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Volumn 1778, Issue 11, 2008, Pages 2469-2479

Ryanoids and imperatoxin affect the modulation of cardiac ryanodine receptors by dihydropyridine receptor Peptide A

Author keywords

Ball peptide; Cardiac muscle; Excitation contraction coupling; Ryanodol; Sarcoplasmic reticulum

Indexed keywords

1,4 DIHYDROPYRIDINE RECEPTOR; CALCIUM CHANNEL L TYPE; IMPERATOXIN; PEPTIDE A; PEPTIDE DERIVATIVE; RYANODINE; RYANODINE RECEPTOR; RYANODOL; SHAKER POTASSIUM CHANNEL; SODIUM CHANNEL; UNCLASSIFIED DRUG;

EID: 54049130761     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2008.07.024     Document Type: Article
Times cited : (8)

References (59)
  • 1
    • 0034093987 scopus 로고    scopus 로고
    • Excitation-contraction coupling in skeletal muscle: comparisons with cardiac muscle
    • Lamb G.D. Excitation-contraction coupling in skeletal muscle: comparisons with cardiac muscle. Clin. Exp. Pharmacol. Physiol. 27 (2000) 216-224
    • (2000) Clin. Exp. Pharmacol. Physiol. , vol.27 , pp. 216-224
    • Lamb, G.D.1
  • 3
    • 0036788917 scopus 로고    scopus 로고
    • Ryanodine receptor calcium release channels
    • Fill M., and Copello J.A. Ryanodine receptor calcium release channels. Physiol. Rev. 82 (2002) 893-922
    • (2002) Physiol. Rev. , vol.82 , pp. 893-922
    • Fill, M.1    Copello, J.A.2
  • 5
    • 0023903046 scopus 로고
    • Purification and reconstitution of the calcium release channel from skeletal muscle
    • Lai F.A., Erickson H.P., Rousseau E., Liu Q.Y., and Meissner G. Purification and reconstitution of the calcium release channel from skeletal muscle. Nature 331 (1988) 315-319
    • (1988) Nature , vol.331 , pp. 315-319
    • Lai, F.A.1    Erickson, H.P.2    Rousseau, E.3    Liu, Q.Y.4    Meissner, G.5
  • 7
    • 2442549767 scopus 로고    scopus 로고
    • Molecular regulation of cardiac ryanodine receptor ion channel
    • Meissner G. Molecular regulation of cardiac ryanodine receptor ion channel. Cell Calcium 35 (2004) 621-628
    • (2004) Cell Calcium , vol.35 , pp. 621-628
    • Meissner, G.1
  • 8
    • 2442602416 scopus 로고    scopus 로고
    • Putting out the fire: what terminates calcium-induced calcium release in cardiac muscle?
    • Stern M.D., and Cheng H. Putting out the fire: what terminates calcium-induced calcium release in cardiac muscle?. Cell Calcium 35 (2004) 591-601
    • (2004) Cell Calcium , vol.35 , pp. 591-601
    • Stern, M.D.1    Cheng, H.2
  • 9
    • 26044458246 scopus 로고    scopus 로고
    • Functional implications of RyR-dHPR relationships in skeletal and cardiac muscles
    • Franzini-Armstrong C. Functional implications of RyR-dHPR relationships in skeletal and cardiac muscles. Biol. Res. 37 (2004) 507-512
    • (2004) Biol. Res. , vol.37 , pp. 507-512
    • Franzini-Armstrong, C.1
  • 10
    • 0027231287 scopus 로고
    • The ratio of ryanodine: dihydropyridine receptors in cardiac and skeletal muscle and implications for E-C coupling
    • Bers D.M., and Stiffel V.M. The ratio of ryanodine: dihydropyridine receptors in cardiac and skeletal muscle and implications for E-C coupling. Am. J. Physiol. 264 (1993) C1587-C1593
    • (1993) Am. J. Physiol. , vol.264
    • Bers, D.M.1    Stiffel, V.M.2
  • 13
    • 0035890102 scopus 로고    scopus 로고
    • 2+ sparks in ferret ventricular myocytes
    • 2+ sparks in ferret ventricular myocytes. J. Physiol. 537 (2001) 17-26
    • (2001) J. Physiol. , vol.537 , pp. 17-26
    • Li, Y.1    Bers, D.M.2
  • 15
    • 0028352089 scopus 로고
    • Activation of the skeletal muscle calcium release channel by a cytoplasmic loop of the dihydropyridine receptor
    • Lu X., Xu L., and Meissner G. Activation of the skeletal muscle calcium release channel by a cytoplasmic loop of the dihydropyridine receptor. J. Biol. Chem. 269 (1994) 6511-6516
    • (1994) J. Biol. Chem. , vol.269 , pp. 6511-6516
    • Lu, X.1    Xu, L.2    Meissner, G.3
  • 16
    • 0029083935 scopus 로고
    • Identification of calcium release-triggering and blocking regions of the II-III loop of the skeletal muscle dihydropyridine receptor
    • el-Hayek R., Antoniu B., Wang J., Hamilton S.L., and Ikemoto N. Identification of calcium release-triggering and blocking regions of the II-III loop of the skeletal muscle dihydropyridine receptor. J. Biol. Chem. 270 (1995) 22116-22118
    • (1995) J. Biol. Chem. , vol.270 , pp. 22116-22118
    • el-Hayek, R.1    Antoniu, B.2    Wang, J.3    Hamilton, S.L.4    Ikemoto, N.5
  • 17
    • 0039374471 scopus 로고    scopus 로고
    • Activation of ryanodine receptors by imperatoxin A and a peptide segment of the II-III loop of the dihydropyridine receptor
    • Gurrola G.B., Arevalo C., Sreekumar R., Lokuta A.J., Walker J.W., and Valdivia H.H. Activation of ryanodine receptors by imperatoxin A and a peptide segment of the II-III loop of the dihydropyridine receptor. J. Biol. Chem. 274 (1999) 7879-7886
    • (1999) J. Biol. Chem. , vol.274 , pp. 7879-7886
    • Gurrola, G.B.1    Arevalo, C.2    Sreekumar, R.3    Lokuta, A.J.4    Walker, J.W.5    Valdivia, H.H.6
  • 18
    • 0035016222 scopus 로고    scopus 로고
    • Structural determinants for activation or inhibition of ryanodine receptors by basic residues in the dihydropyridine receptor II-III loop
    • Casarotto M.G., Green D., Pace S.M., Curtis S.M., and Dulhunty A.F. Structural determinants for activation or inhibition of ryanodine receptors by basic residues in the dihydropyridine receptor II-III loop. Biophys. J. 80 (2001) 2715-2726
    • (2001) Biophys. J. , vol.80 , pp. 2715-2726
    • Casarotto, M.G.1    Green, D.2    Pace, S.M.3    Curtis, S.M.4    Dulhunty, A.F.5
  • 19
    • 0037059333 scopus 로고    scopus 로고
    • 2+-dependent dual functions of peptide C. The peptide corresponding to the Glu724-Pro760 region (the so-called determinant of excitation-contraction coupling) of the dihydropyridine receptor alpha 1 subunit II-III loop
    • 2+-dependent dual functions of peptide C. The peptide corresponding to the Glu724-Pro760 region (the so-called determinant of excitation-contraction coupling) of the dihydropyridine receptor alpha 1 subunit II-III loop. J. Biol. Chem. 277 (2002) 993-1001
    • (2002) J. Biol. Chem. , vol.277 , pp. 993-1001
    • Yamamoto, T.1    Rodriguez, J.2    Ikemoto, N.3
  • 20
    • 0037662824 scopus 로고    scopus 로고
    • The random-coil 'C' fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors
    • Haarmann C.S., Green D., Casarotto M.G., Laver D.R., and Dulhunty A.F. The random-coil 'C' fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors. Biochem. J. 372 (2003) 305-316
    • (2003) Biochem. J. , vol.372 , pp. 305-316
    • Haarmann, C.S.1    Green, D.2    Casarotto, M.G.3    Laver, D.R.4    Dulhunty, A.F.5
  • 21
    • 1642456657 scopus 로고    scopus 로고
    • Removal of clustered positive charge from dihydropyridine receptor II-III loop peptide augments activation of ryanodine receptors
    • Bannister M.L., Williams A.J., and Sitsapesan R. Removal of clustered positive charge from dihydropyridine receptor II-III loop peptide augments activation of ryanodine receptors. Biochem. Biophys. Res. Commun. 314 (2004) 667-674
    • (2004) Biochem. Biophys. Res. Commun. , vol.314 , pp. 667-674
    • Bannister, M.L.1    Williams, A.J.2    Sitsapesan, R.3
  • 22
    • 13444278746 scopus 로고    scopus 로고
    • The recombinant dihydropyridine receptor II-III loop and partly structured "C" region peptides modify cardiac ryanodine receptor activity
    • Dulhunty A.F., Karunasekara Y., Curtis S.M., Harvey P.J., Board P.G., and Casarotto M.G. The recombinant dihydropyridine receptor II-III loop and partly structured "C" region peptides modify cardiac ryanodine receptor activity. Biochem. J. 385 (2005) 803-813
    • (2005) Biochem. J. , vol.385 , pp. 803-813
    • Dulhunty, A.F.1    Karunasekara, Y.2    Curtis, S.M.3    Harvey, P.J.4    Board, P.G.5    Casarotto, M.G.6
  • 23
    • 14244256206 scopus 로고    scopus 로고
    • Maurocalcine and domain A of the II-III loop of the dihydropyridine receptor Cav 1.1 subunit share common binding sites on the skeletal ryanodine receptor
    • Altafaj X., Cheng W., Esteve E., Urbani J., Grunwald D., Sabatier J.M., Coronado R., De Waard M., and Ronjat M. Maurocalcine and domain A of the II-III loop of the dihydropyridine receptor Cav 1.1 subunit share common binding sites on the skeletal ryanodine receptor. J. Biol. Chem. 280 (2005) 4013-4016
    • (2005) J. Biol. Chem. , vol.280 , pp. 4013-4016
    • Altafaj, X.1    Cheng, W.2    Esteve, E.3    Urbani, J.4    Grunwald, D.5    Sabatier, J.M.6    Coronado, R.7    De Waard, M.8    Ronjat, M.9
  • 25
    • 0032975217 scopus 로고    scopus 로고
    • Activation and inhibition of skeletal RyR channels by a part of the skeletal DHPR II-III loop: effects of DHPR Ser687 and FKBP12
    • Dulhunty A.F., Laver D.R., Gallant E.M., Casarotto M.G., Pace S.M., and Curtis S. Activation and inhibition of skeletal RyR channels by a part of the skeletal DHPR II-III loop: effects of DHPR Ser687 and FKBP12. Biophys. J. 77 (1999) 189-203
    • (1999) Biophys. J. , vol.77 , pp. 189-203
    • Dulhunty, A.F.1    Laver, D.R.2    Gallant, E.M.3    Casarotto, M.G.4    Pace, S.M.5    Curtis, S.6
  • 26
    • 0038182563 scopus 로고    scopus 로고
    • Maurocalcine and Peptide A stabilize distinct subconductance states of ryanodine receptor type 1, revealing a proportional gating mechanism
    • Chen L., Esteve E., Sabatier J.M., Ronjat M., De Waard M., Allen P.D., and Pessah I.N. Maurocalcine and Peptide A stabilize distinct subconductance states of ryanodine receptor type 1, revealing a proportional gating mechanism. J. Biol. Chem. 278 (2003) 16095-16106
    • (2003) J. Biol. Chem. , vol.278 , pp. 16095-16106
    • Chen, L.1    Esteve, E.2    Sabatier, J.M.3    Ronjat, M.4    De Waard, M.5    Allen, P.D.6    Pessah, I.N.7
  • 28
    • 1642564510 scopus 로고    scopus 로고
    • Multiple actions of imperatoxin A on ryanodine receptors: interactions with the II-III loop "A" fragment
    • Dulhunty A.F., Curtis S.M., Watson S., Cengia L., and Casarotto M.G. Multiple actions of imperatoxin A on ryanodine receptors: interactions with the II-III loop "A" fragment. J. Biol. Chem. 279 (2004) 11853-11862
    • (2004) J. Biol. Chem. , vol.279 , pp. 11853-11862
    • Dulhunty, A.F.1    Curtis, S.M.2    Watson, S.3    Cengia, L.4    Casarotto, M.G.5
  • 30
    • 1842415474 scopus 로고    scopus 로고
    • Adaptation of single cardiac ryanodine receptor channels
    • Velez P., Gyorke S., Escobar A.L., Vergara J., and Fill M. Adaptation of single cardiac ryanodine receptor channels. Biophys. J. 72 (1997) 691-697
    • (1997) Biophys. J. , vol.72 , pp. 691-697
    • Velez, P.1    Gyorke, S.2    Escobar, A.L.3    Vergara, J.4    Fill, M.5
  • 31
    • 0034981326 scopus 로고    scopus 로고
    • Light at the end of the Ca(2+)-release channel tunnel: structures and mechanisms involved in ion translocation in ryanodine receptor channels
    • Williams A.J., West D.J., and Sitsapesan R. Light at the end of the Ca(2+)-release channel tunnel: structures and mechanisms involved in ion translocation in ryanodine receptor channels. Q. Rev. Biophys. 34 (2001) 61-104
    • (2001) Q. Rev. Biophys. , vol.34 , pp. 61-104
    • Williams, A.J.1    West, D.J.2    Sitsapesan, R.3
  • 32
    • 0032103030 scopus 로고    scopus 로고
    • Evidence for negative charge in the conduction pathway of the cardiac ryanodine receptor channel provided by the interaction of K+ channel N-type inactivation peptides
    • Mead F.C., Sullivan D., and Williams A.J. Evidence for negative charge in the conduction pathway of the cardiac ryanodine receptor channel provided by the interaction of K+ channel N-type inactivation peptides. J. Membr. Biol. 163 (1998) 225-234
    • (1998) J. Membr. Biol. , vol.163 , pp. 225-234
    • Mead, F.C.1    Sullivan, D.2    Williams, A.J.3
  • 34
    • 54049147882 scopus 로고    scopus 로고
    • Modulation of ryanodine receptors (RyRs) channels by dihydropyridine receptor (DHPR) peptide A (PepA)
    • Porta M., Nani A., Ramos-Franco J., Fill M., Ikemoto N., and Copello J. Modulation of ryanodine receptors (RyRs) channels by dihydropyridine receptor (DHPR) peptide A (PepA). Biophys. J. 84a (2003) 2078-Pos
    • (2003) Biophys. J. , vol.84 a
    • Porta, M.1    Nani, A.2    Ramos-Franco, J.3    Fill, M.4    Ikemoto, N.5    Copello, J.6
  • 35
    • 54049091274 scopus 로고    scopus 로고
    • Voltage dependent modulation of ryanodine receptors (RyRs) by peptide probes
    • Diaz-Sylvester P.L., Porta M., Escobar A.L., and Copello J.A. Voltage dependent modulation of ryanodine receptors (RyRs) by peptide probes. Biophys. J. 88a (2007) 408-Pos
    • (2007) Biophys. J. , vol.88 a
    • Diaz-Sylvester, P.L.1    Porta, M.2    Escobar, A.L.3    Copello, J.A.4
  • 37
    • 0021137066 scopus 로고
    • Preparation and morphology of sarcoplasmic reticulum terminal cisternae from rabbit skeletal muscle
    • Saito A., Seiler S., Chu A., and Fleischer S. Preparation and morphology of sarcoplasmic reticulum terminal cisternae from rabbit skeletal muscle. J. Cell. Biol. 99 (1984) 875-885
    • (1984) J. Cell. Biol. , vol.99 , pp. 875-885
    • Saito, A.1    Seiler, S.2    Chu, A.3    Fleischer, S.4
  • 39
    • 0025237716 scopus 로고
    • Mechanisms of caffeine activation of single calcium-release channels of sheep cardiac sarcoplasmic reticulum
    • Sitsapesan R., and Williams A.J. Mechanisms of caffeine activation of single calcium-release channels of sheep cardiac sarcoplasmic reticulum. J. Physiol. 423 (1990) 425-439
    • (1990) J. Physiol. , vol.423 , pp. 425-439
    • Sitsapesan, R.1    Williams, A.J.2
  • 40
    • 0015879604 scopus 로고
    • Ionic blockage of sodium channels in nerve
    • Woodhull A.M. Ionic blockage of sodium channels in nerve. J. Gen. Physiol. 61 (1973) 687-708
    • (1973) J. Gen. Physiol. , vol.61 , pp. 687-708
    • Woodhull, A.M.1
  • 41
    • 0036212694 scopus 로고    scopus 로고
    • Block of the ryanodine receptor channel by neomycin is relieved at high holding potentials
    • Mead F., and Williams A.J. Block of the ryanodine receptor channel by neomycin is relieved at high holding potentials. Biophys. J. 82 (2002) 1953-1963
    • (2002) Biophys. J. , vol.82 , pp. 1953-1963
    • Mead, F.1    Williams, A.J.2
  • 42
    • 33748997977 scopus 로고    scopus 로고
    • State-dependent block of BK channels by synthesized shaker ball peptides
    • Li W., and Aldrich R.W. State-dependent block of BK channels by synthesized shaker ball peptides. J. Gen. Physiol. 128 (2006) 423-441
    • (2006) J. Gen. Physiol. , vol.128 , pp. 423-441
    • Li, W.1    Aldrich, R.W.2
  • 44
    • 0025301950 scopus 로고
    • Ryanodine as a probe for the functional state of the skeletal muscle sarcoplasmic reticulum calcium release channel
    • Chu A., Díaz-Muñoz M., Hawkes M.J., Brush K., and Hamilton S.L. Ryanodine as a probe for the functional state of the skeletal muscle sarcoplasmic reticulum calcium release channel. Mol. Pharmacol. 37 (1990) 735-741
    • (1990) Mol. Pharmacol. , vol.37 , pp. 735-741
    • Chu, A.1    Díaz-Muñoz, M.2    Hawkes, M.J.3    Brush, K.4    Hamilton, S.L.5
  • 47
    • 0033947144 scopus 로고    scopus 로고
    • The interaction of a neutral ryanoid with the ryanodine receptor channel provides insights into the mechanisms by which ryanoid binding is modulated by voltage
    • Tanna B., Welch W., Ruest L., Sutko J.L., and Williams A.J. The interaction of a neutral ryanoid with the ryanodine receptor channel provides insights into the mechanisms by which ryanoid binding is modulated by voltage. J. Gen. Physiol. 116 (2000) 1-9
    • (2000) J. Gen. Physiol. , vol.116 , pp. 1-9
    • Tanna, B.1    Welch, W.2    Ruest, L.3    Sutko, J.L.4    Williams, A.J.5
  • 50
    • 0026320451 scopus 로고
    • Examination of subconductance levels arising from a single ion channel
    • Dani J.A., and Fox J.A. Examination of subconductance levels arising from a single ion channel. J. Theor. Biol. 153 (1991) 401-423
    • (1991) J. Theor. Biol. , vol.153 , pp. 401-423
    • Dani, J.A.1    Fox, J.A.2
  • 51
    • 23744511543 scopus 로고    scopus 로고
    • K channel subconductance levels result from heteromeric pore conformations
    • Chapman M.L., and VanDongen A.M. K channel subconductance levels result from heteromeric pore conformations. J. Gen. Physiol. 126 (2005) 87-103
    • (2005) J. Gen. Physiol. , vol.126 , pp. 87-103
    • Chapman, M.L.1    VanDongen, A.M.2
  • 53
    • 0028967877 scopus 로고
    • Desensitization of the skeletal muscle ryanodine receptor: evidence for heterogeneity of calcium release channels
    • Ma J. Desensitization of the skeletal muscle ryanodine receptor: evidence for heterogeneity of calcium release channels. Biophys. J. 68 (1995) 893-899
    • (1995) Biophys. J. , vol.68 , pp. 893-899
    • Ma, J.1
  • 56
    • 0035878882 scopus 로고    scopus 로고
    • Effects of ryanodine on calcium sparks in cut twitch fibres of Rana temporaria
    • Hui C.S., Bidasee K.R., and Besch Jr. H.R. Effects of ryanodine on calcium sparks in cut twitch fibres of Rana temporaria. J. Physiol. 534 (2001) 327-342
    • (2001) J. Physiol. , vol.534 , pp. 327-342
    • Hui, C.S.1    Bidasee, K.R.2    Besch Jr., H.R.3
  • 57
    • 0035201898 scopus 로고    scopus 로고
    • A Component of excitation-contraction coupling triggered in the absence of the T671-L690 and L720-Q765 regions of the II-III loop of the Dihydropyridine receptor alpha 1 s pore subunit
    • Ahern C.A., Bhattacharya D., Mortenson L., and Coronado R. A Component of excitation-contraction coupling triggered in the absence of the T671-L690 and L720-Q765 regions of the II-III loop of the Dihydropyridine receptor alpha 1 s pore subunit. Biophys. J. 81 (2001) 3294-3307
    • (2001) Biophys. J. , vol.81 , pp. 3294-3307
    • Ahern, C.A.1    Bhattacharya, D.2    Mortenson, L.3    Coronado, R.4
  • 59
    • 26044462648 scopus 로고    scopus 로고
    • 2+ release events in permeabilized skeletal muscle fibers
    • 2+ release events in permeabilized skeletal muscle fibers. Biol. Res. 37 (2004) 613-616
    • (2004) Biol. Res. , vol.37 , pp. 613-616
    • Schneider, M.F.1    Rodney, G.G.2


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