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Updated: Sep 28, 2026

Preparation of the Rat Vocal Fold for Neuromuscular Analyses
Published on: May 15, 2020
Age-related alterations in myosin heavy chain isoforms in rat intrinsic laryngeal muscles
Tatsutoshi Suzuki1, Nadine P Connor, Kyungah Lee
1Department of Surgery, Division of Otolaryngology-Head and Neck Surgery, University of Wisconsin, Madison, USA.
Abstract:
Deficits in voice and swallowing are found in the elderly, but the underlying neuromuscular mechanisms are unclear. A potential mechanism may be denervation-induced muscle fiber transformation to a slower-contracting type of muscle fiber. This study examined young, old, and denervated rat laryngeal muscles (lateral thyroarytenoid, lateral cricoarytenoid, and posterior cricoarytenoid) to examine differences in myosin heavy chain (MHC) composition. Results of sodium dodecyl sulfate-polyacrylamide gel electrophoresis analyses indicated that all muscles were composed predominately of type IIB MHC. With aging and denervation, type IIB was reduced and type IIX, a slower-contracting isoform, was increased in the lateral thyroarytenoid and lateral cricoarytenoid muscles. In the posterior cricoarytenoid muscle, the MHC composition was relatively unchanged. These findings suggest that aging may affect laryngeal adductory function by altering muscle fiber type composition to a slower-contracting isoform, in a manner similar to that observed with denervation.
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