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Abstract
PURPOSE: To determine whether the levator palpebrae superioris (LPS) and the retractor bulbi (RB) muscles, which share contractile characteristics with extraocular muscles (EOMs), express fast EOM-specific myosin heavy chain (MyHC) in the rabbit and other mammalian species. METHODS: Cryostat sections of rabbit eye and limb muscles were stained by indirect peroxidase immunohistochemical procedures using monoclonal antibodies (MAbs), including one (4A6) against EOM-specific fast MyHC. Myosin heavy chain isoforms from these muscles were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and the 4A6-reactive component was identified by immunoblotting. RESULTS: MAb 4A6 stained muscle fibers in rabbit LPS and RB. SDS-PAGE resolved a rabbit EOM-specific MyHC isoform (band 1) from two other components (bands 2 and 3) that comigrated with limb fast MyHCs. MAb 4A6 reacted only with band 1. Rabbit LPS and RB also displayed corresponding MyHC components with the same mobilities and immunoreactivities as bands 1 to 3 in the EOM. MAb 4A6 also stained muscle fibers in monkey and cat LPS, but it failed to stain muscle fibers in cat RB and rat LPS and RB. CONCLUSIONS: The expression of EOM-specific fast MyHC in EOM, LPS, and RB reflect their common developmental origin and similar contractile characteristics. These properties set them apart from other skeletal muscle groups. Eye muscles may constitute a distinct muscle group or allotype characterized by unique properties, including their propensity or resistance to disease.