Myosin and Contractile Activity in Smooth Muscle

  • D. J. Hartshorne
  • M. Ito
  • M. Ikebe
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 255)


In relaxed smooth muscle the contractile apparatus is dormant and the initiation of contraction requires an activation. It is generally agreed that the activation is achieved by phosphorylation of the two 20,000-dalton light chains of myosin (LC20) and usually Serine 19 is phosphorylated. This process is catalyzed by myosin light chain kinase (MLCK) and the Ca2+-dependence of the system is due to the activation of the MLCK apoenzyme by the Ca2+4 calmodulin (CaM) complex. Dephosphorylation and inactivation of the contractile apparatus, reflects the activity of a light chain phosphatase. The latter, however, has not been well characterized and it is not known, for example, if one or more phosphatases are involved or, if the phosphatase activity is regulated.


ATPase Activity Myosin Head Smooth Muscle Myosin Cross Bridge Chicken Gizzard 
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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  1. 1.
    D. J. Hartshorne, Biochemistry of the contractile process in smooth muscle, in “Physiology of the Gastrointestinal Tract” 2nd. Ed. L. R. Johnson, ed., Raven Press, N.Y. pp. 423–482 (1987).Google Scholar
  2. 2.
    P. F. Dillon, M. O. Aksoy, S. P. Driska, and R. A. Murphy, Myosin phosphorylation and the cross bridge cycle in arterial smooth muscle, Science. 211:495–497 (1981).PubMedCrossRefGoogle Scholar
  3. 3.
    M. O. Aksoy, S. Mras, K. E. Kamm, and R. A. Murphy, Ca++, cAMP, and changes in myosin phosphorylation during contraction of smooth muscle, Am. J. Physiol.. 245: C255–C270 (1983).PubMedGoogle Scholar
  4. 4.
    P. J. Silver, and J. T. Stull, Regulation of myosin light chain and Phosphorylase phosphorylation in tracheal smooth muscle, J. Biol. Chem., 257:6145–6150 (1982).PubMedGoogle Scholar
  5. 5.
    P. J. Silver, and J. T. Stull, Phosphorylation of myosin light chain and Phosphorylase in tracheal smooth muscle in response to KCl and carbachol, Mol. Pharmacol.. 25:267–274 (1984).PubMedGoogle Scholar
  6. 6.
    R. A. Murphy, Myosin phosphorylation and cross bridge regulation in arterial smooth muscle, State-of-the-art review, Hypertension, 4(Suppl. 2):3–7 (1982).Google Scholar
  7. 7.
    C-M. Hai, and R. A. Murphy, Cross bridge phosphorylation and regulation of latch state in smooth muscle, Am. J. Physiol. 254:C99–C106 (1988).PubMedGoogle Scholar
  8. 8.
    S. P. Driska, High myosin light chain phosphatase activity in arterial smooth muscle: can it explain the latch phenomenon? in “Smooth Muscle Contraction”, M. J. Siegman, ed., A. R. Liss, Inc., N.Y. 387–398 (1987).Google Scholar
  9. 9.
    H. Suzuki, H. Onishi, K. Takahashi, and S. Watanabe, Structure and function of chicken gizzard myosin, J. Biochem (Tokyo), 84:1529–1542 (1978).PubMedGoogle Scholar
  10. 10.
    M. Ikebe, S. Hinkins, and D. J. Hartshorne, Correlation of enzymatic properties and conformation of smooth muscle myosin, Biochemistry. 22:4580–4587 (1983).PubMedCrossRefGoogle Scholar
  11. 11.
    D. J. Hartshorne, R. F. Siemankowski, and O. M. Aksoy, Ca regulation in smooth muscle and phosphorylation: Some properties of the myosin light chain kinase. In: Regulatory Mechanism of Muscle Contraction, S. Ebashi, K. Maruyama, and M. Endo, ed., Japan Society for the Promotion of Science and Fujihara Foundation of Science, Tokyo, 287–301, (1980).Google Scholar
  12. 12.
    M. Ikebe, R. J. Barsotti, S. Hinkins, and D. J. Hartshorne, Effects of magnesium chloride on smooth muscle actomyosin adenosine-5′-triphosphatase activity, myosin conformation and tension development in glycerinated smooth muscle fibers, Biochemistry 23:5062–5068 (1984).PubMedCrossRefGoogle Scholar
  13. 13.
    E. M. V. Pires, and S. V. Perry, Purification and properties of myosin light-chain kinase from fast skeletal muscle, Biochem. J., 167:137–146 (1977).PubMedGoogle Scholar
  14. 14.
    T. S. Chandra, N. Nath, H. Suzuki, and J. C. Seidel, Modification of thiols of gizzard myosin alters ATPase activity, stability of myosin filaments, and the 6–10S conformational transition, J. Biol. Chem. 260:202–207 (1985).PubMedGoogle Scholar
  15. 15.
    S. Srivastava, M. Ikebe, and D. J. Hartshorne, Trinitrophenylation of smooth muscle myosin, Biochem. Biophys. Res. Commun.. 126:748–755 (1985).PubMedCrossRefGoogle Scholar
  16. 16.
    H. Onishi, and S. Watanabe, Correlation between the papain digestibility and the conformation of 10S-myosin from chicken gizzard, J. Biochem. (Tokyo), 95:899–902 (1984).PubMedGoogle Scholar
  17. 17.
    M. Ikebe, and D. J. Hartshorne, Conformation-dependent proteolysis of smooth-muscle myosin, J. Biol. Chem. 259:11639–11642 (1984).PubMedGoogle Scholar
  18. 18.
    M. Ikebe, and D. J. Hartshorne, Proteolysis of smooth muscle myosin by Staphylococcus aureus protease: Preparation of heavy meromyosin and subfragment 1 with intact 20,000-dalton light chains, Biochemistry. 24:2380–2386 (1985).PubMedCrossRefGoogle Scholar
  19. 19.
    M. Ikebe, and D. J. Hartshorne, Proteolysis and actin-binding properties of 10S and 6S smooth muscle myosin, Identification of a site protected from proteolysis in the 10S conformation and by the binding of actin, Biochemistry. 25:6177–6185 (1986).PubMedCrossRefGoogle Scholar
  20. 20.
    T. Marianne-Pepin, D. Mornet, R. Bertrand, J-P. Labbe, and R. Kassab, Interaction of the heavy chain of gizzard myosin heads with skeletal F-actin, Biochemistry. 24:3024–3029 (1985).PubMedCrossRefGoogle Scholar
  21. 21.
    T. Katoh, and F. Morita, Interaction between myosin and F-actin. Correlation with actin-binding sites on subfragment-1, J. Biochem. (Tokyo), 96: 1223–1230 (1984).PubMedGoogle Scholar
  22. 22.
    A. Muhlrad, and M. F. Morales, Isolation and partial renaturation of proteolytic fragments of the myosin head, Proc. Natl. Acad. Sci. USA, 81:1003–1007 (1984).PubMedCrossRefGoogle Scholar
  23. 23.
    D. Mornet, R. Bertrand, P. Pantel, E. Audemard, and R. Kassab, Structure of the actin-myosin interface, Nature 292:301–306 (1981).PubMedCrossRefGoogle Scholar
  24. 24.
    M. Ikebe, Y. Tonomura, H. Onishi, and S. Watanabe, Elementary steps in the F-actin activated Mg2+-ATPase reaction of gizzard H-mero myosin:effects of phosphorylation of the light-chain subunit. J. Biochem. (Tokyo), 90:61–77 (1981).PubMedGoogle Scholar
  25. 25.
    H. Suzuki, W. F. Stafford III, H. S. Slayter, and J. C. Seidel, A conformational transition in gizzard heavy meromyosin involving the head-tail junction resulting in changes in sedimentation coefficient, ATPase activity, and orientation of heads, J. Biol. Chem., 260:14810–14817 (1985).PubMedGoogle Scholar
  26. 26.
    M. Ikebe, S. Hinkins, and D. J. Hartshorne, Correlation of intrinsic fluorescence and conformation of smooth muscle myosin, J. Biol. Chem., 258:14770–14773 (1983).PubMedGoogle Scholar
  27. 27.
    M. Higashihara, and M. Ikebe, Inhibition of 10S-6S conformational change of smooth muscle myosin by a monoclonal antibody, Biophys. J., 53:578a (1988).Google Scholar
  28. 28.
    A. V. Somlyo, T. M. Butler, M. Bond, and A. P. Somlyo, Myosin filaments have non-phosphorylated light chains in relaxed smooth muscle, Nature. 294:567–569 (1981).PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • D. J. Hartshorne
    • 1
  • M. Ito
    • 1
  • M. Ikebe
    • 2
  1. 1.Muscle Biology GroupUniversity of ArizonaTucsonUSA
  2. 2.Dept. of Physiology and BiophysicsCase Western Reserve UniversityClevelandUSA

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