Prof. Masataka Kawai
The University of Iowa, USA



1971-1974 Postdoctor, Columbia University, USA

1971 Ph.D., Biology, Princeton University, USA
1968 M.A., Physiology Course, Marine Biological Laboratory, USA
1962-1966 B.A., Science University of Tokyo, Japan

Publications (Selected)

  1. Kawai, M. and Kuntz, I. D. 1973. Optical diffraction studies of muscle fibers. Biophys. J. 13:857-876.
  2. Kawai, M. and Brandt, P. W. 1976. Two rigor states in skinned crayfish single muscle fibers. J. Gen. Physiol. 68:267-280.
  3. Kawai, M., Brandt, P. W. and Orentlicher, M. 1977. Dependence of energy transduction in intact skeletal muscles on the time in tension. Biophys. J. 18:161-172.
  4. Kawai, M. and Brandt, P. W. 1977. Effect of MgATP on stiffness measured at two frequencies in Ca activated muscle fibers. Proc. Natl. Acad. Sci. (USA) 74:4073-4075.
  5. Kawai, M. 1978. Head rotation or dissociation? A study of exponential rate processes in chemically skinned rabbit muscle fibers when MgATP concentration is changed. Biophys. J. 22:97-103.
  6. Cox, R. N., Kawai, M., Karlin, A. and Brandt, P. W. 1979. Voltage fluctuations at the frog sartorius motor endplate produced by a covalently attached activator. J. Membrane Biol. 51:145-159.
  7. Kawai, M. and Brandt, P. W. 1980. Sinusoidal analysis: a high resolution method for correlating biochemical reactions with physiological processes in activated skeletal muscles of rabbit, frog and crayfish. J. Muscle Res. Cell Mot. 1:279-303.
  8. Brandt, P. W., Cox, R. N. and Kawai, M. 1980. Can the binding of Ca++ to two regulatory sites on troponin C determine the steep pCa/tension of relationship of skeletal muscle? Proc. Natl. Acad. Sci. USA 77:4717-4720.
  9. Cox, R. N. and Kawai, M. 1981. Alternate energy transduction routes in chemically skinned rabbit psoas muscle fibers: a further study of the effect of MgATP over a wide concentration range. J. Muscle Res. Cell Mot. 2:203-214.
  10. Kawai, M., Cox, R. N. and Brandt, P. W. 1981. Effect of Ca ion concentration on cross-bridge kinetics in rabbit psoas fibers. Evidence for the presence of two Ca-activated states of thin filament. Biophys. J. 35:375-384.
  11. Brandt, P. W., Cox, R. N., Kawai, M. and Robinson, T. 1982. Regulation of tension in skinned muscle fibers: effect of cross-bridge rate constants on apparent Ca sensitivity. J. Gen. Physiol. 79:997-1016.
  12. Brandt, P. W., Diamond, M. S., Gluck, B., Kawai, M. and Schachat, F. H. 1984. Molecular basis of cooperativity in vertebrate muscle thin filaments. Carlsberg Research Communication (Copenhagen), 49:155-167.
  13. Kawai, M. and Schachat, F. H. 1984. Differences in the transient response to fast and slow skeletal muscle fibers: correlations between complex modulus and myosin light chains. Biophys. J. 45:1145-1151.
  14. Feit, H., Kawai, M. and Schulman, M. I. 1985. Stiffness and contractile properties of avian normal and dystrophic muscle bundles as measured by sinusoidal length perturbations. Muscle and Nerve, 8:503-510.
  15. Kawai, M. and Schulman, M. I. 1985. Cross-bridge kinetics in chemically skinned rabbit psoas fibres when the actin-myosin lattice spacing is altered by dextran T-500. J. Muscle Res. Cell Mot., 6:313-332.
  16. Feit, H. and Kawai, M. 1985. Physiological and biochemical characterization of avian dystrophic muscle reveals alterations of collagen. Annals of the New York Academy of Sciences, 460:431-433.
  17. Feit, H., Hammon, K. and Kawai, M. 1985. Collagen in chemically skinned, extracted dystrophic myofibers. Muscle and Nerve 8:806-807.
  18. Kawai, M. 1986. The role of orthophosphate in crossbridge kinetics in chemically skinned rabbit psoas fibers as detected with sinusoidal and step length alterations. J. Muscle Res. Cell Mot., 7:421-434.
  19. Diamond, M. S, Brandt, P. W. and Kawai, M. 1986. Comments on the "Critical dependence of calcium-activated force on width in highly compressed fibers of the frog." Biophys. J. 50:1215-1216.
  20. Kawai, M., Güth, K., Winnikes, K., Haist, C. and Rüegg, J. C. 1987. The effect of inorganic phosphate on the ATP hydrolysis rate and the tension transients in chemically skinned rabbit psoas fibers. Pflügers Archiv., 408:1-9.
  21. Feit, H., Kawai, M. and Mostafapour, A. S. 1989. Increased resistance of the collagen in avian dystrophic muscle to collagenolytic attack. Evidence for increased crosslinking. Muscle and Nerve 12:476-485.
  22. Feit, H., Kawai, M. and Mostafapour, A. S. 1989. The role of collagen crosslinking in the increased stiffness of avian dystrophic muscle.  Muscle and Nerve 12:486-492.
  23. Kawai, M. and Halvorson, H. R. 1989. Role of MgATP and MgADP in the crossbridge kinetics in chemically skinned rabbit psoas fibers. Study of a fast exponential process (C). Biophys. J. 55:595-603.
  24. Tawada, K. and Kawai, M. 1990. Covalent cross-linking of single muscle fibers from rabbit psoas increases oscillatory power. Biophys. J. 57:643-647.
  25. Kawai, M., Güth, K. and Wray, J. 1990. Effect of ionic strength on crossbridge kine­tics as studied by sinusoidal analysis, ATP hydrolysis rate, and X-ray diffraction tech­niques in chemically skinned rabbit psoas fibres. J. Muscle Res. Cell Mot. 11:392-402.
  26. Kawai, M. and Halvorson, H. R. 1991. Two step mechanism of phosphate release and the mechanism of force generation in chemically skinned rabbit psoas muscle. Biophys. J. 59:329-342.
  27. Saeki, Y., Kawai, M. and Zhao, Y. 1991. Comparison of the cross-bridge dynamics between intact and skinned myocardium from ferret right ventricles. Circ. Res. 68:772-781.
  28. Kawai, M, Wray, J. S. and Zhao, Y. 1993. The effect of the lattice spacing change on cross-bridge kinetics in chemically skinned rabbit psoas muscle fibers. I. Proportionality between the lattice spacing and the fiber width. Biophys. J. 64:187-196.
  29. Zhao, Y. and Kawai, M. 1993. The effect of the lattice spacing change on cross-bridge kinetics in chemically skinned rabbit psoas muscle fibers. II. Elementary steps affected by the spacing change. Biophys. J. 64:197-210.
  30. Kawai, M., Saeki, Y. and Zhao, Y. 1993. Cross-bridge scheme and the kinetic constants of elementary steps deduced from chemically skinned papillary and trabecular muscles of the ferret. Circ. Res. 73:35-50.
  31. Kawai, M. and Zhao, Y. 1993. Cross-bridge scheme and force per cross-bridge state in skinned rabbit psoas muscle fibers. Biophys. J. 65:638-651.
  32. Kawai, M. 1993. Kawai's response to Horiuti and Sakoda. Biophys. J. 65:2263-2264.
  33. Zhao, Y. and Kawai, M. 1994. BDM affects nucleotide binding and force generation steps of the cross-bridge cycle in rabbit psoas muscle fibers. Am. J. Physiol. 266 (Cell Physiol. 35): C437-C447.
  34. Schraeger, J. A., Canby, C. A., Rongish, B. J., Kawai, M., Tomanek, R. J. 1994. Normal left ventricular diastolic compliance following regression of hypertrophy. J. Cardiovascular Pharmacology 23:349-357
  35. Zhao, Y. and Kawai, M. 1994. Kinetic and Thermodynamic studies of the cross-bridge cycle in rabbit psoas muscle fibers. Biophys. J. 67:1655-1668.
  36. Raucher, D., Fajer, E. A., Sar, C., Hideg, K., Zhao, Y., Kawai, M., and Fajer, P. G. 1995. A novel electron paramagnetic resonance spin label and its application to study the cross-bridge cycle. Biophys. J. 68:128s-134s.
  37. Wang, G. and Kawai, M. 1996. Effects of MgATP and MgADP on the cross-bridge kinetics of rabbit soleus slow-twitch muscle fibers. Biophys. J. 71:1450-1461.
  38. Zhao, Y. and Kawai, M. 1996. Inotropic agent EMD-53998 weakens nucleotide and phosphate binding to cross-bridges in porcine myocardium. Am. J. Physiol. 271 (Heart Circ. Physiol. 40): H1394-1406.
  39. Zhao, Y., Swamy, P. M. G., Humphries, K. A. and Kawai, M. 1996. The effect of partial extraction of troponin C on the elementary steps of the cross-bridge cycle in rabbit psoas fibers. Biophys. J. 2759-2773.
  40. Murphy, K. P., Zhao, Y., and Kawai, M. 1996. Molecular forces involved in force generation during skeletal muscle contraction. J. Exptl. Biol. 199:2565-2571.
  41. Wang, G. and Kawai, M. 1997. Force generation and phosphate release steps in skinned rabbit soleus slow-twitch muscle fibers. Biophys. J. 73:878-894.
  42. Kawai, M. 1998. Comments on the paper by Dr. David Smith entitled “A strain-dependent ratchet model for [phosphate]- and [ATP]-dependent muscle contraction.” J. Muscle Res. Cell Mot. 19:713-715.
  43. Wang, G., Ding, W., and Kawai, M. 1999. Does thin filament compliance diminish thecross-bridge kinetics? A study in rabbit psoas fibers. Biophys. J. 76:978-984.
  44. Kawai, M., Kawaguchi, K., Saito, M., and Ishiwata, S. 2000. Temperature change does not affect force between single actin filaments and HMM from rabbit muscles. Biophys. J. 78:3112-3119.
  45. Wang, G., and Kawai, M. 2001. Effect of temperature on elementary steps of the cross-bridge cycle in rabbit soleus slow-twitch muscle fibres. J. Physiology 531.1:219-234.
  46. Fujita, H., Sasaki, D., Ishiwata, S. and Kawai, M. 2002. Elementary steps of the cross-bridge cycle in bovine myocardium with and without regulatory proteins. Biophys. J. 82:915-928.
  47. Fujita, H. and Kawai, M. 2002. Temperature effect on isometric tension is mediated by regulatory proteins tropomyosin and troponin in bovine myocardium. J. Physiology, 539.1:267-276.
  48. Ding, W., Fujita, H., and Kawai, M. 2002. The length of cooperative units on the thin filament in rabbit psoas muscle fibres. Experimental Physiology, 87.6:691-697.
  49. Kawai, M. 2003. What do we learn by studying the tempera­ture effect on isometric tension and tension transients in mammalian striated muscle fibres?  J. Muscle Res. Cell Motil. 24:127-138.
  50. Lu, X., L. S. Tobacman, and M. Kawai. 2003. 23Tm on isometric tension andDEffects of tropo­myosin internal deletion the cross-bridge kinetics in bovine myocardium. J. Physiology. 553.2:457-471.
  51. Fujita, H., X. Lu, M. Suzuki, S. Ishiwata, and M. Kawai. 2004. The effect of tropomyosin on force and elementary steps of the cross-bridge cycle in bovine myocardium. J. Physiology.  556.2: 637-649.
  52. Lu, X., M. K. Bryant, K. Bryan, P. A. Rubenstein, and M. Kawai. 2005. Role of the N-terminal negative charge of actin in cross-bridge kinetics and force generation in reconstituted bovine myocardium. J. Physiology. 564.1: 65-82.
  53. Galler S, Wang BG, Kawai M. 2005. Elementary steps of the cross-bridge cycle in fast-twitch fiber types from rabbit skeletal muscles. Biophys. J. 89: 3248-3260.
  54. Kawai M, Kido T, Vogel M, Fink RHA and Ishiwata S. 2006. Temperature change does not affect force between regulated actin filaments and HMM in single molecule experiments. J Physiol574.3: 877–887.
  55. Kawai M and Ishiwata S. 2006. Use of thin filament reconstituted muscle fibres to probe the mechanism of force generation. J Muscle Res Cell Motil 27: 455-468.
  56. Lu X, Tobacman LS and Kawai M. 2006. Temperature depen­dence of isometric tension and cross-bridge kinetics of cardiac muscle fibers reconstituted with a tropomyosin internal deletion mutant. Biophys J 91: 4230-4240.
  57. Kawai M, Halvorson HR (2007) Force transients and minimum cross-bridge models in muscular contraction. J Muscle Res Cell Motil 28:371-395.
  58. Kawai M, Lu X, Hitchcock-DeGregori SE, Stanton KJ, Wandling MW (2009) Tropomyosin period 3 is essential for enhancement of isometric tension in thin filament-reconstituted bovine myocardium. J Biophysics 2009: 1-17.
  59. Lu X, Heeley DH, Smillie LB, Kawai M (2010) The role of tropo­myosin isoforms and phosphorylation in force generation in thin-filament reconstituted bovine cardiac muscle fibres. J Muscle Res Cell Motil 31:93–109.
  60. Bai F, Weis A, Takeda AK, Chase PB, Kawai M (2011) Enhanced active cross-bridges during diastole: molecular pathogenesis of tropomyosin’s HCM mutations. Biophys J 100: 1014-1023.