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Single-Fiber Analyses of Myosin Heavy-Chain Isoform Composition

Ya Zhen Wu, MD; Roger L. Crumley, MD; Vincent J. Caiozzo, PhD

Arch Otolaryngol Head Neck Surg. 2000;126:865-873.

Background  The canine lateral cricoarytenoid muscle contains a large proportion of muscle fibers that coexpress various combinations of myosin heavy-chain isoforms (ie, so-called hybrid fibers).

Objective  To test the hypothesis that hybrid fibers are a common motif throughout laryngeal muscles.

Design  The posterior cricoarytenoid, canine cricothyroid, and thyroarytenoid muscles were removed from 5 beagle dogs. The posterior cricoarytenoid and canine cricothyroid muscles were each dissected into horizontal, oblique, and rectus regions. The thyroarytenoid was separated into medial and lateral regions. Approximately 40 single fibers were microdissected from each region (1800 total fibers were sampled) and placed into a denaturing sample buffer. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis was then used to separate the individual myosin heavy-chain isoforms.

Results  Each laryngeal muscle contained hybrid fibers; however, the types and proportions of hybrid fibers were clearly muscle specific. Within a given muscle, there were relatively minor regional differences in the types and proportions of hybrid fibers.

Conclusion  If the myosin heavy-chain isoform composition of a single fiber can be used as a "physiological marker," then the extent of hybridism may reveal the diversity of activity required of a given laryngeal muscle.

From the Departments of Otolaryngology–Head and Neck Surgery (Drs Wu and Crumley), Orthopaedics (Dr Caiozzo), and Physiology and Biophysics (Dr Caiozzo), College of Medicine, University of California, Irvine.

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