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A Model for Caldesmon in Latch-Bridge Formation in Smooth Muscle

  • Michael P. Walsh
  • Cindy Sutherland
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 255)

Abstract

The primary mechanism of regulation of smooth muscle contraction involves the Ca+-dependent and reversible phosphorylation of myosin1. Stimulation of the smooth muscle cell leads to an elevation of cytosolic free Ca2+ concentration whereupon Ca2+ binds to calmodulin. Formation of the Ca2+-calmodulin complex is accompanied by a conformational change in the Ca2+-binding protein which is then capable of interaction with a target enzyme, in this case myosin light chain kinase (MLCK). The binding of calmodulin converts the kinase from the inactive apoenzyme form found in the resting cell to the active Ca2+-calmodulin-MLCK ternary complex. The active kinase catalyzes transfer of the terminal phosphoryl group of ATP to serine-19 on each of the two 20 kDa light chains of myosin. In the phosphorylated state, the MgATPase activity of myosin is substantially enhanced by actin. This biochemical parameter is thought to reflect a cross-bridge cycling mechanism whereby actin and myosin filaments slide relative to one another, the required energy being provided by the hydrolysis of ATP. At the level of the intact cell this process would result in force development.

Keywords

Thin Filament Myosin Light Chain Kinase Smooth Muscle Myosin Chicken Gizzard Myosin Phosphorylation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • Michael P. Walsh
    • 1
  • Cindy Sutherland
    • 1
  1. 1.Department of Medical BiochemistryUniversity of CalgaryCalgaryCanada

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