FREE SHIPPING over $40
OVER 10000 FIVE-STAR REVIEWS
5% OFF ALL SUBSCRIPTIONS
100% HAPPINESS GUARANTEE
Analyze Diet
0
Journal of muscle research and cell motility2000; 21(3); 235-245; doi: 10.1023/a:1005642632711

Myosin heavy chain profile of equine gluteus medius muscle following prolonged draught-exercise training and detraining.

Abstract: Fourteen 4-year old Andalusian mares were used to examine the plasticity of myosin heavy chain (MHC) composition in horse skeletal muscle with heavy draught-exercise training and detraining. Seven horses underwent a training programme based on carriage exercises for 8 months. Afterwards, they were kept in paddocks for 3 months. The remaining seven animals were used as control horses. Three gluteus medius muscle biopsies were removed at depths of 20, 40 and 60 mm from each horse before (month 0), during the training (months 3 and 8) and after detraining (month 11). Myosin heavy chain composition was analysed by electrophoresis and immunohistochemically with anti-MHC monoclonal antibodies. Fibre areas, oxidative capacity and capillaries were studied histochemically. After 8 months of training, MHC-IIX and IIX fibres decreased whereas MHC-I and type I and I + IIA fibres increased. Neither MHC-IIA nor the percentage of IIA fibres changed when the data were considered as a whole, but the proportion of MHC-IIA increased in the superficial region of the muscle after 8 months of training. Mean areas of type II fibres were not affected by training and detraining, but the cross-sectional of type I fibres increased after 3 month of training and not further increases were recorded afterward. The percentage of high-oxidative capacity fibres and the number of capillaries per mm2 increased with training. Most of these muscular adaptations reverted after detraining. These results indicate that long term draught-exercise training induces a reversible transition of MHC composition in equine muscle in the order IIX --> IIA --> I. The physiological implication of these changes is an impact on the velocity of shortening and fatigue resistance of muscle fibres.
Get Full Text
Publication Date: 2000-08-22 PubMed ID: 10952171DOI: 10.1023/a:1005642632711Google Scholar: Lookup
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
LinkedInCopy
  • Journal Article

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research studies the impact of long-term heavy exercise and subsequent inactivity on the muscle fibers of young horses, particularly focusing on myosin heavy chain (MHC) composition. The study reveals that harder workouts led to changes in muscle fiber types, an increase in oxygen capacity of certain fibers, and a greater number of capillaries but these adaptations reverted when the horses reverted to inactivity.

Methodology and Research Design

  • The study was conducted on fourteen 4-year old Andalusian mares.
  • Seven of the horses were subjected to an 8-month training programme focusing on carriage exercises, followed by a period of detraining, wherein they were kept in paddocks for 3 months.
  • The remaining seven horses were untrained and acted as a control group.
  • Three muscle biopsies were extracted from each horse before, during, and after the exercise regimen. The MHC composition was analyzed in these samples.
  • The research team also conducted histochemical examinations to study fiber areas, oxidative capacity, and capillaries.

Findings and Results

  • The study found that after 8 months of training, MHC-IIX and IIX fibers decreased while MHC-I and type I and I + IIA fibers increased.
  • However, the proportion of MHC-IIA increased in the superficial region of the muscle after 8 months of training.
  • The cross-sectional of type I fibers increased after 3 months of training, but no further increases were recorded afterward.
  • Training led to an increase in the percentage of high-oxidative capacity fibers and the number of capillaries per square millimeter, indicating significant muscular adaptations.
  • Most of these muscular adaptations were found to be reversible after a period of detraining.

Implications and Conclusion

  • The study concludes that long-term draught-exercise training induces a reversible transition of MHC composition in equine muscle.
  • The physiological implication of these changes is an impact on the velocity of shortening and fatigue resistance of muscle fibers, possibly leading to improved performance during the training period.
  • However, the reversal of these adaptations upon detraining points out the importance of consistent training to maintain these muscle changes.

Cite This Article

APA
Serrano AL, Rivero JL. (2000). Myosin heavy chain profile of equine gluteus medius muscle following prolonged draught-exercise training and detraining. J Muscle Res Cell Motil, 21(3), 235-245. https://doi.org/10.1023/a:1005642632711

Publication

Journal of muscle research and cell motility
ISSN: 0142-4319
NlmUniqueID: 8006298
Country: Netherlands
Language: English
Volume: 21
Issue: 3
Pages: 235-245

Researcher Affiliations

Serrano, A L
  • Department of Comparative Anatomy and Pathological Anatomy, Faculty of Veterinary Science, University of Cordoba, Spain.
Rivero, J L

    MeSH Terms

    • Animals
    • Horses
    • Immunohistochemistry
    • Muscle Contraction / physiology
    • Muscle, Skeletal / physiology
    • Myosin Heavy Chains / physiology
    • Physical Conditioning, Animal / physiology
    • Time Factors

    References

    This article includes 31 references
    1. López-Rivero JL, Serrano AL, Diz AM, Galisteo AM. Variability of muscle fibre composition and fibre size in the horse gluteus medius: an enzyme-histochemical and morphometric study.. J Anat 1992 Aug;181 ( Pt 1)(Pt 1):1-10.
      pubmed: 1284127
    2. Roy RR, Baldwin KM, Edgerton VR. The plasticity of skeletal muscle: effects of neuromuscular activity.. Exerc Sport Sci Rev 1991;19:269-312.
      pubmed: 1936088
    3. Pette D, Vrbová G. Adaptation of mammalian skeletal muscle fibers to chronic electrical stimulation.. Rev Physiol Biochem Pharmacol 1992;120:115-202.
      pubmed: 1519018doi: 10.1007/BFb0036123google scholar: lookup
    4. Rivero JL, Talmadge RJ, Edgerton VR. Myosin heavy chain isoforms in adult equine skeletal muscle: an immunohistochemical and electrophoretic study.. Anat Rec 1996 Oct;246(2):185-94.
      pubmed: 8888960doi: 10.1002/(SICI)1097-0185(199610)246:2<185::AID-AR5>3.0.CO;2-0google scholar: lookup
    5. Goldspink G. Selective gene expression during adaptation of muscle in response to different physiological demands.. Comp Biochem Physiol B Biochem Mol Biol 1998 May;120(1):5-15.
      pubmed: 9787775doi: 10.1016/s0305-0491(98)00018-2google scholar: lookup
    6. Pette D, Staron RS. Mammalian skeletal muscle fiber type transitions.. Int Rev Cytol 1997;170:143-223.
      pubmed: 9002237doi: 10.1016/s0074-7696(08)61622-8google scholar: lookup
    7. Rivero JL, Ruz MC, Serrano AL, Diz AM. Effects of a 3 month endurance training programme on skeletal muscle histochemistry in Andalusian, Arabian and Anglo-Arabian horses.. Equine Vet J 1995 Jan;27(1):51-9.
      pubmed: 7774548doi: 10.1111/j.2042-3306.1995.tb03033.xgoogle scholar: lookup
    8. Talmadge RJ, Roy RR. Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms.. J Appl Physiol (1985) 1993 Nov;75(5):2337-40.
      pubmed: 8307894doi: 10.1152/jappl.1993.75.5.2337google scholar: lookup
    9. Rivero JL, Talmadge RJ, Edgerton VR. Correlation between myofibrillar ATPase activity and myosin heavy chain composition in equine skeletal muscle and the influence of training.. Anat Rec 1996 Oct;246(2):195-207.
      pubmed: 8888961doi: 10.1002/(SICI)1097-0185(199610)246:2<195::AID-AR6>3.0.CO;2-0google scholar: lookup
    10. Hu P, Zhang KM, Feher JJ, Wang SW, Wright LD, Wechsler AS, Spratt JA, Briggs FN. Salbutamol and chronic low-frequency stimulation of canine skeletal muscle.. J Physiol 1996 Oct 1;496 ( Pt 1)(Pt 1):221-7.
      pubmed: 8910210doi: 10.1113/jphysiol.1996.sp021679google scholar: lookup
    11. Brooke MH, Kaiser KK. Muscle fiber types: how many and what kind?. Arch Neurol 1970 Oct;23(4):369-79.
      pubmed: 4248905doi: 10.1001/archneur.1970.00480280083010google scholar: lookup
    12. Serrano AL, Petrie JL, Rivero JL, Hermanson JW. Myosin isoforms and muscle fiber characteristics in equine gluteus medius muscle.. Anat Rec 1996 Apr;244(4):444-51.
      pubmed: 8694280doi: 10.1002/(SICI)1097-0185(199604)244:4<444::AID-AR3>3.0.CO;2-Vgoogle scholar: lookup
    13. Rivero JL, Serrano AL, Barrey E, Valette JP, Jouglin M. Analysis of myosin heavy chains at the protein level in horse skeletal muscle.. J Muscle Res Cell Motil 1999 Feb;20(2):211-21.
      pubmed: 10412092doi: 10.1023/a:1005461214800google scholar: lookup
    14. Rivero JL, Serrano AL, Henckel P. Activities of selected aerobic and anaerobic enzymes in the gluteus medius muscle of endurance horses with different performance records.. Vet Rec 1995 Aug 19;137(8):187-92.
      pubmed: 8560724doi: 10.1136/vr.137.8.187google scholar: lookup
    15. Rivero JL, Talmadge RJ, Edgerton VR. A sensitive electrophoretic method for the quantification of myosin heavy chain isoforms in horse skeletal muscle: histochemical and immunocytochemical verifications.. Electrophoresis 1997 Oct;18(11):1967-72.
      pubmed: 9420154doi: 10.1002/elps.1150181115google scholar: lookup
    16. Rome LC, Sosnicki AA, Goble DO. Maximum velocity of shortening of three fibre types from horse soleus muscle: implications for scaling with body size.. J Physiol 1990 Dec;431:173-85.
      pubmed: 2100306doi: 10.1113/jphysiol.1990.sp018325google scholar: lookup
    17. Rivero JL, Talmadge RJ, Edgerton VR. Interrelationships of myofibrillar ATPase activity and metabolic properties of myosin heavy chain-based fibre types in rat skeletal muscle.. Histochem Cell Biol 1999 Apr;111(4):277-87.
      pubmed: 10219627doi: 10.1007/s004180050358google scholar: lookup
    18. Goldspink G, Scutt A, Loughna PT, Wells DJ, Jaenicke T, Gerlach GF. Gene expression in skeletal muscle in response to stretch and force generation.. Am J Physiol 1992 Mar;262(3 Pt 2):R356-63.
      pubmed: 1373039doi: 10.1152/ajpregu.1992.262.3.R356google scholar: lookup
    19. Talmadge RJ, Grossman EJ, Roy RR. Myosin heavy chain composition of adult feline (Felis catus) limb and diaphragm muscles.. J Exp Zool 1996 Aug 15;275(6):413-20.
      pubmed: 8795286doi: 10.1002/(SICI)1097-010X(19960815)275:6<413::AID-JEZ3>3.0.CO;2-Rgoogle scholar: lookup
    20. Pereira Sant'Ana JA, Ennion S, Sargeant AJ, Moorman AF, Goldspink G. Comparison of the molecular, antigenic and ATPase determinants of fast myosin heavy chains in rat and human: a single-fibre study.. Pflugers Arch 1997 Dec;435(1):151-63.
      pubmed: 9359915doi: 10.1007/s004240050495google scholar: lookup
    21. Gottlieb M, Essén-Gustavsson B, Lindholm A, Persson SG. Effects of a draft-loaded interval-training program on skeletal muscle in the horse.. J Appl Physiol (1985) 1989 Aug;67(2):570-7.
      pubmed: 2793658doi: 10.1152/jappl.1989.67.2.570google scholar: lookup
    22. Schiaffino S, Reggiani C. Molecular diversity of myofibrillar proteins: gene regulation and functional significance.. Physiol Rev 1996 Apr;76(2):371-423.
      pubmed: 8618961doi: 10.1152/physrev.1996.76.2.371google scholar: lookup
    23. Smerdu V, Karsch-Mizrachi I, Campione M, Leinwand L, Schiaffino S. Type IIx myosin heavy chain transcripts are expressed in type IIb fibers of human skeletal muscle.. Am J Physiol 1994 Dec;267(6 Pt 1):C1723-8.
      pubmed: 7545970doi: 10.1152/ajpcell.1994.267.6.C1723google scholar: lookup
    24. Schiaffino S, Gorza L, Sartore S, Saggin L, Ausoni S, Vianello M, Gundersen K, Lømo T. Three myosin heavy chain isoforms in type 2 skeletal muscle fibres.. J Muscle Res Cell Motil 1989 Jun;10(3):197-205.
      pubmed: 2547831doi: 10.1007/BF01739810google scholar: lookup
    25. Lindholm A, Piehl K. Fibre composition, enzyme activity and concentrations of metabolites and electrolytes in muscles of standardbred horses.. Acta Vet Scand 1974;15(3):287-309.
      pubmed: 4137664doi: 10.1186/BF03547460google scholar: lookup
    26. Blanco CE, Sieck GC, Edgerton VR. Quantitative histochemical determination of succinic dehydrogenase activity in skeletal muscle fibres.. Histochem J 1988 Apr;20(4):230-43.
      pubmed: 3209423doi: 10.1007/BF01747468google scholar: lookup
    27. Andersen P, Henriksson J. Capillary supply of the quadriceps femoris muscle of man: adaptive response to exercise.. J Physiol 1977 Sep;270(3):677-90.
      pubmed: 198532doi: 10.1113/jphysiol.1977.sp011975google scholar: lookup
    28. Nwoye L, Mommaerts WF, Simpson DR, Seraydarian K, Marusich M. Evidence for a direct action of thyroid hormone in specifying muscle properties.. Am J Physiol 1982 Mar;242(3):R401-8.
      pubmed: 6461259doi: 10.1152/ajpregu.1982.242.3.R401google scholar: lookup
    29. Galler S, Hilber K, Pette D. Stretch activation and myosin heavy chain isoforms of rat, rabbit and human skeletal muscle fibres.. J Muscle Res Cell Motil 1997 Aug;18(4):441-8.
      pubmed: 9276337doi: 10.1023/a:1018646814843google scholar: lookup
    30. Ennion S, Sant'ana Pereira J, Sargeant AJ, Young A, Goldspink G. Characterization of human skeletal muscle fibres according to the myosin heavy chains they express.. J Muscle Res Cell Motil 1995 Feb;16(1):35-43.
      pubmed: 7751403doi: 10.1007/BF00125308google scholar: lookup
    31. Pette D. Training effects on the contractile apparatus.. Acta Physiol Scand 1998 Mar;162(3):367-76.
      pubmed: 9578383doi: 10.1046/j.1365-201X.1998.0296e.xgoogle scholar: lookup

    Citations

    This article has been cited 6 times.
    1. Lee HY, Kim JY, Kim KH, Jeong S, Cho Y, Kim N. Gene Expression Profile in Similar Tissues Using Transcriptome Sequencing Data of Whole-Body Horse Skeletal Muscle. Genes (Basel) 2020 Nov 17;11(11).
      doi: 10.3390/genes11111359pubmed: 33213000google scholar: lookup
    2. Hyytiäinen HK, Mykkänen AK, Hielm-Björkman AK, Stubbs NC, McGowan CM. Muscle fibre type distribution of the thoracolumbar and hindlimb regions of horses: relating fibre type and functional role. Acta Vet Scand 2014 Jan 27;56(1):8.
      doi: 10.1186/1751-0147-56-8pubmed: 24468115google scholar: lookup
    3. Naylor RJ, Livesey L, Schumacher J, Henke N, Massey C, Brock KV, Fernandez-Fuente M, Piercy RJ. Allele copy number and underlying pathology are associated with subclinical severity in equine type 1 polysaccharide storage myopathy (PSSM1). PLoS One 2012;7(7):e42317.
      doi: 10.1371/journal.pone.0042317pubmed: 22860112google scholar: lookup
    4. Kariya F, Yamauchi H, Kobayashi K, Narusawa M, Nakahara Y. Effects of prolonged voluntary wheel-running on muscle structure and function in rat skeletal muscle. Eur J Appl Physiol 2004 Jun;92(1-2):90-7.
      doi: 10.1007/s00421-004-1061-1pubmed: 15014999google scholar: lookup
    5. Gmel AI, Mikko S, Ricard A, Velie BD, Gerber V, Hamilton NA, Neuditschko M. Using high-density SNP data to unravel the origin of the Franches-Montagnes horse breed. Genet Sel Evol 2024 Jul 10;56(1):53.
      doi: 10.1186/s12711-024-00922-6pubmed: 38987703google scholar: lookup
    6. Vidal Moreno de Vega C, de Meeûs d'Argenteuil C, Boshuizen B, De Mare L, Gansemans Y, Van Nieuwerburgh F, Deforce D, Goethals K, De Spiegelaere W, Leybaert L, Verdegaal EJMM, Delesalle C. Baselining physiological parameters in three muscles across three equine breeds. What can we learn from the horse?. Front Physiol 2024;15:1291151.
      doi: 10.3389/fphys.2024.1291151pubmed: 38384798google scholar: lookup
    Subscribe to our newsletter
    Join 99,727 horse owners like you who receive our email updates on horse health and nutrition.