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Volumn 92, Issue 10, 2007, Pages 3379-3396

Protein geometry and placement in the cardiac dyad influence macroscopic properties of calcium-induced calcium release

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM CHANNEL L TYPE; CALCIUM ION; RYANODINE RECEPTOR;

EID: 34247887625     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.089425     Document Type: Article
Times cited : (49)

References (61)
  • 3
    • 0030033865 scopus 로고    scopus 로고
    • Calcium concentration and movement in the diadic cleft space of the cardiac ventricular cell
    • Langer, G. A., and A. Peskoff. 1996. Calcium concentration and movement in the diadic cleft space of the cardiac ventricular cell. Biophys. J. 70:1169-1182.
    • (1996) Biophys. J , vol.70 , pp. 1169-1182
    • Langer, G.A.1    Peskoff, A.2
  • 4
    • 0031005989 scopus 로고    scopus 로고
    • Numerical simulation of local calcium movements during L-type calcium channel gating in the cardiac diad
    • Soeller, C., and M. B. Cannell. 1997. Numerical simulation of local calcium movements during L-type calcium channel gating in the cardiac diad. Biophys. J. 73:97-111.
    • (1997) Biophys. J , vol.73 , pp. 97-111
    • Soeller, C.1    Cannell, M.B.2
  • 5
    • 4143118798 scopus 로고    scopus 로고
    • Signaling in small subcellular volumes. I. Stochastic and diffusion effects on individual pathways
    • Bhalla, U. S. 2004. Signaling in small subcellular volumes. I. Stochastic and diffusion effects on individual pathways. Biophys. J. 87:733-744.
    • (2004) Biophys. J , vol.87 , pp. 733-744
    • Bhalla, U.S.1
  • 7
    • 2242464846 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of the recombinant type 2 ryanodine receptor and localization of its divergent region 1
    • Liu, Z., J. Zhang, P. Li, S. R. W. Chen, and T. Wagenknecht. 2002. Three-dimensional reconstruction of the recombinant type 2 ryanodine receptor and localization of its divergent region 1. J. Biol. Chem. 277:46712-46719.
    • (2002) J. Biol. Chem , vol.277 , pp. 46712-46719
    • Liu, Z.1    Zhang, J.2    Li, P.3    Chen, S.R.W.4    Wagenknecht, T.5
  • 8
    • 0142155040 scopus 로고    scopus 로고
    • What we don't know about the structure of ryanodine receptor calcium release channels
    • Dulhunty, A. F., and P. Pouliquin. 2003. What we don't know about the structure of ryanodine receptor calcium release channels. Clin. Exp. Pharmacol. Physiol. 30:713-723.
    • (2003) Clin. Exp. Pharmacol. Physiol , vol.30 , pp. 713-723
    • Dulhunty, A.F.1    Pouliquin, P.2
  • 9
    • 22444444618 scopus 로고    scopus 로고
    • Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EM
    • Samso, M., T. Wagenknecht, and P. D. Allen. 2005. Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EM. Nat. Struct. Mol. Biol. 12:539-544.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 539-544
    • Samso, M.1    Wagenknecht, T.2    Allen, P.D.3
  • 11
    • 0026589932 scopus 로고
    • Cryo-EM of the native structure of the calcium release channel/ryanodine receptor from sarcoplasmic reticulum
    • Radermacher, M., T. Wagenknecht, R. Grassucci, J. Frank, M. Inui, C. Chadwick, and S. Fleischer. 1992. Cryo-EM of the native structure of the calcium release channel/ryanodine receptor from sarcoplasmic reticulum. Biophys. J. 61:936-940.
    • (1992) Biophys. J , vol.61 , pp. 936-940
    • Radermacher, M.1    Wagenknecht, T.2    Grassucci, R.3    Frank, J.4    Inui, M.5    Chadwick, C.6    Fleischer, S.7
  • 12
    • 1342282941 scopus 로고    scopus 로고
    • The three-dimensional structure of the cardiac L-type voltage-gated calcium channel: Comparison with the skeletal muscle form reveals a common architectural motif
    • Wang, M.C., R. F. Collins, R. C. Ford, N.S. Berrow, A. C. Dolphin, and A. Kitmitto. 2004. The three-dimensional structure of the cardiac L-type voltage-gated calcium channel: comparison with the skeletal muscle form reveals a common architectural motif. J. Biol. Chem. 279:7159-7168.
    • (2004) J. Biol. Chem , vol.279 , pp. 7159-7168
    • Wang, M.C.1    Collins, R.F.2    Ford, R.C.3    Berrow, N.S.4    Dolphin, A.C.5    Kitmitto, A.6
  • 14
    • 0034257929 scopus 로고    scopus 로고
    • 2+-bound calmodulin: An analysis of disorder and implications for functionally relevant plasticity
    • 2+-bound calmodulin: an analysis of disorder and implications for functionally relevant plasticity. J. Mol. Biol. 301:1237-1256.
    • (2000) J. Mol. Biol , vol.301 , pp. 1237-1256
    • Wilson, M.A.1    Brunger, A.T.2
  • 15
    • 0034737734 scopus 로고    scopus 로고
    • Three-dimensional structure of ryanodine receptor isoform three in two conformational states as visualized by cryo-electron microscopy
    • Sharma, M. R., L. H. Jeyakumar, S. Fleischer, and T. Wagenknecht. 2000. Three-dimensional structure of ryanodine receptor isoform three in two conformational states as visualized by cryo-electron microscopy. J. Biol. Chem. 275:9485-9491.
    • (2000) J. Biol. Chem , vol.275 , pp. 9485-9491
    • Sharma, M.R.1    Jeyakumar, L.H.2    Fleischer, S.3    Wagenknecht, T.4
  • 16
    • 0031464972 scopus 로고    scopus 로고
    • Locations of calmodulin and FK506-binding protein on the three-dimensional architecture of the skeletal muscle ryanodine receptor
    • Wagenknecht, T., M. Radermacher, R. Grassucci, J. Berkowitz, H.-B. Xin, and S. Fleischer. 1997. Locations of calmodulin and FK506-binding protein on the three-dimensional architecture of the skeletal muscle ryanodine receptor. J. Biol. Chem. 272:32463-32471.
    • (1997) J. Biol. Chem , vol.272 , pp. 32463-32471
    • Wagenknecht, T.1    Radermacher, M.2    Grassucci, R.3    Berkowitz, J.4    Xin, H.-B.5    Fleischer, S.6
  • 17
    • 0027231287 scopus 로고
    • Ratio of ryanodine to dihydropyridine receptors in cardiac and skeletal muscle and implications for E-C coupling
    • Bers, D. M., and V. M. Stiffel. 1993. Ratio of ryanodine to dihydropyridine receptors in cardiac and skeletal muscle and implications for E-C coupling. Am. J. Physiol. 264:C1587-C1593.
    • (1993) Am. J. Physiol , vol.264
    • Bers, D.M.1    Stiffel, V.M.2
  • 21
    • 0026613088 scopus 로고
    • 2+ release channel (ryanodine receptor) of rabbit skeletal muscle sarcoplasmic reticulum
    • 2+ release channel (ryanodine receptor) of rabbit skeletal muscle sarcoplasmic reticulum. J. Biol. Chem. 267:23318-23326.
    • (1992) J. Biol. Chem , vol.267 , pp. 23318-23326
    • Chen, S.R.1    Zhang, L.2    MacLennan, D.H.3
  • 23
    • 0034049351 scopus 로고    scopus 로고
    • Amino acid residues 4425-4621 localized on the three-dimensional structure of the skeletal muscle ryanodine receptor
    • Benacquista, B. L., M. R. Sharma, M. Samso, F. Zorzato, S. Treves, and T. Wagenknecht. 2000. Amino acid residues 4425-4621 localized on the three-dimensional structure of the skeletal muscle ryanodine receptor. Biophys. J. 78:1349-1358.
    • (2000) Biophys. J , vol.78 , pp. 1349-1358
    • Benacquista, B.L.1    Sharma, M.R.2    Samso, M.3    Zorzato, F.4    Treves, S.5    Wagenknecht, T.6
  • 24
    • 11144220469 scopus 로고    scopus 로고
    • Mutational analysis of putative calcium binding motifs within the skeletal ryanodine receptor isoform, RyR1
    • Fessenden, J. D., W. Feng, I. N. Pessah, and P. D. Allen. 2004. Mutational analysis of putative calcium binding motifs within the skeletal ryanodine receptor isoform, RyR1. J. Biol. Chem. 279:53028-53035.
    • (2004) J. Biol. Chem , vol.279 , pp. 53028-53035
    • Fessenden, J.D.1    Feng, W.2    Pessah, I.N.3    Allen, P.D.4
  • 25
    • 0034943174 scopus 로고    scopus 로고
    • 2+ release channel (ryanodine receptor)
    • 2+ release channel (ryanodine receptor). J. Gen. Physiol. 118:33-44.
    • (2001) J. Gen. Physiol , vol.118 , pp. 33-44
    • Li, P.1    Chen, S.R.2
  • 26
    • 0034981326 scopus 로고    scopus 로고
    • 2+-release channel tunnel: Structures and mechanisms involved in ion translocation in ryanodine receptor channels
    • 2+-release channel tunnel: structures and mechanisms involved in ion translocation in ryanodine receptor channels. Q. Rev. Biophys. 34:61-104.
    • (2001) Q. Rev. Biophys , vol.34 , pp. 61-104
    • Williams, A.J.1    West, D.J.2    Sitsapesan, R.3
  • 27
    • 0011126683 scopus 로고    scopus 로고
    • 2+ inactivation sites are located in the COOH-terminal quarter of recombinant rabbit skeletal muscle Ca21 release channels (ryanodine receptors)
    • 2+ inactivation sites are located in the COOH-terminal quarter of recombinant rabbit skeletal muscle Ca21 release channels (ryanodine receptors). J. Biol. Chem. 274:26120-26126.
    • (1999) J. Biol. Chem , vol.274 , pp. 26120-26126
    • Du, G.G.1    MacLennan, D.H.2
  • 28
    • 33646130504 scopus 로고    scopus 로고
    • Cryo-electron microscopy and 3D reconstructions of ryanodine receptors and their interactions with E-C coupling proteins
    • Sharma, M. R., and T. Wagenknecht. 2004. Cryo-electron microscopy and 3D reconstructions of ryanodine receptors and their interactions with E-C coupling proteins. Basic Appl. Myol. 14:299-306.
    • (2004) Basic Appl. Myol , vol.14 , pp. 299-306
    • Sharma, M.R.1    Wagenknecht, T.2
  • 29
    • 17444376389 scopus 로고    scopus 로고
    • 2+ sensitivity of RyR2 mutations reveals distinct mechanisms of channel dysfunction in sudden cardiac death
    • 2+ sensitivity of RyR2 mutations reveals distinct mechanisms of channel dysfunction in sudden cardiac death. Biochem. Biophys. Res. Commun. 331:231-238.
    • (2005) Biochem. Biophys. Res. Commun , vol.331 , pp. 231-238
    • Thomas, N.L.1    Lai, F.A.2    George, C.H.3
  • 35
    • 0034743560 scopus 로고    scopus 로고
    • 2+ channels: Is a unifying mechanism at hand?
    • 2+ channels: is a unifying mechanism at hand? J. Mol. Cell. Cardiol. 33:639-650.
    • (2001) J. Mol. Cell. Cardiol , vol.33 , pp. 639-650
    • Anderson, M.E.1
  • 36
    • 0031594597 scopus 로고    scopus 로고
    • 2+ dynamics: The roles of ryanodine receptor adaptation and sarcoplasmic reticulum load
    • 2+ dynamics: the roles of ryanodine receptor adaptation and sarcoplasmic reticulum load. Biophys. J. 74:1149-1168.
    • (1998) Biophys. J , vol.74 , pp. 1149-1168
    • Jafri, S.1    Rice, J.J.2    Winslow, R.L.3
  • 37
    • 0032876356 scopus 로고    scopus 로고
    • 2+ release in the functional unit of the cardiac diadic space
    • 2+ release in the functional unit of the cardiac diadic space. Biophys. J. 77:1871-1884.
    • (1999) Biophys. J , vol.77 , pp. 1871-1884
    • Rice, J.J.1    Jafri, M.S.2    Winslow, R.L.3
  • 38
    • 0032949168 scopus 로고    scopus 로고
    • Local control models of cardiac excitation- contraction coupling. A possible role for allosteric interactions between ryanodine receptors
    • Stern, M. D., L. S. Song, H. Cheng, J. S. Sham, H. T. Yang, K. R. Boheler, and E. Rios. 1999. Local control models of cardiac excitation- contraction coupling. A possible role for allosteric interactions between ryanodine receptors. J. Gen. Physiol. 113:469-489.
    • (1999) J. Gen. Physiol , vol.113 , pp. 469-489
    • Stern, M.D.1    Song, L.S.2    Cheng, H.3    Sham, J.S.4    Yang, H.T.5    Boheler, K.R.6    Rios, E.7
  • 40
    • 0345634227 scopus 로고    scopus 로고
    • Rapid activation of the cardiac ryanodine receptor by submillisecond calcium stimuli
    • Zahradnikova, A., I. Zahradnik, I. Gyorke, and S. Gyorke. 1999. Rapid activation of the cardiac ryanodine receptor by submillisecond calcium stimuli. J. Gen. Physiol. 114:787-798.
    • (1999) J. Gen. Physiol , vol.114 , pp. 787-798
    • Zahradnikova, A.1    Zahradnik, I.2    Gyorke, I.3    Gyorke, S.4
  • 42
    • 0031836773 scopus 로고    scopus 로고
    • A simple numerical model of calcium spark formation and detection in cardiac myocytes
    • Smith, G. D., J. E. Keizer, M. D. Stern, W. J. Lederer, and H. Cheng. 1998. A simple numerical model of calcium spark formation and detection in cardiac myocytes. Biophys. J. 75:15-32.
    • (1998) Biophys. J , vol.75 , pp. 15-32
    • Smith, G.D.1    Keizer, J.E.2    Stern, M.D.3    Lederer, W.J.4    Cheng, H.5
  • 44
    • 0037459899 scopus 로고    scopus 로고
    • A robust numerical algorithm for studying biomolecular transport processes
    • Wang, H., C. S. Peskin, and T. C. Elston. 2003. A robust numerical algorithm for studying biomolecular transport processes. J. Theor. Biol. 221:491-511.
    • (2003) J. Theor. Biol , vol.221 , pp. 491-511
    • Wang, H.1    Peskin, C.S.2    Elston, T.C.3
  • 45
    • 0002296942 scopus 로고
    • A new algorithm for Monte Carlo simulation of Ising spin systems
    • Bortz, A. B., M. H. Kalos, and J. L. Lebowitz. 1975. A new algorithm for Monte Carlo simulation of Ising spin systems. J. Comput. Phys. 17:10-18.
    • (1975) J. Comput. Phys , vol.17 , pp. 10-18
    • Bortz, A.B.1    Kalos, M.H.2    Lebowitz, J.L.3
  • 46
    • 24144453060 scopus 로고    scopus 로고
    • From continuum Fokker-Planck models to discrete kinetic models
    • Xing, J., H. Wang, and G. Oster. 2005. From continuum Fokker-Planck models to discrete kinetic models. Biophys. J. 89:1551-1563.
    • (2005) Biophys. J , vol.89 , pp. 1551-1563
    • Xing, J.1    Wang, H.2    Oster, G.3
  • 47
    • 21244502885 scopus 로고    scopus 로고
    • Dynamics of myosin-V processivity
    • Lan, G., and S. X. Sun. 2005. Dynamics of myosin-V processivity. Biophys. J. 88:999-1008.
    • (2005) Biophys. J , vol.88 , pp. 999-1008
    • Lan, G.1    Sun, S.X.2
  • 48
    • 0031599142 scopus 로고    scopus 로고
    • Mersenne twister: A 623-dimensionally equidistributed uniform pseudo-random number generator
    • Matsumoto, M., and T. Nishimura. 1998. Mersenne twister: a 623-dimensionally equidistributed uniform pseudo-random number generator. ACM Trans. Model. Comput. Simul. 8:3-30.
    • (1998) ACM Trans. Model. Comput. Simul , vol.8 , pp. 3-30
    • Matsumoto, M.1    Nishimura, T.2
  • 51
    • 0027979619 scopus 로고
    • Local control of excitation-contraction coupling in rat heart cells
    • Wier, W. G., T. M. Egan, J. R. Lopez-Lopez, and C. W. Balke. 1994. Local control of excitation-contraction coupling in rat heart cells. J. Physiol. 474:463-471.
    • (1994) J. Physiol , vol.474 , pp. 463-471
    • Wier, W.G.1    Egan, T.M.2    Lopez-Lopez, J.R.3    Balke, C.W.4
  • 52
    • 0034031592 scopus 로고    scopus 로고
    • Reverse mode of the sarcoplasmic reticulum calcium pump and load-dependent cytosolic calcium decline in voltage-clamped cardiac ventricular myocytes
    • Shannon, T. R., K. S. Ginsburg, and D. M. Bers. 2000. Reverse mode of the sarcoplasmic reticulum calcium pump and load-dependent cytosolic calcium decline in voltage-clamped cardiac ventricular myocytes. Biophys. J. 78:322-333.
    • (2000) Biophys. J , vol.78 , pp. 322-333
    • Shannon, T.R.1    Ginsburg, K.S.2    Bers, D.M.3
  • 53
    • 0027426069 scopus 로고
    • Calcium sparks: Elementary events underlying excitation-contraction coupling in heart muscle
    • Cheng, H., W. J. Lederer, and M. B. Cannell. 1993. Calcium sparks: elementary events underlying excitation-contraction coupling in heart muscle. Science. 262:740-744.
    • (1993) Science , vol.262 , pp. 740-744
    • Cheng, H.1    Lederer, W.J.2    Cannell, M.B.3
  • 57
    • 0026733599 scopus 로고
    • Theory of excitation-contraction coupling in cardiac muscle
    • Stern, M. D. 1992. Theory of excitation-contraction coupling in cardiac muscle. Biophys. J. 63:497-517.
    • (1992) Biophys. J , vol.63 , pp. 497-517
    • Stern, M.D.1
  • 58
    • 0032589749 scopus 로고    scopus 로고
    • 2+ current through cardiac ryanodine receptor channels under quasi-physiological ionic conditions
    • 2+ current through cardiac ryanodine receptor channels under quasi-physiological ionic conditions. J. Gen. Physiol. 113:177-186.
    • (1999) J. Gen. Physiol , vol.113 , pp. 177-186
    • Mejia-Alvarez, R.1    Kettlun, C.2    Rios, E.3    Stern, M.4    Fill, M.5
  • 60
    • 33645992160 scopus 로고    scopus 로고
    • A 3D Monte Carlo analysis of the role of dyadic space geometry in spark generation
    • Koh, X., B.Srinivasan, H. S. Ching, and A. Levchenko. 2006. A 3D Monte Carlo analysis of the role of dyadic space geometry in spark generation. Biophys. J. 90:1999-2014.
    • (2006) Biophys. J , vol.90 , pp. 1999-2014
    • Koh, X.1    Srinivasan, B.2    Ching, H.S.3    Levchenko, A.4
  • 61
    • 14044265753 scopus 로고    scopus 로고
    • Stochastic amplification and signaling in enzymatic futile cycles through noise-induced bistability with oscillations
    • Samoilov, M., S. Plyasunov, and A. P. Arkin. 2005. Stochastic amplification and signaling in enzymatic futile cycles through noise-induced bistability with oscillations. Proc. Natl. Acad. Sci. USA. 102:2310-2315.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 2310-2315
    • Samoilov, M.1    Plyasunov, S.2    Arkin, A.P.3


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