메뉴 건너뛰기




Volumn 87, Issue 3, 2004, Pages 1784-1794

Cardiac length dependence of force and force redevelopment kinetics with altered cross-bridge cycling

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CALCIUM ION; DEOXYADENOSINE TRIPHOSPHATE;

EID: 4444343856     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.103.039131     Document Type: Article
Times cited : (67)

References (45)
  • 1
    • 85030827774 scopus 로고    scopus 로고
    • At similar activation levels the rate of force redevelopment is faster at short sarcomere lengths and increased myfilament lattice spacing in skinned cardiac muscle
    • Adhikari, B., M. Regnier, and D. A. Martyn. 2004. At similar activation levels the rate of force redevelopment is faster at short sarcomere lengths and increased myfilament lattice spacing in skinned cardiac muscle. Biophys. J. 86:207a.
    • (2004) Biophys. J. , vol.86
    • Adhikari, B.1    Regnier, M.2    Martyn, D.A.3
  • 2
    • 0346057933 scopus 로고    scopus 로고
    • Interplay of troponin- and myosin-based pathways of calcium activation in skeletal and cardiac muscle: The use of W7 as an inhibitor of thin filament activation
    • Adhikari, B. B., and K. Wang. 2004. Interplay of troponin- and myosin-based pathways of calcium activation in skeletal and cardiac muscle: the use of W7 as an inhibitor of thin filament activation. Biophys. J. 86: 359-370.
    • (2004) Biophys. J. , vol.86 , pp. 359-370
    • Adhikari, B.B.1    Wang, K.2
  • 3
    • 0024007477 scopus 로고
    • 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: Implications for regulation of muscle contraction
    • 2+ 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
  • 4
    • 2042451727 scopus 로고
    • Rate of force generation in muscle: Correlation with actomyosin ATPase activity in solution
    • Brenner, B., and E. Eisenberg. 1986. Rate of force generation in muscle: correlation with actomyosin ATPase activity in solution. Proc. Natl. Acad. Sci. USA. 83:3542-3546.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3542-3546
    • Brenner, B.1    Eisenberg, E.2
  • 5
    • 0022407356 scopus 로고
    • Equatorial x-ray diffraction from single skinned rabbit psoas fibers at various degrees of activation. Changes in intensities and lattice spacing
    • Brenner, B., and L. C. Yu. 1985. Equatorial x-ray diffraction from single skinned rabbit psoas fibers at various degrees of activation. Changes in intensities and lattice spacing. Biophys. J. 48:829-834.
    • (1985) Biophys. J. , vol.48 , pp. 829-834
    • Brenner, B.1    Yu, L.C.2
  • 6
    • 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
  • 7
    • 0035947754 scopus 로고    scopus 로고
    • Titin-based modulation of calcium sensitivity of active tension in mouse skinned cardiac myocytes
    • Cazorla, O., Y. Wu, T. C. Irving, and H. Granzier. 2001. Titin-based modulation of calcium sensitivity of active tension in mouse skinned cardiac myocytes. Circ. Res. 88:1028-1035.
    • (2001) Circ. Res. , vol.88 , pp. 1028-1035
    • Cazorla, O.1    Wu, Y.2    Irving, T.C.3    Granzier, H.4
  • 8
    • 0028203450 scopus 로고
    • Activation dependence and kinetics of force and stiffness inhibition by aluminiofluoride, a slowly dissociating analogue of inorganic phosphate, in chemically skinned fibres from rabbit psoas muscle
    • Chase, P. B., D. A. Martyn, and J. D. Hannon. 1994a. Activation dependence and kinetics of force and stiffness inhibition by aluminiofluoride, a slowly dissociating analogue of inorganic phosphate, in chemically skinned fibres 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
  • 10
    • 0016656759 scopus 로고
    • Mechanical deactivation induced by active shortening in isolated muscle fibres of the frog
    • Edman, K. A. 1975. Mechanical deactivation induced by active shortening in isolated muscle fibres of the frog. J. Physiol. 246:255-275.
    • (1975) J. Physiol. , vol.246 , pp. 255-275
    • Edman, K.A.1
  • 11
    • 0019769492 scopus 로고
    • Myoplasmic free calcium concentration reached during the twitch of an intact isolated cardiac cell and during calcium-induced release of calcium from the sarcoplasmic reticulum of a skinned cardiac cell from the adult rat or rabbit ventricle
    • Fabiato, A. 1981. Myoplasmic free calcium concentration reached during the twitch of an intact isolated cardiac cell and during calcium-induced release of calcium from the sarcoplasmic reticulum of a skinned cardiac cell from the adult rat or rabbit ventricle. J. Gen. Physiol. 78:457-497.
    • (1981) J. Gen. Physiol. , vol.78 , pp. 457-497
    • Fabiato, A.1
  • 12
    • 0032555957 scopus 로고    scopus 로고
    • 2+ activation of rat ventricular myocytes
    • 2+ 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
  • 13
    • 1242326460 scopus 로고    scopus 로고
    • The Frank-Starling relationship: Cellular and molecular mechanisms
    • R. J. Solaro and R. L. Moss, editors. Dordrecht, Kluwer, The Netherlands
    • Fuchs, F. 2002. The Frank-Starling Relationship: Cellular and Molecular Mechanisms. In Advances in Muscle Research. R. J. Solaro and R. L. Moss, editors. Dordrecht, Kluwer, The Netherlands. 379-407.
    • (2002) Advances in Muscle Research , pp. 379-407
    • Fuchs, F.1
  • 15
    • 0032438165 scopus 로고    scopus 로고
    • Regulatory roles of MgADP and calcium in tension development of skinned cardiac muscle
    • Fukuda, N., H. Fujita, T. Fujita, and S. Ishiwata. 1998. Regulatory roles of MgADP and calcium in tension development of skinned cardiac muscle. J. Muscle Res. Cell Motil. 19:909-921.
    • (1998) J. Muscle Res. Cell Motil. , vol.19 , pp. 909-921
    • Fukuda, N.1    Fujita, H.2    Fujita, T.3    Ishiwata, S.4
  • 16
    • 0034614288 scopus 로고    scopus 로고
    • Effects of MgADP on length dependence of tension generation in skinned rat cardiac muscle
    • Fukuda, N., H. Kajiwara, S. Ishiwata, and S. Kurihara. 2000. Effects of MgADP on length dependence of tension generation in skinned rat cardiac muscle. Circ. Res. 86:E1-E6.
    • (2000) Circ. Res. , vol.86
    • Fukuda, N.1    Kajiwara, H.2    Ishiwata, S.3    Kurihara, S.4
  • 17
    • 0035797846 scopus 로고    scopus 로고
    • Length dependence of tension generation in rat skinned cardiac muscle: Role of titin in the Frank-Starling mechanism of the heart
    • Fukuda, N., D. Sasaki, S. Ishiwata, and S. Kurihara. 2001. Length dependence of tension generation in rat skinned cardiac muscle: role of titin in the Frank-Starling mechanism of the heart. Circ. Res. 104:1639-1645.
    • (2001) Circ. Res. , vol.104 , pp. 1639-1645
    • Fukuda, N.1    Sasaki, D.2    Ishiwata, S.3    Kurihara, S.4
  • 18
    • 0344896768 scopus 로고    scopus 로고
    • Titin isoform variance and length dependence of activation in skinned bovine cardiac muscle
    • 553.1
    • Fukuda, N., Y. Wu, T. C. Irving, and H. Granzier. 2003. Titin isoform variance and length dependence of activation in skinned bovine cardiac muscle. J. Physiol. 553.1:147-154.
    • (2003) J. Physiol. , pp. 147-154
    • Fukuda, N.1    Wu, Y.2    Irving, T.C.3    Granzier, H.4
  • 19
    • 0032883413 scopus 로고    scopus 로고
    • Structural mechanism of muscle contraction
    • Geeves, M. A., and K. C. Holmes. 1999. Structural mechanism of muscle contraction. Anna. Rev. Biochem. 68:687-728.
    • (1999) Anna. Rev. Biochem. , vol.68 , pp. 687-728
    • Geeves, M.A.1    Holmes, K.C.2
  • 20
    • 0022558278 scopus 로고
    • The stiffness of frog skinned muscle fibres at altered lateral filament spacing
    • Goldman, Y. E., and R. M. Simmons. 1986. The stiffness of frog skinned muscle fibres at altered lateral filament spacing. J. Physiol. 378:175-194.
    • (1986) J. Physiol. , vol.378 , pp. 175-194
    • Goldman, Y.E.1    Simmons, R.M.2
  • 21
    • 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
  • 22
    • 0030687665 scopus 로고    scopus 로고
    • Models of calcium activation account for differences between skeletal and cardiac force redevelopment kinetics
    • Hancock, W. O., L. L. Huntsman, and A. M. Gordon. 1997. Models of calcium activation account for differences between skeletal and cardiac force redevelopment kinetics. J. Muscle Res. Cell Motil. 18:671-681.
    • (1997) J. Muscle Res. Cell Motil. , vol.18 , pp. 671-681
    • Hancock, W.O.1    Huntsman, L.L.2    Gordon, A.M.3
  • 24
    • 0036304749 scopus 로고    scopus 로고
    • Energetics of the Frank-Starling effect in rabbit myocardium: Economy and efficiency depend on muscle length
    • Holmes, J. W., M. Hunlich, and G. Hasenfuss. 2002. Energetics of the Frank-Starling effect in rabbit myocardium: economy and efficiency depend on muscle length. Am. J. Physiol. Heart Circ. Physiol. 283: H324-H330.
    • (2002) Am. J. Physiol. Heart Circ. Physiol. , vol.283
    • Holmes, J.W.1    Hunlich, M.2    Hasenfuss, G.3
  • 26
    • 0028325201 scopus 로고
    • Differential effects of length on maximum force production and myofibrillar ATPase activity in rat skinned cardiac muscle
    • Kentish, J. C., and G. J. Stienen. 1994. Differential effects of length on maximum force production and myofibrillar ATPase activity in rat skinned cardiac muscle. J. Physiol. 475:175-184.
    • (1994) J. Physiol. , vol.475 , pp. 175-184
    • Kentish, J.C.1    Stienen, G.J.2
  • 27
    • 0036454919 scopus 로고    scopus 로고
    • Frank-Starling law of the heart and the cellular mechanisms of length-dependent activation
    • Konhilas, J. P., T. C. Irving, and P. P. de Tombe. 2002a. Frank-Starling law of the heart and the cellular mechanisms of length-dependent activation. Pflugers Arch. 445:305-310.
    • (2002) Pflugers Arch. , vol.445 , pp. 305-310
    • Konhilas, J.P.1    Irving, T.C.2    De Tombe, P.P.3
  • 28
    • 0037059456 scopus 로고    scopus 로고
    • Myofilament calcium sensitivity in skinned rat cardiac trabeculae: Role of interfilament spacing
    • Konhilas, J. P., T. C. Irving, and P. P. de Tombe. 2002b. Myofilament calcium sensitivity in skinned rat cardiac trabeculae: role of interfilament spacing. Circ. Res. 90:59-65.
    • (2002) Circ. Res. , vol.90 , pp. 59-65
    • Konhilas, J.P.1    Irving, T.C.2    De Tombe, P.P.3
  • 29
    • 4243258379 scopus 로고    scopus 로고
    • Effect of cross-bridge (CB) kinetics on sarcomere length (SL) dependence of force development in cardiac muscle
    • Kreutziger, K. L., A. J. Rivera, D. A. Martyn. and M. Regnier. 2003. Effect of cross-bridge (CB) kinetics on sarcomere length (SL) dependence of force development in cardiac muscle. Biophys. J. 84:449a.
    • (2003) Biophys. J. , vol.84
    • Kreutziger, K.L.1    Rivera, A.J.2    Martyn, D.A.3    Regnier, M.4
  • 30
    • 0032540229 scopus 로고    scopus 로고
    • The muscle thin filament as a classical cooperative/allosleric regulatory system
    • Lehrer, S. S., and M. A. Geeves. 1998. The muscle thin filament as a classical cooperative/allosleric regulatory system. J. Mol. Biol. 277: 1081-1089.
    • (1998) J. Mol. Biol. , vol.277 , pp. 1081-1089
    • Lehrer, S.S.1    Geeves, M.A.2
  • 31
    • 1142298529 scopus 로고    scopus 로고
    • Response of equatorial x-ray reflections and stiffness to altered sarcomere length and myofilament lattice spacing in relaxed skinned cardiac muscle
    • Martyn, D. A., B. B. Adhikari, M. Regnier, J. Gu, S. Xu, and L. C. Yu. 2004. Response of equatorial x-ray reflections and stiffness to altered sarcomere length and myofilament lattice spacing in relaxed skinned cardiac muscle. Biophys. J. 86:1002-1011.
    • (2004) Biophys. J. , vol.86 , pp. 1002-1011
    • Martyn, D.A.1    Adhikari, B.B.2    Regnier, M.3    Gu, J.4    Xu, S.5    Yu, L.C.6
  • 32
    • 0035006418 scopus 로고    scopus 로고
    • Influence of length on force and activation-dependent changes in troponin c structure in skinned cardiac and fast skeletal muscle
    • Martyn, D. A., and A. M. Gordon. 2001. Influence of length on force and activation-dependent changes in troponin c structure in skinned cardiac and fast skeletal muscle. Biophys. J. 80:2798-2808.
    • (2001) Biophys. J. , vol.80 , pp. 2798-2808
    • Martyn, D.A.1    Gordon, A.M.2
  • 33
    • 0034746350 scopus 로고    scopus 로고
    • 2+- and cross-bridge-dependent changes in N- and C-terminal structure of troponin C in rat cardiac muscle
    • 2+- and cross-bridge-dependent changes in N- and C-terminal structure of troponin C in rat cardiac muscle. Biophys. J. 80:360-370.
    • (2001) Biophys. J. , vol.80 , pp. 360-370
    • Martyn, D.A.1    Regnier, M.2    Xu, D.3    Gordon, A.M.4
  • 34
    • 0029029477 scopus 로고
    • 2+ sensitivity of tension at short sarcomere length
    • 2+ sensitivity of tension at short sarcomere length. Circ. Res. 77:199-205.
    • (1995) Circ. Res. , vol.77 , pp. 199-205
    • McDonald, K.S.1    Moss, R.L.2
  • 35
    • 0030764505 scopus 로고    scopus 로고
    • Sarcomere length dependence of the rate of tension redevelopment and submaximal tension in rat and rabbit skinned skeletal muscle fibres
    • McDonald, K. S., M. R. Wolff, and R. L. Moss. 1997. Sarcomere length dependence of the rate of tension redevelopment and submaximal tension in rat and rabbit skinned skeletal muscle fibres. J. Physiol. 501:607-621.
    • (1997) J. Physiol. , vol.501 , pp. 607-621
    • McDonald, K.S.1    Wolff, M.R.2    Moss, R.L.3
  • 36
    • 0028944618 scopus 로고
    • Myosin binding-induced cooperative activation of the thin filament in cardiac myocytes and skeletal muscle fibers
    • Metzger, J. M. 1995. Myosin binding-induced cooperative activation of the thin filament in cardiac myocytes and skeletal muscle fibers. Biophys. J. 68:1430-1442.
    • (1995) Biophys. J. , vol.68 , pp. 1430-1442
    • Metzger, J.M.1
  • 37
    • 0037059562 scopus 로고    scopus 로고
    • Frank-Starling relationship: Long on importance, short on mechanism
    • Moss, R. L., and D. P. Fitzsimons. 2002. Frank-Starling relationship: long on importance, short on mechanism. Circ. Res. 90:11-13.
    • (2002) Circ. Res. , vol.90 , pp. 11-13
    • Moss, R.L.1    Fitzsimons, D.P.2
  • 38
    • 0031834714 scopus 로고    scopus 로고
    • The effect of ATP analogs on posthydrolytic and force development steps in skinned skeletal muscle fibers
    • Regnier, M., and E. Homsher. 1998. The effect of ATP analogs on posthydrolytic and force development steps in skinned skeletal muscle fibers. Biophys. J. 74:3059-3071.
    • (1998) Biophys. J. , vol.74 , pp. 3059-3071
    • Regnier, M.1    Homsher, E.2
  • 39
    • 4444334713 scopus 로고    scopus 로고
    • Cross-bridge versus thin filament contributions to the level and rate of force development in cardiac muscle
    • Regnier, M., H. Martin, R. J. Barsotti, A. J. Rivera, D. A. Martyn, and E. Clemmens. 2004. Cross-bridge versus thin filament contributions to the level and rate of force development in cardiac muscle. Biophys. J. 87:1815-1824.
    • (2004) Biophys. J. , vol.87 , pp. 1815-1824
    • Regnier, M.1    Martin, H.2    Barsotti, R.J.3    Rivera, A.J.4    Martyn, D.A.5    Clemmens, E.6
  • 40
    • 0029657778 scopus 로고    scopus 로고
    • 2+ regulation of tension redevelopment rate in skinned skeletal muscle
    • 2+ regulation of tension redevelopment rate in skinned skeletal muscle. Biophys. J. 71:2786-2794.
    • (1996) Biophys. J. , vol.71 , pp. 2786-2794
    • Regnier, M.1    Martyn, D.A.2    Chase, P.B.3
  • 41
    • 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
  • 43
    • 0034705580 scopus 로고    scopus 로고
    • 2-Deoxy-ATP enhances contractility of rat cardiac muscle
    • Regnier, M., A. J. Rivera, Y. Chen, and P. B. Chase. 2000. 2-deoxy-ATP enhances contractility of rat cardiac muscle. Circ. Res. 86:1211-1217.
    • (2000) Circ. Res. , vol.86 , pp. 1211-1217
    • Regnier, M.1    Rivera, A.J.2    Chen, Y.3    Chase, P.B.4
  • 44
    • 0027974349 scopus 로고
    • 2+-troponin C affinity in cardiac and slow skeletal muscle
    • 2+-troponin C affinity in cardiac and slow skeletal muscle. Am. J. Physiol. 266:C1077-C1082.
    • (1994) Am. J. Physiol. , vol.266
    • Wang, Y.P.1    Fuchs, F.2
  • 45
    • 33751264946 scopus 로고    scopus 로고
    • The Frank-Starling mechanism is not mediated by changes in rate of cross-bridge detachment
    • Wannenburg, T., P. M. Janssen, D. Fan, and P. P. de Tombe. 1997. The Frank-Starling mechanism is not mediated by changes in rate of cross-bridge detachment. Am. J. Physiol. 273:H2428-H2435.
    • (1997) Am. J. Physiol. , vol.273
    • Wannenburg, T.1    Janssen, P.M.2    Fan, D.3    De Tombe, P.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.