Population
Skinned single fibers from rabbit psoas and rat superficial vastus lateralis fast-twitch skeletal muscles
Comparison
Phosphorylation of myosin light chain 2 via… vs Control fibers
Design
Preclinical
Key result
Phosphorylation of myosin light chain 2 in skinned skeletal muscle fibers significantly increased the rate constant of tension redevelopment at intermediate levels of Ca2+ activation.
Authors
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Caution against clinical translation; extends mechanistic insight into cross-bridge kinetics in mammalian muscle.
Phosphorylation of myosin light chain 2 increases the calcium sensitivity of the rate of cross-bridge reattachment and steady-state isometric force in mammalian skeletal muscle fibers.
Metzger et al. (1989) studied Mammalian skinned skeletal muscle fibers. Phosphorylation of myosin light chain 2 (LC2) vs. Control fibers (approximately 10% LC2 phosphorylation) was evaluated on Rate constant of tension redevelopment (ktr) and isometric force during steady-state activation. Phosphorylation of myosin light chain 2 in skinned skeletal muscle fibers significantly increased the rate constant of tension redevelopment at intermediate levels of Ca2+ activation.