메뉴 건너뛰기




Volumn 55, Issue 1, 2014, Pages 17-23

Genetic modulation of the SERCA activity does not affect the Ca2+ leak from the cardiac sarcoplasmic reticulum

Author keywords

Aequorin; Cardiac muscle; Excitation contraction coupling; Transgenic mouse

Indexed keywords

CALCIUM ION; REGULATOR PROTEIN; SARCOLIPIN; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; UNCLASSIFIED DRUG;

EID: 84896724996     PISSN: 01434160     EISSN: 15321991     Source Type: Journal    
DOI: 10.1016/j.ceca.2013.10.005     Document Type: Article
Times cited : (6)

References (42)
  • 1
    • 0037049977 scopus 로고    scopus 로고
    • Cardiac excitation-contraction coupling
    • Bers D.M. Cardiac excitation-contraction coupling. Nature 2002, 415:198-205.
    • (2002) Nature , vol.415 , pp. 198-205
    • Bers, D.M.1
  • 2
    • 17944398302 scopus 로고
    • Calcium-induced release of calcium from the cardiac sarcoplasmic reticulum
    • Fabiato A. Calcium-induced release of calcium from the cardiac sarcoplasmic reticulum. Am. J. Physiol. 1983, 245:C1-C14.
    • (1983) Am. J. Physiol. , vol.245
    • Fabiato, A.1
  • 4
    • 0034640113 scopus 로고    scopus 로고
    • PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts
    • Marx S.O., 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
  • 6
    • 77955887705 scopus 로고    scopus 로고
    • Genetic background affects function and intracellular calcium regulation of mouse hearts
    • Shah A.P., Siedlecka U., Gandhi A., et al. Genetic background affects function and intracellular calcium regulation of mouse hearts. Cardiovasc. Res. 2010, 87:683-693.
    • (2010) Cardiovasc. Res. , vol.87 , pp. 683-693
    • Shah, A.P.1    Siedlecka, U.2    Gandhi, A.3
  • 7
    • 31444444347 scopus 로고    scopus 로고
    • Ca2+/calmodulin-dependent protein kinase modulates cardiac ryanodine receptor phosphorylation and sarcoplasmic reticulum Ca2+ leak in heart failure
    • Ai X., Curran J.W., Shannon T.R., Bers D.M., Pogwizd S.M. Ca2+/calmodulin-dependent protein kinase modulates cardiac ryanodine receptor phosphorylation and sarcoplasmic reticulum Ca2+ leak in heart failure. Circ. Res. 2005, 97:1314-1322.
    • (2005) Circ. Res. , vol.97 , pp. 1314-1322
    • Ai, X.1    Curran, J.W.2    Shannon, T.R.3    Bers, D.M.4    Pogwizd, S.M.5
  • 8
    • 84859886974 scopus 로고    scopus 로고
    • Elementary calcium release events from the sarcoplasmic reticulum in the heart
    • Brochet D.X., Yang D., Cheng H., Lederer W.J. Elementary calcium release events from the sarcoplasmic reticulum in the heart. Adv. Exp. Med. Biol. 2012, 740:499-509.
    • (2012) Adv. Exp. Med. Biol. , vol.740 , pp. 499-509
    • Brochet, D.X.1    Yang, D.2    Cheng, H.3    Lederer, W.J.4
  • 9
    • 0141817953 scopus 로고    scopus 로고
    • Sorcin inhibits calcium release and modulates excitation-contraction coupling in the heart
    • Farrell E.F., Antaramian A., Rueda A., Gómez A.M., Valdivia H.H. Sorcin inhibits calcium release and modulates excitation-contraction coupling in the heart. J. Biol. Chem. 2003, 278:34660-34666.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34660-34666
    • Farrell, E.F.1    Antaramian, A.2    Rueda, A.3    Gómez, A.M.4    Valdivia, H.H.5
  • 10
    • 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
  • 12
    • 34250891879 scopus 로고    scopus 로고
    • Intracellular mechanism of the negative inotropic effect induced by alpha1-adrenoceptor stimulation in mouse myocardium
    • Hirano S., Kusakari Y., O-Uchi J., et al. Intracellular mechanism of the negative inotropic effect induced by alpha1-adrenoceptor stimulation in mouse myocardium. J. Physiol. Sci. 2006, 56:297-304.
    • (2006) J. Physiol. Sci. , vol.56 , pp. 297-304
    • Hirano, S.1    Kusakari, Y.2    O-Uchi, J.3
  • 13
    • 0027526474 scopus 로고
    • 2+ transients by beta- and muscarinic receptor stimulation in ferret myocardium
    • 2+ transients by beta- and muscarinic receptor stimulation in ferret myocardium. J. Physiol. 1993, 461:167-184.
    • (1993) J. Physiol. , vol.461 , pp. 167-184
    • Hongo, K.1    Tanaka, E.2    Kurihara, S.3
  • 14
    • 0028133162 scopus 로고
    • Measurement of sarcoplasmic reticulum calcium content in skinned mammalian cardiac muscle
    • Kawai M., Konishi M. Measurement of sarcoplasmic reticulum calcium content in skinned mammalian cardiac muscle. Cell Calcium 1994, 16:123-136.
    • (1994) Cell Calcium , vol.16 , pp. 123-136
    • Kawai, M.1    Konishi, M.2
  • 15
    • 67649114167 scopus 로고    scopus 로고
    • Moderate heart dysfunction in mice with inducible cardiomyocyte-specific excision of the Serca2 gene
    • Andersson K.B., Birkeland J.A., Finsen A.V., et al. Moderate heart dysfunction in mice with inducible cardiomyocyte-specific excision of the Serca2 gene. J. Mol. Cell. Cardiol. 2009, 47:180-187.
    • (2009) J. Mol. Cell. Cardiol. , vol.47 , pp. 180-187
    • Andersson, K.B.1    Birkeland, J.A.2    Finsen, A.V.3
  • 16
    • 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 N.R., MacLennan D.H., Barton P., Periasamy M. 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    Barton, P.4    Periasamy, M.5
  • 17
    • 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
  • 18
    • 0028882650 scopus 로고
    • Unchanged protein levels of SERCA II and phospholamban but reduced Ca2+ uptake and Ca(2+)-ATPase activity of cardiac sarcoplasmic reticulum from dilated cardiomyopathy patients compared with patients with nonfailing hearts
    • Schwinger R.H., Böhm M., Schmidt U., et al. Unchanged protein levels of SERCA II and phospholamban but reduced Ca2+ 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    Böhm, M.2    Schmidt, U.3
  • 19
    • 0035916903 scopus 로고    scopus 로고
    • Decreased sarcoplasmic reticulum calcium content is responsible for defective excitation-contraction coupling in canine heart failure
    • Hobai I.A., O'Rourke B. Decreased sarcoplasmic reticulum calcium content is responsible for defective excitation-contraction coupling in canine heart failure. Circulation 2001, 103:1577-1584.
    • (2001) Circulation , vol.103 , pp. 1577-1584
    • Hobai, I.A.1    O'Rourke, B.2
  • 20
    • 0344284562 scopus 로고    scopus 로고
    • Cellular basis of abnormal calcium transients of failing human ventricular myocytes
    • Piacentino V., Weber C.R., Chen X., et al. Cellular basis of abnormal calcium transients of failing human ventricular myocytes. Circ. Res. 2003, 92:651-658.
    • (2003) Circ. Res. , vol.92 , pp. 651-658
    • Piacentino, V.1    Weber, C.R.2    Chen, X.3
  • 21
    • 12944332074 scopus 로고    scopus 로고
    • Adenoviral gene transfer of SERCA2a improves left-ventricular function in aortic-banded rats in transition to heart failure
    • Miyamoto M.I., 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
  • 22
    • 40649106736 scopus 로고    scopus 로고
    • Reversal of cardiac dysfunction after long-term expression of SERCA2a by gene transfer in a pre-clinical model of heart failure
    • Kawase Y., Ly H.Q., Prunier F., et al. Reversal of cardiac dysfunction after long-term expression of SERCA2a by gene transfer in a pre-clinical model of heart failure. J. Am. Coll. Cardiol. 2008, 51:1112-1119.
    • (2008) J. Am. Coll. Cardiol. , vol.51 , pp. 1112-1119
    • Kawase, Y.1    Ly, H.Q.2    Prunier, F.3
  • 23
    • 62649133817 scopus 로고    scopus 로고
    • Calcium upregulation by percutaneous administration of gene therapy in cardiac disease (CUPID Trial), a first-in-human phase 1/2 clinical trial
    • Jaski B.E., Jessup M.L., Mancini D.M., et al. Calcium upregulation by percutaneous administration of gene therapy in cardiac disease (CUPID Trial), a first-in-human phase 1/2 clinical trial. J. Card. Fail. 2009, 15:171-181.
    • (2009) J. Card. Fail. , vol.15 , pp. 171-181
    • Jaski, B.E.1    Jessup, M.L.2    Mancini, D.M.3
  • 24
    • 0342546511 scopus 로고    scopus 로고
    • Modulation of CICR has no maintained effect on systolic Ca2+: simultaneous measurements of sarcoplasmic reticulum and sarcolemmal Ca2+ fluxes in rat ventricular myocytes
    • Trafford A.W., Díaz M.E., Sibbring G.C., Eisner D.A. Modulation of CICR has no maintained effect on systolic Ca2+: simultaneous measurements of sarcoplasmic reticulum and sarcolemmal Ca2+ fluxes in rat ventricular myocytes. J. Physiol. 2000, 522:259-270.
    • (2000) J. Physiol. , vol.522 , pp. 259-270
    • Trafford, A.W.1    Díaz, M.E.2    Sibbring, G.C.3    Eisner, D.A.4
  • 25
    • 85047691575 scopus 로고    scopus 로고
    • Altered intracellular Ca2+ handling in heart failure
    • Yano M., Ikeda Y., Matsuzaki M. Altered intracellular Ca2+ handling in heart failure. J. Clin. Invest. 2005, 115:556-564.
    • (2005) J. Clin. Invest. , vol.115 , pp. 556-564
    • Yano, M.1    Ikeda, Y.2    Matsuzaki, M.3
  • 27
    • 3042763171 scopus 로고    scopus 로고
    • Ca2+/calmodulin-dependent protein kinase II phosphorylation regulates the cardiac ryanodine receptor
    • Wehrens X.H.T., Lehnart S.E., Reiken S.R., Marks A.R. Ca2+/calmodulin-dependent protein kinase II phosphorylation regulates the cardiac ryanodine receptor. Circ. Res. 2004, 94:e61-e70.
    • (2004) Circ. Res. , vol.94
    • Wehrens, X.H.T.1    Lehnart, S.E.2    Reiken, S.R.3    Marks, A.R.4
  • 28
    • 33646771721 scopus 로고    scopus 로고
    • Ser-2030, but not Ser-2808, is the major phosphorylation site in cardiac ryanodine receptors responding to protein kinase A activation upon β-adrenergic stimulation in normal and failing hearts
    • Xiao B., Zhong G., Obayashi M., et al. Ser-2030, but not Ser-2808, is the major phosphorylation site in cardiac ryanodine receptors responding to protein kinase A activation upon β-adrenergic stimulation in normal and failing hearts. Biochem. J. 2006, 396:7-16.
    • (2006) Biochem. J. , vol.396 , pp. 7-16
    • Xiao, B.1    Zhong, G.2    Obayashi, M.3
  • 29
    • 79957481291 scopus 로고    scopus 로고
    • The relationship between arrhythmogenesis and impaired contractility in heart failure: role of altered ryanodine receptor function
    • Belevych A.E., Terentyev D., Terentyeva R., et al. The relationship between arrhythmogenesis and impaired contractility in heart failure: role of altered ryanodine receptor function. Cardiovasc. Res. 2011, 90:493-502.
    • (2011) Cardiovasc. Res. , vol.90 , pp. 493-502
    • Belevych, A.E.1    Terentyev, D.2    Terentyeva, R.3
  • 30
    • 84861591191 scopus 로고    scopus 로고
    • Role of RyR2 phosphorylation at S2814 during heart failure progression
    • Respress J.L., van Oort R.J., Li N., et al. Role of RyR2 phosphorylation at S2814 during heart failure progression. Circ. Res. 2012, 110:1474-1483.
    • (2012) Circ. Res. , vol.110 , pp. 1474-1483
    • Respress, J.L.1    van Oort, R.J.2    Li, N.3
  • 31
    • 59449094232 scopus 로고    scopus 로고
    • Epac and phospholipase Cepsilon regulate Ca2+ release in the heart by activation of protein kinase Cepsilon and calcium-calmodulin kinase II
    • Oestreich E.A., Malik S., Goonasekera S.A., et al. Epac and phospholipase Cepsilon regulate Ca2+ release in the heart by activation of protein kinase Cepsilon and calcium-calmodulin kinase II. J. Biol. Chem. 2009, 284:1514-1522.
    • (2009) J. Biol. Chem. , vol.284 , pp. 1514-1522
    • Oestreich, E.A.1    Malik, S.2    Goonasekera, S.A.3
  • 32
    • 74149088545 scopus 로고    scopus 로고
    • β-Adrenergic receptor signaling in the heart: role of CaMKII
    • Grimm M., Brown J.H. β-Adrenergic receptor signaling in the heart: role of CaMKII. J. Mol. Cell. Cardiol. 2010, 48:322-330.
    • (2010) J. Mol. Cell. Cardiol. , vol.48 , pp. 322-330
    • Grimm, M.1    Brown, J.H.2
  • 33
    • 84874472807 scopus 로고    scopus 로고
    • Epac2 mediates cardiac β1-adrenergic-dependent sarcoplasmic reticulum Ca2+ leak and arrhythmia
    • Pereira L., Cheng H., Lao D.H., et al. Epac2 mediates cardiac β1-adrenergic-dependent sarcoplasmic reticulum Ca2+ leak and arrhythmia. Circulation 2013, 127:913-922.
    • (2013) Circulation , vol.127 , pp. 913-922
    • Pereira, L.1    Cheng, H.2    Lao, D.H.3
  • 34
    • 84883206388 scopus 로고    scopus 로고
    • Ca2+/calmodulin-dependent protein kinase II and protein kinase A differentially regulate sarcoplasmic reticulum Ca2+ leak in human cardiac pathology
    • Fischer T.H., Herting J., Tirilomis T., et al. Ca2+/calmodulin-dependent protein kinase II and protein kinase A differentially regulate sarcoplasmic reticulum Ca2+ leak in human cardiac pathology. Circulation 2013, 128:970-981.
    • (2013) Circulation , vol.128 , pp. 970-981
    • Fischer, T.H.1    Herting, J.2    Tirilomis, T.3
  • 35
    • 80052342152 scopus 로고    scopus 로고
    • SERCA2a gene transfer decreases sarcoplasmic reticulum calcium leak and reduces ventricular arrhythmias in a model of chronic heart failure
    • Lyon A.R., Bannister M.L., Collins T.T., et al. SERCA2a gene transfer decreases sarcoplasmic reticulum calcium leak and reduces ventricular arrhythmias in a model of chronic heart failure. Circ. Arrhythm. Electrophysiol. 2011, 4:362-372.
    • (2011) Circ. Arrhythm. Electrophysiol. , vol.4 , pp. 362-372
    • Lyon, A.R.1    Bannister, M.L.2    Collins, T.T.3
  • 36
    • 84867764589 scopus 로고    scopus 로고
    • Targeted sarcoplasmic reticulum Ca2+ ATPase 2a gene delivery to restore electrical stability in the failing heart
    • Cutler M.J., Wan X., Plummer B.N., et al. Targeted sarcoplasmic reticulum Ca2+ ATPase 2a gene delivery to restore electrical stability in the failing heart. Circulation 2012, 126:2095-2104.
    • (2012) Circulation , vol.126 , pp. 2095-2104
    • Cutler, M.J.1    Wan, X.2    Plummer, B.N.3
  • 37
    • 79961032369 scopus 로고    scopus 로고
    • Calcium upregulation by percutaneous administration of gene therapy in cardiac disease (CUPID): a phase 2 trial of intracoronary gene therapy of sarcoplasmic reticulum Ca2+-ATPase in patients with advanced heart failure
    • Jessup M., Greenberg B., Mancini D., et al. Calcium upregulation by percutaneous administration of gene therapy in cardiac disease (CUPID): a phase 2 trial of intracoronary gene therapy of sarcoplasmic reticulum Ca2+-ATPase in patients with advanced heart failure. Circulation 2011, 124:304-313.
    • (2011) Circulation , vol.124 , pp. 304-313
    • Jessup, M.1    Greenberg, B.2    Mancini, D.3
  • 38
    • 25144457698 scopus 로고    scopus 로고
    • The three-dimensional solution structure of Ca(2+)-bound S100A1 as determined by NMR spectroscopy
    • Wright N.T., Varney K.M., Ellis K.C., et al. The three-dimensional solution structure of Ca(2+)-bound S100A1 as determined by NMR spectroscopy. J. Mol. Biol. 2005, 353:410-426.
    • (2005) J. Mol. Biol. , vol.353 , pp. 410-426
    • Wright, N.T.1    Varney, K.M.2    Ellis, K.C.3
  • 40
    • 79953693561 scopus 로고    scopus 로고
    • S100A1 gene therapy for heart failure: a novel strategy on the verge of clinical trials
    • Rohde D., Brinks H., Ritterhoff J., Qui G., Ren S., Most P. S100A1 gene therapy for heart failure: a novel strategy on the verge of clinical trials. J. Mol. Cell. Cardiol. 2011, 50:777-784.
    • (2011) J. Mol. Cell. Cardiol. , vol.50 , pp. 777-784
    • Rohde, D.1    Brinks, H.2    Ritterhoff, J.3    Qui, G.4    Ren, S.5    Most, P.6
  • 41
    • 0035860835 scopus 로고    scopus 로고
    • Effects of cytosolic ATP on Ca(2+) sparks and SR Ca(2+) content in permeabilized cardiac myocytes
    • Yang Z., Steele D.S. Effects of cytosolic ATP on Ca(2+) sparks and SR Ca(2+) content in permeabilized cardiac myocytes. Circ. Res. 2001, 89:526-533.
    • (2001) Circ. Res. , vol.89 , pp. 526-533
    • Yang, Z.1    Steele, D.S.2
  • 42
    • 0035395972 scopus 로고    scopus 로고
    • A comparison of the effects of ATP and tetracaine on spontaneous Ca(2+) release from rat permeabilised cardiac myocytes
    • Smith G.L., O'Neill S.C. A comparison of the effects of ATP and tetracaine on spontaneous Ca(2+) release from rat permeabilised cardiac myocytes. J. Physiol. 2001, 534:37-47.
    • (2001) J. Physiol. , vol.534 , pp. 37-47
    • Smith, G.L.1    O'Neill, S.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.