title: 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.
authors.affiliation: Department of Clinical Studies, New Bolton Center, 382 West Street Road, Kennett Square, PA 19348, USA. adreani@vet.upenn.edu
authors.forename: C M
authors.initials: CM
authors.lastname: Adreani
authors.forename: Z B
authors.initials: ZB
authors.lastname: Li
authors.forename: M
authors.initials: M
authors.lastname: Lehar
authors.forename: L L
authors.initials: LL
authors.lastname: Southwood
authors.forename: P L
authors.initials: PL
authors.lastname: Habecker
authors.forename: P W
authors.initials: PW
authors.lastname: Flint
authors.forename: E J
authors.initials: EJ
authors.lastname: Parente
mesh_terms: D000818:Animals; D005786:Gene Expression Regulation; D006734:Horse Diseases / Q000378:metabolism* / Q000473:pathology*; D006736:Horses; D007830:Larynx / Q000378:metabolism* / Q000473:pathology; D008297:Male; D018482:Muscle, Skeletal / Q000166:cytology / Q000378:metabolism* / Q000473:pathology*; D009133:Muscular Atrophy / Q000378:metabolism / Q000473:pathology / Q000662:veterinary*; D018995:Myosin Heavy Chains / Q000378:metabolism*; D020033:Protein Isoforms / Q000378:metabolism
chemical_list: D020033:Protein Isoforms; D018995:Myosin Heavy Chains