User menu

Accès à distance ? S'identifier sur le proxy UCLouvain

Analysis of the birefringence of the smooth muscle anococcygeus of the rat, at rest and in contraction. I.

  1. Adelstein, R. S. &Eisenberg (1980) Regulation and kinetics of the actin-myosin ATP interaction.Ann. Rev. Biochem. 49, 921–56.
  2. Bennett, H. S. (1950) The microscopical investigation of biological material with polarized light. InMcClung's Handbook of Microscopical Techniques (edited byJones, R. M.) pp. 591–677, New York: Hoeber.
  3. Craig, R., Smith, R. &Kendrick-Jones, J. (1983) Light chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin molecules.Nature 302, 436–9.
  4. Fischer E., THE SUBMICROSCOPICAL STRUCTURE OF MUSCLE AND ITS CHANGES DURING CONTRACTION AND STRETCH, 10.1101/sqb.1936.004.01.023
  5. Fischer, E. (1938) The birefringence of smooth muscle (phascolosoma and thyone) as related to muscle length, tension and tone.J. Cell. comp. Physiol. 12, 85–101.
  6. Fischer, E. (1944) The birefringence of striated and smooth mammalian muscles.J. Cell. comp. Physiol. 23, 113–29.
  7. Fischer, E. (1947) Birefringence and ultrastructure of muscle.Ann. N.Y. Acad. Sci. 47, 783–97.
  8. Fisher, B. A. &Bagby, R. M. (1977) Reorientation of myofilaments during contraction of a vertebrate smooth muscle.Am. J. Physiol. 232, C5-C14.
  9. Gillespie, J. S., Creed, K. E. &Muir, T. C. (1973) Electrical changes underlying excitation in intestinal and related smooth muscle.Phil. Trans. R. Soc. Lond. B,265, 95–106.
  10. Gillespie, J. S. (1980) The physiology and pharmacology of the anococcygeus muscle.Trends Pharmacol. Sci. 1, 453–7.
  11. Gillis, J. M., Cao, M. L. &Godfraind-De Becker, A. (1988) Density of myosin filaments in the rat anococcygeus muscle, at rest and in contraction. II.J. Muscle Res. Cell Mot. 9, 18–28.
  12. Godfraind-De Becker, A. &Gillis, J. M. (1982a) The birefringence of a smooth muscle, its change during contraction.Archs int. physiol. Biochim. 90, P6-P7.
  13. Godfraind-De Becker, A. &Gillis, J. M. (1982b) Living and extracted strips of taenia coli: optical retardation and birefringence at rest and in contraction.J. Muscle Res. Cell Mot. 3, 475.
  14. Godfraind-De Becker, A. &Gillis, J. M. (1987) Polarized light microscopy of the smooth muscle anococcygeus of the rat. InMolecular Mechanism of Muscle Contraction (edited bySugi, H. &Pollack, G. F.) New York: Plenum (in Press).
  15. Hamoir, G. (1973) Extractability and properties of the contractile proteins of vertebrate smooth muscle.Phil. Trans. R. Soc. Lond. B 265, 169–81.
  16. Hartshorne, D. J. &Siemankowski, R. E. (1980) Regulation of smooth muscle actomyosin.Ann. Rev. Physiol. 43, 519–30.
  17. Huxley A. F., Niedergerke R., Measurement of the striations of isolated muscle fibres with the interference microscope, 10.1113/jphysiol.1958.sp006110
  18. Inoue, S. &Sato, H. (1967) Cell motility by labile association of molecules. The nature of the mitotic spindle fibres and their role in chromosome movement.J. gen. Physiol. 50, 259–92.
  19. Kelly, R. E. &Rice, R. V. (1968) Localization of myosin filaments in smooth muscle.J. Cell. Biol. 37, 105–116.
  20. Kelly, R. E. &Rice, R. V. (1969) Ultrastructural studies on the contractile mechanism of smooth muscle.J. Cell. Biol. 42, 683–94.
  21. Laszt, L. &Hamoir, G. (1961) Etude par électrophorése et ultracentrifugation de la composition protéinique de la couche musculaire de la carotide de bovidés.Biochim. biophys. Acta 50, 430–49.
  22. Noll, D. &Weber, H. H. (1934) Polarisationoptik und molekulärer Feinbau der Q-Abschnitte des Froschmuskels.Pflüg. Arch. ges. Physiol. 235, 234–46.
  23. Onishi, H., Suzuki, H., Nakamura, K., Takahashi, K. &Watanabe, S. (1978) Adenosine triphosphate activity and thick filament formation of chicken gizzard myosin in low salt media.J. Biochem. 83, 835–47.
  24. Onishi, H. &Wakabayashi, T. (1982) Electron microscope studies of myosin molecules from chicken gizzard muscle. I: The formation of the intramolecular loop in the myosin tail.J. Biochem. 92, 871–9.
  25. Onishi, H., Wakabayashi, T., Kamata, T. &Watanabe, S. (1983) Electron microscope studies of myosin molecules from chicken gizzard. II: The effect of thiophosphorylation of the 20k-dalton light chain on the ATP induced change of the conformation of myosin monomers.J. Biochem. 94, 1147–54.
  26. Oster, G. (1955) Birefringence and dichroism. InPhysical Techniques in Biological Research, Vol. I (edited byOster, G. &Pollister, A. W.) pp. 439–60. New York: Academic Press.
  27. Scholey, J. M., Taylor, K. A. &Kendrick-Jones, J. (1980) Regulation of non-muscle myosin assembly by calmodulin-dependent light chain kinase.Nature 287, 233–5.
  28. Sherry, J. M., Gorecka, A., Askoy, M. O., Dabroska, R. &Hartshorne, D. J. (1978) Roles of calcium and phosphorylation in the regulation of the activity of gizzard myosin.Biochemistry 17, 4411–18.
  29. Shoenberg, C. F. (1969) An electron microscope study of the influence of divalent ions on myosin filament formation in chicken gizzard extracts and homogenates.Tissue and Cell 1, 83–96.
  30. Small, J. V. &Sobieszek, A. (1980) The contractile apparatus of smooth muscle.Internat. Rev. Cytol. 64, 241–306.
  31. Sobieszek, A. (1977) Ca-linked phosphorylation of a light chain of vertebrate smooth muscle myosin.Eur. J. Biochem. 73, 477–83.
  32. Somlyo, A. V., Butler, T. M., Bond, M. &Somlyo, A. P. (1981) Myosin filaments have non-phosphorylated light chain in relaxed smooth muscle.Nature 294, 567–9.
  33. Suzuki, H., Onishi, H., Takahashi, K. &Watanabe, S. (1978) Structure and function of chicken gizzard myosin.J. Biochem. 84, 1529–42.
  34. Trybus, K. M., Huiatt, T. W. &Lowey, S. (1982) A bent monomeric conformation of myosin from smooth muscle.Proc. Nat. Acad. Sci. USA 79, 6151–5.
  35. Wiener, O. (1912) Die Theorie des Mischkörpers für das Feld der stationären Strömung.Abh. sächs. ges. Akad. Wiss. 32, 509–604.
Bibliographic reference Godfraind-De Becker, A ; Gillis, Jean-Marie. Analysis of the birefringence of the smooth muscle anococcygeus of the rat, at rest and in contraction. I.. In: Journal of muscle research and cell motility, Vol. 9, no. 1, p. 9-17 (1988)
Permanent URL http://hdl.handle.net/2078.1/11788