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  • Title: Phosphorylation-dependent activated tension in skinned gizzard muscle fibers in the absence of Ca2+.
    Author: Walsh MP, Bridenbaugh R, Hartshorne DJ, Kerrick WG.
    Journal: J Biol Chem; 1982 Jun 10; 257(11):5987-90. PubMed ID: 6896202.
    Abstract:
    A Ca2+-insensitive myosin light chain kinase was prepared and used in experiments with skinned gizzard fibers. In the absence of Ca2+, this kinase activated isometric force development. The force development was associated with phosphorylation of the 20,000-dalton myosin light chains and addition of Ca2+ did not activate the fibers further. Pretreatment of the fibers with Ca2+-insensitive myosin light chain kinase and adenosine 5'-O-(3-thiotriphosphate) in the absence of Ca2+ caused thiophosphorylation of the light chains and, on the addition of ATP, an activation of isometric tension was observed. The subsequent addition of Ca2+ did not increase force development. A comparison of Ca2+-activated tension in the skinned gizzard muscle fibers with Ca2+-insensitive myosin light chain kinase-activated tension suggests that the phosphorylation of the myosin light chains is the dominant factor in the development of tension in smooth muscle.
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