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Home / Equine Research Bank / Equine Vet J / Muscle fibre transition and transcriptional changes of horse...
Equine veterinary journal2023; 56(1); 178-192; doi: 10.1111/evj.13968

Muscle fibre transition and transcriptional changes of horse skeletal muscles during traditional Mongolian endurance training.

Abstract: Traditional Mongolian endurance training is an effective way to improve the athletic ability of the horse for endurance events and is widely used. This incorporates aerobic exercise and intermittent fasting and these altered physiologic conditions are associated with switches between muscle fibre types. Objective: To better understand the adaption of horse skeletal muscle to traditional Mongolian endurance training from muscle fibre characteristics and transcriptional levels and to explore possible molecular mechanisms associated with the endurance performance of horses. Methods: Before-after study. Methods: Muscle fibre type switches and muscle transcriptome changes in six Mongolian horses were assessed during 4 weeks of training. Transcriptomic and histochemical analyses were performed. The activities of oxidative and glycolytic metabolic enzymes were analysed and we generated deep RNA-sequencing data relating to skeletal muscles. Results: A fast-to-slow muscle fibre transition occurred in horse skeletal muscles, with a concomitant increase of oxidative enzyme activity and decreased glycolytic enzyme activity. Numerous differentially expressed genes were involved in the control of muscle protein balance and degradation. Differential alternative splicing events were also found during training which included exon-skipping events in Ttn that were associated with muscle atrophy. Differentially expressed noncoding RNAs showed connections with muscle protein balance-related pathways and fibre type specification via the post-transcriptional regulation of miRNA. Conclusions: The study focuses on horse athletic ability only from the aspect of muscular adaptation. Conclusions: Traditional Mongolian endurance training-induced muscle fibre transition and metabolic and transcriptional changes. Muscle-specific non-coding RNAs could contribute to these transcriptomic changes during training.
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Publication Date: 2023-06-22 PubMed ID: 37345447DOI: 10.1111/evj.13968Google Scholar: Lookup
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Summary

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This study investigates the effects of traditional Mongolian endurance training on horse muscle adaptation by examining changes in muscle fibre types and analyzing transcriptome level changes. The research found muscle fibre transitions and metabolic and transcriptional shifts related to this training.

Research Objectives and Methods

  • The study aimed to understand how horse skeletal muscles adapt to traditional Mongolian endurance training. This understanding was sought at the level of muscle fibre characteristics and the transcriptional level, with the aim of identifying molecular mechanisms associated with endurance performance in horses.
  • The researchers used a before-and-after study design, assessing changes in Mongolian horses’ muscle fibre types and muscle transcriptome over a four-week training period.
  • Histochemical and transcriptomic analyses were performed, alongside the analysis of the activity of oxidative and glycolytic metabolic enzymes. The researchers also generated deep RNA-sequencing data related to the skeletal muscles.

Research Findings

  • A transition from fast to slow muscle fibre types was observed in the skeletal muscles of the horses, accompanied by an increase in oxidative enzyme activity and a decrease in glycolytic enzyme activity.
  • Both the balance and degradation of muscle protein were found to be linked with various differentially expressed genes.
  • The study recorded differential alternative splicing events during training, including exon-skipping events in the Ttn gene associated with muscle atrophy.
  • Differentially expressed noncoding RNAs were found to be related to muscle protein balance-related pathways and fibre type specification, largely through the post-transcriptional regulation of miRNA.

Conclusions

  • The study concluded that traditional Mongolian endurance training leads to muscle fibre transitions as well as metabolic and transcriptional changes in the skeletal muscles of horses.
  • It was also suggested that muscle-specific non-coding RNAs could contribute to these transcriptomic changes seen during endurance training. However, the study emphasized that the focus was only on muscular adaptation as a factor in horse athletic ability.

Cite This Article

APA
Bou T, Ding W, Ren X, Liu H, Gong W, Jia Z, Zhang X, Dugarjaviin M, Bai D. (2023). Muscle fibre transition and transcriptional changes of horse skeletal muscles during traditional Mongolian endurance training. Equine Vet J, 56(1), 178-192. https://doi.org/10.1111/evj.13968

Publication

Equine veterinary journal
ISSN: 2042-3306
NlmUniqueID: 0173320
Country: United States
Language: English
Volume: 56
Issue: 1
Pages: 178-192

Researcher Affiliations

Bou, Tugeqin
  • Key Laboratory of Equus Germplasm Innovation (Co-construction by Ministry and Province), Ministry of Agriculture and Rural Affairs; Inner Mongolia Key Laboratory of Equine Genetics, Breeding and Reproduction; Equus Research Center, College of Animal Science, Inner Mongolia Agricultural University, Hohhot, China.
Ding, Wenqi
  • Key Laboratory of Equus Germplasm Innovation (Co-construction by Ministry and Province), Ministry of Agriculture and Rural Affairs; Inner Mongolia Key Laboratory of Equine Genetics, Breeding and Reproduction; Equus Research Center, College of Animal Science, Inner Mongolia Agricultural University, Hohhot, China.
Ren, Xiujuan
  • Key Laboratory of Equus Germplasm Innovation (Co-construction by Ministry and Province), Ministry of Agriculture and Rural Affairs; Inner Mongolia Key Laboratory of Equine Genetics, Breeding and Reproduction; Equus Research Center, College of Animal Science, Inner Mongolia Agricultural University, Hohhot, China.
Liu, Huiying
  • Key Laboratory of Equus Germplasm Innovation (Co-construction by Ministry and Province), Ministry of Agriculture and Rural Affairs; Inner Mongolia Key Laboratory of Equine Genetics, Breeding and Reproduction; Equus Research Center, College of Animal Science, Inner Mongolia Agricultural University, Hohhot, China.
Gong, Wendian
  • Key Laboratory of Equus Germplasm Innovation (Co-construction by Ministry and Province), Ministry of Agriculture and Rural Affairs; Inner Mongolia Key Laboratory of Equine Genetics, Breeding and Reproduction; Equus Research Center, College of Animal Science, Inner Mongolia Agricultural University, Hohhot, China.
Jia, Zijie
  • Key Laboratory of Equus Germplasm Innovation (Co-construction by Ministry and Province), Ministry of Agriculture and Rural Affairs; Inner Mongolia Key Laboratory of Equine Genetics, Breeding and Reproduction; Equus Research Center, College of Animal Science, Inner Mongolia Agricultural University, Hohhot, China.
Zhang, Xinzhuang
  • Key Laboratory of Equus Germplasm Innovation (Co-construction by Ministry and Province), Ministry of Agriculture and Rural Affairs; Inner Mongolia Key Laboratory of Equine Genetics, Breeding and Reproduction; Equus Research Center, College of Animal Science, Inner Mongolia Agricultural University, Hohhot, China.
Dugarjaviin, Manglai
  • Key Laboratory of Equus Germplasm Innovation (Co-construction by Ministry and Province), Ministry of Agriculture and Rural Affairs; Inner Mongolia Key Laboratory of Equine Genetics, Breeding and Reproduction; Equus Research Center, College of Animal Science, Inner Mongolia Agricultural University, Hohhot, China.
Bai, Dongyi
  • Key Laboratory of Equus Germplasm Innovation (Co-construction by Ministry and Province), Ministry of Agriculture and Rural Affairs; Inner Mongolia Key Laboratory of Equine Genetics, Breeding and Reproduction; Equus Research Center, College of Animal Science, Inner Mongolia Agricultural University, Hohhot, China.

MeSH Terms

  • Horses
  • Animals
  • Endurance Training / veterinary
  • Muscle, Skeletal / metabolism
  • Muscle Fibers, Skeletal / metabolism
  • Muscle Proteins / metabolism
  • Sports
  • Physical Endurance / physiology

Grant Funding

  • 2019MS03064 / Inner Mongolia Science and Technology Department Construction Project
  • 2021ZD0018 / Inner Mongolia Science and Technology Department Construction Project
  • ZD20190039 / Inner Mongolia Science and Technology Department Construction Project
  • 31960657 / National Natural Science Foundation of China
  • 31902188 / National Natural Science Foundation of China International (Regional)
  • 31961143025 / National Natural Science Foundation of China International (Regional)

References

This article includes 65 references
  1. Haffner JC, Juergens T, Yagaan B, Mendjargal A, Yandag G. Mongolian horses: training and racing.. J Equine Vet 2004;24(1):5-8.
  2. Zouhal H, Saeidi A, Salhi A, Li H, Essop MF, Laher I. Exercise training and fasting: current insights.. Open Access J Sports Med 2020;11:1-28.
  3. Goodpaster BH, Katsiaras A, Kelley DE. Enhanced fat oxidation through physical activity is associated with improvements in insulin sensitivity in obesity.. Diabetes 2003;52(9):2191-7.
  4. Vieira AF, Costa RR, Macedo RC, Coconcelli L, Kruel LF. Effects of aerobic exercise performed in fasted v. fed state on fat and carbohydrate metabolism in adults: a systematic review and meta-analysis.. Br J Nutr 2016;116(7):1153-64.
  5. Serrano AL, Quiroz-Rothe E, Rivero JL. Early and long-term changes of equine skeletal muscle in response to endurance training and detraining.. Pflug Arch Eur J Physiol 2000;441(2-3):263-74.
  6. Votion DM, Navet R, Lacombe VA, Sluse F, Essen-Gustavsson B, Hinchcliff KW. Muscle energetics in exercising horses.. Equine Comp Exerc Physiol 2007;4(3-4):105-18.
  7. Rivero JL, Agüera E, Monterde JG, Barbudo MV, Miró F. Comparative study of muscle fibre type composition in the middle gluteal muscle of Andalusian, thoroughbred and Arabian horses.. J Equine Vet 1989;9(6):337-40.
  8. Rivero JL, Serrano AL, Henckel P, Agüera E. Muscle fibre type composition and fibre size in successfully and unsuccessfully endurance-raced horses.. J Appl Physiol (Bethesda, Md: 1985) 1993;75(4):1758-66.
  9. Van Proeyen K, Szlufcik K, Nielens H, Ramaekers M, Hespel P. Beneficial metabolic adaptations due to endurance exercise training in the fasted state.. J Appl Physiol (Bethesda, Md: 1985) 2011;110(1):236-45.
  10. Bouguerra L, Ben Abderrahman A, Chtourou H, Zouhal H, Tabka Z, Prioux J. The effect of time-of-day of training during Ramadan on physiological parameters in highly trained endurance athletes.. Biol Rhythm Res 2017;48(4):541-55.
  11. Kim D, Langmead B, Salzberg SL. HISAT: a fast spliced aligner with low memory requirements.. Nat Methods 2015;12(4):357-60.
  12. Kovaka S, Zimin AV, Pertea GM, Razaghi R, Salzberg SL, Pertea M. Transcriptome assembly from long-read RNA-seq alignments with StringTie2.. Genome Biol 2019;20(1):278.
  13. Love MI, Huber W, Anders S. Moderated estimation of fold change and dispersion for RNA-seq data with DESeq2.. Genome Biol 2014;15(12):550.
  14. Shen S, Park JW, Lu ZX, Lin L, Henry MD, Wu YN. rMATS: robust and flexible detection of differential alternative splicing from replicate RNA-Seq data.. Proc Natl Acad Sci USA 2014;111(51):E5593-601.
  15. Wang L, Park HJ, Dasari S, Wang S, Kocher JP, Li W. CPAT: coding-potential assessment tool using an alignment-free logistic regression model.. Nucleic Acids Res 2013;41(6):e74.
  16. Sun L, Luo H, Bu D, Zhao G, Yu K, Zhang C. Utilizing sequence intrinsic composition to classify protein-coding and long non-coding transcripts.. Nucleic Acids Res 2013;41(17):e166.
  17. Kang YJ, Yang DC, Kong L, Hou M, Meng YQ, Wei L. CPC2: a fast and accurate coding potential calculator based on sequence intrinsic features.. Nucleic Acids Res 2017;45(W1):W12-w16.
  18. Gao Y, Zhang J, Zhao F. Circular RNA identification based on multiple seed matching.. Brief Bioinform 2018;19(5):803-10.
  19. Zhang XO, Dong R, Zhang Y, Zhang JL, Luo Z, Zhang J. Diverse alternative back-splicing and alternative splicing landscape of circular RNAs.. Genome Res 2016;26(9):1277-87.
  20. Langmead B, Salzberg SL. Fast gapped-read alignment with Bowtie 2.. Nat Methods 2012;9(4):357-9.
  21. Friedländer MR, Mackowiak SD, Li N, Chen W, Rajewsky N. miRDeep2 accurately identifies known and hundreds of novel microRNA genes in seven animal clades.. Nucleic Acids Res 2012;40(1):37-52.
  22. Enright AJ, John B, Gaul U, Tuschl T, Sander C, Marks DS. MicroRNA targets in drosophila.. Genome Biol 2003;5(1):R1.
  23. Agarwal V, Bell GW, Nam JW, Bartel DP. Predicting effective microRNA target sites in mammalian mRNAs.. Elife 2015;4:4.
  24. Aleman M, Nieto JE. Gene expression of proteolytic systems and growth regulators of skeletal muscle in horses with myopathy associated with pituitary pars intermedia dysfunction.. Am J Vet Res 2010;71(6):664-70.
  25. Eivers SS, McGivney BA, Gu J, MacHugh DE, Katz LM, Hill EW. PGC-1α encoded by the PPARGC1A gene regulates oxidative energy metabolism in equine skeletal muscle during exercise.. Anim Genet 2012;43(2):153-62.
  26. Mach N, Plancade S, Pacholewska A, Lecardonnel J, Rivière J, Moroldo M. Integrated mRNA and miRNA expression profiling in blood reveals candidate biomarkers associated with endurance exercise in the horse.. Sci Rep 2016;6:22932.
  27. Shannon P, Markiel A, Ozier O, Baliga NS, Wang JT, Ramage D. Cytoscape: a software environment for integrated models of biomolecular interaction networks.. Genome Res 2003;13(11):2498-504.
  28. Schiaffino S, Reggiani C. Fibre types in mammalian skeletal muscles.. Physiol Rev 2011;91(4):1447-531.
  29. Labeit S, Kolmerer B. Titins: giant proteins in charge of muscle ultrastructure and elasticity.. Science (New York, NY) 1995;270(5234):293-6.
  30. Ottenheijm CA, Knottnerus AM, Buck D, Luo X, Greer K, Hoying A. Tuning passive mechanics through differential splicing of titin during skeletal muscle development.. Biophys J 2009;97(8):2277-86.
  31. van Rooij E, Quiat D, Johnson BA, Sutherland LB, Qi X, Richardson JA. A family of microRNAs encoded by myosin genes governs myosin expression and muscle performance.. Dev Cell 2009;17(5):662-73.
  32. Chu W, Zhang F, Song R, Li Y, Wu P, Chen L. Proteomic and microRNA transcriptome analysis revealed the microRNA-SmyD1 network regulation in skeletal muscle fibres performance of Chinese perch.. Sci Rep 2017;7(1):16498.
  33. Elia L, Contu R, Quintavalle M, Varrone F, Chimenti C, Russo MA. Reciprocal regulation of microRNA-1 and insulin-like growth factor-1 signal transduction cascade in cardiac and skeletal muscle in physiological and pathological conditions.. Circulation 2009;120(23):2377-85.
  34. Lyu M, Wang X, Meng X, Qian H, Li Q, Ma B. Chi-miR-487b-3p inhibits goat myoblast proliferation and differentiation by targeting IRS1 through the IRS1/PI3K/Akt signaling pathway.. Int J Mol Sci 2021;23(1):115.
  35. Wang J, Tan J, Qi Q, Yang L, Wang Y, Zhang C. miR-487b-3p suppresses the proliferation and differentiation of myoblasts by targeting IRS1 in skeletal muscle myogenesis.. Int J Biol Sci 2018;14(7):760-74.
  36. Wang X, Cao X, Dong D, Shen X, Cheng J, Jiang R. Circular RNA TTN acts as a miR-432 sponge to facilitate proliferation and differentiation of myoblasts via the IGF2/PI3K/AKT signaling pathway.. Mol Ther Nucleic Acids 2019;18:966-80.
  37. Ma M, Wang X, Chen X, Cai R, Chen F, Dong W. MicroRNA-432 targeting E2F3 and P55PIK inhibits myogenesis through PI3K/AKT/mTOR signaling pathway.. RNA Biol 2017;14(3):347-60.
  38. Gil N, Ulitsky I. Regulation of gene expression by cis-acting long non-coding RNAs.. Nat Rev Genet 2020;21(2):102-17.
  39. Rivero JL, Henckel P. Muscle biopsy index for discriminating between endurance horses with different performance records.. Res Vet Sci 1996;61(1):49-54.
  40. Gondim FJ, Modolo LV, Campos GE, Salgado I. Neuronal nitric oxide synthase is heterogeneously distributed in equine myofibres and highly expressed in endurance trained horses.. Can J Vet Res 2005;69(1):46-52.
  41. MacArthur DG, Seto JT, Chan S, Quinlan KG, Raftery JM, Turner N. An Actn3 knockout mouse provides mechanistic insights into the association between alpha-actinin-3 deficiency and human athletic performance.. Hum Mol Genet 2008;17(8):1076-86.
  42. MacArthur DG, Seto JT, Raftery JM, Quinlan KG, Huttley GA, Hook JW. Loss of ACTN3 gene function alters mouse muscle metabolism and shows evidence of positive selection in humans.. Nat Genet 2007;39(10):1261-5.
  43. Quinlan KG, Seto JT, Turner N, Vandebrouck A, Floetenmeyer M, Macarthur DG. Alpha-actinin-3 deficiency results in reduced glycogen phosphorylase activity and altered calcium handling in skeletal muscle.. Hum Mol Genet 2010;19(7):1335-46.
  44. Ropka-Molik K, Stefaniuk-Szmukier M, Zu K, Piórkowska K, Bugno-Poniewierska M. Exercise-induced modification of the skeletal muscle transcriptome in Arabian horses.. Physiol Genomics 2017;49(6):318-26.
  45. Ibrahim M, Wasselin T, Challet E, Van Dorsselaer A, Le Maho Y, Raclot T. Transcriptional changes involved in atrophying muscles during prolonged fasting in rats.. Int J Mol Sci 2020;21(17):5984.
  46. Cherel Y, Attaix D, Rosolowska-Huszcz D, Belkhou R, Robin JP, Arnal M. Whole-body and tissue protein synthesis during brief and prolonged fasting in the rat.. Clinical Science 1991;81(5):611-9.
  47. Bertile F, Le Maho Y, Raclot T. Coordinate upregulation of proteolytic-related genes in rat muscle during late fasting.. Biochem Biophys Res Commun 2003;311(4):929-34.
  48. Rahmani J, Kord Varkaneh H, Clark C, Zand H, Bawadi H, Ryan PM. The influence of fasting and energy restricting diets on IGF-1 levels in humans: a systematic review and meta-analysis.. Ageing Res Rev 2019;53:100910.
  49. Schiaffino S, Dyar KA, Ciciliot S, Blaauw B, Sandri M. Mechanisms regulating skeletal muscle growth and atrophy.. FEBS J 2013;280(17):4294-314.
  50. Schiaffino S, Mammucari C. Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models.. Skelet Muscle 2011;1(1):4.
  51. Milan G, Romanello V, Pescatore F, Armani A, Paik JH, Frasson L. Regulation of autophagy and the ubiquitin-proteasome system by the FoxO transcriptional network during muscle atrophy.. Nat Commun 2015;6:6670.
  52. Zhao J, Brault JJ, Schild A, Goldberg AL. Coordinate activation of autophagy and the proteasome pathway by FoxO transcription factor.. Autophagy 2008;4(3):378-80.
  53. Trapnell C, Williams BA, Pertea G, Mortazavi A, Kwan G, van Baren MJ. Transcript assembly and quantification by RNA-Seq reveals unannotated transcripts and isoform switching during cell differentiation.. Nat Biotechnol 2010;28(5):511-5.
  54. Bland CS, Wang ET, Vu A, David MP, Castle JC, Johnson JM. Global regulation of alternative splicing during myogenic differentiation.. Nucleic Acids Res 2010;38(21):7651-64.
  55. Sebastian S, Faralli H, Yao Z, Rakopoulos P, Palii C, Cao Y. Tissue-specific splicing of a ubiquitously expressed transcription factor is essential for muscle differentiation.. Genes Dev 2013;27(11):1247-59.
  56. Farah CS, Reinach FC. The troponin complex and regulation of muscle contraction.. FASEB J 1995;9(9):755-67.
  57. Zot AS, Potter JD. Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction.. Annu Rev Biophys Biophys Chem 1987;16:535-59.
  58. Qiu J, Wu L, Chang Y, Sun H, Sun J. Alternative splicing transitions associate with emerging atrophy phenotype during denervation-induced skeletal muscle atrophy.. J Cell Physiol 2021;236(6):4496-514.
  59. Sun J, Yang H, Yang X, Chen X, Xu H, Shen Y. Global alternative splicing landscape of skeletal muscle atrophy induced by hindlimb unloading.. Ann Transl Med 2021;9(8):643.
  60. Henrich M, Ha P, Wang Y, Ting K, Stodieck L, Soo C. Alternative splicing diversifies the skeletal muscle transcriptome during prolonged spaceflight.. Skelet Muscle 2022;12(1):11.
  61. Cesana M, Cacchiarelli D, Legnini I, Santini T, Sthandier O, Chinappi M. A long noncoding RNA controls muscle differentiation by functioning as a competing endogenous RNA.. Cell 2011;147(2):358-69.
  62. Legnini I, Morlando M, Mangiavacchi A, Fatica A, Bozzoni I. A feedforward regulatory loop between HuR and the long noncoding RNA linc-MD1 controls early phases of myogenesis.. Mol Cell 2014;53(3):506-14.
  63. Li H, Yang J, Jiang R, Wei X, Song C, Huang Y. Long non-coding RNA profiling reveals an abundant MDNCR that promotes differentiation of myoblasts by sponging miR-133a.. Mol Ther Nucleic Acid 2018;12:610-25.
  64. Liang T, Zhou B, Shi L, Wang H, Chu Q, Xu F. lncRNA AK017368 promotes proliferation and suppresses differentiation of myoblasts in skeletal muscle development by attenuating the function of miR-30c.. FASEB J 2018;32(1):377-89.
  65. Sun X, Li M, Sun Y, Cai H, Lan X, Huang Y. The developmental transcriptome sequencing of bovine skeletal muscle reveals a long noncoding RNA, lncMD, promotes muscle differentiation by sponging miR-125b.. Biochim Biophys Acta 2016;1863(11):2835-45.
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