The myosin content of rat posterior cricoarytenoid and thyroarytenoid muscles was described by means of histochemical, immunohistochemical, and electrophoretic techniques. Laryngeal muscles were dissected and frozen, together with other muscles (extraocular, diaphragm, extensor digitorum longus, and soleus) for comparative purposes, then sectioned serially and stained: 1) histochemically for myofibrillar adenosine triphosphatase reactivity and 2) immunohistochemically for myosin heavy chain (MHC) content with six different antibodies. Other portions of the muscle samples were electrophoresed by a glycerol sodium dodecyl sulfatepolyacrylamide gel electrophoresis technique that separates the MHC protein into its specific isoforms. In electrophoretic comparison it limb muscles, the laryngeal muscles contained an additional MHC band we designated as type IIL (type II laryngeal) MHC. On histochemical and immunohistochemical staining, no fibers from the thyroarytenoid muscle and few fibers from the posterior cricoarytenoid muscle could be classified according to the standard fiber type categories established for limb muscles (types I, IIA, IIB, and IIX). These laryngeal muscle fibers appear to represent an atypical fiber type.
Four novel myosin heavy chain transcripts define a molecular basis for muscle fibre types inRanapipiens