Abstract
The effects of length changes applied to resting, contracting and rigor muscles on the reflection spacings of the X-ray diffraction patterns were summarized. The spacing changes of the actin- and myosin-based meridional reflections as a function of tension relative to an isometric tension of active muscle (P0) were linear and almost indentical in the active and rigor states, showing that the extension of both filaments is Hookenian and does not depend upon the states of muscle. In addition to their length changes caused by tension generation, there are small but significant length changes of both filaments due purely to activation of muscle. The actin and myosin filaments are elongated by ∼0.36% and ∼0.43%, respectively under the maximum active tension. The results indicate that a large part of the sarcomere compliance of an active muscle is caused by the extensibility of the myofilaments.
Inspection of the behavior of the meridional and layer-line reflection spacings reveals that there is a close relationship between the extensibility and helical twisting of the actin filaments under active and passive forces. The extension caused by tension is associated with an unwinding of right-handed helices following the actin monomers in the filament. At the pointed end of the filament could rotate anticlockwise through one fifth the complete turn during contraction.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Goldman, Y. E. & Huxley, A. F. Biophys. J. 67, 2131–2136 (1994).
Huxley, H. E., Stewart, A., Sosa, H. & Irving, T. C. Biophys. J. 67, 2411–2421 (1994).
Wakabayashi, K., Sugimoto, Y., Tanaka, H., Ueno, Y., Takezawa. Y. & Amemiya, Y Biophys. J. 67, 2422–2435 (1994).
Takezawa, Y., Sugimoto, Y & Wakabayashi, K. J. Muscle Res. Cell Motility. 18, 485a (1997).
Huxley, H. E., Stewart, A. & Irving, T. C. Biophys. J. 74, A22 (1998).
Amemiya, Y., Wakabayashi, K., Hamanaka, T., Wakabayashi, T., Hashizume, H. & Matsushita, T. Nucl. Instrum. Methods. 208, 471–477 (1983).
Amemiya, Y & Wakabayashi, K. Adv. Biophys. 27, 115–127 (1991).
Huxley, H. E. & Brown, W. J. Molec. Biol. 30, 383–434 (1967).
Takezawa, Y. Ph. D thesis, Osaka University (1998).
Haselgrove, J. C. J. Molec. Biol., 92, 113–143 (1975).
Martin-Fernandez, M. L., Bordas, J., Diakun, G., Harries, J., Lowy, J., Mant, G. R., Svensson, A. & Towns-Andrews, E. J. Muscle Res. Cell Motility. 15, 319–348 (1994).
Takezawa, Y., Kim, D-S., Kobayashi, T., Tanaka, H. & Wakabayashi, K. J. Muscle Res. Cell Motility. 17, 278a (1996).
Wakabayashi, K., Higuchi, H. & Takezawa, Y. Butsuri. 52, 599–605 (1997).
Higuchi, H., Yanagida, T. & Goldman, Y E. Biophys. J. 69, 1000–1010 (1995).
Kojima, H., Ishijima, A.& Yanagida, T. Proc. Natl. Acad. Sci. U.S.A. 91, 12962–12966 (1994).
Fraser, R. D. B. & MacRae, T. P. Conformation in Fibrous Proteins, Chap. 1 & 15 (Academic Press, New York and London, 1973).
O’Brien, E. J., Gillis, J. M. & Couch, J. J. Molec. Biol. 99, 461–475 (1995).
Nishizaka, T., Yagi, T., Tanaka, Y & Ishiwata, S. Nature, 361, 269–271 (1993).
Sase, I., Miyata, H., Ishiwata, S. & Kinoshita, K. Proc. Natl. Acad. Sci. U.S.A. 94, 5646–5650 (1997).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1998 Plenum Press, New York
About this chapter
Cite this chapter
Takezawa, Y., Sugimoto, Y., Wakabayashi, K. (1998). Extensibility of the Actin and Myosin Filaments in Various States of Skeletal Muscle as Studied by X-Ray Diffraction. In: Sugi, H., Pollack, G.H. (eds) Mechanisms of Work Production and Work Absorption in Muscle. Advances in Experimental Medicine and Biology, vol 453. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-6039-1_36
Download citation
DOI: https://doi.org/10.1007/978-1-4684-6039-1_36
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-6041-4
Online ISBN: 978-1-4684-6039-1
eBook Packages: Springer Book Archive