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Volumn 271, Issue 6 PART 1, 1996, Pages

Ca2+-force relationship of frog skeletal muscle: A dynamic model for parameter estimation

Author keywords

Excitation contraction coupling; Fluorescence; Indo 1; Mathematical model

Indexed keywords

CALCIUM ION; INDO 1;

EID: 0030460590     PISSN: 00029513     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.1996.271.6.c2062     Document Type: Article
Times cited : (9)

References (32)
  • 2
    • 0027990262 scopus 로고
    • Protein and acidosis alter calcium-binding and fluorescence spectra of the calcium indicator indo-1
    • Baker, A. J.,R. Brandes, J. Schreur, S. A. Camacho, and M. W. Weiner. Protein and acidosis alter calcium-binding and fluorescence spectra of the calcium indicator indo-1. Biophys. J. 67: 1645-1654, 1994.
    • (1994) Biophys. J. , vol.67 , pp. 1645-1654
    • Baker, A.J.1    Brandes, R.2    Schreur, J.3    Camacho, S.A.4    Weiner, M.W.5
  • 3
    • 0028896288 scopus 로고
    • 2+ activation, contraction, and relaxation of frog skeletal muscle
    • 2+ activation, contraction, and relaxation of frog skeletal muscle. Am. J. Physiol. 268 (Cell Physiol. 37): C55-C63, 1995.
    • (1995) Am. J. Physiol. , vol.268
    • Baker, A.J.1    Brandes, R.2    Weiner, M.W.3
  • 6
    • 0023006793 scopus 로고
    • The cross-bridge cycle in muscle. Mechanical, biochemical and structural studies on single skinned rabbit psoas fibers to characterize cross-bridge kinetics in muscle for correlation with actomyosin-ATPase in solution
    • Brenner, B. The cross-bridge cycle in muscle. Mechanical, biochemical and structural studies on single skinned rabbit psoas fibers to characterize cross-bridge kinetics in muscle for correlation with actomyosin-ATPase in solution. Basic Res. Cardiol. 81, Suppl. 1: 1-15, 1986.
    • (1986) Basic Res. Cardiol. , vol.81 , Issue.1 SUPPL. , pp. 1-15
    • Brenner, B.1
  • 7
    • 0024007477 scopus 로고
    • Effect of [Ca] on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: Implications for regulation of muscle contraction
    • Brenner, B. Effect of [Ca] 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.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3265-3269
    • Brenner, B.1
  • 8
    • 0028050276 scopus 로고
    • Explaining load dependence of ventricular contractile properties with a model of excitation-contraction coupling
    • Burkhoff, D. Explaining load dependence of ventricular contractile properties with a model of excitation-contraction coupling. J. Mol. Cell. Cardiol. 26: 959-978, 1994.
    • (1994) J. Mol. Cell. Cardiol. , vol.26 , pp. 959-978
    • Burkhoff, D.1
  • 9
    • 0028180439 scopus 로고
    • Calcium transient decline and myocardial relaxation are slowed during low-flow ischemia in rat hearts
    • Camacho, S. A.,R. Brandes, V. M. Figueredo, and M. W. Weiner. Calcium transient decline and myocardial relaxation are slowed during low-flow ischemia in rat hearts. J. Clin. Invest. 93: 951-957, 1994.
    • (1994) J. Clin. Invest. , vol.93 , pp. 951-957
    • Camacho, S.A.1    Brandes, R.2    Figueredo, V.M.3    Weiner, M.W.4
  • 10
    • 0020425131 scopus 로고
    • Orientation of spin labels attached to cross-bridges in contracting muscle fibres
    • Cooke, R.,M. S. Crowder, and D. D. Thomas. Orientation of spin labels attached to cross-bridges in contracting muscle fibres. Nature Lond. 300: 776-778, 1982.
    • (1982) Nature Lond. , vol.300 , pp. 776-778
    • Cooke, R.1    Crowder, M.S.2    Thomas, D.D.3
  • 11
    • 0024381499 scopus 로고
    • Effects of fatigue and reduced intracellular pH on segment dynamics in isometric relaxation of frog muscle fibres
    • Curtin, N. A.,and A. P. Edman. Effects of fatigue and reduced intracellular pH on segment dynamics in isometric relaxation of frog muscle fibres. J. Physiol. Lond. 413: 159-174, 1989.
    • (1989) J. Physiol. Lond. , vol.413 , pp. 159-174
    • Curtin, N.A.1    Edman, A.P.2
  • 12
    • 0025150667 scopus 로고
    • Myosin heads have a broad orientational distribution during isometric muscle contraction: Time resolved EPR studies using caged ATP
    • Fajer, P. G.,E. A. Fajer, and D. D. Thomas. Myosin heads have a broad orientational distribution during isometric muscle contraction: time resolved EPR studies using caged ATP. Proc. Natl. Acad. Sci. USA 87: 5538-5542, 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5538-5542
    • Fajer, P.G.1    Fajer, E.A.2    Thomas, D.D.3
  • 14
    • 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. Changes of intracellular milieu with fatigue or hypoxia depress contraction of skinned rabbit skeletal and cardiac muscle. J. Physiol. Lond. 412: 155-180, 1989.
    • (1989) J. Physiol. Lond. , vol.412 , pp. 155-180
    • Godt, R.E.1    Nosek, T.M.2
  • 16
    • 0020973460 scopus 로고
    • Cooperative binding to the calcium-specific sites of troponin C in regulated actin and actomyosin
    • Grabarek, Z.,J. Grabarek, P. C. Leavis, and J. Gergely. Cooperative binding to the calcium-specific sites of troponin C in regulated actin and actomyosin. J. Biol. Chem. 258: 14098-14102, 1983.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14098-14102
    • Grabarek, Z.1    Grabarek, J.2    Leavis, P.C.3    Gergely, J.4
  • 18
    • 0023645610 scopus 로고
    • Effect of rigor and cycling cross-bridges on the structure of troponin C and on the calcium affinity of the calcium-specific regulatory sites in skinned rabbit psoas fibers
    • Guth, K.,and J. D. Potter. Effect of rigor and cycling cross-bridges on the structure of troponin C and on the calcium affinity of the calcium-specific regulatory sites in skinned rabbit psoas fibers. J. Biol. Chem. 262: 13627-13635, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13627-13635
    • Guth, K.1    Potter, J.D.2
  • 19
    • 0027337513 scopus 로고
    • 2+ and segment length dependence of isometric force kinetics in intact ferret cardiac muscle
    • 2+ and segment length dependence of isometric force kinetics in intact ferret cardiac muscle. Circ Res. 73: 603-611, 1993.
    • (1993) Circ Res. , vol.73 , pp. 603-611
    • Hancock, W.O.1    Martyn, D.A.2    Huntsman, L.L.3
  • 20
    • 0023488538 scopus 로고
    • Evidence for a force-dependent component of calcium binding to cardiac troponin C
    • Hofmann, P.A.,and F. Fuchs. Evidence for a force-dependent component of calcium binding to cardiac troponin C. Am. J. Physiol. 253 (Cell Physiol. 22): C541-C546, 1987.
    • (1987) Am. J. Physiol. , vol.253
    • Hofmann, P.A.1    Fuchs, F.2
  • 21
    • 0020653743 scopus 로고
    • Time-resolved X-ray diffraction studies on vertebrate striated muscle
    • Huxley, H. E.,and A. R. Faruqi. Time-resolved X-ray diffraction studies on vertebrate striated muscle. Annu. Rev. Biophys. Bioeng. 12: 381-417, 1983.
    • (1983) Annu. Rev. Biophys. Bioeng. , vol.12 , pp. 381-417
    • Huxley, H.E.1    Faruqi, A.R.2
  • 23
    • 0028132934 scopus 로고
    • Mechanical regulation of cardiac muscle by coupling calcium kinetics with cross-bridge cycling: A dynamic model
    • Landesberg, A.,and S. Sideman. Mechanical regulation of cardiac muscle by coupling calcium kinetics with cross-bridge cycling: a dynamic model. Am. J. Physiol. 267 (Heart Circ. Physiol. 36): H779-H795, 1994.
    • (1994) Am. J. Physiol. , vol.267
    • Landesberg, A.1    Sideman, S.2
  • 24
    • 0022929836 scopus 로고
    • Maximal Ca-activated force elicited by tetanization of ferret papillary muscle and whole heart: Mechanism and characteristics of steady contractile activation in intact myocardium
    • Marban, E.,H. Kusuoka, D. T. Yue, M. L. Weisfeldt, and W. G. Wier. Maximal Ca-activated force elicited by tetanization of ferret papillary muscle and whole heart: mechanism and characteristics of steady contractile activation in intact myocardium. Circ. Res. 59: 262-269, 1986.
    • (1986) Circ. Res. , vol.59 , pp. 262-269
    • Marban, E.1    Kusuoka, H.2    Yue, D.T.3    Weisfeldt, M.L.4    Wier, W.G.5
  • 25
    • 0025271805 scopus 로고
    • Calcium-sensitive cross-bridge transitions in mammalian fast and slow skeletal muscle fibers
    • Metzger, J. M.,and R. L. Moss. Calcium-sensitive cross-bridge transitions in mammalian fast and slow skeletal muscle fibers. Science Wash. DC 247: 247-259, 1990.
    • (1990) Science Wash. DC , vol.247 , pp. 247-259
    • Metzger, J.M.1    Moss, R.L.2
  • 26
    • 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.
    • (1992) Circ. Res. , vol.70 , pp. 865-884
    • Moss, R.L.1
  • 27
    • 0025909936 scopus 로고
    • 2+ bound to troponin C during relaxation in isolated cardiac muscle
    • Heart Circ. Physiol. 29
    • 2+ bound to troponin C during relaxation in isolated cardiac muscle. Am. J. Physiol. 260 (Heart Circ. Physiol. 29): H1013-H1024, 1991.
    • (1991) Am. J. Physiol. , vol.260
    • Peterson, J.N.1    Hunter, W.C.2    Berman, M.R.3
  • 28
    • 0025061076 scopus 로고
    • Alteration of cross-bridge kinetics by myosin light chain phosphorylation in rabbit skeletal muscle: Implications for regulation of actin-myosin interaction
    • Sweeney, H. L.,and J. T. Stull. Alteration of cross-bridge kinetics by myosin light chain phosphorylation in rabbit skeletal muscle: implications for regulation of actin-myosin interaction. Proc. Natl. Acad. Sci. USA 87: 414-418, 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 414-418
    • Sweeney, H.L.1    Stull, J.T.2
  • 29
    • 0026767223 scopus 로고
    • Endothelin reverses the effects of acidosis on the intracellular calcium transient and contractility in ferret myocardium
    • Wang, J.,and J. P. Morgan. Endothelin reverses the effects of acidosis on the intracellular calcium transient and contractility in ferret myocardium. Circ. Res. 71: 631-639, 1992.
    • (1992) Circ. Res. , vol.71 , pp. 631-639
    • Wang, J.1    Morgan, J.P.2
  • 30
    • 0023747148 scopus 로고
    • Cooperative turning on of myosin subfragment 1 adenosinetriphospha-tase activity by the troponin-tropomyosin-actin complex
    • Williams, D. L.,Jr.,L. E. Greene, and E. Eisenberg. Cooperative turning on of myosin subfragment 1 adenosinetriphospha-tase activity by the troponin-tropomyosin-actin complex. Biochemistry 27: 6987-6993, 1988.
    • (1988) Biochemistry , vol.27 , pp. 6987-6993
    • Williams, D.L.1    Jr2    Greene, L.E.3    Eisenberg, E.4
  • 31
    • 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. Rate of tension development in cardiac muscle varies with level of activator calcium. Circ. Res. 76: 154-160, 1995.
    • (1995) Circ. Res. , vol.76 , pp. 154-160
    • Wolff, M.R.1    McDonald, K.S.2    Moss, R.L.3
  • 32
    • 0023318184 scopus 로고
    • 2+] related to rate offeree development in twitch contraction of heart
    • 2+] related to rate offeree development in twitch contraction of heart. Am. J. Physiol. 252 (Heart Circ. Physiol. 21): H760-H770, 1987.
    • (1987) Am. J. Physiol. , vol.252
    • Yue, D.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.