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Volumn 19, Issue 12, 2008, Pages 1332-1336

CaMKII and its role in cardiac arrhythmia: Molecular perspectives

Author keywords

Arrhythmia; CaMKII; Hypertrophy; Oxidation

Indexed keywords

BETA ADRENERGIC RECEPTOR BLOCKING AGENT; PROTEIN KINASE (CALCIUM,CALMODULIN) II; PROTEIN SERINE THREONINE KINASE INHIBITOR;

EID: 56749104358     PISSN: 10453873     EISSN: 15408167     Source Type: Journal    
DOI: 10.1111/j.1540-8167.2008.01295.x     Document Type: Review
Times cited : (35)

References (42)
  • 1
    • 33748636707 scopus 로고    scopus 로고
    • Sudden cardiac death: Better understanding of risks, mechanisms, and treatment
    • Lopshire JC, Zipes DP : Sudden cardiac death: Better understanding of risks, mechanisms, and treatment. Circulation 2006 114 : 1134 1136.
    • (2006) Circulation , vol.114 , pp. 1134-1136
    • Lopshire, J.C.1    Zipes, D.P.2
  • 3
    • 0034676762 scopus 로고    scopus 로고
    • Effect of dofetilide in patients with recent myocardial infarction and left-ventricular dysfunction: A randomised trial. Danish Investigations of Arrhythmia and Mortality on Dofetilide (DIAMOND) Study Group
    • Kober L, Bloch Thomsen PE, Moller M, Torp-Pedersen C, Carlsen J, Sandoe E, Egstrup K, Agner E, Videbaek J, Marchant B, Camm AJ : Effect of dofetilide in patients with recent myocardial infarction and left-ventricular dysfunction: A randomised trial. Danish Investigations of Arrhythmia and Mortality on Dofetilide (DIAMOND) Study Group. Lancet 2000 356 : 2052 2058.
    • (2000) Lancet , vol.356 , pp. 2052-2058
    • Kober, L.1    Bloch Thomsen, P.E.2    Moller, M.3    Torp-Pedersen, C.4    Carlsen, J.5    Sandoe, E.6    Egstrup, K.7    Agner, E.8    Videbaek, J.9    Marchant, B.10    Camm, A.J.11
  • 5
    • 28344445756 scopus 로고    scopus 로고
    • Structure of the autoinhibited kinase domain of CaMKII and SAXS analysis of the holoenzyme
    • Rosenberg OS, Deindl S, Sung RJ, Nairn AC, Kuriyan J : Structure of the autoinhibited kinase domain of CaMKII and SAXS analysis of the holoenzyme. Cell 2005 123 : 849 860.
    • (2005) Cell , vol.123 , pp. 849-860
    • Rosenberg, O.S.1    Deindl, S.2    Sung, R.J.3    Nairn, A.C.4    Kuriyan, J.5
  • 6
    • 0037097022 scopus 로고    scopus 로고
    • 2+/calmodulin- dependent protein kinase II
    • 2+/calmodulin-dependent protein kinase II. Biochem J 2002 364 : 593 611.
    • (2002) Biochem J , vol.364 , pp. 593-611
    • Hudmon, A.1    Schulman, H.2
  • 7
    • 0026718175 scopus 로고
    • Calmodulin trapping by calcium-calmodulin-dependent protein kinase
    • Meyer T, Hanson PI, Stryer L, Schulman H : Calmodulin trapping by calcium-calmodulin-dependent protein kinase. Science 1992 256 : 1199 1202.
    • (1992) Science , vol.256 , pp. 1199-1202
    • Meyer, T.1    Hanson, P.I.2    Stryer, L.3    Schulman, H.4
  • 9
    • 33746611555 scopus 로고    scopus 로고
    • Modulation of vascular smooth muscle signaling by reactive oxygen species
    • Lyle AN, Griendling KK : Modulation of vascular smooth muscle signaling by reactive oxygen species. Physiology 2006 21 : 269 280.
    • (2006) Physiology , vol.21 , pp. 269-280
    • Lyle, A.N.1    Griendling, K.K.2
  • 11
    • 0028918056 scopus 로고
    • Phosphorylation modulates the function of the calcium release channel of sarcoplasmic reticulum from cardiac muscle
    • Hain J, Onoue H, Mayrleitner M, Fleischer S, Schindler H : Phosphorylation modulates the function of the calcium release channel of sarcoplasmic reticulum from cardiac muscle. J Biol Chem 1995 270 : 2074 2081.
    • (1995) J Biol Chem , vol.270 , pp. 2074-2081
    • Hain, J.1    Onoue, H.2    Mayrleitner, M.3    Fleischer, S.4    Schindler, H.5
  • 12
    • 0025772161 scopus 로고
    • Unique phosphorylation site on the cardiac ryanodine receptor regulates calcium channel activity
    • Witcher DR, Kovacs RJ, Schulman H, Cefali DC, Jones LR : Unique phosphorylation site on the cardiac ryanodine receptor regulates calcium channel activity. J Biol Chem 1991 266 : 11144 11152.
    • (1991) J Biol Chem , vol.266 , pp. 11144-11152
    • Witcher, D.R.1    Kovacs, R.J.2    Schulman, H.3    Cefali, D.C.4    Jones, L.R.5
  • 13
    • 3042763171 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II phosphorylation regulates the cardiac ryanodine receptor
    • 2+/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.1    Lehnart, S.E.2    Reiken, S.R.3    Marks, A.R.4
  • 15
    • 0021023746 scopus 로고
    • Regulation of cardiac sarcoplasmic reticulum calcium transport by calcium-calmodulin-dependent phosphorylation
    • Davis BA, Schwartz A, Samaha FJ, Kranias EG : Regulation of cardiac sarcoplasmic reticulum calcium transport by calcium-calmodulin-dependent phosphorylation. J Biol Chem 1983 258 : 13587 13591.
    • (1983) J Biol Chem , vol.258 , pp. 13587-13591
    • Davis, B.A.1    Schwartz, A.2    Samaha, F.J.3    Kranias, E.G.4
  • 16
    • 0022921924 scopus 로고
    • Sequence analysis of phospholamban. Identification of phosphorylation sites and two major structural domains
    • Simmerman HK, Collins JH, Theibert JL, Wegener AD, Jones LR : Sequence analysis of phospholamban. Identification of phosphorylation sites and two major structural domains. J Biol Chem 1986 261 : 13333 13341.
    • (1986) J Biol Chem , vol.261 , pp. 13333-13341
    • Simmerman, H.K.1    Collins, J.H.2    Theibert, J.L.3    Wegener, A.D.4    Jones, L.R.5
  • 17
    • 0034509410 scopus 로고    scopus 로고
    • Phospholamban and cardiac contractile function
    • Brittsan AG, Kranias EG : Phospholamban and cardiac contractile function. J Mol Cell Card 2000 32 : 2131 2139.
    • (2000) J Mol Cell Card , vol.32 , pp. 2131-2139
    • Brittsan, A.G.1    Kranias, E.G.2
  • 19
    • 33745614665 scopus 로고    scopus 로고
    • 2+ release from IP3-sensitive stores and calcium/calmodulin kinase II phosphorylation of the alpha1 subunit EF hand
    • 2+ release from IP3-sensitive stores and calcium/calmodulin kinase II phosphorylation of the alpha1 subunit EF hand. J Neurosci 2006 26 : 6259 62568.
    • (2006) J Neurosci , vol.26 , pp. 6259-62568
    • Gao, L.1    Blair, L.A.2    Salinas, G.D.3    Needleman, L.A.4    Marshall, J.5
  • 20
    • 33748741562 scopus 로고    scopus 로고
    • Calmodulin kinase II is involved in voltage-dependent facilitation of the L-type Cav1.2 calcium channel: Identification of the phosphorylation sites
    • Lee TS, Karl R, Moosmang S, Lenhardt P, Klugbauer N, Hofmann F, Kleppisch T, Welling A : Calmodulin kinase II is involved in voltage-dependent facilitation of the L-type Cav1.2 calcium channel: Identification of the phosphorylation sites. J Biol Chem 2006 281 : 25560 25567.
    • (2006) J Biol Chem , vol.281 , pp. 25560-25567
    • Lee, T.S.1    Karl, R.2    Moosmang, S.3    Lenhardt, P.4    Klugbauer, N.5    Hofmann, F.6    Kleppisch, T.7    Welling, A.8
  • 24
    • 0038643573 scopus 로고    scopus 로고
    • The deltaC isoform of CaMKII is activated in cardiac hypertrophy and induces dilated cardiomyopathy and heart failure
    • Zhang T, Maier LS, Dalton ND, Miyamoto S, Ross J Jr., Bers DM, Brown JH : The deltaC isoform of CaMKII is activated in cardiac hypertrophy and induces dilated cardiomyopathy and heart failure. Circ Res 2003 92 : 912 919.
    • (2003) Circ Res , vol.92 , pp. 912-919
    • Zhang, T.1    Maier, L.S.2    Dalton, N.D.3    Miyamoto, S.4    Ross Jr., J.5    Bers, D.M.6    Brown, J.H.7
  • 28
    • 0033781028 scopus 로고    scopus 로고
    • Calmodulin kinase determines calcium-dependent facilitation of L-type calcium channels
    • Dzhura I, Wu Y, Colbran RJ, Balser JR, Anderson ME : Calmodulin kinase determines calcium-dependent facilitation of L-type calcium channels. Nat Cell Biol 2000 2 : 173 177.
    • (2000) Nat Cell Biol , vol.2 , pp. 173-177
    • Dzhura, I.1    Wu, Y.2    Colbran, R.J.3    Balser, J.R.4    Anderson, M.E.5
  • 29
    • 0036702654 scopus 로고    scopus 로고
    • Frequency-dependent acceleration of relaxation in the heart depends on CaMKII, but not phospholamban
    • DeSantiago J, Maier LS, Bers DM : Frequency-dependent acceleration of relaxation in the heart depends on CaMKII, but not phospholamban. J Mol Cell Cardiol 2002 34 : 975 984.
    • (2002) J Mol Cell Cardiol , vol.34 , pp. 975-984
    • Desantiago, J.1    Maier, L.S.2    Bers, D.M.3
  • 30
    • 33845624704 scopus 로고    scopus 로고
    • CaMKII inhibition targeted to the sarcoplasmic reticulum inhibits frequency-dependent acceleration of relaxation and calcium current facilitation
    • Picht E, DeSantiago J, Huke S, Kaetzel MA, Dedman JR, Bers DM : CaMKII inhibition targeted to the sarcoplasmic reticulum inhibits frequency-dependent acceleration of relaxation and calcium current facilitation. J Mol Cell Cardiol 2007 42 : 196 205.
    • (2007) J Mol Cell Cardiol , vol.42 , pp. 196-205
    • Picht, E.1    Desantiago, J.2    Huke, S.3    Kaetzel, M.A.4    Dedman, J.R.5    Bers, D.M.6
  • 36
  • 37
    • 0030016356 scopus 로고    scopus 로고
    • Dynamic modulation of excitation-contraction coupling by protein phosphatases in rat ventricular myocytes
    • duBell WH, Lederer WJ, Rogers TB : Dynamic modulation of excitation-contraction coupling by protein phosphatases in rat ventricular myocytes. J Physiol 1996 493 : 793 800.
    • (1996) J Physiol , vol.493 , pp. 793-800
    • Dubell, W.H.1    Lederer, W.J.2    Rogers, T.B.3
  • 40
    • 34250689781 scopus 로고    scopus 로고
    • Molecular and electrophysiological bases of catecholaminergic polymorphic ventricular tachycardia
    • Mohamed U, Napolitano C, Priori SG : Molecular and electrophysiological bases of catecholaminergic polymorphic ventricular tachycardia. J Cardiovasc Electrophysiol 2007 18 : 791 797.
    • (2007) J Cardiovasc Electrophysiol , vol.18 , pp. 791-797
    • Mohamed, U.1    Napolitano, C.2    Priori, S.G.3
  • 41
    • 0029080486 scopus 로고
    • Modulation of cardiac ryanodine receptors of swine and rabbit by a phosphorylation-dephosphorylation mechanism
    • Lokuta AJ, Rogers TB, Lederer WJ, Valdivia HH : Modulation of cardiac ryanodine receptors of swine and rabbit by a phosphorylation-dephosphorylation mechanism. J Physiol 1995 487 (Pt 3 609 622.
    • (1995) J Physiol , vol.487 , Issue.3 , pp. 609-622
    • Lokuta, A.J.1    Rogers, T.B.2    Lederer, W.J.3    Valdivia, H.H.4
  • 42
    • 0035957010 scopus 로고    scopus 로고
    • Calmodulin kinase is a molecular switch for cardiac excitation- contraction coupling
    • Wu Y, Colbran RJ, Anderson ME : Calmodulin kinase is a molecular switch for cardiac excitation-contraction coupling. Proc Natl Acad Sci USA 2001 98 : 2877 2881.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2877-2881
    • Wu, Y.1    Colbran, R.J.2    Anderson, M.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.