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Volumn 83, Issue 6, 2002, Pages 3425-3434

A simple model with myofilament compliance predicts activation-dependent crossbridge kinetics in skinned skeletal fibers

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CALCIUM ION; GLYCEROL; MYOSIN ADENOSINE TRIPHOSPHATASE;

EID: 0036924212     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(02)75342-3     Document Type: Article
Times cited : (46)

References (44)
  • 1
    • 0029975892 scopus 로고    scopus 로고
    • Orientation changes in myosin regulatory light chains following photorelease of ATP in skinned muscle fibers
    • Allen, T. S., N. Ling, M. Irving, and Y. E. Goldman. 1996. Orientation changes in myosin regulatory light chains following photorelease of ATP in skinned muscle fibers. Biophys. J. 70:1847-1862.
    • (1996) Biophys. J. , vol.70 , pp. 1847-1862
    • Allen, T.S.1    Ling, N.2    Irving, M.3    Goldman, Y.E.4
  • 2
    • 0032846792 scopus 로고    scopus 로고
    • Sarcomere tension-stiffness relation during the tetanus rise in single frog muscle fibers
    • Bagni, M. A., G. Cecchi, B. Colombini, and F. Colomo. 1999. Sarcomere tension-stiffness relation during the tetanus rise in single frog muscle fibers. J. Muscle Res. Cell Motil. 20:469-476.
    • (1999) J. Muscle Res. Cell Motil. , vol.20 , pp. 469-476
    • Bagni, M.A.1    Cecchi, G.2    Colombini, B.3    Colomo, F.4
  • 3
    • 0025094287 scopus 로고
    • Tension and stiffness of frog muscle fibers at full filament overlap
    • Bagni, M. A., G. Cecchi, F. Colomo, and C. Poggesi. 1990. Tension and stiffness of frog muscle fibers at full filament overlap. J. Muscle Res. Cell Motil. 11:371-377.
    • (1990) J. Muscle Res. Cell Motil. , vol.11 , pp. 371-377
    • Bagni, M.A.1    Cecchi, G.2    Colomo, F.3    Poggesi, C.4
  • 4
    • 0024216304 scopus 로고
    • A model of force production that explains the lag between cross-bridge attachment and force after electrical stimulation of striated muscle fibers
    • 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.
    • (1988) Biophys. J. , vol.54 , pp. 1105-1114
    • Bagni, M.A.1    Cecchi, G.2    Schoenberg, M.3
  • 5
    • 0020536686 scopus 로고
    • Technique for stabilizing the striation pattern in maximally calcium-activated skinned rabbit psoas fibers
    • Brenner, B. 1983. Technique for stabilizing the striation pattern in maximally calcium-activated skinned rabbit psoas fibers. Biophys. J. 41:99-102.
    • (1983) Biophys. J. , vol.41 , pp. 99-102
    • Brenner, B.1
  • 6
    • 0023889297 scopus 로고
    • Effects of pH on contraction of rabbit fast and slow skeletal muscle fibers
    • Chase, P. B., and M. J. Kushmerick. 1988. Effects of pH on contraction of rabbit fast and slow skeletal muscle fibers. Biophys. J. 53:935-946.
    • (1988) Biophys. J. , vol.53 , pp. 935-946
    • Chase, P.B.1    Kushmerick, M.J.2
  • 7
    • 0028203450 scopus 로고
    • Activation dependence and kinetics of force and stiffness inhibition by aluminofiuoride, a slowly dissociating analogue of inorganic phosphate, in chemically skinned fibers from rabbit psoas muscle
    • Chase, P. B., D. A. Martyn, and J. D. Hannon. 1994. Activation dependence and kinetics of force and stiffness inhibition by aluminofiuoride, a slowly dissociating analogue of inorganic phosphate, in chemically skinned fibers from rabbit psoas muscle. J. Muscle Res. Cell Motil. 15:119-129.
    • (1994) J. Muscle Res. Cell Motil. , vol.15 , pp. 119-129
    • Chase, P.B.1    Martyn, D.A.2    Hannon, J.D.3
  • 8
    • 0027407920 scopus 로고
    • Effects of inorganic phosphate analogues on stiffness and unloaded shortening of skinned muscle fibers from rabbit
    • Chase, P. B., D. A. Martyn, M. J. Kushmerick, and A. M. Gordon. 1993. Effects of inorganic phosphate analogues on stiffness and unloaded shortening of skinned muscle fibers from rabbit. J. Physiol. (Lond.). 460:231-246.
    • (1993) J. Physiol. (Lond.) , vol.460 , pp. 231-246
    • Chase, P.B.1    Martyn, D.A.2    Kushmerick, M.J.3    Gordon, A.M.4
  • 10
    • 0031953771 scopus 로고    scopus 로고
    • Compliant realignment of binding sites in muscle: Transient behavior and mechanical tuning
    • Daniel, T. L., A. C. Trimble, and P. B. Chase. 1998. Compliant realignment of binding sites in muscle: Transient behavior and mechanical tuning. Biophys. J. 74:1611-1621.
    • (1998) Biophys. J. , vol.74 , pp. 1611-1621
    • Daniel, T.L.1    Trimble, A.C.2    Chase, P.B.3
  • 11
    • 0026694489 scopus 로고
    • Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibers
    • Dantzig, J. A., Y. E. Goldman, N. C. Millar, J. Lacktis, and E. Homsher. 1992. Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibers. J. Physiol. 451:247-278.
    • (1992) J. Physiol. , vol.451 , pp. 247-278
    • Dantzig, J.A.1    Goldman, Y.E.2    Millar, N.C.3    Lacktis, J.4    Homsher, E.5
  • 12
    • 0028918704 scopus 로고
    • Force generation and temperaturejump and length-jump tension transients in muscle fibers
    • Davis, J. S., and M. E. Rodgers. 1995. Force generation and temperaturejump and length-jump tension transients in muscle fibers. Biophys. J. 68:2032-2040.
    • (1995) Biophys. J. , vol.68 , pp. 2032-2040
    • Davis, J.S.1    Rodgers, M.E.2
  • 13
    • 0017385529 scopus 로고
    • Tension responses to sudden length change in stimulated frog muscle fibers near slack length
    • 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.
    • (1977) J. Physiol. , vol.269 , pp. 441-515
    • Ford, L.E.1    Huxley, A.F.2    Simmons, R.M.3
  • 14
    • 0019390452 scopus 로고
    • The relation between stiffness and filament overlap in stimulated frog muscle fibers
    • Ford, L. E., A. F. Huxley, and R. M. Simmons. 1981. The relation between stiffness and filament overlap in stimulated frog muscle fibers. J. Physiol. 311:219-249.
    • (1981) J. Physiol. , vol.311 , pp. 219-249
    • Ford, L.E.1    Huxley, A.F.2    Simmons, R.M.3
  • 15
    • 0022555623 scopus 로고
    • Tension transients during the rise of tetanic tension in frog muscle fibers
    • Ford, L. E., A. F. Huxley, and R. M. Simmons. 1986. Tension transients during the rise of tetanic tension in frog muscle fibers. J. Physiol. 372:595-609.
    • (1986) J. Physiol. , vol.372 , pp. 595-609
    • Ford, L.E.1    Huxley, A.F.2    Simmons, R.M.3
  • 16
    • 0028340236 scopus 로고
    • Dynamics of the muscle thin filament regulatory switch: The size of the cooperative unit
    • Geeves, M. A., and S. S. Lehrer. 1994. Dynamics of the muscle thin filament regulatory switch: The size of the cooperative unit. Biophys. J. 67:273-282.
    • (1994) Biophys. J. , vol.67 , pp. 273-282
    • Geeves, M.A.1    Lehrer, S.S.2
  • 17
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon, A. M., E. Homsher, and M. Regnier. 2000. Regulation of contraction in striated muscle. Physiol. Rev. 80:853-924.
    • (2000) Physiol. Rev. , vol.80 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 18
    • 0013905011 scopus 로고
    • The variation in isometric tension with sarcomere length in vertebrate muscle fibers
    • 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.
    • (1966) J. Physiol. , vol.184 , pp. 170-192
    • Gordon, A.M.1    Huxley, A.F.2    Julian, F.J.3
  • 19
    • 0027205101 scopus 로고
    • Calcium-independent activation of skeletal muscle fibers by a modified form of cardiac troponin C
    • Hannon, J. D., P. B. Chase, D. A. Martyn, L. L. Huntsman, M. J. Kushmerick, and A. M. Gordon. 1993. Calcium-independent activation of skeletal muscle fibers by a modified form of cardiac troponin C. Biophys. J. 64:1632-1637.
    • (1993) Biophys. J. , vol.64 , pp. 1632-1637
    • Hannon, J.D.1    Chase, P.B.2    Martyn, D.A.3    Huntsman, L.L.4    Kushmerick, M.J.5    Gordon, A.M.6
  • 20
    • 0029162081 scopus 로고
    • Compliance of thin filaments in skinned fibers of rabbit skeletal muscle
    • 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.
    • (1995) Biophys. J. , vol.69 , pp. 1000-1010
    • Higuchi, H.1    Yanagida, T.2    Goldman, Y.E.3
  • 21
    • 0030773824 scopus 로고    scopus 로고
    • Molecular motors: Structural adaptations to cellular functions
    • Howard, J. 1997. Molecular motors: Structural adaptations to cellular functions. Nature. 389:561-567.
    • (1997) Nature , vol.389 , pp. 561-567
    • Howard, J.1
  • 22
    • 0015236610 scopus 로고
    • Proposed mechanism of force generation in striated muscle
    • Huxley, A. F., and R. M. Simmons. 1971. Proposed mechanism of force generation in striated muscle. Nature. 233:533-538.
    • (1971) Nature , vol.233 , pp. 533-538
    • Huxley, A.F.1    Simmons, R.M.2
  • 24
    • 0028081493 scopus 로고
    • X-ray diffraction measurements of the extensibility of actin and myosin filaments in contracting muscle
    • 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.
    • (1994) Biophys. J. , vol.67 , pp. 2411-2421
    • Huxley, H.E.1    Stewart, A.2    Sosa, H.3    Irving, T.4
  • 25
    • 0029046139 scopus 로고
    • Flexibility of actin filaments derived from thermal fluctuations: Effect of bound nucleotide, phalloidin, and muscle regulatory proteins
    • Isambert, H., P. Venier, A. C. Maggs, A. Fattoum, R. Kassab, D. Pantaloni, and M.-F. Carlier. 1995. Flexibility of actin filaments derived from thermal fluctuations: Effect of bound nucleotide, phalloidin, and muscle regulatory proteins. J. Biol. Chem. 270:11437-11444.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11437-11444
    • Isambert, H.1    Venier, P.2    Maggs, A.C.3    Fattoum, A.4    Kassab, R.5    Pantaloni, D.6    Carlier, M.-F.7
  • 26
    • 0019447614 scopus 로고
    • 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
    • Kawai, M., R. N. Cox, and P. W. Brandt. 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.
    • (1981) Biophys. J. , vol.35 , pp. 375-384
    • Kawai, M.1    Cox, R.N.2    Brandt, P.W.3
  • 27
    • 0028607563 scopus 로고
    • Direct measurement of stiffness of single actin filaments with and without tropomyosin by in vitro nanomanipulation
    • Kojima, H., A. Ishijima, and T. Yanagida. 1994. Direct measurement of stiffness of single actin filaments with and without tropomyosin by in vitro nanomanipulation. Proc. Natl. Acad. Sci. U.S.A.. 91:12962-12966.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12962-12966
    • Kojima, H.1    Ishijima, A.2    Yanagida, T.3
  • 28
    • 0031958205 scopus 로고    scopus 로고
    • The stiffness of skeletal muscle in isometric contraction and rigor: The fraction of heads bound to actin
    • Linari, M., I. Dobbie, M. Reconditi, N. Koubassova, M. Irving, G. Piazzesi, and V. Lombardi. 1998. The stiffness of skeletal muscle in isometric contraction and rigor: The fraction of heads bound to actin. Biophys. J. 74:2459-2473.
    • (1998) Biophys. J. , vol.74 , pp. 2459-2473
    • Linari, M.1    Dobbie, I.2    Reconditi, M.3    Koubassova, N.4    Irving, M.5    Piazzesi, G.6    Lombardi, V.7
  • 29
    • 4243244079 scopus 로고    scopus 로고
    • Effects of N-benzyl-P-toluene sulfonamide (BTS) on force and stiffness of active single fibers of frog skeletal muscle
    • Abstr.
    • Linari, M., G. Piazzesi, and V. Lombardi. 2002. Effects of N-benzyl-P-toluene sulfonamide (BTS) on force and stiffness of active single fibers of frog skeletal muscle. Biophys. J. 82:377a. (Abstr.)
    • (2002) Biophys. J. , vol.82
    • Linari, M.1    Piazzesi, G.2    Lombardi, V.3
  • 30
    • 0028601298 scopus 로고
    • Effect of series elasticity on delay in development of tension relative to stiffness during muscle activation
    • Luo, Y., R. Cooke, and E. Pate. 1994. Effect of series elasticity on delay in development of tension relative to stiffness during muscle activation. Am. J. Physiol. 267:C1598-C1606.
    • (1994) Am. J. Physiol. , vol.267
    • Luo, Y.1    Cooke, R.2    Pate, E.3
  • 32
    • 0028804446 scopus 로고
    • 2+ activation of skinned psoas fibers from rabbit
    • 2+ activation of skinned psoas fibers from rabbit. Biophys. J. 68:235-242.
    • (1995) Biophys. J. , vol.68 , pp. 235-242
    • Martyn, D.A.1    Chase, P.B.2
  • 33
    • 0026711203 scopus 로고
    • Force and stiffness in glycerinated rabbit psoas fibers: Effects of calcium and elevated phosphate
    • Martyn, D. A., and A. M. Gordon. 1992. Force and stiffness in glycerinated rabbit psoas fibers: Effects of calcium and elevated phosphate. J. Gen. Physiol. 99:795-816.
    • (1992) J. Gen. Physiol. , vol.99 , pp. 795-816
    • Martyn, D.A.1    Gordon, A.M.2
  • 34
    • 0021895457 scopus 로고
    • Lateral filamentary spacing in chemically skinned murine muscles during contraction
    • Matsubara, I., Y. Umazume, and N. Yagi. 1985. Lateral filamentary spacing in chemically skinned murine muscles during contraction. J. Physiol. 360:135-148.
    • (1985) J. Physiol. , vol.360 , pp. 135-148
    • Matsubara, I.1    Umazume, Y.2    Yagi, N.3
  • 35
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament
    • McKillop, D. F. A., and M. A. Geeves. 1993. Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament. Biophys. J. 65:693-701.
    • (1993) Biophys. J. , vol.65 , pp. 693-701
    • McKillop, D.F.A.1    Geeves, M.A.2
  • 36
    • 0029758343 scopus 로고    scopus 로고
    • On the theory of muscle contraction: Filament extensibility and the development of isometric force and stiffness
    • Mijailovich, S. M., J. Fredberg, and J. P. Butler. 1996. On the theory of muscle contraction: Filament extensibility and the development of isometric force and stiffness. Biophys. J. 71:1475-1484.
    • (1996) Biophys. J. , vol.71 , pp. 1475-1484
    • Mijailovich, S.M.1    Fredberg, J.2    Butler, J.P.3
  • 37
    • 0026567953 scopus 로고
    • Tension transients during steady lengthening of tetanized muscle fibers of the frog
    • Piazzesi, G., F. Francini, M. Linari, and V. Lombardi. 1992. Tension transients during steady lengthening of tetanized muscle fibers of the frog. J. Physiol. 445:659-711.
    • (1992) J. Physiol. , vol.445 , pp. 659-711
    • Piazzesi, G.1    Francini, F.2    Linari, M.3    Lombardi, V.4
  • 38
    • 0027479115 scopus 로고
    • Formation of interand intramolecular disulfide bonds can activate cardiac troponin C
    • Putkey, J. A., D. G. Dotson, and P. Mouawad. 1993. Formation of interand intramolecular disulfide bonds can activate cardiac troponin C. J. Biol. Chem. 268:6827-6830.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6827-6830
    • Putkey, J.A.1    Dotson, D.G.2    Mouawad, P.3
  • 39
    • 0029792684 scopus 로고    scopus 로고
    • Endothermic force generation in fast and slow mammalian (rabbit) muscle fibers
    • Ranatunga, K. W. 1996. Endothermic force generation in fast and slow mammalian (rabbit) muscle fibers. Biophys. J. 71:1905-1913.
    • (1996) Biophys. J. , vol.71 , pp. 1905-1913
    • Ranatunga, K.W.1
  • 40
    • 0029177764 scopus 로고
    • Regulation of the cross-bridge transition from a weakly to strongly bound state in skinned rabbit muscle fibers
    • Regnier, M., C. Morris, and E. Homsher. 1995. Regulation of the cross-bridge transition from a weakly to strongly bound state in skinned rabbit muscle fibers. Am. J. Physiol. 269:C1532-C1539.
    • (1995) Am. J. Physiol. , vol.269
    • Regnier, M.1    Morris, C.2    Homsher, E.3
  • 41
    • 0029960235 scopus 로고
    • X-ray structure of the magnesium(II)· ADP·vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å resolution
    • Smith, C. A., and I. Rayment. 1995. X-ray structure of the magnesium(II)· ADP·vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å resolution. Biochemistry. 35:5404-5417.
    • (1995) Biochemistry , vol.35 , pp. 5404-5417
    • Smith, C.A.1    Rayment, I.2
  • 42
    • 0029840598 scopus 로고    scopus 로고
    • Calcium alone does not fully activate the thin filament for S1 binding to rigor myofibrils
    • Swartz, D. R., R. L. Moss, and M. L. Greaser. 1996. Calcium alone does not fully activate the thin filament for S1 binding to rigor myofibrils. Biophys. J. 71:1891-1904.
    • (1996) Biophys. J. , vol.71 , pp. 1891-1904
    • Swartz, D.R.1    Moss, R.L.2    Greaser, M.L.3
  • 43
    • 0021402066 scopus 로고
    • Stiffness of glycerinated rabbit psoas fibers in the rigor state: Filament-overlap relation
    • Tawada, K., and M. Kimura. 1984. Stiffness of glycerinated rabbit psoas fibers in the rigor state: Filament-overlap relation. Biophys. J. 45:593-602.
    • (1984) Biophys. J. , vol.45 , pp. 593-602
    • Tawada, K.1    Kimura, M.2
  • 44
    • 0028081494 scopus 로고
    • X-ray diffraction evidence for the extensibility of actin and myosin filaments during muscle contraction
    • Wakabayashi, K., Y. Sugimoto, H. Tanaka, Y. Ueno, Y. Takezawa, and Y. Amemiya. 1994. X-ray diffraction evidence for the extensibility of actin and myosin filaments during muscle contraction. Biophys. J. 67:2422-2435.
    • (1994) Biophys. J. , vol.67 , pp. 2422-2435
    • Wakabayashi, K.1    Sugimoto, Y.2    Tanaka, H.3    Ueno, Y.4    Takezawa, Y.5    Amemiya, Y.6


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