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Immunohistochemical Analysis of Myosin Heavy Chain Expression in Laryngeal Muscles of the Rabbit, Cat, and Baboon

Hannah S. Rhee and Joseph F.Y. Hoh

Discipline of Physiology and the Bosch Institute, School of Medical Sciences, Faculty of Medicine, The University of Sydney, Sydney, Australia

Correspondence to: Dr Joseph Hoh, Discipline of Physiology, Building F13, University of Sydney, NSW 2006, Australia. E-mail: joeh{at}physiol.usyd.edu.au

We studied myosin heavy chain (MyHC) expression and fiber type distribution in laryngeal muscles in the rabbit, cat, and baboon using immunohistochemistry with highly MyHC-specific antibodies. Two types of variation in MyHC expression were found: between muscles of different function within species and within specific muscles between species. Within species, thyroarytenoid (Ta), an adductor, had faster MyHCs and fiber type profiles than the abductor, posterior cricoarytenoid (PCA), which expressed faster MyHCs than the vocal fold tensor, cricothyroid (CT). Between species, laryngeal muscles generally expressed faster MyHCs in small animals than in larger ones: extraocular (EO) MyHC was expressed in the Ta and PCA of the rabbit but not in the cat and baboon, whereas 2B MyHC was expressed in these muscles of the cat but not of the baboon. The CT expressed only MyHC isoforms and fiber types found in the limb muscles of the same species. These results are discussed in light of the hypothesis that the between-species variations in laryngeal muscle fiber types are evolutionary adaptations in response to changes in body mass and respiratory frequency. Within-species variations in fiber types ensure that protective closure of the glottis is always faster than movements regulating airflow during respiration. (J Histochem Cytochem 56:929–950, 2008)

Key Words: larynx • muscle fiber types • myosin heavy chain • immunohistochemistry • respiration • contraction • comparative physiology • scaling

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