Smooth and skeletal muscle myosin both exhibit low duty cycles at zero load in vitro.
Smooth muscle's stress equals that of skeletal muscle with less myosin. Thus, under isometric conditions, smooth muscle myosin may spend a greater fraction of its cycle time attached to actin in a high force state (i.e. higher duty cycle). If so, then smooth muscle myosin may also have a higher duty cycle under unloaded conditions. To test this, we used an in vitro motility assay in which fluorescently labeled actin filaments move freely over a sparsely coated (5-100 micrograms/ml) myosin surface. Actin filament velocity (V) was a function of the number of cross-bridges capable of interacting with an actin filament (N) and the duty cycle (f), V = (a x Vmax) x (1-(1-f)N) (Uyeda et al., 1990; Harada et al., 1990). N was estimated from the myosin density on the motility surface and the actin filament length. Data for V versus N were fit to the above equation to predict f. The duty cycle of smooth muscle myosin (4.0 +/- 0.7%) was not significantly different from that of skeletal muscle myosin (3.8 +/- 0.5%) in agreement with values estimated by Uyeda et al. (1990) for skeletal muscle myosin under unloaded conditions. The duty cycles of smooth and skeletal muscle myosin may still differ under isometric conditions.
Harris
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Department of Molecular Physiology and Biophysics, University of Vermont, Burlington 05405.
Warshaw
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D000199:Actins / Q000378:metabolism; D000818:Animals; D002645:Chickens; D007537:Isometric Contraction; D009132:Muscles / Q000378:metabolism* / Q000502:physiology; D009218:Myosins / Q000378:metabolism*; D014422:Turkeys
D000199:Actins; D009218:Myosins