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Journal of Biomedicine and Biotechnology
Volume 2011 (2011), Article ID 592343, 16 pages
Distribution of Myosin Attachment Times Predicted from Viscoelastic Mechanics of Striated Muscle
Department of Molecular Physiology and Biophysics, University of Vermont, 122 HSRF, Beaumont Avenue, Burlington, VT 05405, USA
Received 1 July 2011; Accepted 22 August 2011
Academic Editor: Henk Granzier
Copyright © 2011 Bradley M. Palmer et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- J. T. Finer, R. M. Simmons, and J. A. Spudich, “Single myosin molecule mechanics: piconewton forces and nanometre steps,” Nature, vol. 368, no. 6467, pp. 113–119, 1994.
- J. A. Spudich, “How molecular motors work,” Nature, vol. 372, no. 6506, pp. 515–518, 1994.
- D. M. Warshaw, W. H. Guilford, Y. Freyzon et al., “The light chain binding domain of expressed smooth muscle heavy meromyosin acts as a mechanical lever,” Journal of Biological Chemistry, vol. 275, no. 47, pp. 37167–37172, 2000.
- M. J. Tyska and D. M. Warshaw, “The myosin power stroke,” Cell Motility and the Cytoskeleton, vol. 51, no. 1, pp. 1–15, 2002.
- S. Sugiura, N. Kobayakawa, H. Fujita et al., “Comparison of unitary displacements and forces between 2 cardiac myosin isoforms by the optical trap technique: molecular basis for cardiac adaptation,” Circulation Research, vol. 82, no. 10, pp. 1029–1034, 1998.
- S. Sugiura and H. Yamashita, “Functional characterization of cardiac myosin isoforms,” Japanese Journal of Physiology, vol. 48, no. 3, pp. 173–179, 1998.
- E. Blanchard, C. Seidman, J. G. Seidman, M. LeWinter, and D. Maughan, “Altered crossbridge kinetics in the αMHC403/+ mouse model of familial hypertrophic cardiomyopathy,” Circulation Research, vol. 84, no. 4, pp. 475–483, 1999.
- I. Morano, “Tuning the human heart molecular motors by myosin light chairs,” Journal of Molecular Medicine, vol. 77, no. 7, pp. 544–555, 1999.
- N. R. Alpert, C. Brosseau, A. Federico, M. Krenz, J. Robbins, and D. M. Warshaw, “Molecular mechanics of mouse cardiac myosin isoforms,” American Journal of Physiology, vol. 283, no. 4, pp. H1446–H1454, 2002.
- C. Veigel, J. E. Molloy, S. Schmitz, and J. Kendrick-Jones, “Load-dependent kinetics of force production by smooth muscle myosin measured with optical tweezers,” Nature Cell Biology, vol. 5, no. 11, pp. 980–986, 2003.
- D. M. Swank, J. Braddock, W. Brown, H. Lesage, S. I. Bernstein, and D. W. Maughan, “An alternative domain near the ATP binding pocket of Drosophila myosin affects muscle fiber kinetics,” Biophysical Journal, vol. 90, no. 7, pp. 2427–2435, 2006.
- N. M. Kad, J. B. Patlak, P. M. Fagnant, K. M. Trybus, and D. M. Warshaw, “Mutation of a conserved glycine in the SH1-SH2 helix affects the load-dependent kinetics of myosin,” Biophysical Journal, vol. 92, no. 5, pp. 1623–1631, 2007.
- M. Kawai and P. W. Brandt, “Sinusoidal analysis: a high resolution method for correlating biochemical reactions with physiological processes in activated skeletal muscles of rabbit, frog and crayfish,” Journal of Muscle Research and Cell Motility, vol. 1, no. 3, pp. 279–303, 1980.
- D. Maughan, J. Moore, J. Vigoreaux, B. Barnes, and L. A. Mulieri, “Work production and work absorption in muscle strips from vertebrate cardiac and insect flight muscle fibers,” Advances in Experimental Medicine and Biology, vol. 453, pp. 471–480, 1998.
- M. Kawai and F. H. Schachat, “Differences in the transient response of fast and slow skeletal muscle fibers. Correlations between complex modulus and myosin light chains,” Biophysical Journal, vol. 45, no. 6, pp. 1145–1151, 1984.
- M. Kawai and H. R. Halvorson, “Role of MgATP and MgADP in the cross-bridge kinetics in chemically skinned rabbit psoas fibers. Study of a fast exponential process (C),” Biophysical Journal, vol. 55, no. 4, pp. 595–603, 1989.
- B. L. Marcussen and M. Kawai, “Role of MgATP and inorganic phosphate ions in cross-bridge kinetics in insect (Lethocerus colossicus) flight muscle,” Progress in Clinical and Biological Research, vol. 327, pp. 805–813, 1990.
- G. Wang and M. Kawai, “Effects of MgATP and MgADP on the cross-bridge kinetics of rabbit soleus slow-twitch muscle fibers,” Biophysical Journal, vol. 71, no. 3, pp. 1450–1461, 1996.
- B. M. Palmer, T. Suzuki, Y. Wang, W. D. Barnes, M. S. Miller, and D. W. Maughan, “Two-state model of acto-myosin attachment-detachment predicts C-process of sinusoidal analysis,” Biophysical Journal, vol. 93, no. 3, pp. 760–769, 2007.
- M. Kawai, Y. Saeki, and Y. Zhao, “Crossbridge scheme and the kinetic constants of elementary steps deduced from chemically skinned papillary and trabecular muscles of the ferret,” Circulation Research, vol. 73, no. 1, pp. 35–50, 1993.
- A. F. Huxley, “Muscle structure and theories of contraction,” Progress in Biophysics and Biophysical Chemistry, vol. 7, pp. 255–318, 1957.
- M. Kawai and Y. Zhao, “Cross-bridge scheme and force per cross-bridge state in skinned rabbit psoas muscle fibers,” Biophysical Journal, vol. 65, no. 2, pp. 638–651, 1993.
- H. Higuchi, T. Yanagida, and Y. E. Goldman, “Compliance of thin filaments in skinned fibers of rabbit skeletal muscle,” Biophysical Journal, vol. 69, no. 3, pp. 1000–1010, 1995.
- M. F. Schmid and H. F. Epstein, “Muscle thick filaments are rigid coupled tubules, not flexible ropes,” Cell Motility and the Cytoskeleton, vol. 41, no. 3, pp. 195–201, 1998.
- M. Evans, N. Hastings, and B. Peacock, Statistical Distributions, Wiley, New York, NY, USA, 2000.
- M. Abramowitz and I. A. Stegun, Eds., Handbook of Mathematical Functions with Formulas, Graphs, and Mathematical Tables, 9th Printing, Dover, New York, NY, USA, 1972.
- D. L. Snyder, Random Point Processes, John Wiley and Sons, New York, NY, USA, 1975.
- J. T. Finer, A. D. Mehta, J. A. Spudich et al., “Characterization of single actin-myosin interactions,” Biophysical Journal, vol. 68, supplement 4, pp. 291S–297S, 1995.
- R. E. Godt and B. D. Lindley, “Influence of temperature upon contractile activation and isometric force production in mechanically skinned muscle fibers of the frog,” Journal of General Physiology, vol. 80, no. 2, pp. 279–297, 1982.
- G. H. Rossmanith, “Tension responses of muscle to n-step pseudo-random length reversals: a frequency domain representation,” Journal of Muscle Research and Cell Motility, vol. 7, no. 4, pp. 299–306, 1986.
- M. E. Coupland, E. Puchert, and K. W. Ranatunga, “Temperature dependance of active tension in mammalian (rabbit psoas) muscle fibres: effect of inorganic phosphate,” Journal of Physiology, vol. 536, no. 3, pp. 879–891, 2001.
- B. M. Palmer, “A strain-dependency of Myosin off-rate must be sensitive to frequency to predict the B-process of sinusoidal analysis,” Advances in Experimental Medicine and Biology, vol. 682, pp. 57–75, 2010.
- K. W. Ranatunga and M. E. Coupland, “Crossbridge mechanism(s) examined by temperature perturbation studies on muscle,” Advances in Experimental Medicine and Biology, vol. 682, pp. 247–266, 2010.
- I. S. Gradshteyn and I. M. Ryzhik, Eds., Tables of Integrals, Series, and Products, Academic Press, 1980.