메뉴 건너뛰기




Volumn 78, Issue 6, 2000, Pages 3120-3137

Different myofilament nearest-neighbor interactions have distinctive effects on contractile behavior

Author keywords

[No Author keywords available]

Indexed keywords

MYOSIN; TROPOMYOSIN;

EID: 0034123345     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76849-4     Document Type: Article
Times cited : (93)

References (44)
  • 2
    • 0021755958 scopus 로고
    • The thin filament of vertebrate skeletal muscle cooperatively activates as a unit
    • Brandt, P. W., M. S. Diamond, and F. H. Sachat. 1984. The thin filament of vertebrate skeletal muscle cooperatively activates as a unit. J. Mol. Biol. 180:379-384.
    • (1984) J. Mol. Biol. , vol.180 , pp. 379-384
    • Brandt, P.W.1    Diamond, M.S.2    Sachat, F.H.3
  • 3
    • 0023187156 scopus 로고
    • Co-operative interactions between troponin-tropomyosin units extend the length of the thin filament in skeletal muscle
    • Brandt, P. W., M. S. Diamond, J. S. Rutchik, and F. H. Sachat. 1987. Co-operative interactions between troponin-tropomyosin units extend the length of the thin filament in skeletal muscle. J. Mol. Biol. 195: 885-896.
    • (1987) J. Mol. Biol. , vol.195 , pp. 885-896
    • Brandt, P.W.1    Diamond, M.S.2    Rutchik, J.S.3    Sachat, F.H.4
  • 4
    • 0022253498 scopus 로고
    • Hysteresis of the mammalian pCa/tension relation is small and muscle specific
    • Brandt, P. W., B. Gluck, M. Mini, and C. Cerri. 1985. Hysteresis of the mammalian pCa/tension relation is small and muscle specific. J. Musc. Res. Cell Motil. 6:197-205.
    • (1985) J. Musc. Res. Cell Motil. , vol.6 , pp. 197-205
    • Brandt, P.W.1    Gluck, B.2    Mini, M.3    Cerri, C.4
  • 5
    • 0015525066 scopus 로고
    • Cooperation within actin filament in vertebrate skeletal muscle
    • Bremel, R. D., and A. Weber. 1972. Cooperation within actin filament in vertebrate skeletal muscle. Nat. New Biol. 238:97-101.
    • (1972) Nat. New Biol. , vol.238 , pp. 97-101
    • Bremel, R.D.1    Weber, A.2
  • 6
    • 0024007477 scopus 로고
    • Effect of Ca2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: Implications for regulation of muscle contraction
    • Brenner, B. 1988. Effect of Ca2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: implications for regulation of muscle contraction. Proc. Natl. Acad. Sci. USA. 85:3265-3269.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3265-3269
    • Brenner, B.1
  • 7
    • 0031595411 scopus 로고    scopus 로고
    • Dethiophalloidin increases Ca2+ responsiveness of skinned cardiac muscle
    • Bukatina, A. E., R. D. Kirkpatrick, and K. B. Campbell. 1998. Dethiophalloidin increases Ca2+ responsiveness of skinned cardiac muscle. J. Musc. Res. Cell Motil. 19:515-523.
    • (1998) J. Musc. Res. Cell Motil. , vol.19 , pp. 515-523
    • Bukatina, A.E.1    Kirkpatrick, R.D.2    Campbell, K.B.3
  • 8
    • 0031038445 scopus 로고    scopus 로고
    • Rate constant of muscle force redevelopment reflects cooperative activation as well as cross-bridge kinetics
    • Campbell, K. 1997. Rate constant of muscle force redevelopment reflects cooperative activation as well as cross-bridge kinetics. Biophys. J. 72: 254-262.
    • (1997) Biophys. J. , vol.72 , pp. 254-262
    • Campbell, K.1
  • 9
    • 0031953771 scopus 로고    scopus 로고
    • Compliant realignment of binding sites in muscle: Transient behavior and mechanical tuning
    • Daniels, 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
    • Daniels, T.L.1    Trimble, A.C.2    Chase, P.B.3
  • 10
    • 33750822268 scopus 로고    scopus 로고
    • Right ventricular contractile protein function in rats with left ventricular myocardial infarction
    • Heart Circ. Physiol. 40
    • De Tombe, P. P., T. Wannenburg, D. Feng, and W. C. Little. 1996. Right ventricular contractile protein function in rats with left ventricular myocardial infarction. Am. J. Physiol. 271 (Heart Circ. Physiol. 40): H73-H79.
    • (1996) Am. J. Physiol. , vol.271
    • De Tombe, P.P.1    Wannenburg, T.2    Feng, D.3    Little, W.C.4
  • 11
    • 0028980233 scopus 로고
    • Steady-state [Ca2+]i-force relationship in intact twitching cardiac muscle: Direct evidence for modulation by isoproterenol and EMD 53998
    • Dobrunz L. E., P. H. Backx, and D. T. Yue. 1995. Steady-state [Ca2+]i-force relationship in intact twitching cardiac muscle: direct evidence for modulation by isoproterenol and EMD 53998 Biophys. J. 69:189-201.
    • (1995) Biophys. J. , vol.69 , pp. 189-201
    • Dobrunz, L.E.1    Backx, P.H.2    Yue, D.T.3
  • 12
    • 0032555957 scopus 로고    scopus 로고
    • Strong binding of myosin modulates length-dependent Ca2+ activation of rat ventricular myocytes
    • Fitzsimons, D. P., and R. L. Moss. 1998. Strong binding of myosin modulates length-dependent Ca2+ activation of rat ventricular myocytes. Circ. Res. 83:602-607.
    • (1998) Circ. Res. , vol.83 , pp. 602-607
    • Fitzsimons, D.P.1    Moss, R.L.2
  • 14
    • 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
  • 15
    • 0016248148 scopus 로고
    • Calcium-activated tension of skinned muscle fibers of the frog: Dependence on magnesium adenosine triphosphate concentration
    • Godt, R. 1974. Calcium-activated tension of skinned muscle fibers of the frog: dependence on magnesium adenosine triphosphate concentration. J. Gen. Physiol. 63:722-739.
    • (1974) J. Gen. Physiol. , vol.63 , pp. 722-739
    • Godt, R.1
  • 17
    • 0023900645 scopus 로고
    • Hysteresis and the length dependence of calcium sensitivity in chemically skinned rat cardiac muscle
    • Harrison, S. M., C. Lamont, and D. J. Miller. 1988. Hysteresis and the length dependence of calcium sensitivity in chemically skinned rat cardiac muscle. J. Physiol. 401:115-143.
    • (1988) J. Physiol. , vol.401 , pp. 115-143
    • Harrison, S.M.1    Lamont, C.2    Miller, D.J.3
  • 19
    • 0343435013 scopus 로고
    • Critical behavior of two-state, steady-state Ising system, according to the Bragg-Williams approximation
    • Hill, T. L., and L. Stein. 1978. Critical behavior of two-state, steady-state Ising system, according to the Bragg-Williams approximation. J. Chem. Phys. 69:1139-1150.
    • (1978) J. Chem. Phys. , vol.69 , pp. 1139-1150
    • Hill, T.L.1    Stein, L.2
  • 21
    • 0023488538 scopus 로고
    • Evidence for a force-dependent component of calcium binding to cardiac troponin C
    • Hofmann, P. A., and F. Fuchs. 1987b. Evidence for a force-dependent component of calcium binding to cardiac troponin C. Am. J. Physiol. 253:C541-C546.
    • (1987) Am. J. Physiol. , vol.253
    • Hofmann, P.A.1    Fuchs, F.2
  • 23
    • 0028342760 scopus 로고
    • The regulatory switch of the muscle thin filament: Calcium or myosin heads?
    • Lehrer, S. S. 1994. The regulatory switch of the muscle thin filament: calcium or myosin heads? J. Muscle Res. Cell Motil. 15:232-236.
    • (1994) J. Muscle Res. Cell Motil. , vol.15 , pp. 232-236
    • Lehrer, S.S.1
  • 24
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1
    • McKillop, D. F. A., and M. A. Geeves. 1993. Regulation of the interaction between actin and myosin subfragment 1. Biophys. J. 65:693-701.
    • (1993) Biophys. J. , vol.65 , pp. 693-701
    • McKillop, D.F.A.1    Geeves, M.A.2
  • 25
    • 0025271805 scopus 로고
    • Calcium-sensitive cross-bridge transitions in mammalian fast and slow skeletal muscle fibers
    • Metzger, J. M., and R. L. Moss. 1990. Calcium-sensitive cross-bridge transitions in mammalian fast and slow skeletal muscle fibers. Science 247:1088-1090.
    • (1990) Science , vol.247 , pp. 1088-1090
    • Metzger, J.M.1    Moss, R.L.2
  • 26
    • 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. J. Friedberg, 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    Friedberg, J.J.2    Butler, J.P.3
  • 27
    • 0025251785 scopus 로고
    • The effect of phosphate and calcium on force generation in glycerinated rabbit skeletal muscle fibers: A steady-state and transient kinetic study
    • Millar, N. C., and E. Homsher. 1990. The effect of phosphate and calcium on force generation in glycerinated rabbit skeletal muscle fibers: a steady-state and transient kinetic study. J. Biol. Chem. 265: 20234-20240.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20234-20240
    • Millar, N.C.1    Homsher, E.2
  • 28
    • 0026611165 scopus 로고
    • 2+ regulation of mechanical properties of striated muscle
    • 2+ regulation of mechanical properties of striated muscle. Circ. Res. 70:865-884.
    • (1992) Circ. Res. , vol.70 , pp. 865-884
    • Moss, R.L.1
  • 29
    • 0019888840 scopus 로고
    • Cooperatively of the calcium switch of regulated actomyosin system
    • Murray, J. M., and A. Weber. 1980. Cooperatively of the calcium switch of regulated actomyosin system. Mol. Cell. Biochem. 35:11-15.
    • (1980) Mol. Cell. Biochem. , vol.35 , pp. 11-15
    • Murray, J.M.1    Weber, A.2
  • 30
    • 0032572414 scopus 로고    scopus 로고
    • 2+ activation and relaxation in rat and guinea pig skinned trabeculae
    • 2+ activation and relaxation in rat and guinea pig skinned trabeculae. Circ. Res. 83: 179-186.
    • (1998) Circ. Res. , vol.83 , pp. 179-186
    • Palmer, S.1    Kentish, J.C.2
  • 31
    • 0024349096 scopus 로고
    • Removal of tropomyosin overlap modifies cooperative binding of myosin S-1 to reconstituted thin filaments of rabbit striated muscle
    • Pan, B. S., A. M. Gordon, and Z. Luo. 1989. Removal of tropomyosin overlap modifies cooperative binding of myosin S-1 to reconstituted thin filaments of rabbit striated muscle. J. Biol. Chem. 264:8495-8498.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8495-8498
    • Pan, B.S.1    Gordon, A.M.2    Luo, Z.3
  • 32
    • 0032755956 scopus 로고    scopus 로고
    • Stiffness-distortion sarcomere model for muscle simulation
    • Razumova, M. V., A. E. Bukatina, and K. B. Campbell. 1999. Stiffness-distortion sarcomere model for muscle simulation. J. Appl. Physiol. 87:1861-1876.
    • (1999) J. Appl. Physiol. , vol.87 , pp. 1861-1876
    • Razumova, M.V.1    Bukatina, A.E.2    Campbell, K.B.3
  • 33
    • 0031920485 scopus 로고    scopus 로고
    • Calcium regulation of tension redevelopment kinetics with 2-deoxy-ATP or low [ATP] in rabbit skeletal muscle
    • Regnier, M., D. A. Martyn, and P. B. Chase. 1998. Calcium regulation of tension redevelopment kinetics with 2-deoxy-ATP or low [ATP] in rabbit skeletal muscle. Biophys. J. 74:2005-2015.
    • (1998) Biophys. J. , vol.74 , pp. 2005-2015
    • Regnier, M.1    Martyn, D.A.2    Chase, P.B.3
  • 34
    • 0032992510 scopus 로고    scopus 로고
    • Comparison of putative cooperative mechanisms in cardiac muscle: Length dependence and dynamic responses
    • Heart Circ. Physiol. 45
    • Rice, J. R., R. L. Winslow, and W. C. Hunter. 1999. Comparison of putative cooperative mechanisms in cardiac muscle: length dependence and dynamic responses. Am. J. Physiol. 276 (Heart Circ. Physiol. 45): H1734-H1754.
    • (1999) Am. J. Physiol. , vol.276
    • Rice, J.R.1    Winslow, R.L.2    Hunter, W.C.3
  • 36
    • 0032494188 scopus 로고    scopus 로고
    • Troponin and tropomyosin: Proteins that switch on and tune in the activity of cardiac myofilaments
    • Solaro, R. J., and H. M. Rarick. 1998. Troponin and tropomyosin: proteins that switch on and tune in the activity of cardiac myofilaments. Circ. Res. 83:471-480.
    • (1998) Circ. Res. , vol.83 , pp. 471-480
    • Solaro, R.J.1    Rarick, H.M.2
  • 37
    • 0031777885 scopus 로고    scopus 로고
    • A new look at thin filament regulation in vertebrate skeletal muscle
    • Squire, J. M., and E. P. Morris. 1998. A new look at thin filament regulation in vertebrate skeletal muscle. FASEB J. 12:761-771.
    • (1998) FASEB J. , vol.12 , pp. 761-771
    • Squire, J.M.1    Morris, E.P.2
  • 38
    • 0029840598 scopus 로고    scopus 로고
    • Calcium alone does not fully activate the thin filament for S1 binding in rigor myofibrils
    • Swartz, D. R., M. L. Greaser, and R. L. Moss. 1996. Calcium alone does not fully activate the thin filament for S1 binding in rigor myofibrils. Biophys. J. 71:1891-1904.
    • (1996) Biophys. J. , vol.71 , pp. 1891-1904
    • Swartz, D.R.1    Greaser, M.L.2    Moss, R.L.3
  • 39
    • 0026774946 scopus 로고
    • Influence of a strong-binding myosin analogue on calcium-sensitive mechanical properties of skinned skeletal muscle fibers
    • Swartz, D. R., and R. L. Moss. 1992. Influence of a strong-binding myosin analogue on calcium-sensitive mechanical properties of skinned skeletal muscle fibers. J. Biol. Chem. 267:20497-20506.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20497-20506
    • Swartz, D.R.1    Moss, R.L.2
  • 40
    • 0033033719 scopus 로고    scopus 로고
    • Cross bridge-dependent activation of contraction in cardiac myofibrils at low pH
    • Heart Circ. Physiol. 45
    • Swartz, D. R., D. Zhang, and K. W. Yancey. 1999. Cross bridge-dependent activation of contraction in cardiac myofibrils at low pH. Am. J. Physiol. 276(Heart Circ. Physiol. 45):H1460-H1467.
    • (1999) Am. J. Physiol. , vol.276
    • Swartz, D.R.1    Zhang, D.2    Yancey, K.W.3
  • 41
    • 0030004861 scopus 로고    scopus 로고
    • Thin filament mediated regulation of cardiac contraction
    • Tobacman, L. S. 1996. Thin filament mediated regulation of cardiac contraction. Annu. Rev. Physiol. 58:447-481.
    • (1996) Annu. Rev. Physiol. , vol.58 , pp. 447-481
    • Tobacman, L.S.1
  • 42
    • 0030246902 scopus 로고    scopus 로고
    • Ca-dependence of isometric force kinetics in single skinned ventricular cardiomyocytes from rats
    • Vannier, C., H. Chevassus, and G. Vassort. 1996. Ca-dependence of isometric force kinetics in single skinned ventricular cardiomyocytes from rats. Cardiovasc. Res. 32:580-586.
    • (1996) Cardiovasc. Res. , vol.32 , pp. 580-586
    • Vannier, C.1    Chevassus, H.2    Vassort, G.3
  • 43
    • 0028919177 scopus 로고
    • Rate of tension development in cardiac muscle varies with level of activator calcium
    • Wolff, M. R., K. S. McDonald, and R. L. Moss. 1995. Rate of tension development in cardiac muscle varies with level of activator calcium. Circ. Res. 76:154-160.
    • (1995) Circ. Res. , vol.76 , pp. 154-160
    • Wolff, M.R.1    McDonald, K.S.2    Moss, R.L.3
  • 44
    • 0028290739 scopus 로고
    • A cellular automaton model for the regulatory behavior of muscle thin filaments
    • Zou, G., and G. N. Phillips. 1994. A cellular automaton model for the regulatory behavior of muscle thin filaments. Biophys. J. 67:11-28.
    • (1994) Biophys. J. , vol.67 , pp. 11-28
    • Zou, G.1    Phillips, G.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.