Critical review of the swinging crossbridge theory and of the cardinal active role of water in muscle contraction

Critical Reviews in Biochemistry and Molecular Biology

Volumn 32, Issue 4, 1997, Pages 307-360

  Oplatka, Avraham ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

Hydration forces; Motility; Muscle contraction; Muscle regulation; Water

Indexed keywords

ACTIN; MYOSIN; WATER;

ACTIN MYOSIN INTERACTION; CONFORMATIONAL TRANSITION; HUMAN; HYDRATION; MUSCLE CONTRACTION; MYOFILAMENT; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; REVIEW; THEORY; WATER CONTENT;

EID: 0030826284     PISSN: 10409238     EISSN: None     Source Type: Journal    
DOI: 10.3109/10409239709082575     Document Type: Review

References (69)

1. Arata, T., Y. Mukuhata, and Y. Tonomura (1977). Structure and function of the two heads of the myosin molecule. VI. ATP hydrolysis, shortening and tension development of myofibrils. J. Biochem. 82, 801-812.
2. Ashiba, G., T. Asada, and S. Watanabe (1980). Calcium regulation in clam foot muscle: calcium sensitivity of clam foot myosin. J. Biochem. (Tokyo) 88, 837-846.
3. Bagni, M. A., G. Cecchi, and M. Schoenberg (1988). A model of force production that explains the lag between cross-bridge attachment and force after electrical stimulation of striated muscle fibers. Biophys. J. 54, 1105-1114.
4. Bagni, M. A., G. Cecchi, and F. Colomo (1990). Myofilament spacing and force generation in intact frog muscle fibers. J. Physiol. 430, 61-75.
5. Bárány, M. (1967). ATPase activity of myosin correlated with speed of muscle shortening. J. Gen. Physiol. 50, 197-218.
6. Belton, P. S., R. R. Jackson, and K. J. Packer (1972). Pulsed NMR studies of water in striated muscle. I. Transverse nuclear spin relaxation times and freezing effects. Biochim. Biophys. Acta 286, 16-25.
7. Borejdo, J. and A. Oplatka (1976). Tension development in skinned glycerinated rabbit psoas fiber segments irrigated with soluble myosin fragments. Biochim. Biophys. Acta 440, 241-258.
8. Borejdo, J. and A. Oplatka (1981). Heavy meromyosin cross-links thin filaments in striated muscle myofibrils. Nature 291, 322-323.
9. Botts, J., R. Takashi, P. Torgerson, T. Hozumi, A. Muhlrad, D. Mornet, and M. F. Morales (1984). On the mechanism of transduction in myosin subfragment 1. Proc. Natl. Acad. Sci. U.S.A. 81, 2060-2064.
10. Bratton, C. B., A. L. Hopkins, and J. W. Weinberg (1965). Nuclear magnetic resonance studies of living muscle. Science 147, 738-739.
11. Bremel, R. D. and A. Weber (1972). Cooperation within actin filament in vertebrate skeletal muscle. Nature New Biol. 238, 97-99.
12. Brenner, B. (1997). structural features of crossbridges in skeletal muscle fibers during isometric contraction as revealed by 2D-X-ray diffraction. Eur. J. Physiol. (Pflug. Archiv.) Suppl. to vol. 433, R16.
13. Brenner, B. and L. C. Yu (1993). Evidence for structural changes in crossbridges during force generation. In: Mechanism of Myofilament Sliding in Muscle Contraction (Sugi, H. and Pollack, G. H., Eds.), pp. 461-469. New York: Plenum Press.
14. Brochard-Wyart, F. (1993). Deformations of one tethered chain in strong flows. Europhys. Lett. 23, 105-111.
15. Brune, D. and S. Kim (1994). Hydrodynamic steering effects in protein association. Proc. Natl. Acad. Sci. U.S.A. 91, 2930-2934.
16. Burlacu, S. and J. Borejdo (1992). Motion of actin filaments in the presence of myosin heads and ATP. Biophys. J. 63, 1471-1482.
17. Burton, K. (1992). Myosin step size: estimates from motility assays and shortening muscle. J. Muscle Res. Cell Motil. 13, 590-607.
18. Cecchi, G., M. A. Bagni, P. J. Griffiths, C. C. Ashley, and Y. Maeda (1990). Detection of changes in intact single muscle fibers. Science 250, 1409-1411.
19. Cevc, G. and D. Marsh (1987). Phospholipid Bilayers, Physical Principles and Models. New York: Wiley-Interscience.
20. Coats, J. H., A. H. Criddle, and M. A. Geeves (1985). Pressure-relaxation studies of pyrene-labeled actin and myosin subfragment 1 from rabbit skeletal muscle. Biochem. J. 232, 351-356.
21. Davis, J. S. and W. F. Harrington (1993). A single order-disorder transition generates tension during the Huxley-Simmons phase 2 in muscle. Biophys. J. 65, 1886-1898.
22. Diaz Banos, F. G., J. Bordas, J. Lowy, and A. Svensson (1996). Small segmental rearrangements in the myosin head can explain force generation in muscle. Biophys. J. 71, 576-589.
23. Eberstein, A. and A. Rosenfalck (1963). Birefringence of isolated muscle fibers in twitch and tetanus. Acta Physiol. Scand. 57, 144-166.
24. Endo, M., T. M. Kitazawa, M. Lino, and Y. Kakuta (1979). Effect of "viscosity" of the medium on mechanical properties of skinned skeletal muscle fibers. In: Cross-Bridge Mechanism in Muscle Contraction (Sugi, H. and Pollack, G. H., Eds.) pp. 365-376 New York: Plenum Press.
25. Esmann, M., K. Hideg, and D. Marsh (1994). Influence of poly(ethylene glycol) and aquous viscosity on the rotational diffusion of membraneous Na, K-ATPase. Biochemistry 33, 3696-3697.
26. Fajer, P. G., E. A. Fajer, and D. D. Thomas (1990). Myosin heads have a broad orientational distribution during isometric muscle contraction: time-resolved EPR studies using caged ATP. Proc. Natl. Acad. Sci. U.S.A. 87, 5538-5542.
27. Ford, L. E., A. F. Huxley, and R. M. Simmons (1977). Tension responses to sudden length change in stimulated frog muscle fibers near slack length. J. Physiol. 269, 441-515.
28. Ford, L. E., K. Nakagawa, J. Desper, and C. Y. Seow (1991). Effect of osmotic compression on the force-velocity properties of glycerinated rabbit skeletal muscle. J. Gen. Physiol. 97, 73-88.
29. Frado, L.-L. and R. Craig (1992). Electron microscopy of the actin-myosin head complex in the presence of ATP. J. Mol. Biol. 223, 391-397.
30. Gadasi, H., A. Oplatka, R. Lamed, A. Hochberg, and W. Z. Low (1974). Possible uncoupling of the mechanochemical process in the actomyosin system by covalent crosslinking of F-actin. Biochim. Biophys. Acta 333, 161-168.
31. Geeves, M. A. (1989). Dynamic interaction between actin and myosin subfragment 1 in the presence of ADP. Biochemistry 28, 5864-5871.
32. Geeves, M. A. and D. J. Halsall (1987). Two step ligand binding and cooperativity - a model to describe the cooperative binding of myosin subfragment 1 to regulated actin. Biophys. J. 52, 215-220.
33. Gekko, K. and N. Noguchi (1979). Compressibility of globular proteins in water at 25°C. J. Phys. Chem. 83, 2706-2714.
34. Gerber, B. R. and H. Noguchi (1967). Volume change associated with the G-F transformation of flagellin. J. Mol. Biol. 26, 197-210.
35. Gordon, A. M., A. F. Huxley, and F. J. Julian (1966). The variation in isometric tension with sarcomere length in vertebrate muscle fibers. J. Physiol. 184, 170-192.
36. Gordon, A. R. and M. J. Siegman (1971). Mechanical properties of smooth muscle. I. Length-tension and force-velocity relations. Am. J. Physiol. 221, 1243-1249.
37. Granick, S. (1991). Motions and relaxations of confined liquieds. Science 253, 1374-1379.
38. Grazi, E., C. Schwienbacher, and E. Magri (1993). Osmotic stress is the main determinant of the diameter of the actin filament. Biochim. Biophys. Res. Comm. 197, 1377-1381.
39. Harrington, W. F. (1971). A mechanochemical mechanism for muscle contraction. Proc. Natl. Acad. Sci. U.S.A. 68, 685-689.
40. Hasselbach, W. and G. Schneider (1951). Der L-myosin und aktingehalt des kaninchenmuskels. Biochem. Z. 321, 461.
41. Hatta, I., H. Sugi, and Y. Tamura (1988). Stiffness changes in frog skeletal muscle during contraction recorded using ultrasonic waves. J. Physiol. 403, 193-209.
42. Hazelewood, C. F. and Nichols, B. L. (1969). Evidence for the existence of a minimum of two phases of ordered water in skeletal muscle. Nature 272, 747-750.
43. Highsmith, S. (1977). The effects of temperature and salts on myosin subfragment-1 and F-actin association. Archiv. Biochem. Biophys. 180, 404-408.
44. Highsmith, S., K. Duignan, R. Cooke, and J. Cohen (1996). Osmotic pressure probe of actin-myosin hydration changes during ATP hydrolysis. Biophys. J. 70, 2830-2837.
45. Higuchi, H. and Y. E. Goldman (1991). Sliding distance between actin and myosin filaments per ATP molecule hydrolysed in skinned muscle fibers. Nature 352, 352-354.
46. Higuchi, H., T. Yanagida, and Y. E. Goldman (1995). Compliance of thin filaments in skinned fibers of rabbit skeletal muscle. Biophys. J. 69, 1000-1010.
47. Hill, A. V. (1938). The heat of shortening and the dynamic constants of muscle. Proc. R. Soc. B126, 136-195.
48. Hill, A. V. (1964). The effect of load on the heat of shortening of muscle. Proc. R. Soc. B159, 297-318.
49. Hill, A. V. (1965). Trails and Trials in Physiology. London: Edward Arnold (Publishers).
50. Hirose, K. and T. Wakabayashi (1993). Structural change of crossbridges of rabbit skeletal muscle during isometric contraction. J. Muscle Res. Cell Motil. 14, 432-445.
51. Holroyd, S. M. and C. G. Gibbs (1993). The energetics of shortening amphibian cardiac muscle. Am. J. Physiol. 424, H200-208.
52. Honda, H., H. Nagashima, and S. Asakura (1986). Directional movement of F-actin in vitro. J. Mol. Biol. 191, 131-133.
53. Huxley, A. F. (1957). Muscle structure and theories of contraction. Prog. Biophys. 7, 255-318.
54. Huxley, A. F. (1980). Reflections on Muscle, Liverpool University Press.
55. Huxley, A. F. (1993). Summary and conclusions. In: Mechanism of Myofilament Sliding in Muscle Contraction. (Sugi, H. and Pollack, G. H., Eds.) New York: Plenum Press, pp. 839-847.
56. Huxley, A. F. and R. Niedergerke (1954). Interference microscopy of living muscle fibres. Nature 173, 971-973.
57. Huxley, A. F. and R. M. Simmons (1971). Proposed mechanism of force generation in striated muscle. Nature 233, 533-538.
58. Huxley, H. E. (1953). Electron microscope studies of the organization of the filaments in striated muscle. Biochim. Biophys. Acta 12, 387-394.
59. Huxley, H. E. (1960). Muscle cells. In: The Cell. (Brachet, J. and Mirsky, A. E., Eds.) Vol. 4, New York: Academic Press, pp. 365-481.
60. Huxley, H. E. (1969). The mechanism of muscular contraction. Science 164, 1356-1366.
61. Huxley, H. E. and J. Hanson (1954). Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation. Nature 173, 973-976.
62. Huxley, H. E., A. Stewart, H. Sosa, and T. Irving (1994). X-ray diffraction measurements of the extensibility of actin and myosin filaments in contracting muscle. Biophys. J. 67, 2411-2421.
63. Irving, M. (1987). Muscle mechanics and probes of the crossbridge cycle. In: Fibrous Protein Structure (Squire, J. M. and Vibert, P. J., Eds.) New-York: Academic Press, pp. 495-528.
64. Ishijima, A., Y. Harada, H. Kojima, T. Funatsu, H. Higuchi, and T. Yanagida (1994). Single-molecule analysis of the actomyosin motor using nano-manipulation. Biochem. Biophys. Res. Comm. 199, 1057-1063.
65. Jackson, J. L. and A. Oplatka (1974). A mechanochemical theory of fluctuations in muscles. Biorheology 11, 315-322.
66. Kamikura, S. and K. Takahashi (1981). Direct measurement of the force of microtubule sliding in flagella. Nature 293, 566-568.
67. Kellermayer, M. S. Z. and H. L. Granzier (1996). Calcium-dependent inhibition of in vitro thin-filament motility by native titin. FEBS Lett. 380, 281-286.
68. Knight, P. and G. Offer (1978). p-NN'-phenylene-bismaleimide, a specific cross-linking agent for F-actin. Biochem. J. 175, 1023-1032.
69. Knight, P. J., N. S. Fortune, and M. A. Geeves (1993). Effects of pressure on equatorial X-ray diffraction from skeletal muscle fibers. Biophys. J. 65, 814-822.