Myosin heavy chain composition in normal and atrophic equine laryngeal muscle

Christine M. Adreani, Z. B. Li, M. Lehar, L. L. Southwood, P. L. Habecker, Paul Flint, E. J. Parente

Research output: Contribution to journalArticle

14 Citations (Scopus)

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 (SDSPAGE) 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.

Original languageEnglish (US)
Pages (from-to)881-889
Number of pages9
JournalVeterinary Pathology
Volume43
Issue number6
DOIs
StatePublished - 2006
Externally publishedYes

Fingerprint

Laryngeal Muscles
Myosin Heavy Chains
myosin heavy chains
Horses
horses
muscles
Muscles
Protein Isoforms
Cadaver
Atrophy
Polyacrylamide Gel Electrophoresis
atrophy
muscle fibers
Nonmuscle Myosin Type IIB
Myosin Type I
polyacrylamide gel electrophoresis
Slow-Twitch Muscle Fibers
Hemiplegia
Muscular Atrophy
Muscle Proteins

Keywords

  • Laryngeal muscle
  • Myosin heavy chain
  • Neuromuscular disorders
  • Pathology-muscle
  • Recurrent laryngeal neuropathy

ASJC Scopus subject areas

  • veterinary(all)

Cite this

Adreani, C. M., Li, Z. B., Lehar, M., Southwood, L. L., Habecker, P. L., Flint, P., & Parente, E. J. (2006). Myosin heavy chain composition in normal and atrophic equine laryngeal muscle. Veterinary Pathology, 43(6), 881-889. https://doi.org/10.1354/vp.43-6-881

Myosin heavy chain composition in normal and atrophic equine laryngeal muscle. / Adreani, Christine M.; Li, Z. B.; Lehar, M.; Southwood, L. L.; Habecker, P. L.; Flint, Paul; Parente, E. J.

In: Veterinary Pathology, Vol. 43, No. 6, 2006, p. 881-889.

Research output: Contribution to journalArticle

Adreani, CM, Li, ZB, Lehar, M, Southwood, LL, Habecker, PL, Flint, P & Parente, EJ 2006, 'Myosin heavy chain composition in normal and atrophic equine laryngeal muscle', Veterinary Pathology, vol. 43, no. 6, pp. 881-889. https://doi.org/10.1354/vp.43-6-881
Adreani, Christine M. ; Li, Z. B. ; Lehar, M. ; Southwood, L. L. ; Habecker, P. L. ; Flint, Paul ; Parente, E. J. / Myosin heavy chain composition in normal and atrophic equine laryngeal muscle. In: Veterinary Pathology. 2006 ; Vol. 43, No. 6. pp. 881-889.
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