메뉴 건너뛰기




Volumn 19, Issue 34, 2012, Pages 5782-5792

Regulation of intracellular cardiomyocyte calcium stores by peptides: A new approach to cardiac protection

Author keywords

Calcium; Cardioprotection; ErbB; Excitation contraction coupling; Heart; Mitrochondria; Neuregulin; RISK; Sarcoplasmic reticulum; Signal transduction; Urocortin

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); ANTHRACYCLINE; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CALCIUM ION; CORTICOTROPIN RELEASING FACTOR; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC GMP DEPENDENT PROTEIN KINASE; EPIDERMAL GROWTH FACTOR RECEPTOR 2; EPIDERMAL GROWTH FACTOR RECEPTOR 4; GLYCOGEN SYNTHASE KINASE 3 INHIBITOR; LAPATINIB; MITOCHONDRIAL PERMEABILITY TRANSITION PORE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; NATRIURETIC FACTOR; NEU DIFFERENTIATION FACTOR; PEPTIDE; PERTUZUMAB; PHOSPHATIDYLINOSITOL 3 KINASE; RYANODINE RECEPTOR; RYANODINE RECEPTOR 2; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE 2A; SODIUM CALCIUM EXCHANGE PROTEIN; TRASTUZUMAB; UNCLASSIFIED DRUG; UNINDEXED DRUG; UROCORTIN I; UROCORTIN II; UROCORTIN III; VOLTAGE GATED CHANNEL FORMING PROTEIN;

EID: 84871656632     PISSN: 09298673     EISSN: 1875533X     Source Type: Journal    
DOI: 10.2174/092986712804143295     Document Type: Review
Times cited : (1)

References (155)
  • 2
    • 0034673129 scopus 로고    scopus 로고
    • The herbal history of Digitalis: Lessons for alternative medicine
    • Ritter, G.; Dembicki, E. L., The herbal history of Digitalis: lessons for alternative medicine. JAMA, 2000, 283, (7), 884-886.
    • (2000) JAMA , vol.283 , Issue.7 , pp. 884-886
    • Ritter, G.1    Dembicki, E.L.2
  • 3
    • 0033252825 scopus 로고    scopus 로고
    • Charles Darwin (1758-1778) and the history of the early use of digitalis. 1934
    • Fulton, J. F., Charles Darwin (1758-1778) and the history of the early use of digitalis. 1934. J. Urban Health, 1999, 76, (4), 533-541.
    • (1999) J. Urban Health , vol.76 , Issue.4 , pp. 533-541
    • Fulton, J.F.1
  • 4
    • 0022387153 scopus 로고
    • William Withering and the purple foxglove: A bicentennial tribute
    • Norman, J. N., William Withering and the purple foxglove: a bicentennial tribute. J. Clin. Pharmacol., 1985, 25, (7), 479-483.
    • (1985) J. Clin. Pharmacol. , vol.25 , Issue.7 , pp. 479-483
    • Norman, J.N.1
  • 5
    • 43549098268 scopus 로고    scopus 로고
    • Calcium cycling and signaling in cardiac myocytes
    • Bers, D. M., Calcium cycling and signaling in cardiac myocytes. Ann. Rev. Physiol., 2008, 70, 23-49.
    • (2008) Ann. Rev. Physiol. , vol.70 , pp. 23-49
    • Bers, D.M.1
  • 6
    • 0034683082 scopus 로고    scopus 로고
    • Calcium fluxes involved in control of cardiac myocyte contraction
    • Bers, D. M., Calcium fluxes involved in control of cardiac myocyte contraction. Circ. Res., 2000, 87, (4), 275-281.
    • (2000) Circ. Res. , vol.87 , Issue.4 , pp. 275-281
    • Bers, D.M.1
  • 8
    • 77649270573 scopus 로고    scopus 로고
    • Comparison of the T-tubule system in adult rat ventricular and atrial myocytes, and its role in excitation contraction coupling and inotropic stimulation
    • Smyrnias, I.; Mair, W.; Harzheim, D.; Walker, S. A.; Roderick, H. L.; Bootman, M. D., Comparison of the T-tubule system in adult rat ventricular and atrial myocytes, and its role in excitation contraction coupling and inotropic stimulation. Cell. Calcium, 2010, 47, (3), 210-223.
    • (2010) Cell. Calcium , vol.47 , Issue.3 , pp. 210-223
    • Smyrnias, I.1    Mair, W.2    Harzheim, D.3    Walker, S.A.4    Roderick, H.L.5    Bootman, M.D.6
  • 9
    • 77949379471 scopus 로고    scopus 로고
    • A coupled SYSTEM of intracellular Ca2+ clocks and surface membrane voltage clocks controls the timekeeping mechanism of the heart's pacemaker
    • Lakatta, E. G.; Maltsev, V. A.; Vinogradova, T. M., A coupled SYSTEM of intracellular Ca2+ clocks and surface membrane voltage clocks controls the timekeeping mechanism of the heart's pacemaker. Circ. Res., 2010, 106, (4), 659-673.
    • (2010) Circ. Res. , vol.106 , Issue.4 , pp. 659-673
    • Lakatta, E.G.1    Maltsev, V.A.2    Vinogradova, T.M.3
  • 10
    • 84856167091 scopus 로고    scopus 로고
    • The funny current has a major pacemaking role in the sinus node
    • Difrancesco, D.; Noble, D., The funny current has a major pacemaking role in the sinus node. Heart Rhythm, 2012, 9(2), 299-301.
    • (2012) Heart Rhythm , vol.9 , Issue.2 , pp. 299-301
    • Difrancesco, D.1    Noble, D.2
  • 11
    • 67649104033 scopus 로고    scopus 로고
    • What keeps us ticking: A funny current, a calcium clock, or both?
    • Lakatta, E. G.; Difrancesco, D., What keeps us ticking: a funny current, a calcium clock, or both? J. Mol. Cell. Cardiol., 2009, 47, (2), 157-170.
    • (2009) J. Mol. Cell. Cardiol. , vol.47 , Issue.2 , pp. 157-170
    • Lakatta, E.G.1    Difrancesco, D.2
  • 12
    • 79951929119 scopus 로고    scopus 로고
    • Alterations of atrial Ca2+ handling as cause and consequence of atrial fibrillation
    • Greiser, M.; Lederer, W. J.; Schotten, U., Alterations of atrial Ca2+ handling as cause and consequence of atrial fibrillation. Cardiovas. Res., 2011, 89, (4), 722-733.
    • (2011) Cardiovas. Res. , vol.89 , Issue.4 , pp. 722-733
    • Greiser, M.1    Lederer, W.J.2    Schotten, U.3
  • 14
    • 77955267028 scopus 로고    scopus 로고
    • Interplay of voltage and Ca-dependent inactivation of L-type Ca current
    • Grandi, E.; Morotti, S.; Ginsburg, K.; Severi, S.; Bers, D., Interplay of voltage and Ca-dependent inactivation of L-type Ca current. Prog. Biophys. Mol. Biol., 2010, 103, (1), 44-50.
    • (2010) Prog. Biophys. Mol. Biol. , vol.103 , Issue.1 , pp. 44-50
    • Grandi, E.1    Morotti, S.2    Ginsburg, K.3    Severi, S.4    Bers, D.5
  • 15
    • 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. - Cell. Physiol., 1983, 245, (1), C1-C14.
    • (1983) Am. J. Physiol. - Cell. Physiol. , vol.245 , Issue.1
    • Fabiato, A.1
  • 16
    • 78650392284 scopus 로고    scopus 로고
    • Warm fish with cold hearts: Thermal plasticity of excitation-contraction coupling in bluefin tuna
    • Shiels, H. A.; Di Maio, A.; Thompson, S.; Block, B. A., Warm fish with cold hearts: thermal plasticity of excitation-contraction coupling in bluefin tuna. Proc. Royal. Soc. B-Biolog. Sci., 2010, 278, (1702), 18-27.
    • (2010) Proc. Royal. Soc. B-Biolog. Sci. , vol.278 , Issue.1702 , pp. 18-27
    • Shiels, H.A.1    Di Maio, A.2    Thompson, S.3    Block, B.A.4
  • 20
  • 21
    • 79952478406 scopus 로고    scopus 로고
    • Ryanodine receptors: Structure, expression, molecular details, and function in calcium release
    • Lanner, J. T.; Georgiou, D. K.; Joshi, A. D.; Hamilton, S. L., Ryanodine receptors: structure, expression, molecular details, and function in calcium release. Cold Spring Harbor. Perspect. Biol., 2010, 2, (11), a003996.
    • (2010) Cold Spring Harbor. Perspect. Biol. , vol.2 , Issue.11
    • Lanner, J.T.1    Georgiou, D.K.2    Joshi, A.D.3    Hamilton, S.L.4
  • 22
    • 0036132550 scopus 로고    scopus 로고
    • Involvement of the cardiac ryanodine receptor/calcium release channel in catecholaminergic polymorphic ventricular tachycardia
    • Marks, A. R.; Priori, S.; Memmi, M.; Kontula, K.; Laitinen, P. J., Involvement of the cardiac ryanodine receptor/calcium release channel in catecholaminergic polymorphic ventricular tachycardia. J. Cell. Physiol., 2002, 190, (1), 1-6.
    • (2002) J. Cell. Physiol. , vol.190 , Issue.1 , pp. 1-6
    • Marks, A.R.1    Priori, S.2    Memmi, M.3    Kontula, K.4    Laitinen, P.J.5
  • 23
    • 0037049977 scopus 로고    scopus 로고
    • Cardiac excitation-contraction coupling
    • Bers, D. M., Cardiac excitation-contraction coupling. Nature, 2002, 415, (6868), 198-205.
    • (2002) Nature , vol.415 , Issue.6868 , pp. 198-205
    • Bers, D.M.1
  • 24
    • 0024468221 scopus 로고
    • Excitation-contraction coupling in heart muscle
    • Lederer, W.; Cannell, M.; Cohen, N.; Berlin, J., Excitation-contraction coupling in heart muscle. Mol. Cell. Biochem., 1989, 89, (2), 115-119.
    • (1989) Mol. Cell. Biochem. , vol.89 , Issue.2 , pp. 115-119
    • Lederer, W.1    Cannell, M.2    Cohen, N.3    Berlin, J.4
  • 26
    • 0020585784 scopus 로고
    • Isolation of calcium tolerant myocytes from adult rat hearts: Review of the literature and description of a method
    • Farmer, B. B.; Mancina, M.; Williams, E. S.; Watanabe, A. M., Isolation of calcium tolerant myocytes from adult rat hearts: review of the literature and description of a method. Life Sci, 1983, 33, (1), 1-18.
    • (1983) Life Sci , vol.33 , Issue.1 , pp. 1-18
    • Farmer, B.B.1    Mancina, M.2    Williams, E.S.3    Watanabe, A.M.4
  • 27
    • 17944398210 scopus 로고    scopus 로고
    • Cardioplegic strategies for calcium control: Low Ca (2+), high Mg (2+), citrate, or Na (+)/H (+) exchange inhibitor HOE-642
    • Fukuhiro, Y.; Wowk, M.; Ou, R.; Rosenfeldt, F.; Pepe, S., Cardioplegic strategies for calcium control: low Ca (2+), high Mg (2+), citrate, or Na (+)/H (+) exchange inhibitor HOE-642. Circulation, 2000, 102, (19 Suppl 3), III319-325.
    • (2000) Circulation , vol.102 , Issue.19 SUPPL. 3
    • Fukuhiro, Y.1    Wowk, M.2    Ou, R.3    Rosenfeldt, F.4    Pepe, S.5
  • 28
    • 0031593269 scopus 로고    scopus 로고
    • Comparative ultrastructure of Ca2+ release units in skeletal and cardiac muscle
    • Franzini-Armstrong, C.; Protasi, F.; Ramesh, V., Comparative ultrastructure of Ca2+ release units in skeletal and cardiac muscle. Ann. NY. Acad. Sci, 1998, 853, 20-30.
    • (1998) Ann. NY. Acad. Sci , vol.853 , pp. 20-30
    • Franzini-Armstrong, C.1    Protasi, F.2    Ramesh, V.3
  • 31
    • 0034683082 scopus 로고    scopus 로고
    • Calcium fluxes involved in control of cardiac myocyte contraction
    • Bers, D., Calcium fluxes involved in control of cardiac myocyte contraction. Circ. Res., 2000, 87, (4), 275.
    • (2000) Circ. Res. , vol.87 , Issue.4 , pp. 275
    • Bers, D.1
  • 32
    • 0035827585 scopus 로고    scopus 로고
    • Calmodulin binding and inhibition of cardiac muscle calcium release channel (ryanodine receptor)
    • Balshaw, D. M.; Xu, L.; Yamaguchi, N.; Pasek, D. A.; Meissner, G., Calmodulin binding and inhibition of cardiac muscle calcium release channel (ryanodine receptor). J. Biol. Chem, 2001, 276, (23), 20144-20153.
    • (2001) J. Biol. Chem , vol.276 , Issue.23 , pp. 20144-20153
    • Balshaw, D.M.1    Xu, L.2    Yamaguchi, N.3    Pasek, D.A.4    Meissner, G.5
  • 33
    • 0038607565 scopus 로고    scopus 로고
    • Molecular basis of calmodulin binding to cardiac muscle Ca (2+) release channel (ryanodine receptor)
    • Yamaguchi, N.; Xu, L.; Pasek, D. A.; Evans, K. E.; Meissner, G., Molecular basis of calmodulin binding to cardiac muscle Ca (2+) release channel (ryanodine receptor). J. Biol. Chem, 2003, 278, (26), 23480-23486.
    • (2003) J. Biol. Chem , vol.278 , Issue.26 , pp. 23480-23486
    • Yamaguchi, N.1    Xu, L.2    Pasek, D.A.3    Evans, K.E.4    Meissner, G.5
  • 34
    • 34248186991 scopus 로고    scopus 로고
    • Early cardiac hypertrophy in mice with impaired calmodulin regulation of cardiac muscle Ca release channel
    • Yamaguchi, N.; Takahashi, N.; Xu, L.; Smithies, O.; Meissner, G., Early cardiac hypertrophy in mice with impaired calmodulin regulation of cardiac muscle Ca release channel. J. Clin. Invest, 2007, 117, (5), 1344-1353.
    • (2007) J. Clin. Invest , vol.117 , Issue.5 , pp. 1344-1353
    • Yamaguchi, N.1    Takahashi, N.2    Xu, L.3    Smithies, O.4    Meissner, G.5
  • 35
    • 79952478406 scopus 로고    scopus 로고
    • Ryanodine receptors: Structure, expression, molecular details, and function in calcium release
    • Lanner, J. T.; Georgiou, D. K.; Joshi, A. D.; Hamilton, S. L., Ryanodine receptors: structure, expression, molecular details, and function in calcium release. Cold Spring Harb. Perspect. Biol, 2010, 2, (11), a003996.
    • (2010) Cold Spring Harb. Perspect. Biol , vol.2 , Issue.11
    • Lanner, J.T.1    Georgiou, D.K.2    Joshi, A.D.3    Hamilton, S.L.4
  • 36
    • 58849149051 scopus 로고    scopus 로고
    • Regulation of the cardiac muscle ryanodine receptor by O (2) tension and S-nitrosoglutathione
    • Sun, J.; Yamaguchi, N.; Xu, L.; Eu, J. P.; Stamler, J. S.; Meissner, G., Regulation of the cardiac muscle ryanodine receptor by O (2) tension and S-nitrosoglutathione. Biochemistry, 2008, 47, (52), 13985-13990.
    • (2008) Biochemistry , vol.47 , Issue.52 , pp. 13985-13990
    • Sun, J.1    Yamaguchi, N.2    Xu, L.3    Eu, J.P.4    Stamler, J.S.5    Meissner, G.6
  • 38
    • 0027500789 scopus 로고
    • The calcium release channel of sarcoplasmic reticulum is modulated by FK-506-binding protein. Dissociation and reconstitution of FKBP-12 to the calcium release channel of skeletal muscle sarcoplasmic reticulum
    • Timerman, A. P.; Ogunbumni, E.; Freund, E.; Wiederrecht, G.; Marks, A. R.; Fleischer, S., The calcium release channel of sarcoplasmic reticulum is modulated by FK-506-binding protein. Dissociation and reconstitution of FKBP-12 to the calcium release channel of skeletal muscle sarcoplasmic reticulum. J. Biol. Chem., 1993, 268, (31), 22992-22999.
    • (1993) J. Biol. Chem. , vol.268 , Issue.31 , pp. 22992-22999
    • Timerman, A.P.1    Ogunbumni, E.2    Freund, E.3    Wiederrecht, G.4    Marks, A.R.5    Fleischer, S.6
  • 39
    • 0029807075 scopus 로고    scopus 로고
    • Effects of FK-506 on contraction and Ca2+ transients in rat cardiac myocytes
    • McCall, E.; Li, L.; Satoh, H.; Shannon, T. R.; Blatter, L. A.; Bers, D. M., Effects of FK-506 on contraction and Ca2+ transients in rat cardiac myocytes. Circ. Res., 1996, 79, (6), 1110-1121.
    • (1996) Circ. Res. , vol.79 , Issue.6 , pp. 1110-1121
    • McCall, E.1    Li, L.2    Satoh, H.3    Shannon, T.R.4    Blatter, L.A.5    Bers, D.M.6
  • 41
    • 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, L. R.; Gyorke, S., The role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium. Biophys. J., 2004, 86, (4), 2121-2128.
    • (2004) Biophys. J. , vol.86 , Issue.4 , pp. 2121-2128
    • Gyorke, I.1    Hester, N.2    Jones, L.R.3    Gyorke, S.4
  • 43
    • 16444375139 scopus 로고    scopus 로고
    • Triadin overexpression stimulates excitation-contraction coupling and increases predisposition to cellular arrhythmia in cardiac myocytes
    • Terentyev, D.; Cala, S. E.; Houle, T. D.; Viatchenko-Karpinski, S.; Gyorke, I.; Terentyeva, R.; Williams, S. C.; Gyorke, S., Triadin overexpression stimulates excitation-contraction coupling and increases predisposition to cellular arrhythmia in cardiac myocytes. Circ. Res., 2005, 96, (6), 651-658.
    • (2005) Circ. Res. , vol.96 , Issue.6 , pp. 651-658
    • Terentyev, D.1    Cala, S.E.2    Houle, T.D.3    Viatchenko-Karpinski, S.4    Gyorke, I.5    Terentyeva, R.6    Williams, S.C.7    Gyorke, S.8
  • 45
    • 62149106324 scopus 로고    scopus 로고
    • Physiological implications of the interaction between the plasma membrane calcium pump and nNOS
    • Cartwright, E.; Oceandy, D.; Neyses, L., Physiological implications of the interaction between the plasma membrane calcium pump and nNOS. Pflügers. Arch. Eur. J. Physiol., 2009, 457, (3), 665-671.
    • (2009) Pflügers. Arch. Eur. J. Physiol. , vol.457 , Issue.3 , pp. 665-671
    • Cartwright, E.1    Oceandy, D.2    Neyses, L.3
  • 46
    • 34248583049 scopus 로고    scopus 로고
    • Na: Ca stoichiometry and cytosolic Cadependent activation of NCX in intact cardiomyocytes
    • Bers, D. M.; Ginsburg, K. S., Na: Ca stoichiometry and cytosolic Cadependent activation of NCX in intact cardiomyocytes. Ann. N. Y. Acad. Sci., 2007, 1099, 326-338.
    • (2007) Ann. N. Y. Acad. Sci. , vol.1099 , pp. 326-338
    • Bers, D.M.1    Ginsburg, K.S.2
  • 49
    • 1542347149 scopus 로고    scopus 로고
    • Role of Na+-Ca2+ exchanger in myocardial ischemia/reperfusion injury: Evaluation using a heterozygous Na+-Ca2+ exchanger knockout mouse model
    • Ohtsuka, M.; Takano, H.; Suzuki, M.; Zou, Y.; Akazawa, H.; Tamagawa, M.; Wakimoto, K.; Nakaya, H.; Komuro, I., Role of Na+-Ca2+ exchanger in myocardial ischemia/reperfusion injury: evaluation using a heterozygous Na+-Ca2+ exchanger knockout mouse model. Biochem. Biophys. Res. Commun., 2004, 314, (3), 849-853.
    • (2004) Biochem. Biophys. Res. Commun. , vol.314 , Issue.3 , pp. 849-853
    • Ohtsuka, M.1    Takano, H.2    Suzuki, M.3    Zou, Y.4    Akazawa, H.5    Tamagawa, M.6    Wakimoto, K.7    Nakaya, H.8    Komuro, I.9
  • 50
    • 34548480188 scopus 로고    scopus 로고
    • Diastolic Ca2+ overload caused by Na+/Ca2+ exchanger during the first minutes of reperfusion results in continued myocardial stunning
    • Wei, G. Z.; Zhou, J. J.; Wang, B.; Wu, F.; Bi, H.; Wang, Y. M.; Yi, D. H.; Yu, S. Q.; Pei, J. M., Diastolic Ca2+ overload caused by Na+/Ca2+ exchanger during the first minutes of reperfusion results in continued myocardial stunning. Eur. J. Pharmacol., 2007, 572, (1), 1-11.
    • (2007) Eur. J. Pharmacol. , vol.572 , Issue.1 , pp. 1-11
    • Wei, G.Z.1    Zhou, J.J.2    Wang, B.3    Wu, F.4    Bi, H.5    Wang, Y.M.6    Yi, D.H.7    Yu, S.Q.8    Pei, J.M.9
  • 51
    • 0035196931 scopus 로고    scopus 로고
    • Antisense inhibition of Na+/Ca2+ exchange during anoxia/reoxygenation in ventricular myocytes
    • Eigel, B. N.; Hadley, R. W., Antisense inhibition of Na+/Ca2+ exchange during anoxia/reoxygenation in ventricular myocytes. Am. J. Physiol. Heart Circ. Physiol., 2001, 281, (5), H2184-2190.
    • (2001) Am. J. Physiol. Heart Circ. Physiol. , vol.281 , Issue.5
    • Eigel, B.N.1    Hadley, R.W.2
  • 52
    • 0033837124 scopus 로고    scopus 로고
    • Diminished function and expression of the cardiac Na+-Ca2+ exchanger in diabetic rats: Implication in Ca2+ overload
    • Hattori, Y.; Matsuda, N.; Kimura, J.; Ishitani, T.; Tamada, A.; Gando, S.; Kemmotsu, O.; Kanno, M., Diminished function and expression of the cardiac Na+-Ca2+ exchanger in diabetic rats: implication in Ca2+ overload. J. Physiol., 2000, 527. Pt. 1, 85-94.
    • (2000) J. Physiol. , vol.527 , Issue.PART 1 , pp. 85-94
    • Hattori, Y.1    Matsuda, N.2    Kimura, J.3    Ishitani, T.4    Tamada, A.5    Gando, S.6    Kemmotsu, O.7    Kanno, M.8
  • 53
    • 77949266540 scopus 로고    scopus 로고
    • Multiple and diverse coexpression, location, and regulation of additional SERCA2 and SERCA3 isoforms in nonfailing and failing human heart
    • Dally, S.; Corvazier, E.; Bredoux, R.; Bobe, R.; Enouf, J., Multiple and diverse coexpression, location, and regulation of additional SERCA2 and SERCA3 isoforms in nonfailing and failing human heart. J. Mol. Cell. Cardiol., 2010, 48, (4), 633-644.
    • (2010) J. Mol. Cell. Cardiol. , vol.48 , Issue.4 , pp. 633-644
    • Dally, S.1    Corvazier, E.2    Bredoux, R.3    Bobe, R.4    Enouf, J.5
  • 54
    • 79959372611 scopus 로고    scopus 로고
    • Decreased sarcolipin protein expression and enhanced sarco (endo) plasmic reticulum Ca2+ uptake in human atrial fibrillation
    • Shanmugam, M.; Molina, C. E.; Gao, S.; Severac-Bastide, R.; Fischmeister, R.; Babu, G. J., Decreased sarcolipin protein expression and enhanced sarco (endo) plasmic reticulum Ca2+ uptake in human atrial fibrillation. Biochem. Biophys. Res. Commun, 2011, 410, (1), 97-101.
    • (2011) Biochem. Biophys. Res. Commun , vol.410 , Issue.1 , pp. 97-101
    • Shanmugam, M.1    Molina, C.E.2    Gao, S.3    Severac-Bastide, R.4    Fischmeister, R.5    Babu, G.J.6
  • 55
    • 37849007303 scopus 로고    scopus 로고
    • Structural and dynamic basis of phospholamban and sarcolipin inhibition of Ca (2+)-ATPase
    • Traaseth, N. J.; Ha, K. N.; Verardi, R.; Shi, L.; Buffy, J. J.; Masterson, L. R.; Veglia, G., Structural and dynamic basis of phospholamban and sarcolipin inhibition of Ca (2+)-ATPase. Biochemistry, 2008, 47, (1), 3-13.
    • (2008) Biochemistry , vol.47 , Issue.1 , pp. 3-13
    • Traaseth, N.J.1    Ha, K.N.2    Verardi, R.3    Shi, L.4    Buffy, J.J.5    Masterson, L.R.6    Veglia, G.7
  • 57
    • 0034509410 scopus 로고    scopus 로고
    • Phospholamban and cardiac contractile function
    • Brittsan, A. G.; Kranias, E. G., Phospholamban and cardiac contractile function. J. Mol. Cell. Cardiol, 2000, 32, (12), 2131-2139.
    • (2000) J. Mol. Cell. Cardiol , vol.32 , Issue.12 , pp. 2131-2139
    • Brittsan, A.G.1    Kranias, E.G.2
  • 58
    • 0031794676 scopus 로고    scopus 로고
    • Discovery of phospholamban. A personal history
    • Katz, A. M., Discovery of phospholamban. A personal history. Ann. N. Y. Acad. Sci., 1998, 853, 9-19.
    • (1998) Ann. N. Y. Acad. Sci. , vol.853 , pp. 9-19
    • Katz, A.M.1
  • 59
    • 0038464639 scopus 로고    scopus 로고
    • Phospholamban: A crucial regulator of cardiac contractility
    • MacLennan, D. H.; Kranias, E. G., Phospholamban: a crucial regulator of cardiac contractility. Nat. Rev. Mol. Cell. Biol, 2003, 4, (7), 566-577.
    • (2003) Nat. Rev. Mol. Cell. Biol , vol.4 , Issue.7 , pp. 566-577
    • MacLennan, D.H.1    Kranias, E.G.2
  • 61
    • 52049115619 scopus 로고    scopus 로고
    • Phospholamban phosphorylation by CaMKII under pathophysiological conditions
    • Vittone, L.; Mundina-Weilenmann, C.; Mattiazzi, A., Phospholamban phosphorylation by CaMKII under pathophysiological conditions. Front. Biosci, 2008, 13, 5988-6005.
    • (2008) Front. Biosci , vol.13 , pp. 5988-6005
    • Vittone, L.1    Mundina-Weilenmann, C.2    Mattiazzi, A.3
  • 62
    • 84855748562 scopus 로고    scopus 로고
    • Probing the helical tilt and dynamic properties of membranebound phospholamban in magnetically aligned bicelles using electron paramagnetic resonance spectroscopy
    • Ghimire, H.; Abu-Baker, S.; Sahu, I. D.; Zhou, A.; Mayo, D. J.; Lee, R. T.; Lorigan, G. A., Probing the helical tilt and dynamic properties of membranebound phospholamban in magnetically aligned bicelles using electron paramagnetic resonance spectroscopy. Biochim. Biophys. Acta, 2012, 1818, (3), 645-650.
    • (2012) Biochim. Biophys. Acta , vol.1818 , Issue.3 , pp. 645-650
    • Ghimire, H.1    Abu-Baker, S.2    Sahu, I.D.3    Zhou, A.4    Mayo, D.J.5    Lee, R.T.6    Lorigan, G.A.7
  • 63
    • 45549099461 scopus 로고    scopus 로고
    • Phospholamban oligomerization, quaternary structure, and sarco (endo) plasmic reticulum calcium ATPase binding measured by fluorescence resonance energy transfer in living cells
    • Kelly, E. M.; Hou, Z.; Bossuyt, J.; Bers, D. M.; Robia, S. L., Phospholamban oligomerization, quaternary structure, and sarco (endo) plasmic reticulum calcium ATPase binding measured by fluorescence resonance energy transfer in living cells. J. Biol. Chem., 2008, 283, (18), 12202-12211.
    • (2008) J. Biol. Chem. , vol.283 , Issue.18 , pp. 12202-12211
    • Kelly, E.M.1    Hou, Z.2    Bossuyt, J.3    Bers, D.M.4    Robia, S.L.5
  • 64
    • 34548442113 scopus 로고    scopus 로고
    • Comparing the structure and dynamics of phospholamban pentamer in its unphosphorylated and pseudophosphorylated states
    • Oxenoid, K.; Rice, A. J.; Chou, J. J., Comparing the structure and dynamics of phospholamban pentamer in its unphosphorylated and pseudophosphorylated states. P rotein Sci., 2007, 16, (9), 1977-1983.
    • (2007) P Rotein Sci. , vol.16 , Issue.9 , pp. 1977-1983
    • Oxenoid, K.1    Rice, A.J.2    Chou, J.J.3
  • 68
    • 78049244488 scopus 로고    scopus 로고
    • Calcium signalling: Fishing out molecules of mitochondrial calcium transport
    • Hajnóczky, G.; Csordás, G., Calcium Signalling: Fishing Out Molecules of Mitochondrial Calcium Transport. Curr. Biol.: CB, 2010, 20, (20), R888-R891.
    • (2010) Curr. Biol.: CB , vol.20 , Issue.20
    • Hajnóczky, G.1    Csordás, G.2
  • 69
    • 77952672524 scopus 로고    scopus 로고
    • Mitochondrial calcium channels
    • Hoppe, U. C., Mitochondrial calcium channels. FEBS Lett., 2010, 584, (10), 1975-1981.
    • (2010) FEBS Lett. , vol.584 , Issue.10 , pp. 1975-1981
    • Hoppe, U.C.1
  • 70
    • 84863418960 scopus 로고    scopus 로고
    • Mitochondrial permeability transition in the diabetic heart: Contributions of thiol redox state and mitochondrial calcium to augmented reperfusion injury
    • Sloan, R. C.; Moukdar, F.; Frasier, C. R.; Patel, H. D.; Bostian, P. A.; Lust, R. M.; Brown, D. A., Mitochondrial permeability transition in the diabetic heart: contributions of thiol redox state and mitochondrial calcium to augmented reperfusion injury. J. Mol. Cell. Cardiol., 2012, 52, (5), 1009-1018.
    • (2012) J. Mol. Cell. Cardiol. , vol.52 , Issue.5 , pp. 1009-1018
    • Sloan, R.C.1    Moukdar, F.2    Frasier, C.R.3    Patel, H.D.4    Bostian, P.A.5    Lust, R.M.6    Brown, D.A.7
  • 71
    • 49349102894 scopus 로고    scopus 로고
    • Mitochondrial fusion, fission and autophagy as a quality control axis: The bioenergetic view
    • Twig, G.; Hyde, B.; Shirihai, O. S., Mitochondrial fusion, fission and autophagy as a quality control axis: the bioenergetic view. Biochim. Biophys. Acta, 2008, 1777, (9), 1092-1097.
    • (2008) Biochim. Biophys. Acta , vol.1777 , Issue.9 , pp. 1092-1097
    • Twig, G.1    Hyde, B.2    Shirihai, O.S.3
  • 73
    • 77952236126 scopus 로고    scopus 로고
    • Inhibiting mitochondrial fission protects the heart against ischemia/reperfusion injury
    • Ong, S. B.; Subrayan, S.; Lim, S. Y.; Yellon, D. M.; Davidson, S. M.; Hausenloy, D. J., Inhibiting mitochondrial fission protects the heart against ischemia/reperfusion injury. Circulation, 2010, 121, (18), 2012-2022.
    • (2010) Circulation , vol.121 , Issue.18 , pp. 2012-2022
    • Ong, S.B.1    Subrayan, S.2    Lim, S.Y.3    Yellon, D.M.4    Davidson, S.M.5    Hausenloy, D.J.6
  • 74
    • 34548008730 scopus 로고    scopus 로고
    • Reperfusion injury salvage kinase signalling: Taking a RISK for cardioprotection
    • 217-234
    • Hausenloy, D. J.; Yellon, D. M., Reperfusion injury salvage kinase signalling: taking a RISK for cardioprotection. Heart Fail. Rev., 2007, 12, (3-4), 217-234.
    • (2007) Heart Fail. Rev. , vol.12 , pp. 3-4
    • Hausenloy, D.J.1    Yellon, D.M.2
  • 75
    • 17144405293 scopus 로고    scopus 로고
    • Failure to protect the myocardium against ischemia/reperfusion injury after chronic atorvastatin treatment is recaptured by acute atorvastatin treatment: A potential role for phosphatase and tensin homolog deleted on chromosome ten
    • Mensah, K.; Mocanu, M. M.; Yellon, D. M., Failure to protect the myocardium against ischemia/reperfusion injury after chronic atorvastatin treatment is recaptured by acute atorvastatin treatment: a potential role for phosphatase and tensin homolog deleted on chromosome ten. J. Am. Coll. Cardiol., 2005, 45, (8), 1287-1291.
    • (2005) J. Am. Coll. Cardiol. , vol.45 , Issue.8 , pp. 1287-1291
    • Mensah, K.1    Mocanu, M.M.2    Yellon, D.M.3
  • 76
    • 67650263713 scopus 로고    scopus 로고
    • Cardioprotective growth factors
    • Hausenloy, D. J.; Yellon, D. M., Cardioprotective growth factors. Cardiovasc. Res, 2009, 83, (2), 179-194.
    • (2009) Cardiovasc. Res , vol.83 , Issue.2 , pp. 179-194
    • Hausenloy, D.J.1    Yellon, D.M.2
  • 77
    • 0034533443 scopus 로고    scopus 로고
    • Differential shedding of transmembrane neuregulin isoforms by the tumor necrosis factor-alpha-converting enzyme
    • Montero, J. C.; Yuste, L.; Diaz-Rodriguez, E.; Esparis-Ogando, A.; Pandiella, A., Differential shedding of transmembrane neuregulin isoforms by the tumor necrosis factor-alpha-converting enzyme. Mol. Cell. Neurosci., 2000, 16, (5), 631-648.
    • (2000) Mol. Cell. Neurosci. , vol.16 , Issue.5 , pp. 631-648
    • Montero, J.C.1    Yuste, L.2    Diaz-Rodriguez, E.3    Esparis-Ogando, A.4    Pandiella, A.5
  • 79
    • 0035937787 scopus 로고    scopus 로고
    • Roles of Meltrin beta/ADAM19 in the processing of neuregulin
    • Shirakabe, K.; Wakatsuki, S.; Kurisaki, T.; Fujisawa-Sehara, A., Roles of Meltrin beta/ADAM19 in the processing of neuregulin. J. Biol. Chem., 2001, 276, (12), 9352-9358.
    • (2001) J. Biol. Chem. , vol.276 , Issue.12 , pp. 9352-9358
    • Shirakabe, K.1    Wakatsuki, S.2    Kurisaki, T.3    Fujisawa-Sehara, A.4
  • 80
    • 0037429649 scopus 로고    scopus 로고
    • Neuregulins: Functions, forms, and signaling strategies
    • Falls, D. L., Neuregulins: functions, forms, and signaling strategies. Exp. Cell. Res, 2003, 284, (1), 14-30.
    • (2003) Exp. Cell. Res , vol.284 , Issue.1 , pp. 14-30
    • Falls, D.L.1
  • 81
    • 0028827104 scopus 로고
    • Multiple essential functions of neuregulin in development
    • Meyer, D.; Birchmeier, C., Multiple essential functions of neuregulin in development. Nature, 1995, 378, (6555), 386-390.
    • (1995) Nature , vol.378 , Issue.6555 , pp. 386-390
    • Meyer, D.1    Birchmeier, C.2
  • 82
    • 0028884413 scopus 로고
    • Requirement for neuregulin receptor erbB2 in neural and cardiac development
    • Lee, K. F.; Simon, H.; Chen, H.; Bates, B.; Hung, M. C.; Hauser, C., Requirement for neuregulin receptor erbB2 in neural and cardiac development. Nature, 1995, 378, (6555), 394-398.
    • (1995) Nature , vol.378 , Issue.6555 , pp. 394-398
    • Lee, K.F.1    Simon, H.2    Chen, H.3    Bates, B.4    Hung, M.C.5    Hauser, C.6
  • 83
    • 0028785406 scopus 로고
    • Aberrant neural and cardiac development in mice lacking the ErbB4 neuregulin receptor
    • Gassmann, M.; Casagranda, F.; Orioli, D.; Simon, H.; Lai, C.; Klein, R.; Lemke, G., Aberrant neural and cardiac development in mice lacking the ErbB4 neuregulin receptor. Nature, 1995, 378, (6555), 390-394.
    • (1995) Nature , vol.378 , Issue.6555 , pp. 390-394
    • Gassmann, M.1    Casagranda, F.2    Orioli, D.3    Simon, H.4    Lai, C.5    Klein, R.6    Lemke, G.7
  • 84
    • 0031454062 scopus 로고    scopus 로고
    • ErbB3 is required for normal cerebellar and cardiac development: A comparison with ErbB2-and heregulin-deficient mice
    • Erickson, S.; O'Shea, K.; Ghaboosi, N.; Loverro, L.; Frantz, G.; Bauer, M.; Lu, L.; Moore, M., ErbB3 is required for normal cerebellar and cardiac development: a comparison with ErbB2-and heregulin-deficient mice. Development, 1997, 124, (24), 4999-5011.
    • (1997) Development , vol.124 , Issue.24 , pp. 4999-5011
    • Erickson, S.1    O'Shea, K.2    Ghaboosi, N.3    Loverro, L.4    Frantz, G.5    Bauer, M.6    Lu, L.7    Moore, M.8
  • 85
    • 33745805840 scopus 로고    scopus 로고
    • Role of neuregulin-1/ErbB2 signaling in endothelium-cardiomyocyte cross-talk
    • Lemmens, K.; Segers, V. F.; Demolder, M.; De Keulenaer, G. W., Role of neuregulin-1/ErbB2 signaling in endothelium-cardiomyocyte cross-talk. J. Biol. Chem., 2006, 281, (28), 19469-19477.
    • (2006) J. Biol. Chem. , vol.281 , Issue.28 , pp. 19469-19477
    • Lemmens, K.1    Segers, V.F.2    Demolder, M.3    De Keulenaer, G.W.4
  • 86
  • 87
    • 0032562770 scopus 로고    scopus 로고
    • Neuregulins promote survival and growth of cardiac myocytes. Persistence of ErbB2 and ErbB4 expression in neonatal and adult ventricular myocytes
    • Zhao, Y. Y.; Sawyer, D. R.; Baliga, R. R.; Opel, D. J.; Han, X.; Marchionni, M. A.; Kelly, R. A., Neuregulins promote survival and growth of cardiac myocytes. Persistence of ErbB2 and ErbB4 expression in neonatal and adult ventricular myocytes. J. Biol. Chem., 1998, 273, (17), 10261-10269.
    • (1998) J. Biol. Chem. , vol.273 , Issue.17 , pp. 10261-10269
    • Zhao, Y.Y.1    Sawyer, D.R.2    Baliga, R.R.3    Opel, D.J.4    Han, X.5    Marchionni, M.A.6    Kelly, R.A.7
  • 89
    • 62649116580 scopus 로고    scopus 로고
    • The role of Neuregulin-1beta/ErbB signaling in the heart
    • Pentassuglia, L.; Sawyer, D. B., The role of Neuregulin-1beta/ErbB signaling in the heart. Exp. Cell. Res, 2009, 315, (4), 627-637.
    • (2009) Exp. Cell. Res , vol.315 , Issue.4 , pp. 627-637
    • Pentassuglia, L.1    Sawyer, D.B.2
  • 90
    • 77949272136 scopus 로고    scopus 로고
    • Neuregulin signaling and heart failure
    • Zhenggang, J.; Zhou, M., Neuregulin Signaling and Heart Failure. Curr. Heart Fail. Rep, 2010, 7, 42-47.
    • (2010) Curr. Heart Fail. Rep , vol.7 , pp. 42-47
    • Zhenggang, J.1    Zhou, M.2
  • 91
    • 21644470216 scopus 로고    scopus 로고
    • Expressional reprogramming of servival pathways in rat cardiocytes by neuregulin-1beta
    • Giraud, M.; Fluck, M.; Zuppinger, C; Suter, T., Expressional reprogramming of servival pathways in rat cardiocytes by neuregulin-1beta. J. Appl. Physiol, 2005, 99, (1), 313-322.
    • (2005) J. Appl. Physiol , vol.99 , Issue.1 , pp. 313-322
    • Giraud, M.1    Fluck, M.2    Zuppinger, C.3    Suter, T.4
  • 93
    • 33746048823 scopus 로고    scopus 로고
    • Neuregulin activates erbB2-dependent src/FAK signaling and cytoskeletal remodeling in isolated adult rat cardiac myocytes
    • Kuramochi, Y; Guo, X.; Sawyer, D. B., Neuregulin activates erbB2-dependent src/FAK signaling and cytoskeletal remodeling in isolated adult rat cardiac myocytes. J. Mol. Cell. Cardiol, 2006, 41, (2), 228-235.
    • (2006) J. Mol. Cell. Cardiol , vol.41 , Issue.2 , pp. 228-235
    • Kuramochi, Y.1    Guo, X.2    Sawyer, D.B.3
  • 95
    • 34248525627 scopus 로고    scopus 로고
    • Combination treatment with Grb7 peptide and Doxorubicin or Trastuzumab (Herceptin) results in cooperative cell growth inhibition in breast cancer cells
    • Pero, S. C.; Shukla, G. S.; Cookson, M. M.; Flemer, S., Jr.; Krag, D. N., Combination treatment with Grb7 peptide and Doxorubicin or Trastuzumab (Herceptin) results in cooperative cell growth inhibition in breast cancer cells. Br. J. Cancer, 2007, 96, (10), 1520-1525.
    • (2007) Br. J. Cancer , vol.96 , Issue.10 , pp. 1520-1525
    • Pero, S.C.1    Shukla, G.S.2    Cookson, M.M.3    Flemer Jr., S.4    Krag, D.N.5
  • 97
    • 27344447301 scopus 로고    scopus 로고
    • Neuregulin-1 alpha and beta isoform expression in cardiac microvascular endothelial cells and function in cardiac myocytes in vitro
    • Cote, G. M.; Miller, T. A.; Lebrasseur, N. K.; Kuramochi, Y; Sawyer, D. B., Neuregulin-1 alpha and beta isoform expression in cardiac microvascular endothelial cells and function in cardiac myocytes in vitro. Exp. Cell. Res., 2005, 311, (1), 135-146.
    • (2005) Exp. Cell. Res. , vol.311 , Issue.1 , pp. 135-146
    • Cote, G.M.1    Miller, T.A.2    Lebrasseur, N.K.3    Kuramochi, Y.4    Sawyer, D.B.5
  • 98
    • 0344924865 scopus 로고    scopus 로고
    • Neuregulin-1 protects ventricular myocytes from anthracycline-induced apoptosis via erbB4-dependent activation of PI3-kinase/Akt
    • Fukazawa, R.; Miller, T. A.; Kuramochi, Y; Frantz, S.; Kim, YD.; Marchionni, M. A.; Kelly, R. A.; Sawyer, D. B., Neuregulin-1 protects ventricular myocytes from anthracycline-induced apoptosis via erbB4-dependent activation of PI3-kinase/Akt. J. Mol. Cell. Cardiol, 2003, 35, (12), 1473-1479.
    • (2003) J. Mol. Cell. Cardiol , vol.35 , Issue.12 , pp. 1473-1479
    • Fukazawa, R.1    Miller, T.A.2    Kuramochi, Y.3    Frantz, S.4    Kim, Y.D.5    Marchionni, M.A.6    Kelly, R.A.7    Sawyer, D.B.8
  • 99
    • 1642458136 scopus 로고    scopus 로고
    • Neuregulin-1 induces a negative inotropic effect in cardiac muscle: Role of nitric oxide synthase
    • Lemmens, K.; Fransen, P.; Sys, S. U.; Brutsaert, D. L.; De Keulenaer, G. W., Neuregulin-1 induces a negative inotropic effect in cardiac muscle: role of nitric oxide synthase. Circulation, 2004, 109, (3), 324-326.
    • (2004) Circulation , vol.109 , Issue.3 , pp. 324-326
    • Lemmens, K.1    Fransen, P.2    Sys, S.U.3    Brutsaert, D.L.4    De Keulenaer, G.W.5
  • 100
    • 1642263252 scopus 로고    scopus 로고
    • Restoration of resting sarcomere lenght after uniaxial static strain is regulated by protein kinase C epsilon and focal adhesion kinase
    • Mansour, H.; Tombe, P.d.; Samarel, A.; Russell, B., Restoration of resting sarcomere lenght after uniaxial static strain is regulated by protein kinase C epsilon and focal adhesion kinase. Circ. Res., 2004, 94, (5), 642-649.
    • (2004) Circ. Res. , vol.94 , Issue.5 , pp. 642-649
    • Mansour, H.1    Tombe, P.2    Samarel, A.3    Russell, B.4
  • 101
    • 0037188939 scopus 로고    scopus 로고
    • Importance of integrin signaling in myocyte growth and survival
    • Kuppuswamy, D., Importance of integrin signaling in myocyte growth and survival. Circ. Res., 2002, 90, (12), 1240-1242.
    • (2002) Circ. Res. , vol.90 , Issue.12 , pp. 1240-1242
    • Kuppuswamy, D.1
  • 102
    • 0034682589 scopus 로고    scopus 로고
    • Trastuzumab in the treatment of metastatic breast cancer anticancer therapy versus cardiotoxicity
    • Feldman, A. M.; Lorell, B. H.; Reis, S. E., Trastuzumab in the treatment of metastatic breast cancer anticancer therapy versus cardiotoxicity. Circulation, 2000, 102, (3), 272-274.
    • (2000) Circulation , vol.102 , Issue.3 , pp. 272-274
    • Feldman, A.M.1    Lorell, B.H.2    Reis, S.E.3
  • 104
    • 74049164266 scopus 로고    scopus 로고
    • The vulnerability of the heart as a pluricellular paracrine organ: Lessons from unexpected triggers of heart failure in targeted ErbB2 anticancer therapy
    • Keulenaer, G. D.; Doggen, K.; Lemmens, K., The vulnerability of the heart as a pluricellular paracrine organ: lessons from unexpected triggers of heart failure in targeted ErbB2 anticancer therapy. Circ. Res., 2010, 106, (1), 35-46.
    • (2010) Circ. Res. , vol.106 , Issue.1 , pp. 35-46
    • Keulenaer, G.D.1    Doggen, K.2    Lemmens, K.3
  • 105
    • 34548132413 scopus 로고    scopus 로고
    • Role of neuregulin-1/ErbB signaling in cardiovascular physiology and disease: Implications for therapy of heart failure
    • Lemmens, K.; Doggen, K.; De Keulenaer, G. W., Role of Neuregulin-1/ErbB Signaling in Cardiovascular Physiology and Disease: Implications for Therapy of Heart Failure. Circulation, 2007, 116, (8), 954-960.
    • (2007) Circulation , vol.116 , Issue.8 , pp. 954-960
    • Lemmens, K.1    Doggen, K.2    De Keulenaer, G.W.3
  • 106
    • 0042917516 scopus 로고    scopus 로고
    • Nitric oxide and cardiac function: Ten years after, and continuing
    • Massion, P.; Feron, O.; Dessy, C; Balligand, J., Nitric oxide and cardiac function: ten years after, and continuing. Circ. Res., 2003, 93, 388-398.
    • (2003) Circ. Res. , vol.93 , pp. 388-398
    • Massion, P.1    Feron, O.2    Dessy, C.3    Balligand, J.4
  • 107
    • 4043110498 scopus 로고    scopus 로고
    • Neuregulins regulate cardiac parasympathetic activity: Muscarinic modulation of beta-adrenergic activity in myocytes from mice with neuregulin-1 gene deletion
    • Okoshi, K.; Nakayama, M.; Yan, X.; Okoshi, M. P.; Schuldt, A. J.; Marchionni, M. A.; Lorell, B. H., Neuregulins regulate cardiac parasympathetic activity: muscarinic modulation of beta-adrenergic activity in myocytes from mice with neuregulin-1 gene deletion. Circulation, 2004, 110, (6), 713-717.
    • (2004) Circulation , vol.110 , Issue.6 , pp. 713-717
    • Okoshi, K.1    Nakayama, M.2    Yan, X.3    Okoshi, M.P.4    Schuldt, A.J.5    Marchionni, M.A.6    Lorell, B.H.7
  • 108
    • 78149338262 scopus 로고    scopus 로고
    • Neuregulin-1 β1 rapidly modulates nitric oxide synthesis and calcium handling in rat cardiomyocytes
    • Brero, A.; Ramella, R.; Fitou, A.; Dati, C; Alloatti, G.; Gallo, M. P.; Levi, R., Neuregulin-1 β1 rapidly modulates nitric oxide synthesis and calcium handling in rat cardiomyocytes. Cardiovas. Res., 2010, 88, (3), 443-452.
    • (2010) Cardiovas. Res. , vol.88 , Issue.3 , pp. 443-452
    • Brero, A.1    Ramella, R.2    Fitou, A.3    Dati, C.4    Alloatti, G.5    Gallo, M.P.6    Levi, R.7
  • 109
    • 62249192069 scopus 로고    scopus 로고
    • Neuregulin-1/ErbB signaling: A druggable target for treating heart failure
    • Xu, Y; Li, X.; Zhou, M., Neuregulin-1/ErbB signaling: a druggable target for treating heart failure. Curr. Opin. Pharmacol, 2009, 9, (2), 214-219.
    • (2009) Curr. Opin. Pharmacol , vol.9 , Issue.2 , pp. 214-219
    • Xu, Y.1    Li, X.2    Zhou, M.3
  • 110
    • 33750347979 scopus 로고    scopus 로고
    • Neuregulin-1 beta attenuates doxorubicin-induced alterations of excitation-contraction coupling and reduces oxidative stress in adult rat cardiomyocytes
    • Timolati, F.; Ott, D.; Pentassuglia, L.; Giraud, M.-N; Perriard, J.-C; Suter, T. M.; Zuppinger, C, Neuregulin-1 beta attenuates doxorubicin-induced alterations of excitation-contraction coupling and reduces oxidative stress in adult rat cardiomyocytes. J. Mol Cell. Cardiol, 2006, 41, (5), 845-854.
    • (2006) J. Mol Cell. Cardiol , vol.41 , Issue.5 , pp. 845-854
    • Timolati, F.1    Ott, D.2    Pentassuglia, L.3    Giraud, M.-N.4    Perriard, J.-C.5    Suter, T.M.6    Zuppinger, C.7
  • 111
    • 33748929841 scopus 로고    scopus 로고
    • Neuregulin-1/erbB-activation improves cardiac function and survival in models of ischemic, dilated, and viral cardiomyopathy
    • Liu, X.; Gu, X.; Li, Z.; Li, X.; Li, H.; Chang, J.; Chen, P.; Jin, J.; Xi, B.; Chen, D.; Lai, D.; Graham, R.; Zhou, M., Neuregulin-1/erbB-activation improves cardiac function and survival in models of ischemic, dilated, and viral cardiomyopathy. J. Am. Coll. Cardiol, 2006, 48, 1438-1447.
    • (2006) J. Am. Coll. Cardiol , vol.48 , pp. 1438-1447
    • Liu, X.1    Gu, X.2    Li, Z.3    Li, X.4    Li, H.5    Chang, J.6    Chen, P.7    Jin, J.8    Xi, B.9    Chen, D.10    Lai, D.11    Graham, R.12    Zhou, M.13
  • 112
    • 67349148886 scopus 로고    scopus 로고
    • Mitochondrial calcium transport in the heart: Physiological and pathological roles
    • Griffiths, E. J., Mitochondrial calcium transport in the heart: physiological and pathological roles. J. Mol. Cell. Cardiol, 2009, 46, (6), 789-803.
    • (2009) J. Mol. Cell. Cardiol , vol.46 , Issue.6 , pp. 789-803
    • Griffiths, E.J.1
  • 113
    • 1142273368 scopus 로고    scopus 로고
    • Mitochondrial permeability transition pore opening during myocardial reperfusion-a target for cardioprotection
    • Halestrap, A.; Clarke, S.; Javadov, S., Mitochondrial permeability transition pore opening during myocardial reperfusion-a target for cardioprotection. Cardiovasc. Res., 2004, 61, (3), 372-385.
    • (2004) Cardiovasc. Res. , vol.61 , Issue.3 , pp. 372-385
    • Halestrap, A.1    Clarke, S.2    Javadov, S.3
  • 114
    • 0026058982 scopus 로고
    • Measurement of mitochondrial free Ca2+ concentration in living single rat cardiac myocytes
    • Miyata, H.; Silverman, H. S.; Sollott, S. J.; Lakatta, E. G.; Stern, M. D.; Hansford, R. G., Measurement of mitochondrial free Ca2+ concentration in living single rat cardiac myocytes. Am. J. Physiol, 1991, 261, (4 Pt 2), H1123-1134.
    • (1991) Am. J. Physiol , vol.261 , Issue.4 PART 2
    • Miyata, H.1    Silverman, H.S.2    Sollott, S.J.3    Lakatta, E.G.4    Stern, M.D.5    Hansford, R.G.6
  • 115
    • 70349632998 scopus 로고    scopus 로고
    • Role of sarcoplasmic reticulum in mitochondrial permeability transition and cardiomyocyte death during reperfusion
    • Ruiz-Meana, M.; Abellan, A.; Miro-Casas, E.; Agullo, E.; Garcia-Dorado, D., Role of sarcoplasmic reticulum in mitochondrial permeability transition and cardiomyocyte death during reperfusion. Am. J. Physiol. Heart Circ. Physiol, 2009, 297, (4), H1281-1289.
    • (2009) Am. J. Physiol. Heart Circ. Physiol , vol.297 , Issue.4
    • Ruiz-Meana, M.1    Abellan, A.2    Miro-Casas, E.3    Agullo, E.4    Garcia-Dorado, D.5
  • 116
    • 67349117275 scopus 로고    scopus 로고
    • What is the mitochondrial permeability transition pore?
    • Halestrap, A., What is the mitochondrial permeability transition pore? J. Mol. Cell. Cardiol, 2009, 46, (6), 821-831.
    • (2009) J. Mol. Cell. Cardiol , vol.46 , Issue.6 , pp. 821-831
    • Halestrap, A.1
  • 119
    • 68149166465 scopus 로고    scopus 로고
    • Miura, GSK-3β a therapeutic target for cardiomyocyte protection
    • Miura, GSK-3β a Therapeutic Target for Cardiomyocyte Protection. Circ. J., 2009, 73(7), 1184-1192.
    • (2009) Circ. J. , vol.73 , Issue.7 , pp. 1184-1192
  • 120
    • 64849095173 scopus 로고    scopus 로고
    • Myocardial protection against reperfusion injury: The cGMP pathway
    • Garcia-Dorado, D.; Agulló, L.; Sartorio, C; Ruiz-Meana, M., Myocardial protection against reperfusion injury: the cGMP pathway. Thromb. Haemost, 2009, 101, (4), 635-642.
    • (2009) Thromb. Haemost , vol.101 , Issue.4 , pp. 635-642
    • Garcia-Dorado, D.1    Agulló, L.2    Sartorio, C.3    Ruiz-Meana, M.4
  • 121
    • 10944236872 scopus 로고    scopus 로고
    • Cardiac endothelial cells regulate reactive oxygen species-induced cardiomyocyte apoptosis through neuregulin-1beta/erbB4 signaling
    • Kuramochi, Y; Cote, G.; Guo, X.; Lebrasseur, N; Cui, L.; Liao, R.; Sawyer, D., Cardiac endothelial cells regulate reactive oxygen species-induced cardiomyocyte apoptosis through neuregulin-1beta/erbB4 signaling. J. Biol. Chem., 2004, 279, (49), 1141-1147.
    • (2004) J. Biol. Chem. , vol.279 , Issue.49 , pp. 1141-1147
    • Kuramochi, Y.1    Cote, G.2    Guo, X.3    Lebrasseur, N.4    Cui, L.5    Liao, R.6    Sawyer, D.7
  • 125
  • 127
    • 9144224385 scopus 로고    scopus 로고
    • Urocortin-II and urocortin-III are cardioprotective against ischemia reperfusion injury: An essential endogenous cardioprotective role for corticotropin releasing factor receptor type 2 in the murine heart
    • discussion 21-23
    • Brar, B. K.; Jonassen, A. K.; Egorina, E. M.; Chen, A.; Negro, A.; Perrin, M. H.; Mjos, O. D.; Latchman, D. S.; Lee, K. F.; Vale, W., Urocortin-II and urocortin-III are cardioprotective against ischemia reperfusion injury: an essential endogenous cardioprotective role for corticotropin releasing factor receptor type 2 in the murine heart. Endocrinology, 2004, 145, (1), 24-35; discussion 21-23.
    • (2004) Endocrinology , vol.145 , Issue.1 , pp. 24-35
    • Brar, B.K.1    Jonassen, A.K.2    Egorina, E.M.3    Chen, A.4    Negro, A.5    Perrin, M.H.6    Mjos, O.D.7    Latchman, D.S.8    Lee, K.F.9    Vale, W.10
  • 129
    • 0034796230 scopus 로고    scopus 로고
    • Urocortin protects against ischemic injury via a MAPK-dependent pathway
    • Latchman, D. S., Urocortin protects against ischemic injury via a MAPK-dependent pathway. Trends Cardiovasc. Med., 2001, 11, (5), 167-169.
    • (2001) Trends Cardiovasc. Med. , vol.11 , Issue.5 , pp. 167-169
    • Latchman, D.S.1
  • 130
    • 0036783616 scopus 로고    scopus 로고
    • Urocortin protects the heart from reperfusion injury via upregulation of p42/p44 MAPK signaling pathway
    • Schulman, D.; Latchman, D. S.; Yellon, D. M., Urocortin protects the heart from reperfusion injury via upregulation of p42/p44 MAPK signaling pathway. Am. J. Physiol. Heart. Circ. Physiol, 2002, 283, (4), H1481-1488.
    • (2002) Am. J. Physiol. Heart. Circ. Physiol , vol.283 , Issue.4
    • Schulman, D.1    Latchman, D.S.2    Yellon, D.M.3
  • 133
  • 134
    • 61749091170 scopus 로고    scopus 로고
    • Natriuretic peptides: Their structures, receptors, physiologic functions and therapeutic applications
    • Potter, L. R.; Yoder, A. R.; Flora, D. R.; Antos, L. K.; Dickey, D. M., Natriuretic peptides: their structures, receptors, physiologic functions and therapeutic applications. Handb. Exp. Pharmacol, 2009, (191), 341-366.
    • (2009) Handb. Exp. Pharmacol , Issue.191 , pp. 341-366
    • Potter, L.R.1    Yoder, A.R.2    Flora, D.R.3    Antos, L.K.4    Dickey, D.M.5
  • 135
    • 38149124088 scopus 로고    scopus 로고
    • Natriuretic peptide C receptor signalling in the heart and vasculature
    • Rose, R. A.; Giles, W. R., Natriuretic peptide C receptor signalling in the heart and vasculature. J. Physiol, 2008, 586, (2), 353-366.
    • (2008) J. Physiol , vol.586 , Issue.2 , pp. 353-366
    • Rose, R.A.1    Giles, W.R.2
  • 136
    • 1942533427 scopus 로고    scopus 로고
    • Effects of C-type natriuretic peptide on ionic currents in mouse sinoatrial node: A role for the NPR-C receptor
    • Rose, R. A.; Lomax, A. E.; Kondo, C. S.; Anand-Srivastava, M. B.; Giles, W. R., Effects of C-type natriuretic peptide on ionic currents in mouse sinoatrial node: a role for the NPR-C receptor. Am. J. Physiol. Heart Circ. Physiol, 2004, 286, (5), H1970-1977.
    • (2004) Am. J. Physiol. Heart Circ. Physiol , vol.286 , Issue.5
    • Rose, R.A.1    Lomax, A.E.2    Kondo, C.S.3    Anand-Srivastava, M.B.4    Giles, W.R.5
  • 137
    • 4444335043 scopus 로고    scopus 로고
    • Natriuretic peptide receptor-C regulates coronary blood flow and prevents myocardial ischemia/reperfusion injury: Novel cardioprotective role for endotheliumderived C-type natriuretic peptide
    • Hobbs, A.; Foster, P.; Prescott, C.; Scotland, R.; Ahluwalia, A., Natriuretic peptide receptor-C regulates coronary blood flow and prevents myocardial ischemia/reperfusion injury: novel cardioprotective role for endotheliumderived C-type natriuretic peptide. Circulation, 2004, 110, (10), 1231-1235.
    • (2004) Circulation , vol.110 , Issue.10 , pp. 1231-1235
    • Hobbs, A.1    Foster, P.2    Prescott, C.3    Scotland, R.4    Ahluwalia, A.5
  • 138
    • 12744256779 scopus 로고    scopus 로고
    • C-type natriuretic peptide in vascular physiology and disease
    • Scotland, R. S.; Ahluwalia, A.; Hobbs, A. J., C-type natriuretic peptide in vascular physiology and disease. Pharmacol. Ther., 2005, 105, (2), 85-93.
    • (2005) Pharmacol. Ther. , vol.105 , Issue.2 , pp. 85-93
    • Scotland, R.S.1    Ahluwalia, A.2    Hobbs, A.J.3
  • 139
    • 84859637397 scopus 로고    scopus 로고
    • The natriuretic peptides BNP and CNP increase heart rate and electrical conduction by stimulating ionic currents in the sinoatrial node and atrial myocardium following activation of guanylyl cyclase-linked natriuretic peptide receptors
    • Springer, J.; Azer, J.; Hua, R.; Robbins, C.; Adamczyk, A.; McBoyle, S.; Bissell, M. B.; Rose, R. A., The natriuretic peptides BNP and CNP increase heart rate and electrical conduction by stimulating ionic currents in the sinoatrial node and atrial myocardium following activation of guanylyl cyclase-linked natriuretic peptide receptors. J. Mol. Cell. Cardiol., 2012, 52, (5), 1122-1134.
    • (2012) J. Mol. Cell. Cardiol. , vol.52 , Issue.5 , pp. 1122-1134
    • Springer, J.1    Azer, J.2    Hua, R.3    Robbins, C.4    Adamczyk, A.5    McBoyle, S.6    Bissell, M.B.7    Rose, R.A.8
  • 140
    • 78649396592 scopus 로고    scopus 로고
    • The SUMO pathway: Emerging mechanisms that shape specificity, conjugation and recognition
    • Gareau, J. R.; Lima, C. D., The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nat. Rev. Mol. Cell. Biol., 2010, 11, (12), 861-871.
    • (2010) Nat. Rev. Mol. Cell. Biol. , vol.11 , Issue.12 , pp. 861-871
    • Gareau, J.R.1    Lima, C.D.2
  • 143
    • 10344252331 scopus 로고    scopus 로고
    • SUMO-1 modification activated GATA4-dependent cardiogenic gene activity
    • Wang, J.; Feng, X. H.; Schwartz, R. J., SUMO-1 modification activated GATA4-dependent cardiogenic gene activity. J. Biol. Chem., 2004, 279, (47), 49091-49098.
    • (2004) J. Biol. Chem. , vol.279 , Issue.47 , pp. 49091-49098
    • Wang, J.1    Feng, X.H.2    Schwartz, R.J.3
  • 144
    • 33846182262 scopus 로고    scopus 로고
    • Myocardin sumoylation transactivates cardiogenic genes in pluripotent 10T1/2 fibroblasts
    • Wang, J.; Li, A.; Wang, Z.; Feng, X.; Olson, E. N.; Schwartz, R. J., Myocardin sumoylation transactivates cardiogenic genes in pluripotent 10T1/2 fibroblasts. Mol. Cell. Biol., 2007, 27, (2), 622-632.
    • (2007) Mol. Cell. Biol. , vol.27 , Issue.2 , pp. 622-632
    • Wang, J.1    Li, A.2    Wang, Z.3    Feng, X.4    Olson, E.N.5    Schwartz, R.J.6
  • 145
    • 53149119958 scopus 로고    scopus 로고
    • Regulation of cardiac specific nkx2.5 gene activity by small ubiquitin-like modifier
    • Wang, J.; Zhang, H.; Iyer, D.; Feng, X. H.; Schwartz, R. J., Regulation of cardiac specific nkx2.5 gene activity by small ubiquitin-like modifier. J. Biol. Chem., 2008, 283, (34), 23235-23243.
    • (2008) J. Biol. Chem. , vol.283 , Issue.34 , pp. 23235-23243
    • Wang, J.1    Zhang, H.2    Iyer, D.3    Feng, X.H.4    Schwartz, R.J.5
  • 146
    • 79958198042 scopus 로고    scopus 로고
    • Expression of sumoylation deficient Nkx2.5 mutant in Nkx2.5 haploinsufficient mice leads to congenital heart defects
    • Kim, E. Y.; Chen, L.; Ma, Y.; Yu, W.; Chang, J.; Moskowitz, I. P.; Wang, J., Expression of sumoylation deficient Nkx2.5 mutant in Nkx2.5 haploinsufficient mice leads to congenital heart defects. PLoS ONE, 2011, 6, (6), e20803.
    • (2011) PLoS ONE , vol.6 , Issue.6
    • Kim, E.Y.1    Chen, L.2    Ma, Y.3    Yu, W.4    Chang, J.5    Moskowitz, I.P.6    Wang, J.7
  • 147
    • 84871661643 scopus 로고    scopus 로고
    • Enhanced desumoylation in murine hearts by overexpressed SENP2 leads to congenital heart defects and cardiac dysfunction
    • Kim, E. Y.; Chen, L.; Ma, Y.; Yu, W.; Chang, J.; Moskowitz, I. P.; Wang, J., Enhanced desumoylation in murine hearts by overexpressed SENP2 leads to congenital heart defects and cardiac dysfunction. J. Mol. Cell. Cardiol., 2011.
    • (2011) J. Mol. Cell. Cardiol.
    • Kim, E.Y.1    Chen, L.2    Ma, Y.3    Yu, W.4    Chang, J.5    Moskowitz, I.P.6    Wang, J.7
  • 148
    • 1542380494 scopus 로고    scopus 로고
    • Sumo1 conjugates mitochondrial substrates and participates in mitochondrial fission
    • Harder, Z.; Zunino, R.; McBride, H., Sumo1 conjugates mitochondrial substrates and participates in mitochondrial fission. Curr. Biol., 2004, 14, (4), 340-345.
    • (2004) Curr. Biol. , vol.14 , Issue.4 , pp. 340-345
    • Harder, Z.1    Zunino, R.2    McBride, H.3
  • 149
    • 34248225298 scopus 로고    scopus 로고
    • The SUMO protease SENP5 is required to maintain mitochondrial morphology and function
    • Zunino, R.; Schauss, A.; Rippstein, P.; Andrade-Navarro, M.; McBride, H., The SUMO protease SENP5 is required to maintain mitochondrial morphology and function.. J. Cell. Sci., 2007, 120, 1178-1188.
    • (2007) J. Cell. Sci. , vol.120 , pp. 1178-1188
    • Zunino, R.1    Schauss, A.2    Rippstein, P.3    Andrade-Navarro, M.4    McBride, H.5
  • 150
    • 77953810265 scopus 로고    scopus 로고
    • Regulation of mitochondrial fission by intracellular Ca2+ in rat ventricular myocytes
    • 913-921
    • Hom, J.; Yu, T.; Yoon, Y.; Porter, G.; Sheu, S. S., Regulation of mitochondrial fission by intracellular Ca2+ in rat ventricular myocytes. Biochim. Biophys. Acta, 2010, 1797, (6-7), 913-921.
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 6-7
    • Hom, J.1    Yu, T.2    Yoon, Y.3    Porter, G.4    Sheu, S.S.5
  • 152
    • 80054921669 scopus 로고    scopus 로고
    • All the little pieces. Regulation of mitochondrial fusion and fission by ubiquitin and small ubiquitin-like modifer and their potential relevance in the heart
    • Zungu, M.; Schisler, J.; Willis, M., All the little pieces. Regulation of mitochondrial fusion and fission by ubiquitin and small ubiquitin-like modifer and their potential relevance in the heart. Circ. J., 2011, 75, 2513-2521.
    • (2011) Circ. J. , vol.75 , pp. 2513-2521
    • Zungu, M.1    Schisler, J.2    Willis, M.3
  • 153
    • 0022539556 scopus 로고
    • Atrial natriuretic factor: An overview
    • de Bold, A. J., Atrial natriuretic factor: an overview. Fed. Proc., 1986, 45, (7), 2081-2085.
    • (1986) Fed. Proc. , vol.45 , Issue.7 , pp. 2081-2085
    • De Bold, A.J.1
  • 155
    • 47049131348 scopus 로고    scopus 로고
    • Emerging roles of natriuretic peptides and their receptors in pathophysiology of hypertension and cardiovascular regulation
    • Pandey, K. N., Emerging Roles of Natriuretic Peptides and their Receptors in Pathophysiology of Hypertension and Cardiovascular Regulation. J. Am. Soc. Hypertens, 2008, 2(4), 210-226
    • (2008) J. Am. Soc. Hypertens , vol.2 , Issue.4 , pp. 210-226
    • Pandey, K.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.