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Veterinary pathology2006; 43(6); 881-889; doi: 10.1354/vp.43-6-881

Myosin heavy chain composition in normal and atrophic equine laryngeal muscle.

Abstract: The myosin heavy chain (MHC) composition of a given muscle determines the contractile properties and, therefore, the fiber type distribution of the muscle. MHC isoform expression in the laryngeal muscle is modulated by neural input and function, and it represents the cellular level changes that occur with denervation and reinnervation of skeletal muscle. The objective of this study was to evaluate the pattern of MHC isoform expression in laryngeal muscle harvested from normal cadavers and cadavers with naturally occurring left laryngeal hemiplegia secondary to recurrent laryngeal neuropathy. Left and right thyroarytenoideus (TA) and cricoarytenoideus dorsalis (CAD) were obtained from 7 horses affected with left-sided intrinsic laryngeal muscle atrophy and from 2 normal horses. Frozen sections were evaluated histologically for degree of atrophy and fiber type composition. MHC isoform expression was determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of muscle protein. Histologic atrophy was seen in all atrophic muscles and some right-sided muscles of 3 affected horses, as well as the left TA of 1 normal horse. Fiber type grouping or loss of type I muscle fibers was observed in the left-sided laryngeal muscles in all but 1 affected horse, as well as in the right muscles of 2 affected horses, and the left TA of 1 normal horse. SDS-PAGE showed 2 bands corresponding to the type I and type IIB myosin isoforms in the CAD and TA of the 2 normal horses. Affected horses demonstrated a trend toward increased expression of the type IIB isoform and decreased expression of the type I isoform in atrophic muscles. This study confirmed the presence of histologic abnormalities in grossly normal equine laryngeal muscle, and it demonstrated an increased expression of type IIB MHC with a concurrent decreased expression of type I MHC in affected muscles. Evaluation of muscle fiber changes at the cellular level under denervated and reinnervated conditions may aid in assessing future strategies for reinnervation or regeneration of atrophic laryngeal muscle.
Publication Date: 2006-11-14 PubMed ID: 17099144DOI: 10.1354/vp.43-6-881Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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The study investigates how the composition of myosin heavy chain (MHC) isoforms, proteins that determine muscle contraction properties, differ in the laryngeal muscles of horses diagnosed with a laryngeal condition called left laryngeal hemiplegia and in healthy ones. The results show that affected horses have higher expression of type IIB MHC and lower expression of type I MHC in atrophying muscles, which may be useful for future strategies addressing muscle regeneration.

Background

  • The research focuses on myosin heavy chain (MHC) isoforms in laryngeal muscles. Myosin heavy chains are crucial constituents of muscle tissue, affecting the contractile properties and type of muscle fibers.
  • The expression of these isoforms is modulated by neural input and function, therefore changes in their distribution can indicate muscle denervation or reinnervation.
  • The study was conducted using laryngeal muscle samples from healthy horses and those suffering from left laryngeal hemiplegia, a condition caused by recurrent laryngeal neuropathy. The muscles, thyroarytenoideus (TA) and cricoarytenoideus dorsalis (CAD), will be analysed to reveal the pattern of MHC isoform expression.

Methodology

  • The research obtained laryngeal muscles from 7 horses with left laryngeal hemiplegia and 2 normal horses. The muscle tissues were frozen and prepared for histological evaluation.
  • These tissues were assessed for atrophy (muscle damage) and fiber type composition to see if there’s a change in the muscle fiber types distribution.
  • The MHC isoform expression was determined using a method called sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), which is used to separate proteins based upon their sizes.

Findings

  • The study observed histologic atrophy in all atrophic muscles and some right-sided muscles of 3 affected horses, as well as the left TA of 1 normal horse.
  • A loss or clustering of type I muscle fibers was noticed in the left-sided laryngeal muscles in all but one affected horse, as well as in right-sided muscles of two affected horses, and in the left TA of one normal horse.
  • SDS-PAGE results revealed the existence of two bands corresponding to type I and type IIB myosin isoforms in the CAD and TA muscles of two normal horses.
  • Compared to normal horses, affected ones showed an increased expression of type IIB MHC isoform and a decreased expression of type I MHC isoform in atrophic muscles.

Conclusion

  • This study provides important insights on the changes in MHC isoforms’ composition in the laryngeal muscles of horses affected with left laryngeal hemiplegia.
  • The finding of increased type IIB and decreased type I MHC expression in affected muscles can potentially aid in understanding the changes at a cellular level in denervated or reinnervated conditions.
  • Such knowledge may be useful in developing future strategies for muscle reinnervation or regeneration, thus contributing to a better understanding of laryngeal muscle pathology.

Cite This Article

APA
Adreani CM, Li ZB, Lehar M, Southwood LL, Habecker PL, Flint PW, Parente EJ. (2006). Myosin heavy chain composition in normal and atrophic equine laryngeal muscle. Vet Pathol, 43(6), 881-889. https://doi.org/10.1354/vp.43-6-881

Publication

ISSN: 0300-9858
NlmUniqueID: 0312020
Country: United States
Language: English
Volume: 43
Issue: 6
Pages: 881-889

Researcher Affiliations

Adreani, C M
  • Department of Clinical Studies, New Bolton Center, 382 West Street Road, Kennett Square, PA 19348, USA. adreani@vet.upenn.edu
Li, Z B
    Lehar, M
      Southwood, L L
        Habecker, P L
          Flint, P W
            Parente, E J

              MeSH Terms

              • Animals
              • Gene Expression Regulation
              • Horse Diseases / metabolism
              • Horse Diseases / pathology
              • Horses
              • Larynx / metabolism
              • Larynx / pathology
              • Male
              • Muscle, Skeletal / cytology
              • Muscle, Skeletal / metabolism
              • Muscle, Skeletal / pathology
              • Muscular Atrophy / metabolism
              • Muscular Atrophy / pathology
              • Muscular Atrophy / veterinary
              • Myosin Heavy Chains / metabolism
              • Protein Isoforms / metabolism

              Citations

              This article has been cited 8 times.
              1. Choi H, Yu SS, Choi J, Kim CS. The Regenerative Effects of c-Met Agonistic Antibodies in Vocal Fold Atrophy.. Int J Mol Sci 2022 Jul 15;23(14).
                doi: 10.3390/ijms23147818pubmed: 35887165google scholar: lookup
              2. Glass TJ, Kelm-Nelson CA, Szot JC, Lake JM, Connor NP, Ciucci MR. Functional characterization of extrinsic tongue muscles in the Pink1-/- rat model of Parkinson disease.. PLoS One 2020;15(10):e0240366.
                doi: 10.1371/journal.pone.0240366pubmed: 33064741google scholar: lookup
              3. Glass TJ, Valmadrid LCV, Connor NP. The Adult Ts65Dn Mouse Model of Down Syndrome Shows Altered Swallow Function.. Front Neurosci 2019;13:906.
                doi: 10.3389/fnins.2019.00906pubmed: 31555077google scholar: lookup
              4. Glass TJ, Kelm-Nelson CA, Russell JA, Szot JC, Lake JM, Connor NP, Ciucci MR. Laryngeal muscle biology in the Pink1-/- rat model of Parkinson disease.. J Appl Physiol (1985) 2019 May 1;126(5):1326-1334.
              5. Glass TJ, Connor NP. Digastric Muscle Phenotypes of the Ts65Dn Mouse Model of Down Syndrome.. PLoS One 2016;11(6):e0158008.
                doi: 10.1371/journal.pone.0158008pubmed: 27336944google scholar: lookup
              6. Qiu X, Chen D, Li M, Gao Y, Liu F, Zheng H, Chen S. Transition of myosin heavy chain isoforms in human laryngeal abductors following denervation.. Eur Arch Otorhinolaryngol 2015 Oct;272(10):2915-23.
                doi: 10.1007/s00405-015-3664-zpubmed: 26059207google scholar: lookup
              7. 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
              8. Rhee HS, Steel CM, Derksen FJ, Robinson NE, Hoh JF. Immunohistochemical analysis of laryngeal muscles in normal horses and horses with subclinical recurrent laryngeal neuropathy.. J Histochem Cytochem 2009 Aug;57(8):787-800.
                doi: 10.1369/jhc.2009.953844pubmed: 19398607google scholar: lookup