Abstract
Smooth muscle produces as much stress as skeletal muscle with less myosin. To determine if the actin isoforms specific to smooth muscle contribute to the enhanced force generation, the motility of actin filaments from smooth and skeletal muscle were compared in an in vitro assay in which single fluorescently labeled actin filaments slide over a myosin-coated coverslip. No difference was observed between the velocity of smooth versus skeletal muscle actin filaments over either smooth or skeletal muscle myosin over a large range of assay conditions (changes in pH, ionic strength, and [ATP]). Similarly, no difference was observed between the two actins when the filaments moved under load over mixtures of phosphorylated smooth and skeletal muscle myosin. Thus, it appears that the actin isoforms of smooth and skeletal muscle are mechanically indistinguishable in the motility assay and that smooth muscle's enhanced force generation may originate within the myosin molecule specific to smooth muscle.
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