메뉴 건너뛰기




Volumn 27, Issue 5-7, 2006, Pages 337-350

The elusive role of store depletion in the control of intracellular calcium release

Author keywords

Calcium sparks; Calsequestrin; Cardiac muscle; Sarcoplasmic reticulum; Skeletal muscle

Indexed keywords

CALCIUM CHANNEL; CALCIUM ION; CALSEQUESTRIN; RYANODINE RECEPTOR;

EID: 33748313279     PISSN: 01424319     EISSN: 15732657     Source Type: Journal    
DOI: 10.1007/s10974-006-9082-5     Document Type: Review
Times cited : (20)

References (90)
  • 1
    • 0028950934 scopus 로고
    • Rate of diastolic Ca release from the sarcoplasmic reticulum of intact rabbit and rat ventricular myocytes
    • Bassani RA, Bers DM (1995) Rate of diastolic Ca release from the sarcoplasmic reticulum of intact rabbit and rat ventricular myocytes. Biophys J 68:2015-2022
    • (1995) Biophys J , vol.68 , pp. 2015-2022
    • Bassani, R.A.1    Bers, D.M.2
  • 2
    • 18144396217 scopus 로고    scopus 로고
    • Calcium sparks in skeletal muscle fibers
    • Baylor SM (2005) Calcium sparks in skeletal muscle fibers. Cell Calcium 37(6):513-530
    • (2005) Cell Calcium , vol.37 , Issue.6 , pp. 513-530
    • Baylor, S.M.1
  • 3
    • 0036714304 scopus 로고    scopus 로고
    • Comparison of simulated and measured calcium sparks in intact skeletal muscle fibers of the frog
    • Baylor SM, Hollingworth S, Chandler WK (2002) Comparison of simulated and measured calcium sparks in intact skeletal muscle fibers of the frog. J Gen Physiol 120:349-368
    • (2002) J Gen Physiol , vol.120 , pp. 349-368
    • Baylor, S.M.1    Hollingworth, S.2    Chandler, W.K.3
  • 5
    • 0036219539 scopus 로고    scopus 로고
    • Calsequestrin is an inhibitor of skeletal muscle ryanodine receptor calcium release channels
    • Beard NA, Sakowska MM, Dulhunty AF, Laver DR (2002) Calsequestrin is an inhibitor of skeletal muscle ryanodine receptor calcium release channels. Biophys J 82:310-320
    • (2002) Biophys J , vol.82 , pp. 310-320
    • Beard, N.A.1    Sakowska, M.M.2    Dulhunty, A.F.3    Laver, D.R.4
  • 8
    • 0021269330 scopus 로고
    • Model of calcium movements during activation in the sarcomere of frog skeletal muscle
    • Cannell MB, Allen DG (1984) Model of calcium movements during activation in the sarcomere of frog skeletal muscle. Biophys J 45:913-925
    • (1984) Biophys J , vol.45 , pp. 913-925
    • Cannell, M.B.1    Allen, D.G.2
  • 9
    • 0037388703 scopus 로고    scopus 로고
    • Simulation of calcium sparks in cut skeletal muscle fibers of the frog
    • Chandler WK, Hollingworth S, Baylor SM (2003) Simulation of calcium sparks in cut skeletal muscle fibers of the frog. J Gen Physiol 121(4):311-324
    • (2003) J Gen Physiol , vol.121 , Issue.4 , pp. 311-324
    • Chandler, W.K.1    Hollingworth, S.2    Baylor, S.M.3
  • 10
    • 0029665074 scopus 로고    scopus 로고
    • 2+ in sarcoplasmic reticulum in perfused rabbit heart loaded with 1,2-bis(2-amino-5,6-difluorophenoxy)ethane-N,N, N′,N′-tetraacetic acid by 19F NMR
    • 2+ in sarcoplasmic reticulum in perfused rabbit heart loaded with 1,2-bis(2-amino-5,6-difluorophenoxy)ethane-N,N,N′, N′-tetraacetic acid by 19F NMR. J Biol Chem 271(13):7398-7403
    • (1996) J Biol Chem , vol.271 , Issue.13 , pp. 7398-7403
    • Chen, W.1    Steenbergen, C.2    Levy, L.A.3    Vance, J.4    London, R.E.5    Murphy, E.6
  • 11
    • 0027426069 scopus 로고
    • Calcium sparks: Elementary events underlying excitation-contraction coupling in heart muscle
    • Cheng H, Lederer WJ, Cannell MB (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
  • 12
    • 34548330057 scopus 로고    scopus 로고
    • Voltage-activated calcium release events in mouse skeletal muscle fibers
    • Csernoch L, Pouvreau S, Jacquemond V (2006) Voltage-activated calcium release events in mouse skeletal muscle fibers. Biophys J 90:68a
    • (2006) Biophys J , vol.90
    • Csernoch, L.1    Pouvreau, S.2    Jacquemond, V.3
  • 15
    • 0028836471 scopus 로고
    • Luminal calcium regulates calcium release in triads isolated from frog and rabbit skeletal muscle
    • Donoso P, Prieto H, Hidalgo C (1995) Luminal calcium regulates calcium release in triads isolated from frog and rabbit skeletal muscle. Biophys J 68(2):507-515
    • (1995) Biophys J , vol.68 , Issue.2 , pp. 507-515
    • Donoso, P.1    Prieto, H.2    Hidalgo, C.3
  • 16
    • 0016835791 scopus 로고
    • Stereological analysis of mammalian skeletal muscle. II. White vastus muscle of the adult guinea pig
    • Eisenberg BR, Kuda AM (1975) Stereological analysis of mammalian skeletal muscle. II. White vastus muscle of the adult guinea pig. J Ultrastruct Res 51(2):176-187
    • (1975) J Ultrastruct Res , vol.51 , Issue.2 , pp. 176-187
    • Eisenberg, B.R.1    Kuda, A.M.2
  • 17
    • 0344487761 scopus 로고
    • Calcium release from sarcoplasmic reticulum
    • Endo M (1985) Calcium release from sarcoplasmic reticulum. Physiol Rev 25:181-230
    • (1985) Physiol Rev , vol.25 , pp. 181-230
    • Endo, M.1
  • 18
    • 0015403041 scopus 로고
    • Excitation-contraction coupling of isolated cardiac fibers with disrupted or closed sarcolemmas. Calcium-dependent cyclic and tonic contractions
    • Fabiato A, Fabiato F (1972) Excitation-contraction coupling of isolated cardiac fibers with disrupted or closed sarcolemmas. Calcium-dependent cyclic and tonic contractions. Circ Res 31(3):293-307
    • (1972) Circ Res , vol.31 , Issue.3 , pp. 293-307
    • Fabiato, A.1    Fabiato, F.2
  • 19
    • 0033405549 scopus 로고    scopus 로고
    • The sarcoplasmic reticulum and the control of muscle contraction
    • Franzini-Armstrong C (1999) The sarcoplasmic reticulum and the control of muscle contraction. FASEB J. 13(Suppl 2):S266-S270
    • (1999) FASEB J , vol.13 , Issue.2 SUPPL.
    • Franzini-Armstrong, C.1
  • 20
    • 0023372321 scopus 로고
    • The structure of calsequestrin in triads of vertebrate skeletal muscle: A deep-etch study
    • Franzini-Armstrong C, Kenney LJ, Varriano-Marston E (1987) The structure of calsequestrin in triads of vertebrate skeletal muscle: a deep-etch study. J Cell Biol 105(1):49-56
    • (1987) J Cell Biol , vol.105 , Issue.1 , pp. 49-56
    • Franzini-Armstrong, C.1    Kenney, L.J.2    Varriano-Marston, E.3
  • 22
    • 0028906807 scopus 로고
    • Association of triadin with the ryanodine receptor and calsequestrin in the lumen of the sarcoplasmic reticulum
    • Guo W, Campbell KP (1995) Association of triadin with the ryanodine receptor and calsequestrin in the lumen of the sarcoplasmic reticulum. J Biol Chem 270:9027-9030
    • (1995) J Biol Chem , vol.270 , pp. 9027-9030
    • Guo, W.1    Campbell, K.P.2
  • 23
    • 1942423621 scopus 로고    scopus 로고
    • The role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium
    • Gyorke I, Hester N, Jones LR, Gyorke S (2004) The role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium. Biophys J 86:2121-2128
    • (2004) Biophys J , vol.86 , pp. 2121-2128
    • Gyorke, I.1    Hester, N.2    Jones, L.R.3    Gyorke, S.4
  • 24
    • 0142260723 scopus 로고    scopus 로고
    • Dual effects of tetracaine on spontaneous calcium release in rat ventricular myocytes
    • Gyorke S, Lukyanenko V, Gyorke I. (1997) Dual effects of tetracaine on spontaneous calcium release in rat ventricular myocytes. J Physiol 500(Pt 2):297-309
    • (1997) J Physiol , vol.500 , Issue.2 PART , pp. 297-309
    • Gyorke, S.1    Lukyanenko, V.2    Gyorke, I.3
  • 26
    • 0025886966 scopus 로고
    • Intravesicular calcium transient during calcium release from sarcoplasmic reticulum
    • Ikemoto N, Antoniu B, Kang JJ, Meszaros LG, Ronjat M (1991) Intravesicular calcium transient during calcium release from sarcoplasmic reticulum. Biochemistry 30(21):5230-5237
    • (1991) Biochemistry , vol.30 , Issue.21 , pp. 5230-5237
    • Ikemoto, N.1    Antoniu, B.2    Kang, J.J.3    Meszaros, L.G.4    Ronjat, M.5
  • 28
    • 0037337898 scopus 로고    scopus 로고
    • 2+ release in permeabilized mammalian skeletal muscle fibres
    • 2+ release in permeabilized mammalian skeletal muscle fibres. J Physiol 547:453-462
    • (2003) J Physiol , vol.547 , pp. 453-462
    • Isaeva, E.V.1    Shirokova, N.2
  • 29
    • 0028352967 scopus 로고
    • Regulation of calcium channel in sarcoplasmic reticulum by calsequestrin
    • Kawasaki T, Kasai M (1994) Regulation of calcium channel in sarcoplasmic reticulum by calsequestrin. Biochem Biophys Res Commun 199(3):1120-1127
    • (1994) Biochem Biophys Res Commun , vol.199 , Issue.3 , pp. 1120-1127
    • Kawasaki, T.1    Kasai, M.2
  • 30
    • 0035384875 scopus 로고    scopus 로고
    • The use of the indicator fluo-5N to measure sarcoplasmic reticulum calcium in single muscle fibres of the cane toad
    • Kabbara AA, Allen DG (2001) The use of the indicator fluo-5N to measure sarcoplasmic reticulum calcium in single muscle fibres of the cane toad. J Physiol 534(Pt 1):87-97
    • (2001) J Physiol , vol.534 , Issue.1 PART , pp. 87-97
    • Kabbara, A.A.1    Allen, D.G.2
  • 31
    • 0033567271 scopus 로고    scopus 로고
    • The role of calcium stores in fatigue of isolated single muscle fibres from the cane toad
    • Kabbara AA, Allen DG (1999) The role of calcium stores in fatigue of isolated single muscle fibres from the cane toad. J Physiol 519(Pt 1):169-176
    • (1999) J Physiol , vol.519 , Issue.1 PART , pp. 169-176
    • Kabbara, A.A.1    Allen, D.G.2
  • 32
    • 0035577670 scopus 로고    scopus 로고
    • 2+ release events in skinned fibres of adult mammalian skeletal muscle
    • 2+ release events in skinned fibres of adult mammalian skeletal muscle. J Physiol 537:379-389
    • (2001) J Physiol , vol.537 , pp. 379-389
    • Kirsch, W.G.1    Uttenweiler, D.2    Fink, R.H.A.3
  • 34
    • 0035205336 scopus 로고    scopus 로고
    • A missense mutation in a highly conserved region of CASQ2 is associated with autosomal recessive catecholamine-induced polymorphic ventricular tachycardia in Bedouin families from Israel
    • Lahat H, Pras E, Olender T, Avidan N, Ben-Asher E, Man O, Levy-Nissenbaum E, Khoury A, Lorber A, Goldman B, Lancet D, Eldar M (2001) A missense mutation in a highly conserved region of CASQ2 is associated with autosomal recessive catecholamine-induced polymorphic ventricular tachycardia in Bedouin families from Israel. Am J Hum Genet 69:1378-1384
    • (2001) Am J Hum Genet , vol.69 , pp. 1378-1384
    • Lahat, H.1    Pras, E.2    Olender, T.3    Avidan, N.4    Ben-Asher, E.5    Man, O.6    Levy-Nissenbaum, E.7    Khoury, A.8    Lorber, A.9    Goldman, B.10    Lancet, D.11    Eldar, M.12
  • 35
    • 0035866552 scopus 로고    scopus 로고
    • 2+ releasing action of caffeine and depolarisation in skeletal muscle fibres of the rat
    • 2+ releasing action of caffeine and depolarisation in skeletal muscle fibres of the rat. J Physiol 531:715-728
    • (2001) J Physiol , vol.531 , pp. 715-728
    • Lamb, G.D.1    Cellini, M.A.2    Stephenson, D.G.3
  • 36
    • 21144475523 scopus 로고
    • 2+ in excitation-contraction coupling
    • 2+ in excitation-contraction coupling. NIPS 7:270-274
    • (1992) NIPS , vol.7 , pp. 270-274
    • Lamb, G.D.1    Stephenson, D.G.2
  • 40
    • 0030920356 scopus 로고    scopus 로고
    • Magnesium inhibition of ryanodine-receptor calcium channels: Evidence for two independent mechanisms
    • Laver DR, Baynes TM, Dulhunty AF (1997) Magnesium inhibition of ryanodine-receptor calcium channels: evidence for two independent mechanisms. J Membr Biol 156(3):213-229
    • (1997) J Membr Biol , vol.156 , Issue.3 , pp. 213-229
    • Laver, D.R.1    Baynes, T.M.2    Dulhunty, A.F.3
  • 41
    • 0347357994 scopus 로고    scopus 로고
    • Conformational coupling of DHPR, RyR1 in skeletal myotubes is influenced by long-range allosterism: Evidence for a negative regulatory module
    • Lee EH, Lopez JR, Li J, Protasi F, Pessah IN, Kim do H, Allen PD (2004) Conformational coupling of DHPR, RyR1 in skeletal myotubes is influenced by long-range allosterism: evidence for a negative regulatory module. Am J Physiol Cell Physiol 286(1):C179-C189
    • (2004) Am J Physiol Cell Physiol , vol.286 , Issue.1
    • Lee, E.H.1    Lopez, J.R.2    Li, J.3    Protasi, F.4    Pessah, I.N.5    Kim Do, H.6    Allen, P.D.7
  • 42
    • 0028180422 scopus 로고
    • 2+ release channels and their regulation by endogeneous effectors
    • 2+ release channels and their regulation by endogeneous effectors. Annu Rev Physiol 56:485-508
    • (1994) Annu Rev Physiol , vol.56 , pp. 485-508
    • Meissner, G.1
  • 44
    • 0016792909 scopus 로고
    • Sizes of components in frog skeletal muscle measured by methods of stereology
    • Mobley BA, Eisenberg BR (1975) Sizes of components in frog skeletal muscle measured by methods of stereology. J Gen Physiol 66(1):31-45
    • (1975) J Gen Physiol , vol.66 , Issue.1 , pp. 31-45
    • Mobley, B.A.1    Eisenberg, B.R.2
  • 45
    • 2942670996 scopus 로고    scopus 로고
    • RyR1 exhibits lower gain of CICR activity than RyR3 in the SR: Evidence for selective stabilization of RyR1 channel
    • Murayama T, Ogawa Y (2004) RyR1 exhibits lower gain of CICR activity than RyR3 in the SR: evidence for selective stabilization of RyR1 channel. Am J Physiol Cell Physiol 287:C36-C45
    • (2004) Am J Physiol Cell Physiol , vol.287
    • Murayama, T.1    Ogawa, Y.2
  • 46
    • 17544397465 scopus 로고    scopus 로고
    • Ryanodine receptor isoforms of non-mammalian skeletal muscle
    • Ogawa Y, Murayama T, Kurebayashi N (2002) Ryanodine receptor isoforms of non-mammalian skeletal muscle. Front Biosci 7:d1184-d1194
    • (2002) Front Biosci , vol.7
    • Ogawa, Y.1    Murayama, T.2    Kurebayashi, N.3
  • 48
    • 0015090563 scopus 로고
    • Stereological measurements of cardiac ultrastructures implicated in excitation-contraction coupling
    • Page E, McCallister LP, Power B (1971) Stereological measurements of cardiac ultrastructures implicated in excitation-contraction coupling. Proc Natl Acad Sci USA 68(7):1465-1466
    • (1971) Proc Natl Acad Sci USA , vol.68 , Issue.7 , pp. 1465-1466
    • Page, E.1    McCallister, L.P.2    Power, B.3
  • 50
    • 0031709410 scopus 로고    scopus 로고
    • Effects of partial sarcoplasmic reticulum calcium depletion on calcium release in frog cut muscle fibers equilibrated with 20 mM EGTA
    • Pape PC, Jong DS, Chandler WK (1998) Effects of partial sarcoplasmic reticulum calcium depletion on calcium release in frog cut muscle fibers equilibrated with 20 mM EGTA. J Gen Physiol 112(3):263-295
    • (1998) J Gen Physiol , vol.112 , Issue.3 , pp. 263-295
    • Pape, P.C.1    Jong, D.S.2    Chandler, W.K.3
  • 51
    • 0031872994 scopus 로고    scopus 로고
    • Effect of sarcoplasmic reticulum (SR) calcium content on SR calcium release elicited by small voltage-clamp depolarizations in frog cut skeletal muscle fibers equilibrated with 20 mM EGTA
    • Pape PC, Carrier N (1998) Effect of sarcoplasmic reticulum (SR) calcium content on SR calcium release elicited by small voltage-clamp depolarizations in frog cut skeletal muscle fibers equilibrated with 20 mM EGTA. J Gen Physiol 112:161-179
    • (1998) J Gen Physiol , vol.112 , pp. 161-179
    • Pape, P.C.1    Carrier, N.2
  • 52
    • 0029135359 scopus 로고
    • Calcium release and its voltage dependence in frog cut muscle fibers equilibrated with 20 mM EGTA
    • Pape PC, Jong D-S, Chandler WK (1995) Calcium release and its voltage dependence in frog cut muscle fibers equilibrated with 20 mM EGTA. J Gen Physiol 106:259-336
    • (1995) J Gen Physiol , vol.106 , pp. 259-336
    • Pape, P.C.1    Jong, D.-S.2    Chandler, W.K.3
  • 54
    • 33748317707 scopus 로고    scopus 로고
    • Cardiac-like calcium release units in skeletal muscle fibers expressing uniquely the cardiac isoforms of calsequestrin
    • Paolini C, Allen PD, Protasi F (2005) Cardiac-like calcium release units in skeletal muscle fibers expressing uniquely the cardiac isoforms of calsequestrin. Biophs J 88: 322a
    • (2005) Biophs J , vol.88
    • Paolini, C.1    Allen, P.D.2    Protasi, F.3
  • 55
    • 33748289325 scopus 로고    scopus 로고
    • Any role for calsequestrin in EC coupling? Initial studies on a skeletal calsequestrin knock-out mouse
    • Paolini C, Quarta M, Nori A, Volpe P, Reggian C, Allen PD, Protasi F (2006) Any role for calsequestrin in EC coupling? Initial studies on a skeletal calsequestrin knock-out mouse. Biophys J meeting supplement:5a
    • (2006) Biophys J , Issue.MEETING SUPPLEMENT
    • Paolini, C.1    Quarta, M.2    Nori, A.3    Volpe, P.4    Reggian, C.5    Allen, P.D.6    Protasi, F.7
  • 56
    • 2342444645 scopus 로고    scopus 로고
    • Comparing skeletal and cardiac calsequestrin structures and their calcium binding: A proposed mechanism for coupled calcium binding and protein polymerization
    • Park H, Park IY, Kim E, Youn B, Fields K, Dunker AK, Kang C (2004) Comparing skeletal and cardiac calsequestrin structures and their calcium binding: a proposed mechanism for coupled calcium binding and protein polymerization. J Biol Chem 279:18026-18033
    • (2004) J Biol Chem , vol.279 , pp. 18026-18033
    • Park, H.1    Park, I.Y.2    Kim, E.3    Youn, B.4    Fields, K.5    Dunker, A.K.6    Kang, C.7
  • 57
    • 4544294545 scopus 로고    scopus 로고
    • +] displacement in skeletal muscle
    • +] displacement in skeletal muscle. J Gen Physiol 124(3):239-258
    • (2004) J Gen Physiol , vol.124 , Issue.3 , pp. 239-258
    • Pizarro, G.1    Ríos, E.2
  • 59
    • 5144221528 scopus 로고    scopus 로고
    • 2+ release channels in muscle
    • 2+ release channels in muscle. Biol Res 37(4):583-591
    • (2004) Biol Res , vol.37 , Issue.4 , pp. 583-591
    • Ríos, E.1    Zhou, J.2
  • 61
    • 33646111422 scopus 로고    scopus 로고
    • 2+ and cytosolic cAMP dynamics in mouse skeletal muscle
    • 2+ and cytosolic cAMP dynamics in mouse skeletal muscle. J Cell Biol 173(2):187-193
    • (2006) J Cell Biol , vol.173 , Issue.2 , pp. 187-193
    • Rudolf, R.1    Magalhaes, P.J.2    Pozzan, T.3
  • 62
    • 0023551042 scopus 로고
    • Depletion of calcium from the sarcoplasmic reticulum during calcium release in frog skeletal muscle
    • Schneider MF, Simon BJ, Szucs G (1987) Depletion of calcium from the sarcoplasmic reticulum during calcium release in frog skeletal muscle. J Physiol 392:167-192
    • (1987) J Physiol , vol.392 , pp. 167-192
    • Schneider, M.F.1    Simon, B.J.2    Szucs, G.3
  • 63
    • 0030757931 scopus 로고    scopus 로고
    • Assessment of intra-SR free [Ca] and buffering in rat heart
    • Shannon TR, Bers DM (1997) Assessment of intra-SR free [Ca] and buffering in rat heart. Biophys J 73(3):1524-1531
    • (1997) Biophys J , vol.73 , Issue.3 , pp. 1524-1531
    • Shannon, T.R.1    Bers, D.M.2
  • 64
    • 0034036663 scopus 로고    scopus 로고
    • Potentiation of fractional sarcoplasmic reticulum calcium release by total and free intra-sarcoplasmic reticulum calcium concentration
    • Shannon TR, Ginsburg KS, Bers DM (2000) Potentiation of fractional sarcoplasmic reticulum calcium release by total and free intra-sarcoplasmic reticulum calcium concentration. Biophys J 78(1):334-343
    • (2000) Biophys J , vol.78 , Issue.1 , pp. 334-343
    • Shannon, T.R.1    Ginsburg, K.S.2    Bers, D.M.3
  • 66
    • 0029671198 scopus 로고    scopus 로고
    • 2+ release from the sarcoplasmic reticulum compared in amphibian and mammalian skeletal muscle
    • 2+ release from the sarcoplasmic reticulum compared in amphibian and mammalian skeletal muscle. J Gen Physiol 107(1):1-18
    • (1996) J Gen Physiol , vol.107 , Issue.1 , pp. 1-18
    • Shirokova, N.1    Garcia, J.2    Pizarro, G.3    Ríos, E.4
  • 67
    • 0032532529 scopus 로고    scopus 로고
    • Local calcium release in mammalian skeletal muscle
    • Shirokova N, Garcia J, Ríos E (1998) Local calcium release in mammalian skeletal muscle. J Physiol 512:377-384
    • (1998) J Physiol , vol.512 , pp. 377-384
    • Shirokova, N.1    Garcia, J.2    Ríos, E.3
  • 68
    • 0026135106 scopus 로고
    • 2+ across the sarcoplasmic reticulum of guinea-pig cardiac cells during excitation-contraction coupling
    • 2+ across the sarcoplasmic reticulum of guinea-pig cardiac cells during excitation-contraction coupling. J Physiol 435:605-630
    • (1991) J Physiol , vol.435 , pp. 605-630
    • Sipido, K.R.1    Wier, W.G.2
  • 70
    • 2442602416 scopus 로고    scopus 로고
    • Putting out the fire: What terminates calcium-induced calcium release in cardiac muscle?
    • Stern MD, Cheng H (2004) Putting out the fire: what terminates calcium-induced calcium release in cardiac muscle? Cell Calcium 35:591-601
    • (2004) Cell Calcium , vol.35 , pp. 591-601
    • Stern, M.D.1    Cheng, H.2
  • 71
    • 0030885385 scopus 로고    scopus 로고
    • Local control model of excitation-contraction coupling in skeletal muscle
    • Stern MD, Pizarro G, Ríos E (1997) Local control model of excitation-contraction coupling in skeletal muscle. J Gen Physiol 110:415-440
    • (1997) J Gen Physiol , vol.110 , pp. 415-440
    • Stern, M.D.1    Pizarro, G.2    Ríos, E.3
  • 73
  • 74
    • 0141482017 scopus 로고    scopus 로고
    • Calsequestrin determines the functional size and stability of cardiac intracellular calcium stores: Mechanism for hereditary arrhythmia
    • Terentyev D, Viatchenko-Karpinski S, Gyorke I, Volpe P, Williams SC, Gyorke S (2003) Calsequestrin determines the functional size and stability of cardiac intracellular calcium stores: mechanism for hereditary arrhythmia. Proc Natl Acad Scien USA 100:11759-11764
    • (2003) Proc Natl Acad Scien USA , vol.100 , pp. 11759-11764
    • Terentyev, D.1    Viatchenko-Karpinski, S.2    Gyorke, I.3    Volpe, P.4    Williams, S.C.5    Gyorke, S.6
  • 78
    • 0025924516 scopus 로고
    • 2+ released to the myoplasm is free in the sarcoplasmic reticulum and does not unbind from calsequestrin
    • 2+ released to the myoplasm is free in the sarcoplasmic reticulum and does not unbind from calsequestrin. FEBS Lett 278(2):274-278
    • (1991) FEBS Lett , vol.278 , Issue.2 , pp. 274-278
    • Volpe, P.1    Simon, B.J.2
  • 79
    • 1642375375 scopus 로고    scopus 로고
    • 2+ sparks and in situ operation of the ryanodine receptor array in cardiac cells
    • 2+ sparks and in situ operation of the ryanodine receptor array in cardiac cells. Proc Natl Acad Sci USA 101:3979-3984
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 3979-3984
    • Wang, S.Q.1    Stern, M.D.2    Ríos, E.3    Cheng, H.4
  • 80
  • 81
    • 33744951305 scopus 로고    scopus 로고
    • Knocking down type 2 but not type 1 calsequestrin reduces calcium sequestration and release in C2C12 skeletal muscle myotubes
    • (In press) doi/10.1074/jbc.M600090200
    • Wang Y, Xu L, Duan H, Pasek DA, Eu JP, Meissner G (2006) Knocking down type 2 but not type 1 calsequestrin reduces calcium sequestration and release in C2C12 skeletal muscle myotubes. J Biol Chem (In press) doi/10.1074/jbc. M600090200
    • (2006) J Biol Chem
    • Wang, Y.1    Xu, L.2    Duan, H.3    Pasek, D.A.4    Eu, J.P.5    Meissner, G.6
  • 82
    • 33746839364 scopus 로고    scopus 로고
    • The conformation of calsequestrin determines its ability to regulate skeletal ryanodine receptors
    • (In press) doi:10.1529/biophysj.106.082610
    • Wei L, Varsanyi M, Dulhunty AF, Beard NA (2006) The conformation of calsequestrin determines its ability to regulate skeletal ryanodine receptors. Biophys J (In press) doi:10.1529/biophysj.106.082610
    • (2006) Biophys J
    • Wei, L.1    Varsanyi, M.2    Dulhunty, A.F.3    Beard, N.A.4
  • 83
    • 24644479674 scopus 로고    scopus 로고
    • Calcium signalling in smooth muscle
    • Wray S, Burdyga T, Noble K (2005) Calcium signalling in smooth muscle. Cell Calcium 38:397-407
    • (2005) Cell Calcium , vol.38 , pp. 397-407
    • Wray, S.1    Burdyga, T.2    Noble, K.3
  • 84
    • 0030770826 scopus 로고    scopus 로고
    • Complex formation between junctin, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane
    • Zhang L, Kelley J, Schmeisser G, Kobayashi YM, Jones LR (1997) Complex formation between junctin, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane. J Biol Chem 272:23389-23397
    • (1997) J Biol Chem , vol.272 , pp. 23389-23397
    • Zhang, L.1    Kelley, J.2    Schmeisser, G.3    Kobayashi, Y.M.4    Jones, L.R.5
  • 86
    • 5144228939 scopus 로고    scopus 로고
    • 2+ in mammalian and amphibian muscle. An RyR isoform-specific role in excitation-contraction coupling?
    • 2+ in mammalian and amphibian muscle. An RyR isoform-specific role in excitation-contraction coupling? J Gen Physiol 124:409-428
    • (2004) J Gen Physiol , vol.124 , pp. 409-428
    • Zhou, J.1    Launikonis, B.S.2    Ríos, E.3    Brum, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.