메뉴 건너뛰기




Volumn 286, Issue 1 55-1, 2004, Pages

Conformational coupling of DHPR and RyR1 in skeletal myotubes is influenced by long-range allosterism: Evidence for a negative regulatory module

Author keywords

Dihydropyridine receptor; Excitation contraction coupling; Negative module; Ryanodine receptor type 1

Indexed keywords

1,4 DIHYDROPYRIDINE RECEPTOR; CADMIUM; CAFFEINE; CALCIUM; LANTHANUM; NIFEDIPINE; RYANODINE RECEPTOR;

EID: 0347357994     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.00176.2003     Document Type: Article
Times cited : (36)

References (53)
  • 1
    • 0025336609 scopus 로고
    • Intramembrane charge movement restored in dysgenic skeletal muscle by injection of dihydropyridine receptor cDNAs
    • Adams BA, Tanabe T, Mikami A, Numa S, and Beam KG. Intramembrane charge movement restored in dysgenic skeletal muscle by injection of dihydropyridine receptor cDNAs. Nature 346: 569-572, 1990.
    • (1990) Nature , vol.346 , pp. 569-572
    • Adams, B.A.1    Tanabe, T.2    Mikami, A.3    Numa, S.4    Beam, K.G.5
  • 2
    • 0022640513 scopus 로고
    • A lethal mutation in mice eliminates the slow calcium current in skeletal muscle cells
    • Beam KG, Knudson CM, and Powell JA. A lethal mutation in mice eliminates the slow calcium current in skeletal muscle cells. Nature 320: 168-170, 1986.
    • (1986) Nature , vol.320 , pp. 168-170
    • Beam, K.G.1    Knudson, C.M.2    Powell, J.A.3
  • 3
    • 0030943105 scopus 로고    scopus 로고
    • Numerical analysis of ryanodine receptor activation by L-type channel activity in the cardiac muscle diad
    • Cannell MB and Soeller D. Numerical analysis of ryanodine receptor activation by L-type channel activity in the cardiac muscle diad. Biophys J 73: 112-122, 1997.
    • (1997) Biophys J , vol.73 , pp. 112-122
    • Cannell, M.B.1    Soeller, D.2
  • 4
    • 0020516760 scopus 로고
    • Calcium currents in a fast-twitch skeletal muscle of the rat
    • Donaldson PL and Beam KG. Calcium currents in a fast-twitch skeletal muscle of the rat. J Gen Physiol 82: 449-468, 1983.
    • (1983) J Gen Physiol , vol.82 , pp. 449-468
    • Donaldson, P.L.1    Beam, K.G.2
  • 5
    • 0028836471 scopus 로고
    • Luminal calcium regulates calcium release in triads isolated from frog and rabbit skeletal muscle
    • Donoso P, Prieto H, and Hidalgo C. Luminal calcium regulates calcium release in triads isolated from frog and rabbit skeletal muscle. Biophys J 68: 507-515, 1995.
    • (1995) Biophys J , vol.68 , pp. 507-515
    • Donoso, P.1    Prieto, H.2    Hidalgo, C.3
  • 6
    • 0036112245 scopus 로고    scopus 로고
    • Morphology and molecular composition of sarcoplasmic reticulum surface junctions in the absence of DHPR and RyR in mouse skeletal muscle
    • Felder E, Protasi F, Hirsch R, Franzini-Armstrong C, and Allen PD. Morphology and molecular composition of sarcoplasmic reticulum surface junctions in the absence of DHPR and RyR in mouse skeletal muscle. Biophys J 82: 3144-3149, 2002.
    • (2002) Biophys J , vol.82 , pp. 3144-3149
    • Felder, E.1    Protasi, F.2    Hirsch, R.3    Franzini-Armstrong, C.4    Allen, P.D.5
  • 8
    • 0033729715 scopus 로고    scopus 로고
    • Divergent functional properties of ryanodine receptor types 1 and 3 expressed in a myogenic cell line
    • Fessenden JD, Wang Y, Moore RA, Chen SR, Allen PD, and Pessah IN. Divergent functional properties of ryanodine receptor types 1 and 3 expressed in a myogenic cell line. Biophys J 79: 2509-2525, 2000.
    • (2000) Biophys J , vol.79 , pp. 2509-2525
    • Fessenden, J.D.1    Wang, Y.2    Moore, R.A.3    Chen, S.R.4    Allen, P.D.5    Pessah, I.N.6
  • 10
    • 0029060579 scopus 로고
    • Alternate disposition of tetrads in peripheral couplings of skeletal muscle
    • Franzini-Armstrong C and Kish JW. Alternate disposition of tetrads in peripheral couplings of skeletal muscle. J Muscle Res Cell Motil 16: 319-324, 1995.
    • (1995) J Muscle Res Cell Motil , vol.16 , pp. 319-324
    • Franzini-Armstrong, C.1    Kish, J.W.2
  • 11
    • 0028210105 scopus 로고
    • Calcium-dependent block of ryanodine receptor channel of swine skeletal muscle by direct binding of calmodulin
    • Fuentes O, Valdivia C, Vaughan D, Coronado R, and Valdivia HH. Calcium-dependent block of ryanodine receptor channel of swine skeletal muscle by direct binding of calmodulin. Cell Calcium 15: 305-316, 1994.
    • (1994) Cell Calcium , vol.15 , pp. 305-316
    • Fuentes, O.1    Valdivia, C.2    Vaughan, D.3    Coronado, R.4    Valdivia, H.H.5
  • 14
    • 0024410004 scopus 로고
    • Postulated role of calsequestrin in the regulation of calcium release from sarcoplasmic reticulum
    • Ikemoto N, Ronjat M, Meszaros LG, and Koshita M. Postulated role of calsequestrin in the regulation of calcium release from sarcoplasmic reticulum. Biochemistry 28: 6764-6771, 1989.
    • (1989) Biochemistry , vol.28 , pp. 6764-6771
    • Ikemoto, N.1    Ronjat, M.2    Meszaros, L.G.3    Koshita, M.4
  • 16
    • 0028218914 scopus 로고
    • Effects of nifedipine and Bay K 8644 on contractile activities in single skeletal muscle fibers of the frog
    • Kitamura N, Ohta T, Ito S, and Nakazato Y. Effects of nifedipine and Bay K 8644 on contractile activities in single skeletal muscle fibers of the frog. Eur J Pharmacol 256: 169-176, 1994.
    • (1994) Eur J Pharmacol , vol.256 , pp. 169-176
    • Kitamura, N.1    Ohta, T.2    Ito, S.3    Nakazato, Y.4
  • 17
    • 0023903046 scopus 로고
    • Purification and reconstitution of the calcium release channel from skeletal muscle
    • Lai FA, Erickson HP, Rousseau E, Liu QY, and Meissner G. Purification and reconstitution of the calcium release channel from skeletal muscle. Nature 331: 315-319, 1988.
    • (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
  • 18
    • 0032478812 scopus 로고    scopus 로고
    • A 37-amino acid sequence in the skeletal muscle ryanodine receptor interacts with the cytoplasmic loop between domains II and III in the skeletal muscle dihydropyridine receptor
    • Leong P and MacLennan DH. A 37-amino acid sequence in the skeletal muscle ryanodine receptor interacts with the cytoplasmic loop between domains II and III in the skeletal muscle dihydropyridine receptor. J Biol Chem 273: 7791-7794, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 7791-7794
    • Leong, P.1    MacLennan, D.H.2
  • 20
    • 0029741203 scopus 로고    scopus 로고
    • Fast activation of dihydropyridine-sensitive calcium channels of skeletal muscle. Multiple pathways of channel gating
    • Ma J, Gonzalez A, and Chen R. Fast activation of dihydropyridine-sensitive calcium channels of skeletal muscle. Multiple pathways of channel gating. J Gen Physiol 108: 221-232, 1996.
    • (1996) J Gen Physiol , vol.108 , pp. 221-232
    • Ma, J.1    Gonzalez, A.2    Chen, R.3
  • 21
    • 0022535804 scopus 로고
    • Evidence of a role for calmodulin in the regulation of calcium release from skeletal muscle sarcoplasmic reticulum
    • Meissner G. Evidence of a role for calmodulin in the regulation of calcium release from skeletal muscle sarcoplasmic reticulum. Biochemistry 25: 244-251, 1986.
    • (1986) Biochemistry , vol.25 , pp. 244-251
    • Meissner, G.1
  • 22
    • 0023644601 scopus 로고
    • 2+, adenine nucleotide, and calmodulin
    • 2+, adenine nucleotide, and calmodulin. J Biol Chem 262: 3065-3073, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 3065-3073
    • Meissner, G.1    Henderson, J.S.2
  • 24
    • 0032559630 scopus 로고    scopus 로고
    • A transgenic myogenic cell line lacking ryanodine receptor protein for homologous expression studies: Reconstitution of Ry 1R protein and function
    • Moore RA, Nguyen H, Galceran J, Pessah IN, and Allen PD. A transgenic myogenic cell line lacking ryanodine receptor protein for homologous expression studies: reconstitution of Ry1R protein and function. J Cell Biol 140: 843-851, 1998.
    • (1998) J Cell Biol , vol.140 , pp. 843-851
    • Moore, R.A.1    Nguyen, H.2    Galceran, J.3    Pessah, I.N.4    Allen, P.D.5
  • 25
    • 0024393890 scopus 로고
    • Regulation of calcium release is gated by calcium current, not gating charge, in cardiac myocytes
    • Nabauer M, Callewaert G, Cleemann L, and Morad M. Regulation of calcium release is gated by calcium current, not gating charge, in cardiac myocytes. Science 244: 800-803, 1989.
    • (1989) Science , vol.244 , pp. 800-803
    • Nabauer, M.1    Callewaert, G.2    Cleemann, L.3    Morad, M.4
  • 26
    • 0029983398 scopus 로고    scopus 로고
    • Enhanced dihydropyridine receptor channel activity in the presence of ryanodine receptor
    • Nakai J, Dirksen RT, Nguyen HT, Pessah IN, Beam KG, and Allen PD. Enhanced dihydropyridine receptor channel activity in the presence of ryanodine receptor. Nature 380: 72-75, 1996.
    • (1996) Nature , vol.380 , pp. 72-75
    • Nakai, J.1    Dirksen, R.T.2    Nguyen, H.T.3    Pessah, I.N.4    Beam, K.G.5    Allen, P.D.6
  • 30
    • 0021279736 scopus 로고
    • Voltage-dependent calcium channels from brain incorporated into planar lipid bilayers
    • Nelson MT, French RJ, and Krueger BK. Voltage-dependent calcium channels from brain incorporated into planar lipid bilayers. Nature 308: 77-80, 1984.
    • (1984) Nature , vol.308 , pp. 77-80
    • Nelson, M.T.1    French, R.J.2    Krueger, B.K.3
  • 32
    • 0035957705 scopus 로고    scopus 로고
    • 2+ fluxes by ethanol and higher alcohols in rabbit T-tubule membranes
    • 2+ fluxes by ethanol and higher alcohols in rabbit T-tubule membranes. Eur J Pharmacol 418: 169-176, 2001.
    • (2001) Eur J Pharmacol , vol.418 , pp. 169-176
    • Oz, M.1    Tchugunova, Y.B.2    Dunn, S.M.3
  • 33
    • 0037381720 scopus 로고    scopus 로고
    • RyR1/RyR3 chimeras reveal that multiple domains of RyR1 are involved in skeletal-type E-C coupling
    • Perez CF, Voss A, Pessah IN, and Allen PD. RyR1/RyR3 chimeras reveal that multiple domains of RyR1 are involved in skeletal-type E-C coupling. Biophys J 84: 2655-2663, 2003.
    • (2003) Biophys J , vol.84 , pp. 2655-2663
    • Perez, C.F.1    Voss, A.2    Pessah, I.N.3    Allen, P.D.4
  • 34
    • 0022395442 scopus 로고
    • The calcium-ryanodine receptor complex of skeletal and cardiac muscle
    • Pessah IN, Waterhouse AL, and Casida JE. The calcium-ryanodine receptor complex of skeletal and cardiac muscle. Biochem Biophys Res Commun 128: 449-456, 1985.
    • (1985) Biochem Biophys Res Commun , vol.128 , pp. 449-456
    • Pessah, I.N.1    Waterhouse, A.L.2    Casida, J.E.3
  • 35
    • 0023866790 scopus 로고
    • Inhibition of calcium release from skeletal muscle sarcoplasmic reticulum by calmodulin
    • Plank B, and Wyskovsky W, Hohenegger M, Hellmann G, and Suko J. Inhibition of calcium release from skeletal muscle sarcoplasmic reticulum by calmodulin. Biochim Biophys Acta 938: 79-88, 1988.
    • (1988) Biochim Biophys Acta , vol.938 , pp. 79-88
    • Plank, B.1    Wyskovsky, W.2    Hohenegger, M.3    Hellmann, G.4    Suko, J.5
  • 37
    • 0032559585 scopus 로고    scopus 로고
    • Role of the ryanodine receptors in the assembly of calcium release units in skeletal muscle
    • Protasi F, Franzini-Armstrong C, and Allen PD. Role of the ryanodine receptors in the assembly of calcium release units in skeletal muscle. J Cell Biol 140: 831-842, 1998.
    • (1998) J Cell Biol , vol.140 , pp. 831-842
    • Protasi, F.1    Franzini-Armstrong, C.2    Allen, P.D.3
  • 39
    • 0023113884 scopus 로고
    • Involvement of dihydropyridine receptors in excitation-contraction coupling in skeletal muscle
    • Rios E and Brum G. Involvement of dihydropyridine receptors in excitation-contraction coupling in skeletal muscle. Nature 325: 717-720, 1987.
    • (1987) Nature , vol.325 , pp. 717-720
    • Rios, E.1    Brum, G.2
  • 40
  • 41
    • 0015856482 scopus 로고
    • Voltage dependent charge movement of skeletal muscle: A possible step in excitation-contraction coupling
    • Schneider MF and Chandler WK. Voltage dependent charge movement of skeletal muscle: a possible step in excitation-contraction coupling. Nature 242: 244-246, 1973.
    • (1973) Nature , vol.242 , pp. 244-246
    • Schneider, M.F.1    Chandler, W.K.2
  • 46
    • 0028332473 scopus 로고
    • Excitation-contraction uncoupling and muscular degeneration in mice lacking functional skeletal muscle ryanodine-receptor gene
    • Takeshima H, Iino M, Takekura H, Nishi M, Kuno J, Minowa O, Takano H, and Noda T. Excitation-contraction uncoupling and muscular degeneration in mice lacking functional skeletal muscle ryanodine-receptor gene. Nature 369: 556-559, 1994.
    • (1994) Nature , vol.369 , pp. 556-559
    • Takeshima, H.1    Iino, M.2    Takekura, H.3    Nishi, M.4    Kuno, J.5    Minowa, O.6    Takano, H.7    Noda, T.8
  • 47
    • 0023723765 scopus 로고
    • Restoration of excitation-contraction coupling and slow calcium current in dysgenic muscle by dihydropyridine receptor complementary DNA
    • Tanabe T, Beam KG, Powell JA, and Numa S. Restoration of excitation-contraction coupling and slow calcium current in dysgenic muscle by dihydropyridine receptor complementary DNA. Nature 336: 134-139, 1988.
    • (1988) Nature , vol.336 , pp. 134-139
    • Tanabe, T.1    Beam, K.G.2    Powell, J.A.3    Numa, S.4
  • 51
    • 0029658733 scopus 로고    scopus 로고
    • 2+, and adenine nucleotides under normal and simulated ischemic conditions
    • 2+, and adenine nucleotides under normal and simulated ischemic conditions. Circ Res 79: 1100-1109, 1996.
    • (1996) Circ Res , vol.79 , pp. 1100-1109
    • Xu, L.1    Mann, G.2    Meissner, G.3
  • 52
    • 0025921997 scopus 로고
    • 2+ release from rat cardiac and rabbit skeletal muscle sarcoplasmic reticulum
    • 2+ release from rat cardiac and rabbit skeletal muscle sarcoplasmic reticulum. J Pharmacol Exp Ther 256: 938-946, 1991.
    • (1991) J Pharmacol Exp Ther , vol.256 , pp. 938-946
    • Zimanyi, I.1    Pessah, I.N.2
  • 53
    • 0030610319 scopus 로고    scopus 로고
    • 2+ channel/ryanodine receptor: Modulation by endogenous effectors, drugs and disease states
    • 2+ channel/ryanodine receptor: modulation by endogenous effectors, drugs and disease states. Pharmacol Rev 49: 1-51, 1997.
    • (1997) Pharmacol Rev , vol.49 , pp. 1-51
    • Zucchi, R.1    Ronca-Testoni, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.