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Volumn 31, Issue 2, 2006, Pages 135-143

Mechanical strength of sarcomere structures of skeletal myofibrils studied by submicromanipulation

Author keywords

Atomic force microscope; Mechanical strength; Optical tweezers; Sarcomere; Skeletal muscle

Indexed keywords

ALPHA ACTININ; MYOSIN ADENOSINE TRIPHOSPHATASE;

EID: 33846236014     PISSN: 03867196     EISSN: 13473700     Source Type: Journal    
DOI: 10.1247/csf.06017     Document Type: Article
Times cited : (5)

References (40)
  • 1
    • 33750100539 scopus 로고    scopus 로고
    • Transverse stiffness of myofibrils of skeletal and cardiac muscles studied by atomic force microscopy
    • Akiyama, N., Ohnuki, Y., Kunioka, Y., Saeki, Y., and Yamada, T. 2006. Transverse stiffness of myofibrils of skeletal and cardiac muscles studied by atomic force microscopy. J. Physiol. Sci., 56: 145-151.
    • (2006) J. Physiol. Sci , vol.56 , pp. 145-151
    • Akiyama, N.1    Ohnuki, Y.2    Kunioka, Y.3    Saeki, Y.4    Yamada, T.5
  • 2
    • 0027419031 scopus 로고
    • Effects of different enzymic treatments on the release of titin fragments from rabbit skeletal myofibrils
    • Astier, C., Labbe, J., Roustan, C., and Benyamin, Y. 1993. Effects of different enzymic treatments on the release of titin fragments from rabbit skeletal myofibrils. Biochem. J., 290: 731-734.
    • (1993) Biochem. J , vol.290 , pp. 731-734
    • Astier, C.1    Labbe, J.2    Roustan, C.3    Benyamin, Y.4
  • 4
    • 0000595169 scopus 로고
    • Optical tweezers: A new tool for biophysics
    • Noninvasive techniques in cell biology Foskett, J.K, Grinstein, S, eds, Wiley-Liss, New York, pp
    • Block, S.M. 1990. Optical tweezers: a new tool for biophysics. In Noninvasive techniques in cell biology (Foskett, J.K., Grinstein, S., eds.). Modern Cell Biology vol. 9, Wiley-Liss, New York, pp.375-402.
    • (1990) Modern Cell Biology , vol.9 , pp. 375-402
    • Block, S.M.1
  • 5
    • 0024514118 scopus 로고
    • Compliance of bacterial flagella measured with optical tweezers
    • Block, S.M., Blair, D.F., and Berg, H.C. 1989. Compliance of bacterial flagella measured with optical tweezers. Nature, 338: 514-518.
    • (1989) Nature , vol.338 , pp. 514-518
    • Block, S.M.1    Blair, D.F.2    Berg, H.C.3
  • 6
    • 0019305701 scopus 로고
    • All myosin heads form bonds with actin in rigor rabbit skeletal muscle
    • Cooke, R. and Franks, K. 1980. All myosin heads form bonds with actin in rigor rabbit skeletal muscle. Biochemistry, 19: 2265-2269.
    • (1980) Biochemistry , vol.19 , pp. 2265-2269
    • Cooke, R.1    Franks, K.2
  • 7
    • 0028261701 scopus 로고
    • Single myosin molecule mechanics: Piconewton forces and nanometer steps
    • Finer, J.T., Simmons, R.M., and Spudich, J.A. 1994. Single myosin molecule mechanics: piconewton forces and nanometer steps. Nature, 368: 113-119.
    • (1994) Nature , vol.368 , pp. 113-119
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 8
    • 4344586794 scopus 로고    scopus 로고
    • Simultaneous dynamic stiffness and extension profiles of single titin molecules. Nanomechanical evidence for unfolding intermediates
    • Forbes, J.G. and Wang, K. 2004. Simultaneous dynamic stiffness and extension profiles of single titin molecules. Nanomechanical evidence for unfolding intermediates. J. Vac. Sci. Technol., A22: 1439-1443.
    • (2004) J. Vac. Sci. Technol , vol.A22 , pp. 1439-1443
    • Forbes, J.G.1    Wang, K.2
  • 10
    • 0029823455 scopus 로고    scopus 로고
    • Titin develops restoring force in rat cardiac myocytes
    • Helmes, M., Trombitas, K., and Granzier, H. 1996. Titin develops restoring force in rat cardiac myocytes. Circ. Res., 79: 619-626.
    • (1996) Circ. Res , vol.79 , pp. 619-626
    • Helmes, M.1    Trombitas, K.2    Granzier, H.3
  • 11
    • 0038650860 scopus 로고    scopus 로고
    • Kinetics from nonequilibrium single-molecule pulling experiments
    • Hummer, G. and Szabo, A. 2003. Kinetics from nonequilibrium single-molecule pulling experiments. Biophys. J., 85: 5-15.
    • (2003) Biophys. J , vol.85 , pp. 5-15
    • Hummer, G.1    Szabo, A.2
  • 12
    • 85010249552 scopus 로고
    • The low-angle X-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor
    • Huxley, H.E. and Brown, W. 1967. The low-angle X-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor. J. Mol. Biol., 30: 383-434.
    • (1967) J. Mol. Biol , vol.30 , pp. 383-434
    • Huxley, H.E.1    Brown, W.2
  • 13
    • 0034491563 scopus 로고    scopus 로고
    • Spring mechanics of α-helical polypeptide
    • Idiris, A., Alam, M.T., and Ikai, A. 2000. Spring mechanics of α-helical polypeptide. Protein Eng., 13: 763-770.
    • (2000) Protein Eng , vol.13 , pp. 763-770
    • Idiris, A.1    Alam, M.T.2    Ikai, A.3
  • 16
    • 0026510571 scopus 로고
    • Characterization and localization of alpha-actinin (titin-1): And elastic protein isolated from rabbit skeletal muscle
    • Kimura, S., Matsuura, T., Ohtsuka, S., Nakauchi, Y., Matsuno, A., and Maruyama, K. 1992. Characterization and localization of alpha-actinin (titin-1): and elastic protein isolated from rabbit skeletal muscle. J. Muscle Res. Cell Motil., 13: 39-47.
    • (1992) J. Muscle Res. Cell Motil , vol.13 , pp. 39-47
    • Kimura, S.1    Matsuura, T.2    Ohtsuka, S.3    Nakauchi, Y.4    Matsuno, A.5    Maruyama, K.6
  • 17
    • 0028607563 scopus 로고
    • Direct measurement of stiffness of single actin filaments with and without tropomyosin by in vitro nanomanipulation
    • Kojima, H., Ishijima, A., and Yanagida, T. 1994. Direct measurement of stiffness of single actin filaments with and without tropomyosin by in vitro nanomanipulation. Proc. Natl. Acad. Sci. USA, 91: 12962-12966.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12962-12966
    • Kojima, H.1    Ishijima, A.2    Yanagida, T.3
  • 19
    • 0036841235 scopus 로고    scopus 로고
    • Mechanics of F-actin characterized with microfabricated cantilevers
    • Liu, X. and Pollack, G.H. 2002. Mechanics of F-actin characterized with microfabricated cantilevers. Biophys. J., 83: 2705-2715.
    • (2002) Biophys. J , vol.83 , pp. 2705-2715
    • Liu, X.1    Pollack, G.H.2
  • 20
    • 0019815071 scopus 로고
    • Fraction of myosin heads bound to thin filaments in rigor fibrils from insect flight and vertebrate muscles
    • Lovell, S.J., Knight, P.J., and Harrington, W.F. 1981. Fraction of myosin heads bound to thin filaments in rigor fibrils from insect flight and vertebrate muscles. Nature, 293: 664-666.
    • (1981) Nature , vol.293 , pp. 664-666
    • Lovell, S.J.1    Knight, P.J.2    Harrington, W.F.3
  • 21
    • 0020021291 scopus 로고
    • Preparation of myosin and its subfragments from rabbit skeletal muscle
    • Margossian, S.S. and Lowey, S. 1982. Preparation of myosin and its subfragments from rabbit skeletal muscle. Methods. Enzymol., 85: 55-71.
    • (1982) Methods. Enzymol , vol.85 , pp. 55-71
    • Margossian, S.S.1    Lowey, S.2
  • 22
    • 0029984843 scopus 로고    scopus 로고
    • Strength and lifetime of the bond between actin and skeletal muscle α-actinin studied with an optical trapping technique
    • Miyata, H., Yasuda, R., and Kinosita, K. 1996. Strength and lifetime of the bond between actin and skeletal muscle α-actinin studied with an optical trapping technique. Biochim. Biophys. Acta, 1290: 83-88.
    • (1996) Biochim. Biophys. Acta , vol.1290 , pp. 83-88
    • Miyata, H.1    Yasuda, R.2    Kinosita, K.3
  • 24
    • 0022801965 scopus 로고
    • Active movement of synthetic myosin filaments observed by dark-field light microscopy
    • Nagashima, H. 1986. Active movement of synthetic myosin filaments observed by dark-field light microscopy. J. Biochem. (Tokyo), 100: 1023-1029.
    • (1986) J. Biochem. (Tokyo) , vol.100 , pp. 1023-1029
    • Nagashima, H.1
  • 25
    • 0033884332 scopus 로고    scopus 로고
    • Characterization of single actomyosin rigor bonds: Load dependence of lifetime and mechanical properties
    • Nishizaka, T., Seo, R., Tadakuma, H., Kinosita, K., and Ishiwata, S. 2000. Characterization of single actomyosin rigor bonds: load dependence of lifetime and mechanical properties. Biophys. J., 79: 962-974.
    • (2000) Biophys. J , vol.79 , pp. 962-974
    • Nishizaka, T.1    Seo, R.2    Tadakuma, H.3    Kinosita, K.4    Ishiwata, S.5
  • 26
    • 0034052572 scopus 로고    scopus 로고
    • Morphology and transverse stiffness of Drosophila myofibrils measured by atomic force microscopy
    • Nyland, L.R. and Maughan, D.W. 2000. Morphology and transverse stiffness of Drosophila myofibrils measured by atomic force microscopy. Biophys. J., 78: 1490-1497.
    • (2000) Biophys. J , vol.78 , pp. 1490-1497
    • Nyland, L.R.1    Maughan, D.W.2
  • 27
    • 0016745120 scopus 로고
    • Removal of Z-lines and α-actinin from isolated myofibrils by a calcium-activated neutral protease
    • Reddy, M.K., Etlinger, J.D., Rabinowitz, M., Fischman, D.A., and Zak, R. 1975. Removal of Z-lines and α-actinin from isolated myofibrils by a calcium-activated neutral protease. J. Biol. Chem., 250: 4278-4284.
    • (1975) J. Biol. Chem , vol.250 , pp. 4278-4284
    • Reddy, M.K.1    Etlinger, J.D.2    Rabinowitz, M.3    Fischman, D.A.4    Zak, R.5
  • 29
    • 0030967587 scopus 로고    scopus 로고
    • Architecture and function in the muscle sarcomere
    • Squire, J.M. 1997. Architecture and function in the muscle sarcomere. Curr. Opin. Struct. Biol., 7: 247-257.
    • (1997) Curr. Opin. Struct. Biol , vol.7 , pp. 247-257
    • Squire, J.M.1
  • 30
    • 0020534222 scopus 로고
    • Extensibility of the myofilaments in vertebrate skeletal muscle as revealed by stretching rigor muscle fibers
    • Suzuki, S. and Sugi, H. 1983. Extensibility of the myofilaments in vertebrate skeletal muscle as revealed by stretching rigor muscle fibers. J. Gen. Physiol., 81: 531-546.
    • (1983) J. Gen. Physiol , vol.81 , pp. 531-546
    • Suzuki, S.1    Sugi, H.2
  • 31
    • 0029822651 scopus 로고    scopus 로고
    • Torsional rigidity of single actin filaments and actin-actin bond breaking force under torsion measured directly by in vitro micromanipulation
    • Tsuda, Y., Yasutake, H., Ishijima, A., and Yanagida, T. 1996. Torsional rigidity of single actin filaments and actin-actin bond breaking force under torsion measured directly by in vitro micromanipulation. Proc. Natl. Acad. Sci. USA, 93: 12937-12942.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12937-12942
    • Tsuda, Y.1    Yasutake, H.2    Ishijima, A.3    Yanagida, T.4
  • 32
    • 0033465362 scopus 로고    scopus 로고
    • Muscle contraction: Challenges for synchrotron radiation
    • Wakabayashi, K. and Yagi, N. 1999. Muscle contraction: challenges for synchrotron radiation. J. Synchrotron Rad., 6: 875-890.
    • (1999) J. Synchrotron Rad , vol.6 , pp. 875-890
    • Wakabayashi, K.1    Yagi, N.2
  • 33
    • 0037057823 scopus 로고    scopus 로고
    • Zigzag motions of the myosin-coated beads actively sliding along actin filaments suspended between immobilized beads
    • Wakayama, J., Shohara, M., Yagi, C., Ono, H., Miyake, N., Kunioka, Y., and Yamada, T. 2002. Zigzag motions of the myosin-coated beads actively sliding along actin filaments suspended between immobilized beads. Biochim. Biophys. Acta, 1573: 93-99.
    • (2002) Biochim. Biophys. Acta , vol.1573 , pp. 93-99
    • Wakayama, J.1    Shohara, M.2    Yagi, C.3    Ono, H.4    Miyake, N.5    Kunioka, Y.6    Yamada, T.7
  • 34
    • 0034537985 scopus 로고    scopus 로고
    • Contractility of single myofibrils of rabbit skeletal muscle studied at various MgATP concentrations
    • Wakayama, J. and Yamada, T. 2000. Contractility of single myofibrils of rabbit skeletal muscle studied at various MgATP concentrations. Jap. J. Physiol., 50: 533-542.
    • (2000) Jap. J. Physiol , vol.50 , pp. 533-542
    • Wakayama, J.1    Yamada, T.2
  • 35
    • 0034456653 scopus 로고    scopus 로고
    • Atomic force microscopic evidence for Z-band as a rigid disc fixing the sarcomere structure of skeletal muscle
    • Wakayama, J., Yoshikawa, Y., Yasuike, T., and Yamada, T. 2000. Atomic force microscopic evidence for Z-band as a rigid disc fixing the sarcomere structure of skeletal muscle. Cell Struct. Funct., 25: 361-365.
    • (2000) Cell Struct. Funct , vol.25 , pp. 361-365
    • Wakayama, J.1    Yoshikawa, Y.2    Yasuike, T.3    Yamada, T.4
  • 37
    • 0031951415 scopus 로고    scopus 로고
    • Stepwise dynamics of connecting filaments measured in single myofibrillar sarcomeres
    • Yang, P., Tameyasu, T., and Pollack, G.H. 1998. Stepwise dynamics of connecting filaments measured in single myofibrillar sarcomeres. Biophys. J., 74: 1473-1483.
    • (1998) Biophys. J , vol.74 , pp. 1473-1483
    • Yang, P.1    Tameyasu, T.2    Pollack, G.H.3
  • 38
    • 0030601791 scopus 로고    scopus 로고
    • Direct measurement of the torsional rigidity of single actin filaments
    • Yasuda, R., Miyata, H., and Kinosita, K. 1996a. Direct measurement of the torsional rigidity of single actin filaments. J. Mol. Biol., 263: 227-236.
    • (1996) J. Mol. Biol , vol.263 , pp. 227-236
    • Yasuda, R.1    Miyata, H.2    Kinosita, K.3
  • 39
    • 0029862945 scopus 로고    scopus 로고
    • Synchronous behavior of spontaneous oscillations of sarcomeres in skeletal myofibrils under isotonic conditions
    • Yasuda, K., Shindo, Y., and Ishiwata, S. 1996b. Synchronous behavior of spontaneous oscillations of sarcomeres in skeletal myofibrils under isotonic conditions. Biophys. J., 70: 1823-1829.
    • (1996) Biophys. J , vol.70 , pp. 1823-1829
    • Yasuda, K.1    Shindo, Y.2    Ishiwata, S.3
  • 40
    • 0033525792 scopus 로고    scopus 로고
    • Transverse elasticity of myofibrils of rabbit skeletal muscle studied by atomic force microscopy
    • Yoshikawa, Y., Yasuike, T., Yagi, A., and Yamada, T. 1999. Transverse elasticity of myofibrils of rabbit skeletal muscle studied by atomic force microscopy. Biochem. Biophys. Res. Commun., 256: 13-19.
    • (1999) Biochem. Biophys. Res. Commun , vol.256 , pp. 13-19
    • Yoshikawa, Y.1    Yasuike, T.2    Yagi, A.3    Yamada, T.4


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