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Volumn 98, Issue 2, 2010, Pages 267-276

A metabolite-sensitive, thermodynamically constrained model of cardiac cross-bridge cycling: Implications for force development during ischemia

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EID: 77049096729     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.10.011     Document Type: Article
Times cited : (34)

References (50)
  • 1
    • 0023280509 scopus 로고
    • Myocardial contractile function during ischemia and hypoxia
    • Allen, D. G., and C. H. Orchard. 1987. Myocardial contractile function during ischemia and hypoxia. Circ. Res. 60:153-168.
    • (1987) Circ. Res. , vol.60 , pp. 153-168
    • Allen, D.G.1    Orchard, C.H.2
  • 2
    • 2442509903 scopus 로고    scopus 로고
    • Development of models of active ion transport for whole-cell modeling: Cardiac sodium-potassium pump as a case study
    • Smith, N. P., and E. J. Crampin. 2004. Development of models of active ion transport for whole-cell modeling: cardiac sodium-potassium pump as a case study. Prog. Biophys. Mol. Biol. 85:387-405.
    • (2004) Prog. Biophys. Mol. Biol. , vol.85 , pp. 387-405
    • Smith, N.P.1    Crampin, E.J.2
  • 3
    • 0027216259 scopus 로고
    • Crossbridge scheme and the kinetic constants of elementary steps deduced from chemically skinned papillary and trabecular muscles of the ferret
    • Kawai, M., Y. Saeki, and Y. Zhao. 1993. Crossbridge scheme and the kinetic constants of elementary steps deduced from chemically skinned papillary and trabecular muscles of the ferret. Circ. Res. 73:35-50.
    • (1993) Circ. Res. , vol.73 , pp. 35-50
    • Kawai, M.1    Saeki, Y.2    Zhao, Y.3
  • 6
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley, A. F. 1957. Muscle structure and theories of contraction. Prog. Biophys. Mol. Biol. 7:255-318.
    • (1957) Prog. Biophys. Mol. Biol. , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 7
    • 0024307990 scopus 로고
    • A model of crossbridge action: The effects of ATP, ADP and Pi
    • Pate, E., and R. Cooke. 1989. A model of crossbridge action: the effects of ATP, ADP and Pi. J. Muscle Res. Cell Motil. 10:181-196.
    • (1989) J. Muscle Res. Cell Motil. , vol.10 , pp. 181-196
    • Pate, E.1    Cooke, R.2
  • 8
    • 49549104611 scopus 로고    scopus 로고
    • Approximate model of cooperative activation and crossbridge cycling in cardiac muscle using ordinary differential equations
    • Rice, J. J., F. Wang,., P. P. de Tombe. 2008. Approximate model of cooperative activation and crossbridge cycling in cardiac muscle using ordinary differential equations. Biophys. J. 95:2368-2390.
    • (2008) Biophys. J. , vol.95 , pp. 2368-2390
    • Rice, J.J.1    Wang, F.2    De Tombe, P.P.3
  • 9
    • 33646159067 scopus 로고    scopus 로고
    • A dynamic model of excitationcontraction coupling during acidosis in cardiac ventricular myocytes
    • Crampin, E. J., and N. P. Smith. 2006. A dynamic model of excitationcontraction coupling during acidosis in cardiac ventricular myocytes. Biophys. J. 90:3074-3090.
    • (2006) Biophys. J. , vol.90 , pp. 3074-3090
    • Crampin, E.J.1    Smith, N.P.2
  • 12
    • 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
  • 13
    • 0015214368 scopus 로고
    • Mechanism of adenosine triphosphate hydrolysis by actomyosin
    • Lymn, R. W., and E. W. Taylor. 1971. Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry. 10:4617-4624.
    • (1971) Biochemistry , vol.10 , pp. 4617-4624
    • Lymn, R.W.1    Taylor, E.W.2
  • 14
    • 0023161165 scopus 로고
    • Kinetics of the actomyosin ATPase in muscle fibers
    • Goldman, Y. E. 1987. Kinetics of the actomyosin ATPase in muscle fibers. Annu. Rev. Physiol. 49:637-654.
    • (1987) Annu. Rev. Physiol. , vol.49 , pp. 637-654
    • Goldman, Y.E.1
  • 15
    • 0030791973 scopus 로고    scopus 로고
    • Actomyosin interaction in striated muscle
    • Cooke, R. 1997. Actomyosin interaction in striated muscle. Physiol. Rev. 77:671-697.
    • (1997) Physiol. Rev. , vol.77 , pp. 671-697
    • Cooke, R.1
  • 17
    • 0022405269 scopus 로고
    • The effects of ADP and phosphate on the contraction of muscle fibers
    • Cooke, R., and E. Pate. 1985. The effects of ADP and phosphate on the contraction of muscle fibers. Biophys. J. 48:789-798.
    • (1985) Biophys. J. , vol.48 , pp. 789-798
    • Cooke, R.1    Pate, E.2
  • 18
    • 0035162942 scopus 로고    scopus 로고
    • Effects of MgATP on ATP utilization and force under normal and simulated ischemic conditions in rat cardiac trabeculae
    • Ebus, J. P., Z. Papp,., G. J. Stienen. 2001. Effects of MgATP on ATP utilization and force under normal and simulated ischemic conditions in rat cardiac trabeculae. Pflugers Arch. 443:102-111.
    • (2001) Pflugers Arch. , vol.443 , pp. 102-111
    • Ebus, J.P.1    Papp, Z.2    Stienen, G.J.3
  • 19
    • 0021862562 scopus 로고
    • Phosphate release and force generation in skeletal muscle fibers
    • Hibberd, M. G., J. A. Dantzig,., Y. E. Goldman. 1985. Phosphate release and force generation in skeletal muscle fibers. Science. 228:1317-1319.
    • (1985) Science , vol.228 , pp. 1317-1319
    • Hibberd, M.G.1    Dantzig, J.A.2    Goldman, Y.E.3
  • 20
    • 77049106546 scopus 로고
    • Mechanical transients initiated by photolysis of caged-Pi during active skeletalmuscle contractions
    • Dantzig, J. A., J. W. Lacktis,., Y. E. Goldman. 1987. Mechanical transients initiated by photolysis of caged-Pi during active skeletalmuscle contractions. Biophys. J. 51:A3.
    • (1987) Biophys. J. , vol.51
    • Dantzig, J.A.1    Lacktis, J.W.2    Goldman, Y.E.3
  • 21
    • 0024661091 scopus 로고
    • Changes of intracellular milieu with fatigue or hypoxia depress contraction of skinned rabbit skeletal and cardiac muscle
    • Godt, R. E., and T. M. Nosek. 1989. Changes of intracellular milieu with fatigue or hypoxia depress contraction of skinned rabbit skeletal and cardiac muscle. J. Physiol. 412:155-180.
    • (1989) J. Physiol. , vol.412 , pp. 155-180
    • Godt, R.E.1    Nosek, T.M.2
  • 22
    • 0022560216 scopus 로고
    • The effects of inorganic phosphate and creatine phosphate on force production in skinned muscles from rat ventricle
    • Kentish, J. C. 1986. The effects of inorganic phosphate and creatine phosphate on force production in skinned muscles from rat ventricle. J. Physiol. 370:585-604.
    • (1986) J. Physiol. , vol.370 , pp. 585-604
    • Kentish, J.C.1
  • 23
    • 0017885455 scopus 로고
    • Effects of pH on the myofilaments and the sarcoplasmic reticulum of skinned cells from cardiac and skeletal muscles
    • Fabiato, A., and F. Fabiato. 1978. Effects of pH on the myofilaments and the sarcoplasmic reticulum of skinned cells from cardiac and skeletal muscles. J. Physiol. 276:233-255.
    • (1978) J. Physiol. , vol.276 , pp. 233-255
    • Fabiato, A.1    Fabiato, F.2
  • 24
    • 0025296203 scopus 로고
    • Effects of changes of pH on the contractile function of cardiac muscle
    • Orchard, C. H., and J. C. Kentish. 1990. Effects of changes of pH on the contractile function of cardiac muscle. Am. J. Physiol. 258: C967-C981.
    • (1990) Am. J. Physiol. , vol.258
    • Orchard, C.H.1    Kentish, J.C.2
  • 25
    • 0021141992 scopus 로고
    • Inhibition of the activation and troponin calcium binding of dog cardiac myofibrils by acidic pH
    • Blanchard, E. M., and R. J. Solaro. 1984. Inhibition of the activation and troponin calcium binding of dog cardiac myofibrils by acidic pH. Circ. Res. 55:382-391.
    • (1984) Circ. Res. , vol.55 , pp. 382-391
    • Blanchard, E.M.1    Solaro, R.J.2
  • 27
    • 0016168791 scopus 로고
    • Letter: Crossbridge angle when ADP is bound to myosin
    • Rodger, C. D., and R. T. Tregear. 1974. Letter: Crossbridge angle when ADP is bound to myosin. J. Mol. Biol. 86:495-497.
    • (1974) J. Mol. Biol. , vol.86 , pp. 495-497
    • Rodger, C.D.1    Tregear, R.T.2
  • 28
    • 0023257462 scopus 로고
    • ADP binding to myosin crossbridges and its effect on the cross-bridge detachment rate constants
    • Schoenberg, M., and E. Eisenberg. 1987. ADP binding to myosin crossbridges and its effect on the cross-bridge detachment rate constants. J. Gen. Physiol. 89:905-920.
    • (1987) J. Gen. Physiol. , vol.89 , pp. 905-920
    • Schoenberg, M.1    Eisenberg, E.2
  • 29
    • 4243330361 scopus 로고    scopus 로고
    • Structural changes in rigor (nucleotide- free) cross-bridges induced by the addition of MgADP
    • Xu, S., J. Gu,., L. C. Yu. 1998. Structural changes in rigor (nucleotide- free) cross-bridges induced by the addition of MgADP. Biophys. J. 74:A363.
    • (1998) Biophys. J. , vol.74
    • Xu, S.1    Gu, J.2    Yu, L.C.3
  • 30
    • 0026067741 scopus 로고
    • Cross-bridge kinetics in the presence of MgADP investigated by photolysis of caged ATP in rabbit psoas muscle fibers
    • Dantzig, J. A., M. G. Hibberd,., Y. E. Goldman. 1991. Cross-bridge kinetics in the presence of MgADP investigated by photolysis of caged ATP in rabbit psoas muscle fibers. J. Physiol. 432:639-680.
    • (1991) J. Physiol. , vol.432 , pp. 639-680
    • Dantzig, J.A.1    Hibberd, M.G.2    Goldman, Y.E.3
  • 31
    • 0032999729 scopus 로고    scopus 로고
    • Backward movements of cross-bridges by application of stretch and by binding of MgADP to skeletal muscle fibers in the rigor state as studied by x-ray diffraction
    • Takezawa, Y., D. S. Kim,., K. Wakabayashi. 1999. Backward movements of cross-bridges by application of stretch and by binding of MgADP to skeletal muscle fibers in the rigor state as studied by x-ray diffraction. Biophys. J. 76:1770-1783.
    • (1999) Biophys. J. , vol.76 , pp. 1770-1783
    • Takezawa, Y.1    Kim, D.S.2    Wakabayashi, K.3
  • 32
    • 0037377225 scopus 로고    scopus 로고
    • Effect of an ADP analog on isometric force and ATPase activity of active muscle fibers
    • Karatzaferi, C., K. H. Myburgh,., R. Cooke. 2003. Effect of an ADP analog on isometric force and ATPase activity of active muscle fibers. Am. J. Physiol. Cell Physiol. 284:C816-C825.
    • (2003) Am. J. Physiol. Cell Physiol. , vol.284
    • Karatzaferi, C.1    Myburgh, K.H.2    Cooke, R.3
  • 33
    • 0032438165 scopus 로고    scopus 로고
    • Regulatory roles of MgADP and calcium in tension development of skinned cardiac muscle
    • Fukuda, N., H. Fujita,., 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    Ishiwata, S.3
  • 34
    • 0026009517 scopus 로고
    • Combined inhibitory actions of acidosis and phosphate on maximum force production in rat skinned cardiac muscle
    • Kentish, J. C. 1991. Combined inhibitory actions of acidosis and phosphate on maximum force production in rat skinned cardiac muscle. Pflugers Arch. 419:310-318.
    • (1991) Pflugers Arch. , vol.419 , pp. 310-318
    • Kentish, J.C.1
  • 35
    • 0023915980 scopus 로고
    • Dependence upon highenergy phosphates of the effects of inorganic phosphate on contractile properties in chemically skinned rat cardiac fibers
    • Mekhfi, H., and R. Ventura-Clapier. 1988. Dependence upon highenergy phosphates of the effects of inorganic phosphate on contractile properties in chemically skinned rat cardiac fibers. Pflugers Arch. 411:378-385.
    • (1988) Pflugers Arch. , vol.411 , pp. 378-385
    • Mekhfi, H.1    Ventura-Clapier, R.2
  • 36
    • 0021203107 scopus 로고
    • ADP binds similarly to rigor muscle myofibrils and to actomyosin-subfragment one
    • Johnson, R. E., and P. H. Adams. 1984. ADP binds similarly to rigor muscle myofibrils and to actomyosin-subfragment one. FEBS Lett. 174:11-14.
    • (1984) FEBS Lett. , vol.174 , pp. 11-14
    • Johnson, R.E.1    Adams, P.H.2
  • 37
    • 0018747152 scopus 로고
    • Interaction of ADP with skeletal and cardiac myosin and their active fragments observed by proton release
    • Kardami, E., S. De Bruin, and W. Gratzer. 1979. Interaction of ADP with skeletal and cardiac myosin and their active fragments observed by proton release. Eur. J. Biochem. 97:547-552.
    • (1979) Eur. J. Biochem. , vol.97 , pp. 547-552
    • Kardami, E.1    De Bruin, S.2    Gratzer, W.3
  • 38
    • 0032929224 scopus 로고    scopus 로고
    • Osmotic shock: Modulation of contractile function, pHi, and ischemic damage in perfused guinea pig heart
    • Befroy, D. E., T. Powell,., K. Clarke. 1999. Osmotic shock: modulation of contractile function, pHi, and ischemic damage in perfused guinea pig heart. Am. J. Physiol. 276:H1236-H1244.
    • (1999) Am. J. Physiol. , vol.276
    • Befroy, D.E.1    Powell, T.2    Clarke, K.3
  • 39
    • 0034805469 scopus 로고    scopus 로고
    • Nonlinear myofilament regulatory processes affect frequency-dependent muscle fiber stiffness
    • Campbell, K. B., M. V. Razumova,., B. K. Slinker. 2001. Nonlinear myofilament regulatory processes affect frequency-dependent muscle fiber stiffness. Biophys. J. 81:2278-2296.
    • (2001) Biophys. J. , vol.81 , pp. 2278-2296
    • Campbell, K.B.1    Razumova, M.V.2    Slinker, B.K.3
  • 40
    • 0032755956 scopus 로고    scopus 로고
    • Stiffnessdistortion sarcomere model for muscle simulation
    • Razumova, M. V., A. E. Bukatina, and K. B. Campbell. 1999. Stiffnessdistortion 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
  • 41
    • 0023705863 scopus 로고
    • Effects of acidosis on ventricular muscle from adult and neonatal rats
    • Solaro, R. J., J. A. Lee,., D. G. Allen. 1988. Effects of acidosis on ventricular muscle from adult and neonatal rats. Circ. Res. 63:779-787.
    • (1988) Circ. Res. , vol.63 , pp. 779-787
    • Solaro, R.J.1    Lee, J.A.2    Allen, D.G.3
  • 42
    • 40549085776 scopus 로고    scopus 로고
    • Spatially-compressed cardiac myofilament models generate hysteresis that is not found in real muscle
    • Rice, J. J., Y. Tu,., P. P. De Tombe. 2008. Spatially-compressed cardiac myofilament models generate hysteresis that is not found in real muscle. Pac. Symp. Biocomput. 2008:366-377.
    • (2008) Pac. Symp. Biocomput. , vol.2008 , pp. 366-377
    • Rice, J.J.1    Tu, Y.2    De Tombe, P.P.3
  • 43
    • 0026633883 scopus 로고
    • 2+ Role in spontaneous tension oscillation of skeletal muscle
    • 2+. Role in spontaneous tension oscillation of skeletal muscle. Biophys. J. 61:1087-1098.
    • (1992) Biophys. J. , vol.61 , pp. 1087-1098
    • Shimizu, H.1    Fujita, T.2    Ishiwata, S.3
  • 44
    • 0034614288 scopus 로고    scopus 로고
    • Effects of MgADP on length dependence of tension generation in skinned rat cardiac muscle
    • Fukuda, N., H. Kajiwara,., 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    Kurihara, S.3
  • 45
    • 0029810768 scopus 로고    scopus 로고
    • Spontaneous tension oscillation in skinned bovine cardiac muscle
    • Fukuda, N., H. Fujita,., S. Ishiwata. 1996. Spontaneous tension oscillation in skinned bovine cardiac muscle. Pflugers Arch. 433:1-8.
    • (1996) Pflugers Arch. , vol.433 , pp. 1-8
    • Fukuda, N.1    Fujita, H.2    Ishiwata, S.3
  • 46
    • 67650345313 scopus 로고    scopus 로고
    • The mechanism of spontaneous oscillatory contractions in skeletal muscle
    • Smith, D. A., and D. G. Stephenson. 2009. The mechanism of spontaneous oscillatory contractions in skeletal muscle. Biophys. J. 96:3682-3691.
    • (2009) Biophys. J. , vol.96 , pp. 3682-3691
    • Smith, D.A.1    Stephenson, D.G.2
  • 47
    • 0000280567 scopus 로고
    • Chemical and mechanical changes during stretching of activated frog skeletal-muscle
    • Curtin, N. A., and R. E. Davies. 1973. Chemical and mechanical changes during stretching of activated frog skeletal-muscle. Cold Spring Harb. Symp. Quant. Biol. 37:619-626.
    • (1973) Cold Spring Harb. Symp. Quant. Biol. , vol.37 , pp. 619-626
    • Curtin, N.A.1    Davies, R.E.2
  • 48
    • 0001663646 scopus 로고
    • Adenosine triphosphate: Changes in muscles doing negative work
    • Infante, A. A., D. Klaupiks, and R. E. Davies. 1964. Adenosine triphosphate: changes in muscles doing negative work. Science. 144:1577-1578.
    • (1964) Science. , vol.144 , pp. 1577-1578
    • Infante, A.A.1    Klaupiks, D.2    Davies, R.E.3
  • 49
    • 77049096250 scopus 로고
    • Very low ATP usage with very high tension in activated muscles during a slow stretch
    • Curtin, N. A., D. D. Drobnis,., R. E. Davies. 1969. Very low ATP usage with very high tension in activated muscles during a slow stretch. Fed. Proc. 28:A711.
    • (1969) Fed. Proc. , vol.28
    • Curtin, N.A.1    Drobnis, D.D.2    Davies, R.E.3
  • 50
    • 0038069092 scopus 로고    scopus 로고
    • Energy storage during stretch of active single fibers from frog skeletal muscle
    • Linari, M., R. C. Woledge, and N. A. Curtin. 2003. Energy storage during stretch of active single fibers from frog skeletal muscle. J. Physiol. 548:461-474.
    • (2003) J. Physiol. , vol.548 , pp. 461-474
    • Linari, M.1    Woledge, R.C.2    Curtin, N.A.3


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