In Vitro Evidence for Smooth Muscle Crossbridge Mechanical Interactions

  • David Warshaw
  • Kathleen Trybus
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 304)


Force production and shortening in smooth muscle result from the cyclic interaction between myosin crossbridges and actin filaments. Although the crossbridge mechanism in smooth muscle is qualitatively similar to that in skeletal muscle, smooth muscle has the unique ability of sustaining prolonged contractions with very little energy expenditure (Butler and Siegman, 1983). This economy of energy consumption may reflect a modulation of crossbridge cycling rate within the time course of a contraction. Investigators have postulated that this modulation is related to the regulatory processes that govern the crossbridge’s interaction with actin.


Actin Filament Myosin Light Chain Motility Assay Myosin Filament Smooth Muscle Myosin 
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  1. Brenner, B., Schoenberg, M., Chalovich, J. M., Greene, L. E., and Eisenberg, E., 1982, Evidence for cross-bridge attachment in relaxed muscle at low ionic strength, Proc. Nat’l Acad. Sci. U.S.A., 79: 7288.CrossRefGoogle Scholar
  2. Butler, T. M. and Siegman, M. J., 1983, Chemical energy usage and myosin light chain phosphorylation in mammalian smooth muscle, Fed. Proc, 42: 57.PubMedGoogle Scholar
  3. Dillon, P. F., Aksoy, M. O., Driska, S. P., and Murphy, R. A., 1981, Myosin phosphorylation and the crossbridge cycle in arterial smooth muscle, Science, 211: 495.PubMedCrossRefGoogle Scholar
  4. Greene, L. E., Sellers, J. R., Eisenberg, E., and Adelstein, R. S., 1983, Binding of gizzard smooth muscle myosin subfragment 1 to actin in the presence and absence of adenosine 5′-triphosphate, Biochemistry, 22: 530.PubMedCrossRefGoogle Scholar
  5. Hemric, M. E, and Chalovich, J. M., 1988, Effect of caldesmon on the ATPase activity and the binding of smooth and skeletal myosin subfragments to actin, J. Biol. Chem., 263: 1878.PubMedGoogle Scholar
  6. Kamm, K. E. and Stull, J. T., 1985, The function of myosin and myosin light chain kinase phosphorylation in smooth muscle, Ann. Rev. Pharmacol. Toxicol., 25: 593.CrossRefGoogle Scholar
  7. Sellers, J. R., 1985, Mechanism of the phosphorylation-dependent regulation of smooth muscle heavy meromyosin, J. Biol. Chem., 260: 15815.PubMedGoogle Scholar
  8. Sellers, J. R., Spudich, J. A., and Sheetz, M. P., 1985, Light chain phosphorylation regulates the movement of smooth muscle myosin on actin filaments, J. Cell Biol., 101: 1897.PubMedCrossRefGoogle Scholar
  9. Trybus, K. M. and Henry, L., 1989, Monoclonal antibodies detect and stabilize conformational states of smooth muscle myosin, J. Cell Biol, 109: 2879.PubMedCrossRefGoogle Scholar
  10. Warshaw, D. M., Desrosiers, J. M., Work, S. S., and Trybus, K. M., 1990, Smooth muscle myosin cross-bridge interactions modulate actin filament sliding velocity in vitro, J. Cell Biol, 111: 453.PubMedCrossRefGoogle Scholar
  11. Winder, S. J. and Walsh, M. P., 1990, Smooth muscle calponin. Inhibition of actomyosin MgATPase and the regulation by phosphorylation, J. Biol Chem., 265: 10148.PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1991

Authors and Affiliations

  • David Warshaw
    • 1
  • Kathleen Trybus
    • 2
  1. 1.Department of Physiology & BiophysicsUniversity of VermontBurlingtonUSA
  2. 2.Rosenstiel Research CenterBrandeis UniversityWalthamUSA

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