Con-Ning Yen, Jocelyn S Bodmer, Jordan C Wicks, Morgan D Zumbaugh, Michael E Persia, Tim H Shi, David E Gerrard
{"title":"物种内不同肌肉的线粒体丰度和功能存在差异","authors":"Con-Ning Yen, Jocelyn S Bodmer, Jordan C Wicks, Morgan D Zumbaugh, Michael E Persia, Tim H Shi, David E Gerrard","doi":"10.3390/metabo14100553","DOIUrl":null,"url":null,"abstract":"<p><p><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.</p>","PeriodicalId":18496,"journal":{"name":"Metabolites","volume":"14 10","pages":""},"PeriodicalIF":3.4000,"publicationDate":"2024-10-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11509590/pdf/","citationCount":"0","resultStr":"{\"title\":\"Mitochondrial Abundance and Function Differ Across Muscle Within Species.\",\"authors\":\"Con-Ning Yen, Jocelyn S Bodmer, Jordan C Wicks, Morgan D Zumbaugh, Michael E Persia, Tim H Shi, David E Gerrard\",\"doi\":\"10.3390/metabo14100553\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p><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.</p>\",\"PeriodicalId\":18496,\"journal\":{\"name\":\"Metabolites\",\"volume\":\"14 10\",\"pages\":\"\"},\"PeriodicalIF\":3.4000,\"publicationDate\":\"2024-10-16\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11509590/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Metabolites\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.3390/metabo14100553\",\"RegionNum\":3,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Metabolites","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.3390/metabo14100553","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Mitochondrial Abundance and Function Differ Across Muscle Within Species.
Background: Mitochondria are considered the powerhouse of cells, and skeletal muscle cells are no exception. However, information regarding muscle mitochondria from different species is limited. Methods: Different muscles from cattle, pigs and chickens were analyzed for mitochondrial DNA (mtDNA), protein and oxygen consumption. Results: Bovine oxidative muscle mitochondria contain greater mtDNA (p < 0.05), protein (succinate dehydrogenase, SDHA, p < 0.01; citrate synthase, CS, p < 0.01; complex I, CI, p < 0.05), and oxygen consumption (p < 0.01) than their glycolytic counterpart. Likewise, porcine oxidative muscle contains greater mtDNA (p < 0.01), mitochondrial proteins (SDHA, p < 0.05; CS, p < 0.001; CI, p < 0.01) and oxidative phosphorylation capacity (OXPHOS, p < 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 (p < 0.05) than glycolytic muscle. Conclusions: 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.
MetabolitesBiochemistry, Genetics and Molecular Biology-Molecular Biology
CiteScore
5.70
自引率
7.30%
发文量
1070
审稿时长
17.17 days
期刊介绍:
Metabolites (ISSN 2218-1989) is an international, peer-reviewed open access journal of metabolism and metabolomics. Metabolites publishes original research articles and review articles in all molecular aspects of metabolism relevant to the fields of metabolomics, metabolic biochemistry, computational and systems biology, biotechnology and medicine, with a particular focus on the biological roles of metabolites and small molecule biomarkers. Metabolites encourages scientists to publish their experimental and theoretical results in as much detail as possible. Therefore, there is no restriction on article length. Sufficient experimental details must be provided to enable the results to be accurately reproduced. Electronic material representing additional figures, materials and methods explanation, or supporting results and evidence can be submitted with the main manuscript as supplementary material.