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Volumn 47, Issue 3, 2006, Pages 132-143

Targeting sarcoplasmic reticulum calcium handling proteins as therapy for cardiac disease

Author keywords

Calcium cycling; Heart failure; Histidinerich calcium binding protein; Polymorphisms

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BINDING PROTEIN; CALCIUM; CALCIUM BINDING PROTEIN; CALSEQUESTRIN; PROTEIN JUNCTIN; PROTEIN TRIADIN; RYANODINE RECEPTOR; SODIUM CALCIUM EXCHANGE PROTEIN; UNCLASSIFIED DRUG; ASPH PROTEIN, HUMAN; CARRIER PROTEIN; HRC PROTEIN, HUMAN; MEMBRANE PROTEIN; MIXED FUNCTION OXIDASE; MUSCLE PROTEIN; PHOSPHOLAMBAN; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; TRIADIN;

EID: 35349003721     PISSN: 10117970     EISSN: 10117970     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (6)

References (123)
  • 1
    • 0037049977 scopus 로고    scopus 로고
    • Cardiac excitation-contraction coupling
    • Bers DM: Cardiac excitation-contraction coupling. Nature 2002; 415: 198-205.
    • (2002) Nature , vol.415 , pp. 198-205
    • Bers, D.M.1
  • 2
    • 0034509410 scopus 로고    scopus 로고
    • Phospholamban and cardiac contractile function
    • Brittsan AG, Kranias EG: Phospholamban and cardiac contractile function. J Mol Cell Cardiol 2000, 32: 2131-2139.
    • (2000) J Mol Cell Cardiol , vol.32 , pp. 2131-2139
    • Brittsan, A.G.1    Kranias, E.G.2
  • 3
    • 0025773177 scopus 로고
    • Abnormal intracellular modulation of calcium as a major cause of cardiac contractile dysfunction
    • Morgan JP: Abnormal intracellular modulation of calcium as a major cause of cardiac contractile dysfunction. N Engl J Med 1991; 325: 625-632.
    • (1991) N Engl J Med , vol.325 , pp. 625-632
    • Morgan, J.P.1
  • 4
    • 0001078987 scopus 로고    scopus 로고
    • Alterations of calcium-regulatory proteins in heart failure
    • Hasenfuss G: Alterations of calcium-regulatory proteins in heart failure. Cardiovasc Res 1998; 37: 279-289.
    • (1998) Cardiovasc Res , vol.37 , pp. 279-289
    • Hasenfuss, G.1
  • 5
    • 0033804245 scopus 로고    scopus 로고
    • Abnormalities of calcium cycling in the hypertrophied and failing heart
    • Houser SR, Piacentino V, 3rd, et al: Abnormalities of calcium cycling in the hypertrophied and failing heart. J Mol Cell Cardiol 2000; 32: 1595-1607.
    • (2000) J Mol Cell Cardiol , vol.32 , pp. 1595-1607
    • Houser, S.R.1    Piacentino 3rd, V.2
  • 6
    • 0028987859 scopus 로고
    • 2+]i handling in human ventricular myocytes from patients with terminal heart failure
    • 2+]i handling in human ventricular myocytes from patients with terminal heart failure. Am Heart J 1995; 129: 684-689.
    • (1995) Am Heart J , vol.129 , pp. 684-689
    • Beuckelmann, D.J.1    Nabauer, M.2    Kruger, C.3
  • 7
    • 0027423351 scopus 로고
    • The epidemiology of heart failure: The Framingham Study
    • Ho KK, Pinsky JL, Kannel WB, et al: The epidemiology of heart failure: the Framingham Study. J Am Coll Cardiol 1993, 22: 6A-13A
    • (1993) J Am Coll Cardiol , vol.22
    • Ho, K.K.1    Pinsky, J.L.2    Kannel, W.B.3
  • 8
    • 35348955639 scopus 로고    scopus 로고
    • American Heart Association: In: http://www.americanheart. org/presenter.jhtml?identifier=1486.
    • http
  • 10
    • 0029029280 scopus 로고
    • Fractional SR Ca release is regulated by trigger Ca and SR Ca content in cardiac myocytes
    • Bassani JW, Yuan W, Bers DM: Fractional SR Ca release is regulated by trigger Ca and SR Ca content in cardiac myocytes. Am J Physiol 1995, 268: C1313-1319.
    • (1995) Am J Physiol , vol.268
    • Bassani, J.W.1    Yuan, W.2    Bers, D.M.3
  • 11
    • 0345413285 scopus 로고    scopus 로고
    • Model of intracellular calcium cycling in ventricular myocytes
    • Shiferaw Y, Watanabe MA, Garfinkel A, et al: Model of intracellular calcium cycling in ventricular myocytes. Biophys J 2003; 85: 3666-3686.
    • (2003) Biophys J , vol.85 , pp. 3666-3686
    • Shiferaw, Y.1    Watanabe, M.A.2    Garfinkel, A.3
  • 13
    • 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: Potentiation of fractional sarcoplasmic reticulum calcium release by total and free intra-sarcoplasmic reticulum calcium concentration. Biophys J 2000; 78: 334-343.
    • (2000) Biophys J , vol.78 , pp. 334-343
    • Shannon, T.R.1    Ginsburg, K.S.2    Bers, D.M.3
  • 16
    • 0037465735 scopus 로고    scopus 로고
    • A guide for the perplexed: Towards an understanding of the molecular basis of heart failure
    • Marks AR: A guide for the perplexed: towards an understanding of the molecular basis of heart failure. Circulation 2003; 107: 1456-1459.
    • (2003) Circulation , vol.107 , pp. 1456-1459
    • Marks, A.R.1
  • 17
    • 0030805905 scopus 로고    scopus 로고
    • 2+ ATPase gene in the heart of transgenic mice accelerates calcium transients and cardiac relaxation
    • 2+ ATPase gene in the heart of transgenic mice accelerates calcium transients and cardiac relaxation. J Clin Invest 1997; 100: 380-389.
    • (1997) J Clin Invest , vol.100 , pp. 380-389
    • He, H.1    Giordano, F.J.2    Hilal-Dandan, R.3
  • 18
    • 0032576586 scopus 로고    scopus 로고
    • 2+-ATPase increases cardiac contractility in transgenic mouse hearts
    • 2+-ATPase increases cardiac contractility in transgenic mouse hearts. Circ Res 1998; 83: 1205-1214.
    • (1998) Circ Res , vol.83 , pp. 1205-1214
    • Baker, D.L.1    Hashimoto, K.2    Grupp, I.L.3
  • 19
    • 0037264995 scopus 로고    scopus 로고
    • 2+ affinity mutant of SERCA2a attenuates in vivo pressure overload cardiac hypertrophy
    • 2+ affinity mutant of SERCA2a attenuates in vivo pressure overload cardiac hypertrophy. Faseb J 2003; 17: 61-63.
    • (2003) Faseb J , vol.17 , pp. 61-63
    • Nakayama, H.1    Otsu, K.2    Yamaguchi, O.3
  • 21
    • 0034537410 scopus 로고    scopus 로고
    • 2+ homeostasis and cardiomyocyte function
    • 2+ homeostasis and cardiomyocyte function. J Biol Chem 2000; 275: 38073-38080.
    • (2000) J Biol Chem , vol.275 , pp. 38073-38080
    • Ji, Y.1    Lalli, M.J.2    Babu, G.J.3
  • 22
    • 0030767865 scopus 로고    scopus 로고
    • Adenoviral gene transfer of phospholamban in isolated rat cardiomyocytes. Rescue effects by concomitant gene transfer of sarcoplasmic reticulum Ca(2+)-ATPase
    • Hajjar RJ, Schmidt U, Kang JX, et al: Adenoviral gene transfer of phospholamban in isolated rat cardiomyocytes. Rescue effects by concomitant gene transfer of sarcoplasmic reticulum Ca(2+)-ATPase. Circ Res 1997; 81: 145-153.
    • (1997) Circ Res , vol.81 , pp. 145-153
    • Hajjar, R.J.1    Schmidt, U.2    Kang, J.X.3
  • 23
    • 0035793918 scopus 로고    scopus 로고
    • Adenoviral-mediated serca gene transfer into cardiac myocytes: How much is too much?
    • Periasamy M: Adenoviral-mediated serca gene transfer into cardiac myocytes: how much is too much? Circ Res 2001; 88: 373-375.
    • (2001) Circ Res , vol.88 , pp. 373-375
    • Periasamy, M.1
  • 24
    • 0027932798 scopus 로고
    • Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of beta-agonist stimulation
    • Luo W, Grupp IL, Harrer J, et al: Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of beta-agonist stimulation. Circ Res 1994; 75: 401-409.
    • (1994) Circ Res , vol.75 , pp. 401-409
    • Luo, W.1    Grupp, I.L.2    Harrer, J.3
  • 25
    • 9244255361 scopus 로고    scopus 로고
    • Phospholamban gene dosage effects in the mammalian heart
    • Luo W, Wolska BM, Grupp IL, et al: Phospholamban gene dosage effects in the mammalian heart. Circ Res 1996; 78: 839-847.
    • (1996) Circ Res , vol.78 , pp. 839-847
    • Luo, W.1    Wolska, B.M.2    Grupp, I.L.3
  • 26
    • 0030032378 scopus 로고    scopus 로고
    • Cardiac-specific overexpression of phospholamban alters calcium kinetics and resultant cardiomyocyte mechanics in transgenic mice
    • Kadambi VJ, Ponniah S, Harrer JM, et al: Cardiac-specific overexpression of phospholamban alters calcium kinetics and resultant cardiomyocyte mechanics in transgenic mice. J Clin Invest 1996; 97: 533-539.
    • (1996) J Clin Invest , vol.97 , pp. 533-539
    • Kadambi, V.J.1    Ponniah, S.2    Harrer, J.M.3
  • 27
    • 0030905733 scopus 로고    scopus 로고
    • 2+ pump and phospholamban in Spodoptera frugiperda (Sf21) cells reveals new insights on ATPase regulation
    • 2+ pump and phospholamban in Spodoptera frugiperda (Sf21) cells reveals new insights on ATPase regulation. J Biol Chem 1997; 272: 15872-15880.
    • (1997) J Biol Chem , vol.272 , pp. 15872-15880
    • Autry, J.M.1    Jones, L.R.2
  • 28
    • 0035968264 scopus 로고    scopus 로고
    • Superinhibition of sarcoplasmic reticulum function by phospholamban induces cardiac contractile failure
    • Haghighi K, Schmidt AG, Hoit BD, et al: Superinhibition of sarcoplasmic reticulum function by phospholamban induces cardiac contractile failure. J Biol Chem 2001; 276: 24145-24152.
    • (2001) J Biol Chem , vol.276 , pp. 24145-24152
    • Haghighi, K.1    Schmidt, A.G.2    Hoit, B.D.3
  • 29
    • 0034685881 scopus 로고    scopus 로고
    • The transgenic expression of highly inhibitory monomeric forms of phospholamban in mouse heart impairs cardiac contractility
    • Zvaritch E, Backx PH, Jirik F, et al: The transgenic expression of highly inhibitory monomeric forms of phospholamban in mouse heart impairs cardiac contractility. J Biol Chem 2000; 275: 14985-14991.
    • (2000) J Biol Chem , vol.275 , pp. 14985-14991
    • Zvaritch, E.1    Backx, P.H.2    Jirik, F.3
  • 30
    • 0034616217 scopus 로고    scopus 로고
    • Cardiac-specific overexpression of a superinhibitory pentameric phospholamban mutant enhances inhibition of cardiac function in vivo
    • Zhai J, Schmidt AG, Hoit BD, et al: Cardiac-specific overexpression of a superinhibitory pentameric phospholamban mutant enhances inhibition of cardiac function in vivo. J Biol Chem 2000; 275: 10538-10544.
    • (2000) J Biol Chem , vol.275 , pp. 10538-10544
    • Zhai, J.1    Schmidt, A.G.2    Hoit, B.D.3
  • 31
    • 0031765965 scopus 로고    scopus 로고
    • Sarcoplasmic reticulum proteins in heart failure
    • Lehnart SE, Schillinger W, Pieske B, et al: Sarcoplasmic reticulum proteins in heart failure. Ann N Y Acad Sci 1998; 853: 220-230.
    • (1998) Ann N Y Acad Sci , vol.853 , pp. 220-230
    • Lehnart, S.E.1    Schillinger, W.2    Pieske, B.3
  • 32
    • 0036702666 scopus 로고    scopus 로고
    • Calcium cycling in congestive heart failure
    • Hasenfuss G, Pieske B: Calcium cycling in congestive heart failure. J Mol Cell Cardiol 2002; 34: 951-969.
    • (2002) J Mol Cell Cardiol , vol.34 , pp. 951-969
    • Hasenfuss, G.1    Pieske, B.2
  • 33
    • 0034950082 scopus 로고    scopus 로고
    • Beta-adrenergic receptors and calcium cycling proteins in non-failing, hypertrophied and failing human hearts: Transition from hypertrophy to failure
    • DiPaola NR, Sweet WE, Stull LB, Francis GS, Schomisch Moravec C: Beta-adrenergic receptors and calcium cycling proteins in non-failing, hypertrophied and failing human hearts: transition from hypertrophy to failure. J Mol Cell Cardiol 2001; 33: 1283-1295.
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 1283-1295
    • DiPaola, N.R.1    Sweet, W.E.2    Stull, L.B.3    Francis, G.S.4    Schomisch Moravec, C.5
  • 34
    • 0028101383 scopus 로고
    • Relation between myocardial function and expression of sarcoplasmic reticulum Ca(2+)-ATPase in failing and nonfailing human myocardium
    • Hasenfuss G, Reinecke H, Studer R, et al: Relation between myocardial function and expression of sarcoplasmic reticulum Ca(2+)-ATPase in failing and nonfailing human myocardium. Circ Res 1994; 75: 434-442.
    • (1994) Circ Res , vol.75 , pp. 434-442
    • Hasenfuss, G.1    Reinecke, H.2    Studer, R.3
  • 35
    • 0029092577 scopus 로고
    • Alterations of sarcoplasmic reticulum proteins in failing human dilated cardiomyopathy
    • Meyer M, Schillinger W, Pieske B, et al: Alterations of sarcoplasmic reticulum proteins in failing human dilated cardiomyopathy. Circulation 1995; 92: 778-784.
    • (1995) Circulation , vol.92 , pp. 778-784
    • Meyer, M.1    Schillinger, W.2    Pieske, B.3
  • 37
    • 0033105384 scopus 로고    scopus 로고
    • Reduced Ca(2+)-sensitivity of SERCA 2a in failing human myocardium due to reduced serin-16 phospholamban phosphorylation
    • Schwinger RH, Munch G, Bolck B, et al: Reduced Ca(2+)-sensitivity of SERCA 2a in failing human myocardium due to reduced serin-16 phospholamban phosphorylation. J Mol Cell Cardiol 1999; 31: 479-491.
    • (1999) J Mol Cell Cardiol , vol.31 , pp. 479-491
    • Schwinger, R.H.1    Munch, G.2    Bolck, B.3
  • 38
  • 39
    • 0028882650 scopus 로고
    • 2+ uptake and Ca(2+)-ATPase activity of cardiac sarcoplasmic reticulum from dilated cardiomyopathy patients compared with patients with nonfailing hearts
    • 2+ uptake and Ca(2+)-ATPase activity of cardiac sarcoplasmic reticulum from dilated cardiomyopathy patients compared with patients with nonfailing hearts. Circulation 1995; 92: 3220-3228.
    • (1995) Circulation , vol.92 , pp. 3220-3228
    • Schwinger, R.H.1    Bohm, M.2    Schmidt, U.3
  • 40
    • 12944332074 scopus 로고    scopus 로고
    • Adenoviral gene transfer of SERCA2a improves left-ventricular function in aortic-banded rats in transition to heart failure
    • Miyamoto MI, del Monte F, Schmidt U, et al: Adenoviral gene transfer of SERCA2a improves left-ventricular function in aortic-banded rats in transition to heart failure. Proc Natl Acad Sci U S A 2000; 97: 793-798.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 793-798
    • Miyamoto, M.I.1    del Monte, F.2    Schmidt, U.3
  • 41
    • 0035908945 scopus 로고    scopus 로고
    • Improvement in survival and cardiac metabolism after gene transfer of sarcoplasmic reticulum Ca(2+)-ATPase in a rat model of heart failure
    • del Monte F, Williams E, Lebeche D, et al: Improvement in survival and cardiac metabolism after gene transfer of sarcoplasmic reticulum Ca(2+)-ATPase in a rat model of heart failure. Circulation 2001; 104: 1424-1429.
    • (2001) Circulation , vol.104 , pp. 1424-1429
    • del Monte, F.1    Williams, E.2    Lebeche, D.3
  • 42
    • 0036227758 scopus 로고    scopus 로고
    • Overexpression of the sarcoplasmic reticulum Ca(2+)-ATPase improves myocardial contractility in diabetic cardiomyopathy
    • Trost SU, Belke DD, Bluhm WF, et al: Overexpression of the sarcoplasmic reticulum Ca(2+)-ATPase improves myocardial contractility in diabetic cardiomyopathy. Diabetes 2002; 51: 1166-1171.
    • (2002) Diabetes , vol.51 , pp. 1166-1171
    • Trost, S.U.1    Belke, D.D.2    Bluhm, W.F.3
  • 43
    • 1842732159 scopus 로고    scopus 로고
    • Del Monte F, Lebeche D, Guerrero JL, et al: Abrogation of ventricular arrhythmias in a model of ischemia and reperfusion by targeting myocardial calcium cycling. Proc Natl Acad Sci U S A 2004.
    • Del Monte F, Lebeche D, Guerrero JL, et al: Abrogation of ventricular arrhythmias in a model of ischemia and reperfusion by targeting myocardial calcium cycling. Proc Natl Acad Sci U S A 2004.
  • 44
    • 0036341380 scopus 로고    scopus 로고
    • Chronic supression of heart-failure progression by a pseudophosphorylated mutant of phospholamban via in vivo cardiac rAAV gene delivery
    • Hoshijima M, Ikeda Y, Iwanaga Y, et al: Chronic supression of heart-failure progression by a pseudophosphorylated mutant of phospholamban via in vivo cardiac rAAV gene delivery. Nature Medicine 2002, 8: 864-871.
    • (2002) Nature Medicine , vol.8 , pp. 864-871
    • Hoshijima, M.1    Ikeda, Y.2    Iwanaga, Y.3
  • 45
    • 85047689989 scopus 로고    scopus 로고
    • Chronic phospholamban inhibition prevents progressive cardiac dysfunction and pathological remodeling after infarction in rats
    • Iwanaga Y, Hoshijima M, Gu Y, et al: Chronic phospholamban inhibition prevents progressive cardiac dysfunction and pathological remodeling after infarction in rats. J Clin Invest 2004; 113: 727-736.
    • (2004) J Clin Invest , vol.113 , pp. 727-736
    • Iwanaga, Y.1    Hoshijima, M.2    Gu, Y.3
  • 46
    • 0033615645 scopus 로고    scopus 로고
    • Chronic phospholamban- sarcoplasmic reticulum calcium ATPase interaction is the critical calcium cycling defect in dilated cardiomyopathy
    • Minamisawa S, Hoshijima M, Chu G, et al: Chronic phospholamban- sarcoplasmic reticulum calcium ATPase interaction is the critical calcium cycling defect in dilated cardiomyopathy. Cell 1999; 99: 313-322.
    • (1999) Cell , vol.99 , pp. 313-322
    • Minamisawa, S.1    Hoshijima, M.2    Chu, G.3
  • 47
    • 0035048223 scopus 로고    scopus 로고
    • Alterations in cardiac adrenergic signaling and calcium cycling differentially affect the progression of cardiomyopathy
    • Freeman K, Lerman I, Kranias EG, et al: Alterations in cardiac adrenergic signaling and calcium cycling differentially affect the progression of cardiomyopathy. J Clin Invest 2001; 107: 967-974.
    • (2001) J Clin Invest , vol.107 , pp. 967-974
    • Freeman, K.1    Lerman, I.2    Kranias, E.G.3
  • 48
    • 0035937762 scopus 로고    scopus 로고
    • Rescue of contractile parameters and myocyte hypertrophy in calsequestrin overexpressing myocardium by phospholamban ablation
    • Sato Y, Kiriazis H, Yatani A, et al: Rescue of contractile parameters and myocyte hypertrophy in calsequestrin overexpressing myocardium by phospholamban ablation. J Biol Chem 2001; 276: 9392-9399.
    • (2001) J Biol Chem , vol.276 , pp. 9392-9399
    • Sato, Y.1    Kiriazis, H.2    Yatani, A.3
  • 49
    • 1542409908 scopus 로고    scopus 로고
    • Altered calcium handling is critically involved in the cardiotoxic effects of chronic beta-adrenergic stimulation
    • Engelhardt S, Hein L, Dyachenkow V, et al: Altered calcium handling is critically involved in the cardiotoxic effects of chronic beta-adrenergic stimulation. Circulation 2004; 109: 1154-1160.
    • (2004) Circulation , vol.109 , pp. 1154-1160
    • Engelhardt, S.1    Hein, L.2    Dyachenkow, V.3
  • 50
    • 0033534053 scopus 로고    scopus 로고
    • Restoration of contractile function in isolated cardiomyocytes from failing human hearts by gene transfer of SERCA2a
    • del Monte F, Harding SE, Schmidt U, et al: Restoration of contractile function in isolated cardiomyocytes from failing human hearts by gene transfer of SERCA2a. Circulation 1999; 100: 2308-2311.
    • (1999) Circulation , vol.100 , pp. 2308-2311
    • del Monte, F.1    Harding, S.E.2    Schmidt, U.3
  • 51
    • 0037176978 scopus 로고    scopus 로고
    • Targeting phospholamban by gene transfer in human heart failure
    • del Monte F, Harding SE, Dec GW, et al: Targeting phospholamban by gene transfer in human heart failure. Circulation 2002; 105: 904-907.
    • (2002) Circulation , vol.105 , pp. 904-907
    • del Monte, F.1    Harding, S.E.2    Dec, G.W.3
  • 52
    • 0012300264 scopus 로고    scopus 로고
    • Re-evaluating sarcoplasmic reticulum function in heart failure
    • Delling U, Sussman MA, Molkentin JD: Re-evaluating sarcoplasmic reticulum function in heart failure. Nat Med 2000; 6: 942-943.
    • (2000) Nat Med , vol.6 , pp. 942-943
    • Delling, U.1    Sussman, M.A.2    Molkentin, J.D.3
  • 53
    • 0037362850 scopus 로고    scopus 로고
    • Rescue of cardiomyocyte dysfunction by phospholamban ablation does not prevent ventricular failure in genetic hypertrophy
    • Song Q, Schmidt AG, Hahn HS, et al: Rescue of cardiomyocyte dysfunction by phospholamban ablation does not prevent ventricular failure in genetic hypertrophy. J Clin Invest 2003; 111: 859-867.
    • (2003) J Clin Invest , vol.111 , pp. 859-867
    • Song, Q.1    Schmidt, A.G.2    Hahn, H.S.3
  • 54
    • 2442501143 scopus 로고    scopus 로고
    • Phospholamban gene ablation improves calcium transients but not cardiac function in a heart failure model
    • Janczewski AM, Zahid M, Lemster BH, et al: Phospholamban gene ablation improves calcium transients but not cardiac function in a heart failure model. Cardiovasc Res 2004; 62: 468-480.
    • (2004) Cardiovasc Res , vol.62 , pp. 468-480
    • Janczewski, A.M.1    Zahid, M.2    Lemster, B.H.3
  • 55
    • 0037470512 scopus 로고    scopus 로고
    • Dilated cardiomyopathy and heart failure caused by a mutation in phospholamban
    • Schmitt JP, Kamisago M, Asahi M, et al: Dilated cardiomyopathy and heart failure caused by a mutation in phospholamban. Science 2003; 299: 1410-1413.
    • (2003) Science , vol.299 , pp. 1410-1413
    • Schmitt, J.P.1    Kamisago, M.2    Asahi, M.3
  • 56
    • 85047687537 scopus 로고    scopus 로고
    • Human phospholamban null results in lethal dilated cardiomyopathy revealing a critical difference between mouse and human
    • Haghighi K, Kolokathis F, Pater L, et al: Human phospholamban null results in lethal dilated cardiomyopathy revealing a critical difference between mouse and human. J Clin Invest 2003; 111: 869-876.
    • (2003) J Clin Invest , vol.111 , pp. 869-876
    • Haghighi, K.1    Kolokathis, F.2    Pater, L.3
  • 57
    • 0344406208 scopus 로고    scopus 로고
    • Mutation of the phospholamban promoter associated with hypertrophic cardiomyopathy
    • Minamisawa S, Sato Y, Tatsuguchi Y, et al: Mutation of the phospholamban promoter associated with hypertrophic cardiomyopathy. Biochem Biophys Res Commun 2003; 304: 1-4.
    • (2003) Biochem Biophys Res Commun , vol.304 , pp. 1-4
    • Minamisawa, S.1    Sato, Y.2    Tatsuguchi, Y.3
  • 58
    • 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, et al: Complex formation between junctin, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane. J Biol Chem 1997; 272: 23389-23397.
    • (1997) J Biol Chem , vol.272 , pp. 23389-23397
    • Zhang, L.1    Kelley, J.2    Schmeisser, G.3
  • 59
    • 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, et al: The role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium. Biophys J 2004; 86: 2121-2128.
    • (2004) Biophys J , vol.86 , pp. 2121-2128
    • Gyorke, I.1    Hester, N.2    Jones, L.R.3
  • 60
    • 0033534056 scopus 로고    scopus 로고
    • Molecular inotropy: A future approach to the treatment of heart failure?
    • Barry WH: Molecular inotropy: a future approach to the treatment of heart failure? Circulation 1999; 100: 2303-2304.
    • (1999) Circulation , vol.100 , pp. 2303-2304
    • Barry, W.H.1
  • 61
    • 0036274039 scopus 로고    scopus 로고
    • Regulation of ryanodine receptors via macromolecular complexes: A novel role for leucine/ isoleucine zippers
    • Marks AR, Marx SO, Reiken S: Regulation of ryanodine receptors via macromolecular complexes: a novel role for leucine/ isoleucine zippers. Trends Cardiovasc Med 2002; 12: 166-170.
    • (2002) Trends Cardiovasc Med , vol.12 , pp. 166-170
    • Marks, A.R.1    Marx, S.O.2    Reiken, S.3
  • 62
    • 3242692393 scopus 로고    scopus 로고
    • Macromolecular complexes regulating cardiac ryanodine receptor function
    • Bers DM: Macromolecular complexes regulating cardiac ryanodine receptor function. J Mol Cell Cardiol 2004; 37: 417-429.
    • (2004) J Mol Cell Cardiol , vol.37 , pp. 417-429
    • Bers, D.M.1
  • 63
    • 0032526717 scopus 로고    scopus 로고
    • Embryonic lethality and abnormal cardiac myocytes in mice lacking ryanodine receptor type 2
    • Takeshima H, Komazaki S, Hirose K, et al: Embryonic lethality and abnormal cardiac myocytes in mice lacking ryanodine receptor type 2. Embo J 1998; 17: 3309-3316.
    • (1998) Embo J , vol.17 , pp. 3309-3316
    • Takeshima, H.1    Komazaki, S.2    Hirose, K.3
  • 64
    • 0035827726 scopus 로고    scopus 로고
    • Coupled gating between cardiac calcium release channels (ryanodine receptors)
    • Marx SO, Gaburjakova J, Gaburjakova M, et al: Coupled gating between cardiac calcium release channels (ryanodine receptors). Circ Res 2001; 88: 1151-1158.
    • (2001) Circ Res , vol.88 , pp. 1151-1158
    • Marx, S.O.1    Gaburjakova, J.2    Gaburjakova, M.3
  • 65
    • 0037708928 scopus 로고    scopus 로고
    • FKBP12.6 deficiency and defective calcium release channel (ryanodine receptor) function linked to exercise-induced sudden cardiac death
    • Wehrens XH, Lehnart SE, Huang F, et al: FKBP12.6 deficiency and defective calcium release channel (ryanodine receptor) function linked to exercise-induced sudden cardiac death. Cell 2003; 113: 829-840.
    • (2003) Cell , vol.113 , pp. 829-840
    • Wehrens, X.H.1    Lehnart, S.E.2    Huang, F.3
  • 66
    • 0037149508 scopus 로고    scopus 로고
    • Oestrogen protects FKBP12.6 null mice from cardiac hypertrophy
    • Xin HB, Senbonmatsu T, Cheng DS, et al: Oestrogen protects FKBP12.6 null mice from cardiac hypertrophy. Nature 2002; 416: 334-338.
    • (2002) Nature , vol.416 , pp. 334-338
    • Xin, H.B.1    Senbonmatsu, T.2    Cheng, D.S.3
  • 67
    • 0032576689 scopus 로고    scopus 로고
    • Cardiac defects and altered ryanodine receptor function in mice lacking FKBP12
    • Shou W, Aghdasi B, Armstrong DL, et al: Cardiac defects and altered ryanodine receptor function in mice lacking FKBP12. Nature 1998; 391: 489-492.
    • (1998) Nature , vol.391 , pp. 489-492
    • Shou, W.1    Aghdasi, B.2    Armstrong, D.L.3
  • 68
    • 0028809084 scopus 로고
    • Differential regulation of two types of intracellular calcium release channels during end-stage heart failure
    • Go LO, Moschella MC, Watras J, et al: Differential regulation of two types of intracellular calcium release channels during end-stage heart failure. J Clin Invest 1995; 95: 888-894.
    • (1995) J Clin Invest , vol.95 , pp. 888-894
    • Go, L.O.1    Moschella, M.C.2    Watras, J.3
  • 69
    • 0029620947 scopus 로고
    • The ryanodine binding sarcoplasmic reticulum calcium release channel in nonfailing and in failing human myocardium
    • Schumacher C, Konigs B, Sigmund M, et al: The ryanodine binding sarcoplasmic reticulum calcium release channel in nonfailing and in failing human myocardium. Naunyn Schmiedebergs Arch Pharmacol 1995; 353: 80-85.
    • (1995) Naunyn Schmiedebergs Arch Pharmacol , vol.353 , pp. 80-85
    • Schumacher, C.1    Konigs, B.2    Sigmund, M.3
  • 70
    • 0037195427 scopus 로고    scopus 로고
    • 2+ release, but normal ryanodine receptors, in canine and human heart failure
    • 2+ release, but normal ryanodine receptors, in canine and human heart failure. Circ Res 2002; 91: 1015-1022.
    • (2002) Circ Res , vol.91 , pp. 1015-1022
    • Jiang, M.T.1    Lokuta, A.J.2    Farrell, E.F.3
  • 71
    • 0031127992 scopus 로고    scopus 로고
    • Cardiac calcium release channel (ryanodine receptor) in control and cardiomyopathic human hearts: MRNA and protein contents are differentially regulated
    • Sainte Beuve C, Allen PD, Dambrin G, et al: Cardiac calcium release channel (ryanodine receptor) in control and cardiomyopathic human hearts: mRNA and protein contents are differentially regulated. J Mol Cell Cardiol 1997; 29: 1237-1246.
    • (1997) J Mol Cell Cardiol , vol.29 , pp. 1237-1246
    • Sainte Beuve, C.1    Allen, P.D.2    Dambrin, G.3
  • 72
    • 0024437435 scopus 로고
    • Single channel recordings from human cardiac sarcoplasmic reticulum
    • Holmberg SR, Williams AJ: Single channel recordings from human cardiac sarcoplasmic reticulum. Circ Res 1989; 65: 1445-1449.
    • (1989) Circ Res , vol.65 , pp. 1445-1449
    • Holmberg, S.R.1    Williams, A.J.2
  • 73
    • 0034640113 scopus 로고    scopus 로고
    • PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): Defective regulation in failing hearts
    • Marx SO, Reiken S, Hisamatsu Y, et al: PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts. Cell 2000; 101: 365-376.
    • (2000) Cell , vol.101 , pp. 365-376
    • Marx, S.O.1    Reiken, S.2    Hisamatsu, Y.3
  • 74
    • 0037414827 scopus 로고    scopus 로고
    • Protein kinase A phosphorylation of the cardiac calcium release channel (ryanodine receptor) in normal and failing hearts. Role of phosphatases and response to isoproterenol
    • Reiken S, Gaburjakova M, Guatimosim S, et al: Protein kinase A phosphorylation of the cardiac calcium release channel (ryanodine receptor) in normal and failing hearts. Role of phosphatases and response to isoproterenol. J Biol Chem 2003; 278: 444-453.
    • (2003) J Biol Chem , vol.278 , pp. 444-453
    • Reiken, S.1    Gaburjakova, M.2    Guatimosim, S.3
  • 75
    • 0034711171 scopus 로고    scopus 로고
    • Altered stoichiometry of FKBP12.6 versus ryanodine receptor as a cause of abnormal Ca(2+) leak through ryanodine receptor in heart failure
    • Yano M, Ono K, Ohkusa T, et al: Altered stoichiometry of FKBP12.6 versus ryanodine receptor as a cause of abnormal Ca(2+) leak through ryanodine receptor in heart failure. Circulation 2000; 102: 2131-2136.
    • (2000) Circulation , vol.102 , pp. 2131-2136
    • Yano, M.1    Ono, K.2    Ohkusa, T.3
  • 76
    • 0033770278 scopus 로고    scopus 로고
    • Altered interaction of FKBP 12.6 with ryanodine receptor as a cause of abnormal Ca(2+) release in heart failure
    • Ono K, Yano M, Ohkusa T, et al: Altered interaction of FKBP 12.6 with ryanodine receptor as a cause of abnormal Ca(2+) release in heart failure. Cardiovasc Res 2000; 48: 323-331.
    • (2000) Cardiovasc Res , vol.48 , pp. 323-331
    • Ono, K.1    Yano, M.2    Ohkusa, T.3
  • 77
    • 0037469180 scopus 로고    scopus 로고
    • FKBP12.6-mediated stabilization of calcium-release channel (ryanodine receptor) as a novel therapeutic strategy against heart failure
    • Yano M, Kobayashi S, Kohno M, et al: FKBP12.6-mediated stabilization of calcium-release channel (ryanodine receptor) as a novel therapeutic strategy against heart failure. Circulation 2003; 107: 477-484.
    • (2003) Circulation , vol.107 , pp. 477-484
    • Yano, M.1    Kobayashi, S.2    Kohno, M.3
  • 78
    • 1842482414 scopus 로고    scopus 로고
    • Protection from cardiac arrhythmia through ryanodine receptor-stabilizing protein calstabin2
    • Wehrens XH, Lehnart SE, Reiken SR, et al: Protection from cardiac arrhythmia through ryanodine receptor-stabilizing protein calstabin2. Science 2004; 304: 292-296.
    • (2004) Science , vol.304 , pp. 292-296
    • Wehrens, X.H.1    Lehnart, S.E.2    Reiken, S.R.3
  • 79
    • 0035793341 scopus 로고    scopus 로고
    • Overexpression of FK506-binding protein FKBP12.6 in cardiomyocytes reduces ryanodine receptor-mediated Ca(2+) leak from the sarcoplasmic reticulum and increases contractility
    • Prestle J, Janssen PM, Janssen AP, et al: Overexpression of FK506-binding protein FKBP12.6 in cardiomyocytes reduces ryanodine receptor-mediated Ca(2+) leak from the sarcoplasmic reticulum and increases contractility. Circ Res 2001; 88: 188-194.
    • (2001) Circ Res , vol.88 , pp. 188-194
    • Prestle, J.1    Janssen, P.M.2    Janssen, A.P.3
  • 80
    • 0035969990 scopus 로고    scopus 로고
    • Mutations of the cardiac ryanodine receptor (RyR2) gene in familial polymorphic ventricular tachycardia
    • Laitinen PJ, Brown KM, Piippo K, et al: Mutations of the cardiac ryanodine receptor (RyR2) gene in familial polymorphic ventricular tachycardia. Circulation 2001; 103: 485-490.
    • (2001) Circulation , vol.103 , pp. 485-490
    • Laitinen, P.J.1    Brown, K.M.2    Piippo, K.3
  • 81
    • 0037125396 scopus 로고    scopus 로고
    • Screening for ryanodine receptor type 2 mutations in families with effort-induced polymorphic ventricular arrhythmias and sudden death: Early diagnosis of asymptomatic carriers
    • Bauce B, Rampazzo A, Basso C, et al: Screening for ryanodine receptor type 2 mutations in families with effort-induced polymorphic ventricular arrhythmias and sudden death: early diagnosis of asymptomatic carriers. J Am Coll Cardiol 2002; 40: 341-349.
    • (2002) J Am Coll Cardiol , vol.40 , pp. 341-349
    • Bauce, B.1    Rampazzo, A.2    Basso, C.3
  • 82
    • 0036132550 scopus 로고    scopus 로고
    • Involvement of the cardiac ryanodine receptor/calcium release channel in catecholaminergic polymorphic ventricular tachycardia
    • Marks AR, Priori S, Memmi M, et al: Involvement of the cardiac ryanodine receptor/calcium release channel in catecholaminergic polymorphic ventricular tachycardia. J Cell Physiol 2002; 190: 1-6.
    • (2002) J Cell Physiol , vol.190 , pp. 1-6
    • Marks, A.R.1    Priori, S.2    Memmi, M.3
  • 83
    • 0035895322 scopus 로고    scopus 로고
    • Mutations in the cardiac ryanodine receptor gene (hRyR2) underlie catecholaminergic polymorphic ventricular tachycardia
    • Priori SG, Napolitano C, Tiso N, et al: Mutations in the cardiac ryanodine receptor gene (hRyR2) underlie catecholaminergic polymorphic ventricular tachycardia. Circulation 2001; 103: 196-200.
    • (2001) Circulation , vol.103 , pp. 196-200
    • Priori, S.G.1    Napolitano, C.2    Tiso, N.3
  • 84
    • 0035253502 scopus 로고    scopus 로고
    • Identification of mutations in the cardiac ryanodine receptor gene in families affected with arrhythmogenic right ventricular cardiomyopathy type 2 (ARVD2)
    • Tiso N, Stephan DA, Nava A, et al: Identification of mutations in the cardiac ryanodine receptor gene in families affected with arrhythmogenic right ventricular cardiomyopathy type 2 (ARVD2). Hum Mol Genet 2001; 10: 189-194.
    • (2001) Hum Mol Genet , vol.10 , pp. 189-194
    • Tiso, N.1    Stephan, D.A.2    Nava, A.3
  • 85
    • 3242772173 scopus 로고    scopus 로고
    • Calcium cycling proteins in heart failure, cardiomyopathy and arrhythmias
    • Minamisawa S, Sato Y, Cho MC: Calcium cycling proteins in heart failure, cardiomyopathy and arrhythmias. Exp Mol Med 2004; 36: 193-203.
    • (2004) Exp Mol Med , vol.36 , pp. 193-203
    • Minamisawa, S.1    Sato, Y.2    Cho, M.C.3
  • 86
    • 0345490780 scopus 로고    scopus 로고
    • Altered function and regulation of cardiac ryanodine receptors in cardiac disease
    • Wehrens XH, Marks AR: Altered function and regulation of cardiac ryanodine receptors in cardiac disease. Trends Biochem Sci 2003; 28: 671-678.
    • (2003) Trends Biochem Sci , vol.28 , pp. 671-678
    • Wehrens, X.H.1    Marks, A.R.2
  • 87
    • 0031046227 scopus 로고    scopus 로고
    • The mechanism of catecholaminergic polymorphic ventricular tachycardia may be triggered activity due to delayed afterdepolarization
    • Nakajima T, Kaneko Y, Taniguchi Y, et al: The mechanism of catecholaminergic polymorphic ventricular tachycardia may be triggered activity due to delayed afterdepolarization. Eur Heart J 1997; 18: 530-531.
    • (1997) Eur Heart J , vol.18 , pp. 530-531
    • Nakajima, T.1    Kaneko, Y.2    Taniguchi, Y.3
  • 88
    • 0032038691 scopus 로고    scopus 로고
    • 2+ signaling in transgenic mouse cardiac myocytes overexpressing calsequestrin
    • 2+ signaling in transgenic mouse cardiac myocytes overexpressing calsequestrin. J Clin Invest 1998; 101: 1385-1393.
    • (1998) J Clin Invest , vol.101 , pp. 1385-1393
    • Jones, L.R.1    Suzuki, Y.J.2    Wang, W.3
  • 89
    • 0033794867 scopus 로고    scopus 로고
    • Cardiac-specific overexpression of calsequestrin results in left ventricular hypertrophy, depressed force-frequency relation, and pulsus alternans in vivo
    • Schmidt A, Kadambi V, Ball N, et al: Cardiac-specific overexpression of calsequestrin results in left ventricular hypertrophy, depressed force-frequency relation, and pulsus alternans in vivo. J Mol Cell Cardiol 2000; 32: 1735-1744.
    • (2000) J Mol Cell Cardiol , vol.32 , pp. 1735-1744
    • Schmidt, A.1    Kadambi, V.2    Ball, N.3
  • 90
    • 0037283739 scopus 로고    scopus 로고
    • Compensated hypertrophy of cardiac ventricles in aged transgenic FVB/N mice overexpressing calsequestrin
    • Sato Y, Schmidt AG, Kiriazis H, et al: Compensated hypertrophy of cardiac ventricles in aged transgenic FVB/N mice overexpressing calsequestrin. Mol Cell Biochem 2003; 242: 19-25.
    • (2003) Mol Cell Biochem , vol.242 , pp. 19-25
    • Sato, Y.1    Schmidt, A.G.2    Kiriazis, H.3
  • 91
    • 0032561337 scopus 로고    scopus 로고
    • Cardiac-specific overexpression of mouse cardiac calsequestrin is associated with depressed cardiovascular function and hypertrophy in transgenic mice
    • Sato Y, Ferguson D, Sako H, et al: Cardiac-specific overexpression of mouse cardiac calsequestrin is associated with depressed cardiovascular function and hypertrophy in transgenic mice. J Biological Chemistry 1998; 273: 28470-28477.
    • (1998) J Biological Chemistry , vol.273 , pp. 28470-28477
    • Sato, Y.1    Ferguson, D.2    Sako, H.3
  • 92
    • 0033529637 scopus 로고    scopus 로고
    • Defective beta-adrenergic receptor signaling precedes the development of dilated cardiomyopathy in transgenic mice with calsequestrin overexpression
    • Cho MC, Rapacciuolo A, Koch WJ, et al: Defective beta-adrenergic receptor signaling precedes the development of dilated cardiomyopathy in transgenic mice with calsequestrin overexpression. J Biol Chem 1999; 274: 22251-22256.
    • (1999) J Biol Chem , vol.274 , pp. 22251-22256
    • Cho, M.C.1    Rapacciuolo, A.2    Koch, W.J.3
  • 93
    • 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, et al: Calsequestrin determines the functional size and stability of cardiac intracellular calcium stores: Mechanism for hereditary arrhythmia. Proc Natl Acad Sci U S A 2003; 100: 11759-11764.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 11759-11764
    • Terentyev, D.1    Viatchenko-Karpinski, S.2    Gyorke, I.3
  • 94
    • 12144288503 scopus 로고    scopus 로고
    • Abnormal calcium signaling and sudden cardiac death associated with mutation of calsequestrin
    • Viatchenko-Karpinski S, Terentyev D, Gyorke I, et al: Abnormal calcium signaling and sudden cardiac death associated with mutation of calsequestrin. Circ Res 2004; 94: 471-477.
    • (2004) Circ Res , vol.94 , pp. 471-477
    • Viatchenko-Karpinski, S.1    Terentyev, D.2    Gyorke, I.3
  • 95
    • 0029810545 scopus 로고    scopus 로고
    • Unaltered ryanodine receptor protein levels in ischemic cardiomyopathy
    • Schillinger W, Meyer M, Kuwajima G, et al: Unaltered ryanodine receptor protein levels in ischemic cardiomyopathy. Mol Cell Biochem 1996, 160-161: 297-302.
    • (1996) Mol Cell Biochem
    • Schillinger, W.1    Meyer, M.2    Kuwajima, G.3
  • 96
    • 0026644822 scopus 로고
    • 2+ channel) and calsequestrin genes in the myocardium of patients with end-stage heart failure
    • 2+ channel) and calsequestrin genes in the myocardium of patients with end-stage heart failure. J Clin Invest 1992; 90: 927-935.
    • (1992) J Clin Invest , vol.90 , pp. 927-935
    • Takahashi, T.1    Allen, P.D.2    Lacro, R.V.3
  • 97
    • 0027506532 scopus 로고
    • Alterations in sarcoplasmic reticulum gene expression in human heart failure. A possible mechanism for alterations in systolic and diastolic properties of the failing myocardium
    • Arai M, Alpert NR, MacLennan DH, et al: Alterations in sarcoplasmic reticulum gene expression in human heart failure. A possible mechanism for alterations in systolic and diastolic properties of the failing myocardium. Circ Res 1993; 72: 463-469.
    • (1993) Circ Res , vol.72 , pp. 463-469
    • Arai, M.1    Alpert, N.R.2    MacLennan, D.H.3
  • 98
    • 0028100606 scopus 로고
    • Ca(2+)-transporting ATPase, phospholamban, and calsequestrin levels in nonfailing and failing human myocardium
    • Movsesian MA, Karimi M, Green K, et al: Ca(2+)-transporting ATPase, phospholamban, and calsequestrin levels in nonfailing and failing human myocardium. Circulation 1994; 90: 653-657.
    • (1994) Circulation , vol.90 , pp. 653-657
    • Movsesian, M.A.1    Karimi, M.2    Green, K.3
  • 99
    • 3142538602 scopus 로고    scopus 로고
    • Defective glycosylation of calsequestrin in heart failure
    • Kiarash A, Kelly CE, Phinney BS, et al: Defective glycosylation of calsequestrin in heart failure. Cardiovasc Res 2004; 63: 264-272.
    • (2004) Cardiovasc Res , vol.63 , pp. 264-272
    • Kiarash, A.1    Kelly, C.E.2    Phinney, B.S.3
  • 100
    • 0037131020 scopus 로고    scopus 로고
    • Absence of calsequestrin 2 causes severe forms of catecholaminergic polymorphic ventricular tachycardia
    • Postma AV, Denjoy I, Hoorntje TM, et al: Absence of calsequestrin 2 causes severe forms of catecholaminergic polymorphic ventricular tachycardia. Circ Res 2002, 91: e21-26.
    • (2002) Circ Res , vol.91
    • Postma, A.V.1    Denjoy, I.2    Hoorntje, T.M.3
  • 101
    • 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, et al: 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 2001; 69: 1378-1384.
    • (2001) Am J Hum Genet , vol.69 , pp. 1378-1384
    • Lahat, H.1    Pras, E.2    Olender, T.3
  • 102
    • 5444269245 scopus 로고    scopus 로고
    • Calsequestrin mutant D307H exhibits depressed binding to its protein targets and a depressed response to calcium
    • Houle TD, Ram ML, Cala SE: Calsequestrin mutant D307H exhibits depressed binding to its protein targets and a depressed response to calcium. Cardiovasc Res 2004; 64: 227-233.
    • (2004) Cardiovasc Res , vol.64 , pp. 227-233
    • Houle, T.D.1    Ram, M.L.2    Cala, S.E.3
  • 103
    • 0035830828 scopus 로고    scopus 로고
    • Cardiac hypertrophy and impaired relaxation in transgenic mice overexpressing triadin 1
    • Kirchhefer U, Neumann J, Baba HA, et al: Cardiac hypertrophy and impaired relaxation in transgenic mice overexpressing triadin 1. J Biol Chem 2001; 276: 4142-4149.
    • (2001) J Biol Chem , vol.276 , pp. 4142-4149
    • Kirchhefer, U.1    Neumann, J.2    Baba, H.A.3
  • 104
    • 12144289713 scopus 로고    scopus 로고
    • 2+ handling and leads to a blunted contractile response to beta-adrenergic agonists
    • 2+ handling and leads to a blunted contractile response to beta-adrenergic agonists. Cardiovasc Res 2004; 62: 122-134.
    • (2004) Cardiovasc Res , vol.62 , pp. 122-134
    • Kirchhefer, U.1    Jones, L.R.2    Begrow, F.3
  • 105
    • 10744228510 scopus 로고    scopus 로고
    • Impaired relaxation in transgenic mice overexpressing junctin
    • Kirchhefer U, Neumann J, Bers DM, et al: Impaired relaxation in transgenic mice overexpressing junctin. Cardiovasc Res 2003; 59: 369-379.
    • (2003) Cardiovasc Res , vol.59 , pp. 369-379
    • Kirchhefer, U.1    Neumann, J.2    Bers, D.M.3
  • 106
    • 7244257742 scopus 로고    scopus 로고
    • Age-dependent biochemical and contractile properties in atrium of transgenic mice overexpressing junctin
    • Kirchhefer U, Baba HA, Hanske G, et al: Age-dependent biochemical and contractile properties in atrium of transgenic mice overexpressing junctin. Am J Physiol Heart Circ Physiol 2004; 287: H2216-2225.
    • (2004) Am J Physiol Heart Circ Physiol , vol.287
    • Kirchhefer, U.1    Baba, H.A.2    Hanske, G.3
  • 107
    • 0036674423 scopus 로고    scopus 로고
    • Cardiac remodeling and atrial fibrillation in transgenic mice overexpressing junctin
    • Hong CS, Cho MC, Kwak YG, et al: Cardiac remodeling and atrial fibrillation in transgenic mice overexpressing junctin. Faseb J 2002; 16: 1310-1312.
    • (2002) Faseb J , vol.16 , pp. 1310-1312
    • Hong, C.S.1    Cho, M.C.2    Kwak, Y.G.3
  • 108
    • 0032851553 scopus 로고    scopus 로고
    • Interaction of triadin with histidine-rich Ca(2+)-binding protein at the triadic junction in skeletal muscle fibers
    • Sacchetto R, Turcato F, Damiani E, et al: Interaction of triadin with histidine-rich Ca(2+)-binding protein at the triadic junction in skeletal muscle fibers. J Muscle Res Cell Motil 1999; 20: 403-415.
    • (1999) J Muscle Res Cell Motil , vol.20 , pp. 403-415
    • Sacchetto, R.1    Turcato, F.2    Damiani, E.3
  • 109
    • 0035930972 scopus 로고    scopus 로고
    • Ca(2+)-dependent interaction of triadin with histidine-rich Ca(2+)-binding protein carboxyl-terminal region
    • Sacchetto R, Damiani E, Turcato F, et al: Ca(2+)-dependent interaction of triadin with histidine-rich Ca(2+)-binding protein carboxyl-terminal region. Biochem Biophys Res Commun 2001; 289: 1125-1134.
    • (2001) Biochem Biophys Res Commun , vol.289 , pp. 1125-1134
    • Sacchetto, R.1    Damiani, E.2    Turcato, F.3
  • 110
    • 0025838068 scopus 로고
    • Subcellular fractionation to junctional sarcoplasmic reticulum and biochemical characterization of 170 kDa Ca(2+)- and low-density-lipoprotein-binding protein in rabbit skeletal muscle
    • Damiani E, Margreth A: Subcellular fractionation to junctional sarcoplasmic reticulum and biochemical characterization of 170 kDa Ca(2+)- and low-density-lipoprotein-binding protein in rabbit skeletal muscle. Biochem J 1991, 277 (Pt 3): 825-832.
    • (1991) Biochem J , vol.277 , Issue.PART 3 , pp. 825-832
    • Damiani, E.1    Margreth, A.2
  • 111
    • 0028906112 scopus 로고
    • Identification of triadin and of histidine-rich Ca(2+)-binding protein as substrates of 60 kDa calmodulin-dependent protein kinase in junctional terminal cisternae of sarcoplasmic reticulum of rabbit fast muscle
    • Damiani E, Picello E, Saggin L, et al: Identification of triadin and of histidine-rich Ca(2+)-binding protein as substrates of 60 kDa calmodulin-dependent protein kinase in junctional terminal cisternae of sarcoplasmic reticulum of rabbit fast muscle. Biochem Biophys Res Commun 1995; 209: 457-465.
    • (1995) Biochem Biophys Res Commun , vol.209 , pp. 457-465
    • Damiani, E.1    Picello, E.2    Saggin, L.3
  • 113
    • 0030583215 scopus 로고    scopus 로고
    • Modulation of the skeletal muscle ryanodine receptor by endogenous phosphorylation of 160/150-kDa proteins of the sarcoplasmic reticulum
    • Orr I, Shoshan-Barmatz V: Modulation of the skeletal muscle ryanodine receptor by endogenous phosphorylation of 160/150-kDa proteins of the sarcoplasmic reticulum. Biochim Biophys Acta 1996; 1283: 80-88.
    • (1996) Biochim Biophys Acta , vol.1283 , pp. 80-88
    • Orr, I.1    Shoshan-Barmatz, V.2
  • 114
    • 0030583220 scopus 로고    scopus 로고
    • The identification of the phosphorylated 150/160-kDa proteins of sarcoplasmic reticulum, their kinase and their association with the ryanodine receptor
    • Shoshan-Barmatz V, Orr I, Weil S, et al: The identification of the phosphorylated 150/160-kDa proteins of sarcoplasmic reticulum, their kinase and their association with the ryanodine receptor. Biochim Biophys Acta 1996; 1283: 89-100.
    • (1996) Biochim Biophys Acta , vol.1283 , pp. 89-100
    • Shoshan-Barmatz, V.1    Orr, I.2    Weil, S.3
  • 115
    • 0033527403 scopus 로고    scopus 로고
    • 2+ binding protein) resides in the lumen of sarcoplasmic reticulum as a multimer
    • 2+ binding protein) resides in the lumen of sarcoplasmic reticulum as a multimer. Biochem Biophys Res Commun 1999; 263: 667-671.
    • (1999) Biochem Biophys Res Commun , vol.263 , pp. 667-671
    • Suk, J.Y.1    Kim, Y.S.2    Park, W.J.3
  • 116
    • 0035955601 scopus 로고    scopus 로고
    • Interaction of HRC (histidine-rich Ca(2+)-binding protein) and triadin in the lumen of sarcoplasmic reticulum
    • Lee HG, Kang H, Kim DH, et al: Interaction of HRC (histidine-rich Ca(2+)-binding protein) and triadin in the lumen of sarcoplasmic reticulum. J Biol Chem 2001; 276: 39533-39538.
    • (2001) J Biol Chem , vol.276 , pp. 39533-39538
    • Lee, H.G.1    Kang, H.2    Kim, D.H.3
  • 117
    • 0024419447 scopus 로고
    • 2+-binding protein of sarcoplasmic reticulum that contains highly conserved repeated elements
    • 2+-binding protein of sarcoplasmic reticulum that contains highly conserved repeated elements. J Biol Chem 1989; 264: 18083-18090.
    • (1989) J Biol Chem , vol.264 , pp. 18083-18090
    • Hofmann, S.L.1    Goldstein, J.L.2    Orth, K.3
  • 118
    • 0037207513 scopus 로고    scopus 로고
    • Increased Ca(2+) storage capacity in the sarcoplasmic reticulum by overexpression of HRC (histidine-rich Ca(2+) binding protein)
    • Kim E, Shin DW, Hong CS, et al: Increased Ca(2+) storage capacity in the sarcoplasmic reticulum by overexpression of HRC (histidine-rich Ca(2+) binding protein). Biochem Biophys Res Commun 2003; 300: 192-196.
    • (2003) Biochem Biophys Res Commun , vol.300 , pp. 192-196
    • Kim, E.1    Shin, D.W.2    Hong, C.S.3
  • 119
    • 4744350102 scopus 로고    scopus 로고
    • Regulation of myocardial function by histidine-rich, calcium-binding protein
    • Fan GC, Gregory KN, Zhao W, et al: Regulation of myocardial function by histidine-rich, calcium-binding protein. Am J Physiol Heart Circ Physiol 2004, 287: H1705-1711.
    • (2004) Am J Physiol Heart Circ Physiol , vol.287
    • Fan, G.C.1    Gregory, K.N.2    Zhao, W.3
  • 120
    • 33646093733 scopus 로고    scopus 로고
    • Histidine-rich Ca binding protein: A regulator of sarcoplasmic reticulum calcium sequestration and cardiac function
    • Gregory KN, Ginsburg KS, Bodi I, et al: Histidine-rich Ca binding protein: a regulator of sarcoplasmic reticulum calcium sequestration and cardiac function. J Mol Cell Cardiol 2006; 40: 653-665.
    • (2006) J Mol Cell Cardiol , vol.40 , pp. 653-665
    • Gregory, K.N.1    Ginsburg, K.S.2    Bodi, I.3
  • 121
  • 122
    • 0026080381 scopus 로고
    • cDNA and genomic cloning of HRC, a human sarcoplasmic reticulum protein, and localization of the gene to human chromosome 19 and mouse chromosome 7
    • Hofmann SL, Topham M, Hsieh CL, et al: cDNA and genomic cloning of HRC, a human sarcoplasmic reticulum protein, and localization of the gene to human chromosome 19 and mouse chromosome 7. Genomics 1991; 9: 656-669.
    • (1991) Genomics , vol.9 , pp. 656-669
    • Hofmann, S.L.1    Topham, M.2    Hsieh, C.L.3
  • 123
    • 0029112853 scopus 로고
    • An isolated cardiac conduction disease maps to chromosome 19q
    • de Meeus A, Stephan E, Debrus S, et al: An isolated cardiac conduction disease maps to chromosome 19q. Circ Res 1995; 77: 735-740.
    • (1995) Circ Res , vol.77 , pp. 735-740
    • de Meeus, A.1    Stephan, E.2    Debrus, S.3


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