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Further Studies of the Self-Induced Translation Model of Myosin Head Motion Along the Actin Filament

  • Toshio Mitsui
  • Hiroyuki Ohshima
Chapter
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Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 332)

Abstract

We have extended and refined the model of myosin head motion along the actin filament which we proposed in 1988 (J. Mucscle Res. Cell Motility 9, 248-260), and obtained the following results. (1) We assumed that the height of the induced potential depends upon tension with a maximum around the isometric tension, and got a force-velocity relation similar to the observation by Oiwa et al. (1990) that the velocity of the myosin-coated beads along the actin cables decreases with increasing centrifugal force applied in the direction of bead movement and then the velocity tends to increase when the force increases in the same direction beyond a certain value. (2) We introduced a correction factor in the relation between the measured tension and the microscopic tension produced by myosin head, and got a feature in force-velocity relation similar to the observation by Edman (1988) that the velocity drops sharply as the tension approches to about 80% of the isometric tension. (3) We assumed that binding of an ATP-activated myosin head to an actin filament causes a local structural change extended roughly 20nm long along the filament, which provides a potential well spread over about 16nm for the myosin head, with three shallow potential wells in it. We studied kinetics of the myosin head in the potential well of about 16nm in order to explain the early tension recovery after the sudden change of muscle length observed by Ford, Huxley and Simmons (1977), with results in good agreement with their experimental data.

Keywords

Actin Filament Thin Filament Sarcomere Length Myosin Head Duty Ratio 
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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References

  1. 1.
    Huxley, A.F. Prog. Biophys. Biophys. Chem. 7, 255–318 (1957).PubMedGoogle Scholar
  2. 2.
    Huxley, A.F. & Simmons, R.M. Nature 233, 533–538 (1971).PubMedCrossRefGoogle Scholar
  3. 3.
    Yanagida, T., Arata, T. & Oosawa, F. Nature 316, 366–369 (1985).PubMedCrossRefGoogle Scholar
  4. 4.
    Mitsui, T. & Ohshima, H. J. Muscle Res. Cell Motility 9, 248–260 (1988).CrossRefGoogle Scholar
  5. 5.
    Oiwa, K., Chaen, S., Kamitsubo, E., Shimmen, T. & Sugi, H. Proc. Natl. Acad. Sci. USA 87, 7893–7897 (1990).PubMedCrossRefGoogle Scholar
  6. 6.
    Yamada, T. & Homsher, E. in Contractile Mechanism in Muscle (eds. Pollack, G.H. & Sugi, H.) 883–885 (Plenum, New York, 1984Google Scholar
  7. 7.
    Edman, K.A.P. J. Physiol. (Lond.) 404, 301–321 (1988).Google Scholar
  8. 8.
    Ishijima. A., Doi, T., Sakurada, K. & Yanagida, T. Nature 352, 301–306 (1991).PubMedCrossRefGoogle Scholar
  9. 9.
    Ford, L.E., Huxley, A.F. & Simmons, R.M. J. Physiol. (Lond.) 269, 441–515 (1977).Google Scholar

Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • Toshio Mitsui
    • 1
  • Hiroyuki Ohshima
    • 2
  1. 1.Department physics School of Science and TechnologyMeiji UniverityKawasakiJapan
  2. 2.Facuity of Pharmaceutical SciencesScience University of TokyoIchigaya, Shinjuku-ku 162, TokyoJapan

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