메뉴 건너뛰기




Volumn 18, Issue 9, 2013, Pages 1063-1077

Redox regulation of sodium and calcium handling

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); CALCIUM; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CYCLIC AMP DEPENDENT PROTEIN KINASE; GELATINASE B; ION CHANNEL; PHOSPHATASE 1 INHIBITOR 1; PHOSPHOLAMBAN; PHOSPHOLEMMAN; PROTEIN; PROTEIN KINASE C; PROTEIN SERINE THREONINE KINASE; REACTIVE OXYGEN METABOLITE; RYANODINE RECEPTOR 2; SODIUM; SODIUM CALCIUM EXCHANGE PROTEIN; SODIUM CHANNEL NAV1.5; UNCLASSIFIED DRUG; VOLTAGE GATED CALCIUM CHANNEL; VOLTAGE GATED SODIUM CHANNEL;

EID: 84874093502     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2012.4818     Document Type: Review
Times cited : (133)

References (154)
  • 1
    • 0024401147 scopus 로고
    • Critical sulfhydryls regulate calcium release from sarcoplasmic reticulum
    • Abramson JJ and Salama G. Critical sulfhydryls regulate calcium release from sarcoplasmic reticulum. J Bioenerg Biomembr 21: 283-294, 1989.
    • (1989) J Bioenerg Biomembr , vol.21 , pp. 283-294
    • Abramson, J.J.1    Salama, G.2
  • 2
    • 77951281040 scopus 로고    scopus 로고
    • Upregulation of Nox4 by hypertrophic stimuli promotes apoptosis and mitochondrial dysfunction in cardiac myo-cytes
    • Ago T, Kuroda J, Pain J, Fu C, Li H, and Sadoshima J. Upregulation of Nox4 by hypertrophic stimuli promotes apoptosis and mitochondrial dysfunction in cardiac myo-cytes. Circ Res 106: 1253-1264, 2010.
    • (2010) Circ Res , vol.106 , pp. 1253-1264
    • Ago, T.1    Kuroda, J.2    Pain, J.3    Fu, C.4    Li, H.5    Sadoshima, J.6
  • 3
    • 31044442642 scopus 로고    scopus 로고
    • The mitochondrial origin of postischemic arrhythmias
    • Akar FG, Aon MA, Tomaselli GF, and O'Rourke B. The mitochondrial origin of postischemic arrhythmias. J Clin Invest 115: 3527-3535, 2005.
    • (2005) J Clin Invest , vol.115 , pp. 3527-3535
    • Akar, F.G.1    Aon, M.A.2    Tomaselli, G.F.3    O'Rourke, B.4
  • 5
    • 63849247206 scopus 로고    scopus 로고
    • Redox sensitive signaling pathways in cardiac remodeling, hypertrophy and failure
    • Anilkumar N, Sirker A, and Shah AM. Redox sensitive signaling pathways in cardiac remodeling, hypertrophy and failure. Front Biosci 14: 3168-3187, 2009.
    • (2009) Front Biosci , vol.14 , pp. 3168-3187
    • Anilkumar, N.1    Sirker, A.2    Shah, A.M.3
  • 6
    • 0032575571 scopus 로고    scopus 로고
    • Effects of hydroxyl radical and sulfhydryl reagents on the open probability of the purified cardiac ryanodine receptor channel incorporated into planar lipid bilayers
    • Anzai K, Ogawa K, Kuniyasu A, Ozawa T, Yamamoto H, and Nakayama H. Effects of hydroxyl radical and sulfhydryl reagents on the open probability of the purified cardiac ryanodine receptor channel incorporated into planar lipid bilayers. Biochem Biophys Res Comm 249: 938-942, 1998.
    • (1998) Biochem Biophys Res Comm , vol.249 , pp. 938-942
    • Anzai, K.1    Ogawa, K.2    Kuniyasu, A.3    Ozawa, T.4    Yamamoto, H.5    Nakayama, H.6
  • 7
    • 33845360700 scopus 로고    scopus 로고
    • The fundamental organization of cardiac mitochondria as a network of coupled oscillators
    • Aon MA, Cortassa S, and O'Rourke B. The fundamental organization of cardiac mitochondria as a network of coupled oscillators. Biophys J 91: 4317-4327, 2006.
    • (2006) Biophys J , vol.91 , pp. 4317-4327
    • Aon, M.A.1    Cortassa, S.2    O'Rourke, B.3
  • 8
    • 0242582202 scopus 로고    scopus 로고
    • Synchronized whole cell oscillations in mitochondrial metabolism triggered by a local release of reactive oxygen species in cardiac myocytes
    • Aon MA, Cortassa S, Marban E, and O'Rourke B. Synchronized whole cell oscillations in mitochondrial metabolism triggered by a local release of reactive oxygen species in cardiac myocytes. J Biol Chem 278: 44735-44744, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 44735-44744
    • Aon, M.A.1    Cortassa, S.2    Marban, E.3    O'Rourke, B.4
  • 9
    • 0037488534 scopus 로고    scopus 로고
    • Role of sodium-calcium exchanger in modulating the action potential of ventricular myocytes from normal and failing hearts
    • Armoundas AA, Hobai IA, Tomaselli GF, Winslow RL, and O'Rourke B. Role of sodium-calcium exchanger in modulating the action potential of ventricular myocytes from normal and failing hearts. Circ Res 93: 46-53, 2003.
    • (2003) Circ Res , vol.93 , pp. 46-53
    • Armoundas, A.A.1    Hobai, I.A.2    Tomaselli, G.F.3    Winslow, R.L.4    O'Rourke, B.5
  • 15
    • 0024271839 scopus 로고
    • Abnormal electrical-activity induced by free-radical generating systems in isolated cardiocytes
    • Barrington P, Meier C, and Weglicki W. Abnormal electrical-activity induced by free-radical generating systems in isolated cardiocytes. J Mol Cell Cardiol 20: 1163-1178, 1988.
    • (1988) J Mol Cell Cardiol , vol.20 , pp. 1163-1178
    • Barrington, P.1    Meier, C.2    Weglicki, W.3
  • 16
    • 34547578672 scopus 로고    scopus 로고
    • Augmented protein kinase C-a-induced myofilament protein phosphorylation contributes-myofilament dysfunction in experimental congestive heart failure
    • Belin RJ, Sumandea MP, Allen EJ, Schoenfelt K, Wang H, Solaro RJ, and de Tombe PP. Augmented protein kinase C-a-induced myofilament protein phosphorylation contributes to myofilament dysfunction in experimental congestive heart failure. Circ Res 101: 195-204, 2007.
    • (2007) Circ Res , vol.101 , pp. 195-204
    • Belin, R.J.1    Sumandea, M.P.2    Allen, E.J.3    Schoenfelt, K.4    Wang, H.5    Solaro, R.J.6    De Tombe, P.P.7
  • 18
    • 33845296446 scopus 로고    scopus 로고
    • Altered cardiac myocyte Ca regulation in heart failure
    • Bers DM. Altered cardiac myocyte Ca regulation In heart failure. Physiology (Bethesda) 21: 380-387, 2006.
    • (2006) Physiology (Bethesda) , vol.21 , pp. 380-387
    • Bers, D.M.1
  • 20
    • 0027522647 scopus 로고
    • Characterization of protein kinase C isotype expression in adult rat heart. Protein kinase C-epsilon is a major isotype present, and it is activated by phorbol esters, epinephrine, and en-dothelin
    • Bogoyevitch MA, Parker PJ, and Sugden PH. Characterization of protein kinase C isotype expression in adult rat heart. Protein kinase C-epsilon is a major isotype present, and it is activated by phorbol esters, epinephrine, and en-dothelin. Circ Res 72: 757-767, 1993.
    • (1993) Circ Res , vol.72 , pp. 757-767
    • Bogoyevitch, M.A.1    Parker, P.J.2    Sugden, P.H.3
  • 24
    • 33746922414 scopus 로고    scopus 로고
    • Oxidant-induced activation of type i protein kinase A is mediated by RI subunit interprotein disulfide bond formation
    • Brennan J, Bardswell S, Burgoyne J, Fuller W, Schroder E, Wait R, Begum S, Kentish J, and Eaton P. Oxidant-induced activation of type I protein kinase A is mediated by RI subunit interprotein disulfide bond formation. J Biol Chem 281: 21827-21836, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 21827-21836
    • Brennan, J.1    Bardswell, S.2    Burgoyne, J.3    Fuller, W.4    Schroder, E.5    Wait, R.6    Begum, S.7    Kentish, J.8    Eaton, P.9
  • 26
    • 0029743817 scopus 로고    scopus 로고
    • Redox modulation of L-type calcium channels in ferret ventricular myocytes. Dual mechanism regulation by nitric oxide and S-nitrosothiols
    • Campbell DL, Stamler JS, and Strauss HC. Redox modulation of L-type calcium channels in ferret ventricular myocytes. Dual mechanism regulation by nitric oxide and S-nitrosothiols. J Gen Physiol 108: 277-293, 1996.
    • (1996) J Gen Physiol , vol.108 , pp. 277-293
    • Campbell, D.L.1    Stamler, J.S.2    Strauss, H.C.3
  • 30
    • 36749009773 scopus 로고    scopus 로고
    • The roles of PKCdelta and epsilon isoenzymes in the regulation of myocardial ischaemia/reperfusion injury
    • Churchill EN and Mochly-Rosen D. The roles of PKCdelta and epsilon isoenzymes in the regulation of myocardial ischaemia/reperfusion injury. Biochem Soc Trans 35: 1040-1042, 2007.
    • (2007) Biochem Soc Trans , vol.35 , pp. 1040-1042
    • Churchill, E.N.1    Mochly-Rosen, D.2
  • 31
    • 0026642066 scopus 로고
    • Effects of oxygen free radicals on isolated cardiac myocytes from guinea-pig ventricle: Elec-trophysiological studies
    • Coetzee WA and Opie LH. Effects of oxygen free radicals on isolated cardiac myocytes from guinea-pig ventricle: Elec-trophysiological studies. J Mol Cell Cardiol 24: 651-663, 1992.
    • (1992) J Mol Cell Cardiol , vol.24 , pp. 651-663
    • Coetzee, W.A.1    Opie, L.H.2
  • 32
    • 79961117101 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress mediates induction of autophagy and hypertrophy in an-giotensin-II treated mouse hearts
    • Dai DF and Rabinovitch P. Mitochondrial oxidative stress mediates induction of autophagy and hypertrophy in an-giotensin-II treated mouse hearts. Autophagy 7: 917-918, 2011.
    • (2011) Autophagy , vol.7 , pp. 917-918
    • Dai, D.F.1    Rabinovitch, P.2
  • 34
    • 84555188518 scopus 로고    scopus 로고
    • Mitochondrial proteome remodelling in pressure overload-induced heart failure: The role of mitochondrial oxidative stress
    • Dai DF, Hsieh EJ, Liu Y, Chen T, Beyer RP, Chin MT, MacCoss MJ, and Rabinovitch PS. Mitochondrial proteome remodelling in pressure overload-induced heart failure: The role of mitochondrial oxidative stress. Cardiovasc Res 93: 79-88, 2012.
    • (2012) Cardiovasc Res , vol.93 , pp. 79-88
    • Dai, D.F.1    Hsieh, E.J.2    Liu, Y.3    Chen, T.4    Beyer, R.P.5    Chin, M.T.6    MacCoss, M.J.7    Rabinovitch, P.S.8
  • 36
    • 0029795275 scopus 로고    scopus 로고
    • Specific phosphorylation of a site in the full-length form of the a1 subunit of the cardiac L-type calcium channel by adenosine 3', 5'-cyclic monophosphate-dependent protein kinase
    • De Jongh KS, Murphy BJ, Colvin AA, Hell JW, Takahashi M, and Catterall WA. Specific phosphorylation of a site in the full-length form of the a1 subunit of the cardiac L-type calcium channel by adenosine 3', 5'-cyclic monophosphate-dependent protein kinase. Biochemistry 35: 10392-10402, 1996.
    • (1996) Biochemistry , vol.35 , pp. 10392-10402
    • De Jongh, K.S.1    Murphy, B.J.2    Colvin, A.A.3    Hell, J.W.4    Takahashi, M.5    Catterall, W.A.6
  • 37
    • 23344445947 scopus 로고    scopus 로고
    • Phospholemman-phosphoryla-tion mediates the beta-adrenergic effects on Na/K pump function in cardiac myocytes
    • Despa S, Bossuyt J, Han F, Ginsburg KS, Jia LG, Kutchai H, Tucker AL, and Bers DM. Phospholemman-phosphoryla-tion mediates the beta-adrenergic effects on Na/K pump function in cardiac myocytes. Circ Res 97: 252-259, 2005.
    • (2005) Circ Res , vol.97 , pp. 252-259
    • Despa, S.1    Bossuyt, J.2    Han, F.3    Ginsburg, K.S.4    Jia, L.G.5    Kutchai, H.6    Tucker, A.L.7    Bers, D.M.8
  • 39
    • 14644414790 scopus 로고    scopus 로고
    • Protein kinase cascades in the regulation of cardiac hypertrophy
    • Dorn GW and Force T. Protein kinase cascades in the regulation of cardiac hypertrophy. J Clin Invest 115: 527-537, 2005.
    • (2005) J Clin Invest , vol.115 , pp. 527-537
    • Dorn, G.W.1    Force, T.2
  • 40
  • 41
    • 0033781028 scopus 로고    scopus 로고
    • Calmodulin kinase determines calcium-dependent facilitation of L-type calcium channels
    • Dzhura I, Wu Y, Colbran RJ, Balser JR, and Anderson ME. Calmodulin kinase determines calcium-dependent facilitation of L-type calcium channels. Nat Cell Biol 2: 173-177, 2000.
    • (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
  • 43
  • 45
    • 0028828942 scopus 로고
    • 2+ release channel from skeletal muscle sarcoplasmic reticulum
    • 2+ release channel from skeletal muscle sarcoplasmic reticulum. J Biol Chem 270: 25557-25563, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 25557-25563
    • Favero, T.G.1    Zable, A.C.2    Abramson, J.J.3
  • 47
    • 0031015604 scopus 로고    scopus 로고
    • Modulation of the human cardiac sodium channel a-sub-unit by cAMP-dependent protein kinase and the responsible sequence domain
    • Frohnwieser B, Chen L, Schreibmayer W, and Kallen R. Modulation of the human cardiac sodium channel a-sub-unit by cAMP-dependent protein kinase and the responsible sequence domain. J Physiol (Lond) 498: 309-318, 1997.
    • (1997) J Physiol (Lond) , vol.498 , pp. 309-318
    • Frohnwieser, B.1    Chen, L.2    Schreibmayer, W.3    Kallen, R.4
  • 50
    • 0028911071 scopus 로고
    • 2+ currents in isolated guinea-pig ventricular myocytes
    • 2+ currents in isolated guinea-pig ventricular myocytes. Eur J Pharmacol 292: 337-340, 1995.
    • (1995) Eur J Pharmacol , vol.292 , pp. 337-340
    • Gill, J.S.1    McKenna, W.J.2    Camm, A.3
  • 51
    • 0024308421 scopus 로고
    • Effects of exogenous free radicals on electromechanical function and metabolism in isolated rabbit and guinea pig ventricle. Implications for ischemia and reperfusion injury
    • Goldhaber JI, Ji S, Lamp ST, Weiss JN. Effects of exogenous free radicals on electromechanical function and metabolism in isolated rabbit and guinea pig ventricle. Implications for ischemia and reperfusion injury. J Clin Invest 83: 1800-1809, 1989.
    • (1989) J Clin Invest , vol.83 , pp. 1800-1809
    • Goldhaber, J.I.1    Ji, S.2    Lamp, S.T.3    Weiss, J.N.4
  • 52
    • 33750740174 scopus 로고    scopus 로고
    • 2+ exchange in ventricular myocytes
    • 2+ exchange in ventricular myocytes. Am J Physiol 271: H823-833, 1996.
    • (1996) Am J Physiol , vol.271
    • Goldhaber, J.I.1
  • 53
    • 0024724936 scopus 로고
    • 2+-independent and phospholipid-independent activation of protein kinase C by selective oxidative modification of the regulatory domain
    • 2+-independent and phospholipid-independent activation of protein kinase C by selective oxidative modification of the regulatory domain. Proc Nat Acad Sci 86: 6758-6762, 1989.
    • (1989) Proc Nat Acad Sci , vol.86 , pp. 6758-6762
    • Gopalakrishna, R.1    Anderson, W.2
  • 55
    • 0029750390 scopus 로고    scopus 로고
    • In-vivo phosphorylation of the cardiac L-type calcium channel beta-subunit in response to catecholamines
    • Haase H, Bartel S, Karczewski P, Morano I, and Krause EG. In-vivo phosphorylation of the cardiac L-type calcium channel beta-subunit in response to catecholamines. Mol Cell Biochem 163-164: 99-106, 1996.
    • (1996) Mol Cell Biochem , vol.163-164 , pp. 99-106
    • Haase, H.1    Bartel, S.2    Karczewski, P.3    Morano, I.4    Krause, E.G.5
  • 60
    • 70349668973 scopus 로고    scopus 로고
    • PKC phosphorylation of titin's PEVK element: A novel and conserved pathway for modulating myocardial stiffness
    • Hidalgo C, Hudson B, Bogomolovas J, Zhu Y, Anderson B, Greaser M, Labeit S, and Granzier H. PKC phosphorylation of titin's PEVK element: A novel and conserved pathway for modulating myocardial stiffness. Circ Res 105: 631-638, 2009.
    • (2009) Circ Res , vol.105 , pp. 631-638
    • Hidalgo, C.1    Hudson, B.2    Bogomolovas, J.3    Zhu, Y.4    Anderson, B.5    Greaser, M.6    Labeit, S.7    Granzier, H.8
  • 62
    • 0030754792 scopus 로고    scopus 로고
    • Right and left myocardial antioxi-dant responses during heart failure subsequent to myo-cardial infarction
    • Hill MF and Singal PK. Right and left myocardial antioxi-dant responses during heart failure subsequent to myo-cardial infarction. Circulation 96: 2414-2420, 1997.
    • (1997) Circulation , vol.96 , pp. 2414-2420
    • Hill, M.F.1    Singal, P.K.2
  • 63
    • 0023555557 scopus 로고
    • Protein kinase C contains a pseu-dosubstrate prototope in its regulatory domain
    • House C and Kemp BE. Protein kinase C contains a pseu-dosubstrate prototope in its regulatory domain. Science 238: 1726-1728, 1987.
    • (1987) Science , vol.238 , pp. 1726-1728
    • House, C.1    Kemp, B.E.2
  • 72
    • 0141746553 scopus 로고    scopus 로고
    • Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-a
    • Kang SW, Chae HZ, Seo MS, Kim K, Baines IC, and Rhee SG. Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-a. J Biol Chem 273: 6297-6302, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 6297-6302
    • Kang, S.W.1    Chae, H.Z.2    Seo, M.S.3    Kim, K.4    Baines, I.C.5    Rhee, S.G.6
  • 74
    • 0023822568 scopus 로고
    • 2+ exchange of isolated sarcolemmal membrane: Effects of insulin, oxidants and insulin deficiency
    • 2+ exchange of isolated sarcolemmal membrane: Effects of insulin, oxidants and insulin deficiency. Mol Cell Biochem 83: 15-25, 1988.
    • (1988) Mol Cell Biochem , vol.83 , pp. 15-25
    • Kato, M.1    Kako, K.J.2
  • 79
    • 0024990622 scopus 로고
    • +-ATPase: Inactivation by neutrophil-derived free radicals and oxidants
    • +-ATPase: Inactivation by neutrophil-derived free radicals and oxidants. Am J Physiol 259: H1330-1336, 1990.
    • (1990) Am J Physiol , vol.259
    • Kukreja, R.C.1    Weaver, A.B.2    Hess, M.L.3
  • 80
    • 0021807380 scopus 로고
    • 2+/calmodulin-dependent protein kinase
    • 2+/calmodulin-dependent protein kinase. J Biol Chem 260: 6427-6433, 1985.
    • (1985) J Biol Chem , vol.260 , pp. 6427-6433
    • Kuret, J.1    Schulman, H.2
  • 82
    • 0028851638 scopus 로고
    • Effect of sulfhydryl oxidation on ionic and gating currents associated with L-type calcium channels in isolated guinea-pig ventricular myocytes
    • Lacampagne A, Duittoz A, Bolanos P, Peineau N, and Argibay JA. Effect of sulfhydryl oxidation on ionic and gating currents associated with L-type calcium channels in isolated guinea-pig ventricular myocytes. Cardiovasc Res 30: 799-806, 1995.
    • (1995) Cardiovasc Res , vol.30 , pp. 799-806
    • Lacampagne, A.1    Duittoz, A.2    Bolanos, P.3    Peineau, N.4    Argibay, J.A.5
  • 83
    • 0028031728 scopus 로고
    • Direct evidence for the existence and functional role of hyperreactive sulfhydryls on the ryanodine receptor-triadin complex selectively labeled by the coumarin maleimide 7-diethyla-mino-3-(4-Vmaleimidylphenyl)-4-methylcoumarin
    • Liu G, Abramson JJ, Zable AC, and Pessah IN. Direct evidence for the existence and functional role of hyperreactive sulfhydryls on the ryanodine receptor-triadin complex selectively labeled by the coumarin maleimide 7-diethyla-mino-3-(4-Vmaleimidylphenyl)-4-methylcoumarin. Mol Pharmacol 45: 189-200, 1994.
    • (1994) Mol Pharmacol , vol.45 , pp. 189-200
    • Liu, G.1    Abramson, J.J.2    Zable, A.C.3    Pessah, I.N.4
  • 84
    • 77958501429 scopus 로고    scopus 로고
    • Reactive oxygen species originating from mitochondria regulate the cardiac sodium channel
    • Liu M, Liu H, and Dudley SC Jr. Reactive oxygen species originating from mitochondria regulate the cardiac sodium channel. Circ Res 107: 967-974, 2010.
    • (2010) Circ Res , vol.107 , pp. 967-974
    • Liu, M.1    Liu, H.2    Dudley Jr., S.C.3
  • 85
    • 70350135479 scopus 로고    scopus 로고
    • Endogenous activation of mitochondrial KATP channels protects human failing myocardium from hydroxyl radical-induced stunning
    • Maack C, Dabew ER, Hohl M, Schäfers HJ, and Böhm M. Endogenous activation of mitochondrial KATP channels protects human failing myocardium from hydroxyl radical-induced stunning. Circ Res 105: 811-817, 2009.
    • (2009) Circ Res , vol.105 , pp. 811-817
    • Maack, C.1    Dabew, E.R.2    Hohl, M.3    Schäfers, H.J.4    Böhm, M.5
  • 86
    • 0141841614 scopus 로고    scopus 로고
    • Oxygen free radical release in human failing myocardium is associated with increased activity of rac1-GTPase and represents a target for statin treatment
    • Maack C, Kartes T, Kilter H, Schäfers HJ, Nickenig G, Böhm M, and Laufs U. Oxygen free radical release in human failing myocardium is associated with increased activity of rac1-GTPase and represents a target for statin treatment. Circulation 108: 1567-1574, 2003.
    • (2003) Circulation , vol.108 , pp. 1567-1574
    • Maack, C.1    Kartes, T.2    Kilter, H.3    Schäfers, H.J.4    Nickenig, G.5    Böhm, M.6    Laufs, U.7
  • 87
    • 33846858884 scopus 로고    scopus 로고
    • 2+/calmodulin-depen-dent protein kinase (CaMK) in excitation-contraction coupling in the heart
    • 2+/calmodulin-depen-dent protein kinase (CaMK) in excitation-contraction coupling in the heart. Cardiovasc Res 73: 631-640, 2007.
    • (2007) Cardiovasc Res , vol.73 , pp. 631-640
    • Maier, L.S.1    Bers, D.M.2
  • 89
    • 79952184376 scopus 로고    scopus 로고
    • CaMKII regulation of voltage-gated sodium channels and cell excitability
    • Maier LS. CaMKII regulation of voltage-gated sodium channels and cell excitability. Heart Rhythm 8: 474-477, 2011.
    • (2011) Heart Rhythm , vol.8 , pp. 474-477
    • Maier, L.S.1
  • 91
    • 0032574631 scopus 로고    scopus 로고
    • Elevated levels of 8-iso-prostaglandin F2a in pericardial fluid of patients with heart failure: A potential role for in vivo oxidant stress in ventricular dilatation and progression to heart failure
    • Mallat Z, Philip I, Lebret M, Chatel D, Maclouf J, and Tedgui A. Elevated levels of 8-iso-prostaglandin F2a in pericardial fluid of patients with heart failure: A potential role for in vivo oxidant stress in ventricular dilatation and progression to heart failure. Circulation 97: 1536-1539, 1998.
    • (1998) Circulation , vol.97 , pp. 1536-1539
    • Mallat, Z.1    Philip, I.2    Lebret, M.3    Chatel, D.4    MacLouf, J.5    Tedgui, A.6
  • 92
    • 0031951413 scopus 로고    scopus 로고
    • Sulfhydryl oxidation modifies the calcium dependence of ryanodine-sensitive calcium channels of excitable cells
    • Marengo JJ, Hidalgo C and Bull R. Sulfhydryl oxidation modifies the calcium dependence of ryanodine-sensitive calcium channels of excitable cells. Biophys J 74: 1263-1277, 1998.
    • (1998) Biophys J , vol.74 , pp. 1263-1277
    • Marengo, J.J.1    Hidalgo, C.2    Bull, R.3
  • 93
    • 0024328801 scopus 로고
    • Primary structure and functional expression of the cardiac dihydropyridine-sen-sitive calcium channel
    • Mikami A, Imoto K, Tanabe T, Niidome T, Mori Y, Take-shima H, Narumiya S, and Numa S. Primary structure and functional expression of the cardiac dihydropyridine-sen-sitive calcium channel. Nature 340: 230-233, 1989.
    • (1989) Nature , vol.340 , pp. 230-233
    • Mikami, A.1    Imoto, K.2    Tanabe, T.3    Niidome, T.4    Mori, Y.5    Take-Shima, H.6    Narumiya, S.7    Numa, S.8
  • 94
    • 0025908315 scopus 로고
    • Identification of intracellular receptor proteins for activated protein kinase C
    • Mochly-Rosen D, Khaner H, and Lopez J. Identification of intracellular receptor proteins for activated protein kinase C. Proc Natl Acad Sci USA 88: 3997-4000, 1991.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 3997-4000
    • Mochly-Rosen, D.1    Khaner, H.2    Lopez, J.3
  • 95
    • 0029859988 scopus 로고    scopus 로고
    • 2+-pump dysfunction in rat cardiomyocytes briefly exposed to hydroxyl radicals
    • 2+-pump dysfunction in rat cardiomyocytes briefly exposed to hydroxyl radicals. Free Radic Biol Med 22: 37-47, 1997.
    • (1997) Free Radic Biol Med , vol.22 , pp. 37-47
    • Morris, T.E.1    Sulakhe, P.V.2
  • 96
    • 0017201657 scopus 로고
    • Sulfhydryl group modification of sarcoplasmic reticulum membranes
    • Murphy AJ. Sulfhydryl group modification of sarcoplasmic reticulum membranes. Biochemistry 15: 4492-4496, 1976.
    • (1976) Biochemistry , vol.15 , pp. 4492-4496
    • Murphy, A.J.1
  • 97
    • 0029802816 scopus 로고    scopus 로고
    • CAMP-dependent phosphorylation of two sites in the a subunit of the cardiac sodium channel
    • Murphy BJ, Rogers J, Perdichizzi AP, Colvin AA, and Catterall WA. cAMP-dependent phosphorylation of two sites in the a subunit of the cardiac sodium channel. J Biol Chem 271: 28837-28843, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 28837-28843
    • Murphy, B.J.1    Rogers, J.2    Perdichizzi, A.P.3    Colvin, A.A.4    Catterall, W.A.5
  • 100
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • Pacher P, Beckman JS, and Liaudet L. Nitric oxide and peroxynitrite in health and disease. Physiol Rev 87: 315-424, 2007.
    • (2007) Physiol Rev , vol.87 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 101
    • 0033032888 scopus 로고    scopus 로고
    • Regional differences in non-enzymatic antioxidants in the heart under control and oxidative stress conditions
    • Palace V, Kumar D, Hill MF, Khaper N, and Singal PK. Regional differences in non-enzymatic antioxidants in the heart under control and oxidative stress conditions. J Mol Cell Cardiol 31: 193-202, 1999.
    • (1999) J Mol Cell Cardiol , vol.31 , pp. 193-202
    • Palace, V.1    Kumar, D.2    Hill, M.F.3    Khaper, N.4    Singal, P.K.5
  • 102
    • 82855182299 scopus 로고    scopus 로고
    • Ischemia/reperfu-sion injury and cardioprotective mechanisms: Role of mitochondria and reactive oxygen species
    • Perrelli MG, Pagliaro P, and Penna C. Ischemia/reperfu-sion injury and cardioprotective mechanisms: Role of mitochondria and reactive oxygen species. World J Cardiol 3: 186-200, 2011.
    • (2011) World J Cardiol , vol.3 , pp. 186-200
    • Perrelli, M.G.1    Pagliaro, P.2    Penna, C.3
  • 105
    • 0030744422 scopus 로고    scopus 로고
    • Differential effects of subunit interactions on protein kinase A-and C-mediated phosphorylation of L-type calcium channels
    • Puri TS, Gerhardstein BL, Zhao XL, Ladner MB, and Hosey MM. Differential effects of subunit interactions on protein kinase A-and C-mediated phosphorylation of L-type calcium channels. Biochemistry 36: 9605-9615, 1997.
    • (1997) Biochemistry , vol.36 , pp. 9605-9615
    • Puri, T.S.1    Gerhardstein, B.L.2    Zhao, X.L.3    Ladner, M.B.4    Hosey, M.M.5
  • 107
    • 0028202763 scopus 로고
    • + channels expressed in a mammalian cell line and in ventricular myocytes by protein kinase C
    • + channels expressed in a mammalian cell line and in ventricular myocytes by protein kinase C. Proc Nat Acad Sci 91: 3289-3293, 1994.
    • (1994) Proc Nat Acad Sci , vol.91 , pp. 3289-3293
    • Qu, Y.1    Rogers, J.2    Tanada, T.3    Scheuer, T.4    Catterall, W.5
  • 108
    • 77951621403 scopus 로고    scopus 로고
    • Calcium sensitivity, force frequency relationship and cardiac troponin I: Critical role of PKA and PKC phosphorylation sites
    • Ramirez-Correa GA, Cortassa S, Stanley B, Gao WD, Murphy AM. Calcium sensitivity, force frequency relationship and cardiac troponin I: Critical role of PKA and PKC phosphorylation sites. J Mol Cell Cardiol 48: 943-953, 2010.
    • (2010) J Mol Cell Cardiol , vol.48 , pp. 943-953
    • Ramirez-Correa, G.A.1    Cortassa, S.2    Stanley, B.3    Gao, W.D.4    Murphy, A.M.5
  • 109
    • 0023031882 scopus 로고
    • Redox modification of sodium-calcium exchange activity in cardiac sarcolemmal vesicles
    • Reeves JP, Bailey CA, and Hale CC. Redox modification of sodium-calcium exchange activity in cardiac sarcolemmal vesicles. J Biol Chem 261: 4948-4955, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 4948-4955
    • Reeves, J.P.1    Bailey, C.A.2    Hale, C.C.3
  • 110
    • 0036903347 scopus 로고    scopus 로고
    • + channels in rat ventricular myocytes
    • + channels in rat ventricular myocytes. J Mol Cell Cardiol 34: 1623-1632, 2002.
    • (2002) J Mol Cell Cardiol , vol.34 , pp. 1623-1632
    • Rozanski, G.J.1    Xu, Z.2
  • 112
    • 80053259051 scopus 로고    scopus 로고
    • CaMKII-dependent SR Ca leak contributes to doxorubicin-induced impaired Ca handling in isolated cardiac myo-cytes
    • Sag CM, Köhler AC, Anderson ME, Backs J, and Maier LS. CaMKII-dependent SR Ca leak contributes to doxorubicin-induced impaired Ca handling in isolated cardiac myo-cytes. J Mol Cell Cardiol 51: 749-759, 2011.
    • (2011) J Mol Cell Cardiol , vol.51 , pp. 749-759
    • Sag, C.M.1    Köhler, A.C.2    Anderson, M.E.3    Backs, J.4    Maier, L.S.5
  • 115
    • 0017854367 scopus 로고
    • Stimulation of brain membrane protein phosphorylation by calcium and an endogenous heat-stable protein
    • Schulman H and Greengard P. Stimulation of brain membrane protein phosphorylation by calcium and an endogenous heat-stable protein. Nature 271: 478-479, 1978.
    • (1978) Nature , vol.271 , pp. 478-479
    • Schulman, H.1    Greengard, P.2
  • 116
    • 0022929859 scopus 로고
    • 2+/calmod-ulin-dependent protein kinase II by an autopho-sphorylation mechanism
    • 2+/calmod-ulin-dependent protein kinase II by an autopho-sphorylation mechanism. J Biol Chem 261: 8581-8584, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 8581-8584
    • Schworer, C.M.1    Colbran, R.J.2    Soderling, T.R.3
  • 117
    • 0027198602 scopus 로고
    • + pump current in isolated rabbit ventricular myocytes using the whole-cell voltage-clamp technique. Inhibition of the pump by oxidant stress
    • + pump current in isolated rabbit ventricular myocytes using the whole-cell voltage-clamp technique. Inhibition of the pump by oxidant stress. Circ Res 72: 91-101, 1993.
    • (1993) Circ Res , vol.72 , pp. 91-101
    • Shattock, M.J.1    Matsuura, H.2
  • 118
    • 80054704273 scopus 로고    scopus 로고
    • NADPH oxidases in cardiovascular disease: Insights from in vivo models and clinical studies
    • Sirker A, Zhang M, and Shah AM. NADPH oxidases in cardiovascular disease: Insights from in vivo models and clinical studies. Basic Res Cardiol 106: 735-747, 2011.
    • (2011) Basic Res Cardiol , vol.106 , pp. 735-747
    • Sirker, A.1    Zhang, M.2    Shah, A.M.3
  • 119
    • 33745251122 scopus 로고    scopus 로고
    • Blocking late sodium current reduces hydrogen peroxide-induced arrhythmogenic activity and contractile dysfunction
    • Song Y, Shryock J, Wagner S, Maier LS, and Belardinelli L. Blocking late sodium current reduces hydrogen peroxide-induced arrhythmogenic activity and contractile dysfunction. J Pharmacol Exp Ther 318: 214-222, 2006.
    • (2006) J Pharmacol Exp Ther , vol.318 , pp. 214-222
    • Song, Y.1    Shryock, J.2    Wagner, S.3    Maier, L.S.4    Belardinelli, L.5
  • 122
    • 0041816273 scopus 로고    scopus 로고
    • Identification of a functionally critical protein kinase C phosphorylation residue of cardiac troponin T
    • Sumandea MP, Pyle WG, Kobayashi T, de Tombe PP, and Solaro RJ. Identification of a functionally critical protein kinase C phosphorylation residue of cardiac troponin T. J Biol Chem 278: 35135-35144, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 35135-35144
    • Sumandea, M.P.1    Pyle, W.G.2    Kobayashi, T.3    De Tombe, P.P.4    Solaro, R.J.5
  • 124
    • 0034705485 scopus 로고    scopus 로고
    • Transgenic overexpression of constitutively active protein kinase C epsilon causes concentric cardiac hypertrophy
    • Takeishi Y, Ping P, Bolli R, Kirkpatrick DL, Hoit BD, and Walsh RA. Transgenic overexpression of constitutively active protein kinase C epsilon causes concentric cardiac hypertrophy. Circ Res 86: 1218-1223, 2000.
    • (2000) Circ Res , vol.86 , pp. 1218-1223
    • Takeishi, Y.1    Ping, P.2    Bolli, R.3    Kirkpatrick, D.L.4    Hoit, B.D.5    Walsh, R.A.6
  • 127
    • 0032880331 scopus 로고    scopus 로고
    • Alterations in sarcoplasmic re-ticulum function and gene expression in ischemic-reperfused rat heart
    • Temsah RM, Netticadan T, Chapman D, Takeda S, Mo-chizuki S, and Dhalla NS. Alterations in sarcoplasmic re-ticulum function and gene expression in ischemic-reperfused rat heart. Am J Physiol 277: H584-594, 1999.
    • (1999) Am J Physiol , vol.277
    • Temsah, R.M.1    Netticadan, T.2    Chapman, D.3    Takeda, S.4    Mo-Chizuki, S.5    Dhalla, N.S.6
  • 129
    • 59449104627 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress and dysfunction in myocardial remodelling
    • Tsutsui H, Kinugawa S, and Matsushima S. Mitochondrial oxidative stress and dysfunction in myocardial remodelling. Cardiovasc Res 81: 449-456, 2009.
    • (2009) Cardiovasc Res , vol.81 , pp. 449-456
    • Tsutsui, H.1    Kinugawa, S.2    Matsushima, S.3
  • 131
    • 70349628999 scopus 로고    scopus 로고
    • GPD1L links redox state to cardiac excitability by PKC-dependent phosphorylation of the sodium channel SCN5A
    • Valdivia CR, Ueda K, Ackerman MJ, and Makielski JC. GPD1L links redox state to cardiac excitability by PKC-dependent phosphorylation of the sodium channel SCN5A. Am J Physiol Heart Circ Physiol 297: H1446-1452, 2009.
    • (2009) Am J Physiol Heart Circ Physiol , vol.297
    • Valdivia, C.R.1    Ueda, K.2    Ackerman, M.J.3    Makielski, J.C.4
  • 132
    • 2442603839 scopus 로고    scopus 로고
    • Differential effects of substrate on type i and type II PKA holoenzyme dissociation
    • Vigil D, Blumenthal DK, Brown S, Taylor SS, and Trewhella J. Differential effects of substrate on type I and type II PKA holoenzyme dissociation. Biochemistry 43: 5629-5636, 2004.
    • (2004) Biochemistry , vol.43 , pp. 5629-5636
    • Vigil, D.1    Blumenthal, D.K.2    Brown, S.3    Taylor, S.S.4    Trewhella, J.5
  • 133
    • 17144386191 scopus 로고    scopus 로고
    • Substrate enhances the sensitivity of type i protein kinase A to cAMP
    • Viste K, Kopperud RK, Christensen AE, and Døskeland SO. Substrate enhances the sensitivity of type I protein kinase A to cAMP. J Biol Chem 280: 13279-13284, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 13279-13284
    • Viste, K.1    Kopperud, R.K.2    Christensen, A.E.3    Døskeland, S.O.4
  • 138
    • 0038104862 scopus 로고    scopus 로고
    • Increased expression of protein kinase C isoforms in heart failure due to myocardial infarction
    • Wang J, Liu X, Sentex E, Takeda N, and Dhalla NS. Increased expression of protein kinase C isoforms in heart failure due to myocardial infarction. Am J Physiol Heart Circ Physiol. 284: H2277-2287, 2003.
    • (2003) Am J Physiol Heart Circ Physiol. , vol.284
    • Wang, J.1    Liu, X.2    Sentex, E.3    Takeda, N.4    Dhalla, N.S.5
  • 139
    • 0030957101 scopus 로고    scopus 로고
    • Ionic mechanism of the effects of hydrogen peroxide in rat ventricular myocytes
    • Ward CA and Giles WR. Ionic mechanism of the effects of hydrogen peroxide in rat ventricular myocytes. J Physiol 500: 631-642, 1997.
    • (1997) J Physiol , vol.500 , pp. 631-642
    • Ward, C.A.1    Giles, W.R.2
  • 141
    • 0242298644 scopus 로고    scopus 로고
    • Dynamic regulation of sodium/calcium exchange function in human heart failure
    • Weber CR, Piacentino V, 3rd, Houser SR, and Bers DM. Dynamic regulation of sodium/calcium exchange function in human heart failure. Circulation 108: 2224-2229, 2003.
    • (2003) Circulation , vol.108 , pp. 2224-2229
    • Weber, C.R.1    Piacentino III, V.2    Houser, S.R.3    Bers, D.M.4
  • 142
    • 0037376146 scopus 로고    scopus 로고
    • Calcium entry via Na/Ca exchange during the action potential directly contributes to contraction of failing human ventricular myocytes
    • Weisser-Thomas J, Piacentino V, 3rd, Gaughan JP, Margu-lies K, and Houser SR. Calcium entry via Na/Ca exchange during the action potential directly contributes to contraction of failing human ventricular myocytes. Cardiovasc Res 57: 974-985, 2003.
    • (2003) Cardiovasc Res , vol.57 , pp. 974-985
    • Weisser-Thomas, J.1    Piacentino III, V.2    Gaughan, J.P.3    Margu-Lies, K.4    Houser, S.R.5
  • 143
    • 0038581576 scopus 로고    scopus 로고
    • Myocyte adrenoceptor signaling pathways
    • Xiang Y and Kobilka BK. Myocyte adrenoceptor signaling pathways. Science 300: 1530-1532, 2003.
    • (2003) Science , vol.300 , pp. 1530-1532
    • Xiang, Y.1    Kobilka, B.K.2
  • 144
  • 145
    • 0031015476 scopus 로고    scopus 로고
    • 2+-ATPase function by direct attack on the ATP binding site
    • 2+-ATPase function by direct attack on the ATP binding site. Circ Res 80: 76-81, 1997.
    • (1997) Circ Res , vol.80 , pp. 76-81
    • Xu, K.Y.1    Zweier, J.L.2    Becker, L.C.3
  • 146
    • 0032498185 scopus 로고    scopus 로고
    • Activation of the cardiac calcium release channel (ryanodine receptor) by poly-s-nitrosylation
    • Xu L, Eu JP, Meissner G, and Stamler JS. Activation of the cardiac calcium release channel (ryanodine receptor) by poly-s-nitrosylation. Science 279: 234-237, 1998.
    • (1998) Science , vol.279 , pp. 234-237
    • Xu, L.1    Eu, J.P.2    Meissner, G.3    Stamler, J.S.4
  • 147
    • 0344875019 scopus 로고    scopus 로고
    • Thioredoxin: A key regulator of cardiovascular homeostasis
    • Yamawaki H, Haendeler J, and Berk BC. Thioredoxin: A key regulator of cardiovascular homeostasis. Circ Res 93: 1029-1033, 2003.
    • (2003) Circ Res , vol.93 , pp. 1029-1033
    • Yamawaki, H.1    Haendeler, J.2    Berk, B.C.3
  • 152
  • 154
    • 34147092002 scopus 로고    scopus 로고
    • Redox sensitivity of the ryanodine receptor interaction with FK506-binding protein
    • Zissimopoulos S, Docrat N, and Lai FA. Redox sensitivity of the ryanodine receptor interaction with FK506-binding protein. J Biol Chem 282: 6976-6983, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 6976-6983
    • Zissimopoulos, S.1    Docrat, N.2    Lai, F.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.