3N6.
authors.forename: S C
authors.initials: SC
authors.lastname: Leary
authors.forename: C N
authors.initials: CN
authors.lastname: Lyons
authors.forename: A G
authors.initials: AG
authors.lastname: Rosenberger
authors.forename: J S
authors.initials: JS
authors.lastname: Ballantyne
authors.forename: J
authors.initials: J
authors.lastname: Stillman
authors.forename: C D
authors.initials: CD
authors.lastname: Moyes
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D002352:Carrier Proteins; D019069:Cell Respiration / Q000502:physiology; D002952:Citric Acid Cycle / Q000502:physiology; D004734:Energy Metabolism / Q000502:physiology; D005260:Female; D015971:Gene Expression Regulation, Enzymologic; D007700:Kinetics; D008297:Male; D008560:Membrane Fluidity / Q000502:physiology; D008565:Membrane Proteins / Q000378:metabolism; D008928:Mitochondria / Q000201:enzymology*; D025261:Mitochondrial Proton-Translocating ATPases; D018485:Muscle Fibers, Skeletal / Q000378:metabolism*; D018482:Muscle, Skeletal / Q000166:cytology* / Q000378:metabolism*; D017686:Oncorhynchus mykiss; D010085:Oxidative Phosphorylation; D011451:Prostaglandin-Endoperoxide Synthases / Q000235:genetics / Q000378:metabolism; D011522:Protons; D017382:Reactive Oxygen Species / Q000378:metabolism
chemical_list: D002352:Carrier Proteins; D008565:Membrane Proteins; D011522:Protons; D017382:Reactive Oxygen Species; D011451:Prostaglandin-Endoperoxide Synthases; D000251:Adenosine Triphosphatases; D025261:Mitochondrial Proton-Translocating ATPases; C020439:oligomycin sensitivity-conferring protein