Mitochondrial Abundance and Function Differ Across Muscle Within Species

<i>Background</i>: Mitochondria are considered the powerhouse of cells, and skeletal muscle cells are no exception. However, information regarding muscle mitochondria from different species is limited. <i>Methods</i>: Different muscles from cattle, pigs and chickens were analyzed for mitochondrial DNA (mtDNA), protein and oxygen consumption. <i>Results</i>: Bovine oxidative muscle mitochondria contain greater mtDNA (<i>p</i> < 0.05), protein (succinate dehydrogenase, SDHA, <i>p</i> < 0.01; citrate synthase, CS, <i>p</i> < 0.01; complex I, CI, <i>p</i> < 0.05), and oxygen consumption (<i>p</i> < 0.01) than their glycolytic counterpart. Likewise, porcine oxidative muscle contains greater mtDNA (<i>p</i> < 0.01), mitochondrial proteins (SDHA, <i>p</i> < 0.05; CS, <i>p</i> < 0.001; CI, <i>p</i> < 0.01) and oxidative phosphorylation capacity (OXPHOS, <i>p</i> < 0.05) in comparison to glycolytic muscle. However, avian oxidative skeletal muscle showed no differences in absolute mtDNA, SDHA, CI, complex II, lactate dehydrogenase, or glyceraldehyde 3 phosphate dehydrogenase compared to their glycolytic counterpart. Even so, avian mitochondria isolated from oxidative muscles had greater OXPHOS capacity (<i>p</i> < 0.05) than glycolytic muscle. <i>Conclusions</i>: These data show avian mitochondria function is independent of absolute mtDNA content and protein abundance, and argue that multiple levels of inquiry are warranted to determine the wholistic role of mitochondria in skeletal muscle.

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Publication Details

Journal
Metabolites
Published
2024-10-16
DOI
https://doi.org/10.3390/metabo14100553
Citations
2
Primary Topic
Mitochondrial Function and Pathology
Type
article
Field-Weighted Citation Impact
0.47
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article

Mitochondrial Abundance and Function Differ Across Muscle Within Species

J.C. Wicks, Jocelyn Bodmer, David E. Gerrard, Tim H Shi et al.
2 citations
Metabolites
Mitochondrial Function and Pathology
0.47
article

Mitochondrial Abundance and Function Differ Across Muscle Within Species

J.C. Wicks, Jocelyn Bodmer, David E. Gerrard, Tim H Shi, Morgan D. Zumbaugh, Con‐Ning Yen, Michael E. Persia
article en
2 citations

Abstract

<i>Background</i>: Mitochondria are considered the powerhouse of cells, and skeletal muscle cells are no exception. However, information regarding muscle mitochondria from different species is limited. <i>Methods</i>: Different muscles from cattle, pigs and chickens were analyzed for mitochondrial DNA (mtDNA), protein and oxygen consumption. <i>Results</i>: Bovine oxidative muscle mitochondria contain greater mtDNA (<i>p</i> < 0.05), protein (succinate dehydrogenase, SDHA, <i>p</i> < 0.01; citrate synthase, CS, <i>p</i> < 0.01; complex I, CI, <i>p</i> < 0.05), and oxygen consumption (<i>p</i> < 0.01) than their glycolytic counterpart. Likewise, porcine oxidative muscle contains greater mtDNA (<i>p</i> < 0.01), mitochondrial proteins (SDHA, <i>p</i> < 0.05; CS, <i>p</i> < 0.001; CI, <i>p</i> < 0.01) and oxidative phosphorylation capacity (OXPHOS, <i>p</i> < 0.05) in comparison to glycolytic muscle. However, avian oxidative skeletal muscle showed no differences in absolute mtDNA, SDHA, CI, complex II, lactate dehydrogenase, or glyceraldehyde 3 phosphate dehydrogenase compared to their glycolytic counterpart. Even so, avian mitochondria isolated from oxidative muscles had greater OXPHOS capacity (<i>p</i> < 0.05) than glycolytic muscle. <i>Conclusions</i>: These data show avian mitochondria function is independent of absolute mtDNA content and protein abundance, and argue that multiple levels of inquiry are warranted to determine the wholistic role of mitochondria in skeletal muscle.

MetabolitesVol. 14(10)
Virginia Tech (US)
Life in Land
Openalex Percentile: Top 35%
Mitochondrial Function and Pathology
0.47
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