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Myosin heavy chain isoforms in adult equine skeletal muscle: an immunohistochemical and electrophoretic study.
Abstract: The aim of this study was to characterize the myosin heavy chain (MyHC) isoforms present in equine skeletal muscle. Methods: Muscle biopsies were removed from the superficial region of the gluteus medius muscle of five mature horses and analyzed by immunohistochemistry (using a battery of monoclonal antibodies specific for rat MyHC isoforms) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Results: Immunohistochemistry allowed subdivision of three different muscle fiber populations containing a single MyHC, one slow and two fast, and two hybrid populations, one containing slow and fast MyHCs and another with both fast-MyHC isoforms. Electrophoresis of MyHC confirmed the existence of three resolvable bands, with an electrophoretic mobility parallel to type I, IIa, and IIx rat MyHCs. The identities of two of these MyHCs were easily comparable with slow type I and fast type IIa MyHCs from rat skeletal muscle. However, a precise identification of the second fast MyHC was not made. Conclusions: These results show the presence of three different MyHC isoforms in mature equine skeletal muscle, whose differential distribution defines three fiber types containing a single MyHC and two hybrid fiber populations containing either both slow and fast type IIa MyHCs or both fast MyHC isoforms.
Publication Date: 1996-10-01 PubMed ID: 8888960DOI: 10.1002/(SICI)1097-0185(199610)246:2<185::AID-AR5>3.0.CO;2-0Google 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.
- Journal Article
- Research Support
- Non-U.S. Gov't
- Research Support
- U.S. Gov't
- P.H.S.
Summary
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The research looks into the types of myosin heavy chain (MyHC) isoforms present in the skeletal muscle of adult horses. The study utilizes muscle biopsies from horses and employs immunohistochemistry and sodium dodecyl sulfate-polyacrylamide gel electrophoresis to define three distinct MyHC isoforms and their distribution in the muscle fibers.
Methods
- The research team collected muscle biopsies from the superficial region of the gluteus medius muscle in five mature horses.
- The samples were analyzed by immunohistochemistry, using a variety of monoclonal antibodies that are specifically for rat MyHC isoforms.
- The team also used sodium dodecyl sulfate-polyacrylamide gel electrophoresis as part of the analysis process.
Results
- The immunohistochemistry analysis yielded three distinct muscle fiber populations each containing a unique MyHC. This included one slow and two fast MyHC isoforms.
- Two hybrid fiber populations were also detected, with one containing both a slow and a fast MyHC, and the other presenting both types of fast-MyHC isoforms.
- The electrophoresis of MyHC authorized the existence of three resolvable bands, each featuring an electrophoretic mobility parallel to type I, IIa, and IIx rat MyHCs.
- While the identities of the slow type I and fast type IIa MyHCs were easy to compare with corresponding isoforms in rat skeletal muscle, the second type of fast MyHC remained unidentified.
Conclusions
- The study concludes that there are three distinct MyHC isoforms in the mature equine skeletal muscle.
- The distribution of these isoforms defines three types of muscle fibers that contain a single MyHC along with two hybrid fiber populations.
- These hybrid populations contain either both slow and fast type IIa MyHCs or both types of fast MyHC isoforms.
Cite This Article
APA
Rivero JL, Talmadge RJ, Edgerton VR.
(1996).
Myosin heavy chain isoforms in adult equine skeletal muscle: an immunohistochemical and electrophoretic study.
Anat Rec, 246(2), 185-194.
https://doi.org/10.1002/(SICI)1097-0185(199610)246:2<185::AID-AR5>3.0.CO;2-0 Publication
Researcher Affiliations
- Department of Comparative Anatomy and Pathological Anatomy, Faculty of Veterinary Science, University of Cordoba, Spain.
MeSH Terms
- Animals
- Antibodies, Monoclonal
- Antibody Specificity
- Electrophoresis, Polyacrylamide Gel
- Female
- Horses / anatomy & histology
- Horses / metabolism
- Immunohistochemistry
- Male
- Muscle Fibers, Skeletal / classification
- Muscle Fibers, Skeletal / metabolism
- Muscle, Skeletal / anatomy & histology
- Muscle, Skeletal / metabolism
- Myosin Heavy Chains / immunology
- Myosin Heavy Chains / isolation & purification
- Myosin Heavy Chains / metabolism
- Rats
- Tissue Distribution
Grant Funding
- N01-HD-2-3144 / NICHD NIH HHS
Citations
This article has been cited 12 times.- Latham CM, Owen RN, Dickson EC, Guy CP, White-Springer SH. Skeletal Muscle Adaptations to Exercise Training in Young and Aged Horses. Front Aging 2021;2:708918.
- Sawano S, Mizunoya W. History and development of staining methods for skeletal muscle fiber types. Histol Histopathol 2022 Jun;37(6):493-503.
- García Liñeiro JA, Graziotti GH, Rodríguez Menéndez JM, Ríos CM, Affricano NO, Victorica CL. Structural and functional characteristics of the thoracolumbar multifidus muscle in horses. J Anat 2017 Mar;230(3):398-406.
- Minami Y, Kawai M, Migita TC, Hiraga A, Miyata H. Free radical formation after intensive exercise in thoroughbred skeletal muscles. J Equine Sci 2011;22(2):21-8.
- Yamano S, Kawai M, Minami Y, Hiraga A, Miyata H. Differences in Muscle Fiber Recruitment Patterns between Continuous and Interval Exercises. J Equine Sci 2010;21(4):59-65.
- Minami Y, Yamano S, Kawai M, Hiraga A, Miyata H. Sarcoplasmic Reticulum Ca(2+)-ATPase Activity and Glycogen Content in Various Fiber Types after Intensive Exercise in Thoroughbred Horses. J Equine Sci 2009;20(3):33-40.
- 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.
- Plant DR, Kearns CF, McKeever KH, Lynch GS. Therapeutic clenbuterol treatment does not alter Ca2+ sensitivity of permeabilized fast muscle fibres from exercise trained or untrained horses. J Muscle Res Cell Motil 2003;24(7):471-6.
- Jouffroy FK, Medina MF, Renous S, Gasc JP. Immunocytochemical characteristics of elbow, knee and ankle muscles of the five-toed jerboa (Allactaga elater). J Anat 2003 Apr;202(4):373-86.
- Serrano AL, Rivero JL. Myosin heavy chain profile of equine gluteus medius muscle following prolonged draught-exercise training and detraining. J Muscle Res Cell Motil 2000 Apr;21(3):235-45.
- 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.
- Linnane L, Serrano AL, Rivero JL. Distribution of fast myosin heavy chain-based muscle fibres in the gluteus medius of untrained horses: mismatch between antigenic and ATPase determinants. J Anat 1999 Apr;194 ( Pt 3)(Pt 3):363-72.
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