Regulation of Embryonic Smooth Muscle Myosin by Myosin Light Chain Kinase and by Protein Kinase C

  • Primal de Lanerolle
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 255)


The presence of developmentally regulated myosin isoforms in muscle tissues is well established (1–9). Cardiac myosin has been studied extensively, and three different isoforms have been identified (4,5). These myosin isoforms differ with respect to (a) their mobilities on nondenaturing Polyacrylamide gels (3), (b) subunit composition (3,4), and (c) actomyosin ATPase activities (4). Moreover, specific cardiac myosin isoforms are expressed following volume overload of the heart (2) and change depending upon thyroid hormone levels (5). Similarly, fiberspecific myosin isoforms are expressed in skeletal muscle, and the myosin isoform correlates with both the type of innervation and the sequence of electrical stimulation (6).


Smooth Muscle Myosin Myosin Isoforms Chicken Gizzard Myosin Phosphorylation Dependent ATPase Activity 
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Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • Primal de Lanerolle
    • 1
  1. 1.Department of Physiology and BiophysicsUniversity of Illinois at ChicagoChicagoUSA

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