메뉴 건너뛰기




Volumn 63, Issue 10, 2011, Pages 847-855

Calcium-regulated transcriptional pathways in the normal and pathologic heart

Author keywords

calcium; gene expression; heart; MEF2; NFAT; signaling; transcription

Indexed keywords

ADENOVIRUS VECTOR; CALCINEURIN; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CALCIUM ION; CALSEQUESTRIN; CYCLIC AMP DEPENDENT PROTEIN KINASE; MICRORNA; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE KINASE 1; MYOCYTE ENHANCER FACTOR 2; PROTEIN SERCA2A; RANOLAZINE; RYANODINE RECEPTOR 2; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; TRANSCRIPTION FACTOR NFAT; UNCLASSIFIED DRUG;

EID: 80053296633     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.545     Document Type: Conference Paper
Times cited : (38)

References (64)
  • 1
    • 0037049977 scopus 로고    scopus 로고
    • Cardiac excitation-contraction coupling
    • DOI 10.1038/415198a
    • Bers, D. M., (2002) Cardiac excitation-contraction coupling. Nature 415, 198-205. (Pubitemid 34059525)
    • (2002) Nature , vol.415 , Issue.6868 , pp. 198-205
    • Bers, D.M.1
  • 2
    • 43549098268 scopus 로고    scopus 로고
    • Calcium cycling and signaling in cardiac myocytes
    • DOI 10.1146/annurev.physiol.70.113006.100455
    • Bers, D. M., (2008) Calcium cycling and signaling in cardiac myocytes. Annu. Rev. Physiol. 70, 23-49. (Pubitemid 351738170)
    • (2008) Annual Review of Physiology , vol.70 , pp. 23-49
    • Bers, D.M.1
  • 3
    • 0028025634 scopus 로고
    • Sarcoplasmic reticulum calsequestrins: Structural and functional properties
    • Yano, K., and, Zarain-Herzberg, A., (1994) Sarcoplasmic reticulum calsequestrins: structural and functional properties. Mol. Cell. Biochem. 135, 61-70. (Pubitemid 24279108)
    • (1994) Molecular and Cellular Biochemistry , vol.135 , Issue.1 , pp. 61-70
    • Yano, K.1    Zarain-Herzberg, A.2
  • 4
    • 78651295535 scopus 로고    scopus 로고
    • Silencing calcineurin A subunit reduces SERCA2 expression in cardiac myocytes
    • Prasad, A. M., and, Inesi, G., (2011) Silencing calcineurin A subunit reduces SERCA2 expression in cardiac myocytes. Am. J. Physiol. Heart Circ. Physiol. 300, H173-H180.
    • (2011) Am. J. Physiol. Heart Circ. Physiol. , vol.300
    • Prasad, A.M.1    Inesi, G.2
  • 5
    • 34047249636 scopus 로고    scopus 로고
    • [Function and role of the sarcoplasmic reticulum in heart disease]
    • Reyes-Juarez, J. L., and, Zarain-Herzberg, A., (2006) [Function and role of the sarcoplasmic reticulum in heart disease]. Arch. Cardiol. Mex. 76 (Suppl 4), S18-S32.
    • (2006) Arch. Cardiol. Mex. , vol.76 , Issue.SUPPL. 4
    • Reyes-Juarez, J.L.1    Zarain-Herzberg, A.2
  • 6
    • 33748444015 scopus 로고    scopus 로고
    • 2+-ATPase expression in the hypertrophic and failing heart
    • DOI 10.1139/Y06-023
    • Zarain-Herzberg, A., (2006) Regulation of the sarcoplasmic reticulum Ca2+-ATPase expression in the hypertrophic and failing heart. Can. J. Physiol. Pharmacol. 84, 509-521. (Pubitemid 44350525)
    • (2006) Canadian Journal of Physiology and Pharmacology , vol.84 , Issue.5 , pp. 509-521
    • Zarain-Herzberg, A.1
  • 8
    • 0030246902 scopus 로고    scopus 로고
    • Ca-dependence of isometric force kinetics in single skinned ventricular cardiomyocytes from rats
    • DOI 10.1016/0008-6363(96)00103-4
    • Vannier, C., Chevassus, H., and, Vassort, G., (1996) Ca-dependence of isometric force kinetics in single skinned ventricular cardiomyocytes from rats. Cardiovasc. Res. 32, 580-586. (Pubitemid 26288604)
    • (1996) Cardiovascular Research , vol.32 , Issue.3 , pp. 580-586
    • Vannier, C.1    Chevassus, H.2    Vassort, G.3
  • 9
    • 33750865119 scopus 로고    scopus 로고
    • Ca2+ regulates the kinetics of tension development in intact cardiac muscle
    • Baker, A. J., Figueredo, V. M., Keung, E. C., and, Camacho, S. A., (1998) Ca2+ regulates the kinetics of tension development in intact cardiac muscle. Am. J. Physiol. 275, H744-H750.
    • (1998) Am. J. Physiol. , vol.275
    • Baker, A.J.1    Figueredo, V.M.2    Keung, E.C.3    Camacho, S.A.4
  • 10
    • 0032572414 scopus 로고    scopus 로고
    • 2+ activation and relaxation in rat and guinea pig skinned trabeculae
    • Palmer, S., and, Kentish, J. C., (1998) Roles of Ca2+ and crossbridge kinetics in determining the maximum rates of Ca2+ activation and relaxation in rat and guinea pig skinned trabeculae. Circ. Res. 83, 179-186. (Pubitemid 28354462)
    • (1998) Circulation Research , vol.83 , Issue.2 , pp. 179-186
    • Palmer, S.1    Kentish, J.C.2
  • 12
    • 0028274023 scopus 로고
    • Contractile arrest increases sarcoplasmic reticulum calcium uptake and SERCA2 gene expression in cultured neonatal rat heart cells
    • Bassani, J. W., Qi, M., Samarel, A. M., and, Bers, D. M., (1994) Contractile arrest increases sarcoplasmic reticulum calcium uptake and SERCA2 gene expression in cultured neonatal rat heart cells. Circ. Res. 74, 991-997. (Pubitemid 24121603)
    • (1994) Circulation Research , vol.74 , Issue.5 , pp. 991-997
    • Bassani, J.W.M.1    Qi, M.2    Samarel, A.M.3    Bers, D.M.4
  • 13
    • 0036278933 scopus 로고    scopus 로고
    • Targeting Ca2+ cycling proteins and the action potential in heart failure by gene transfer
    • Kaprielian, R., del Monte, F., and, Hajjar, R. J., (2002) Targeting Ca2+ cycling proteins and the action potential in heart failure by gene transfer. Basic Res. Cardiol. 97 (Suppl 1), I136-I145.
    • (2002) Basic Res. Cardiol. , vol.97 , Issue.SUPPL. 1
    • Kaprielian, R.1    Del Monte, F.2    Hajjar, R.J.3
  • 14
    • 77958154955 scopus 로고    scopus 로고
    • Synergy between CaMKII substrates and beta-adrenergic signaling in regulation of cardiac myocyte Ca(2+) handling
    • Soltis, A. R., and, Saucerman, J. J., (2010) Synergy between CaMKII substrates and beta-adrenergic signaling in regulation of cardiac myocyte Ca(2+) handling. Biophys. J. 99, 2038-2047.
    • (2010) Biophys. J. , vol.99 , pp. 2038-2047
    • Soltis, A.R.1    Saucerman, J.J.2
  • 15
    • 33751065132 scopus 로고    scopus 로고
    • Reversal of Calcium Cycling Defects in Advanced Heart Failure. Toward Molecular Therapy
    • DOI 10.1016/j.jacc.2006.06.070, PII S0735109706019978
    • Hoshijima, M., Knoll, R., Pashmforoush, M., and, Chien, K., (2006) Reversal of calcium cycling defects in advanced heart failure toward molecular therapy. J. Am. Coll. Cardiol. 48, A15-A23. (Pubitemid 44755024)
    • (2006) Journal of the American College of Cardiology , vol.48 , Issue.SUPPL. 9
    • Hoshijima, M.1    Knoll, R.2    Pashmforoush, M.3    Chien, K.R.4
  • 16
    • 0034649248 scopus 로고    scopus 로고
    • Congestive heart failure: Fifty years of progress
    • Braunwald, E., and, Bristow, M. R., (2000) Congestive heart failure: fifty years of progress. Circulation 102, IV14-IV23.
    • (2000) Circulation , vol.102
    • Braunwald, E.1    Bristow, M.R.2
  • 17
    • 31444444347 scopus 로고    scopus 로고
    • Ca2+/calmodulin-dependent protein kinase modulates cardiac ryanodine receptor phosphorylation and sarcoplasmic reticulum Ca2+ leak in heart failure
    • Ai, X., Curran, J. W., Shannon, T. R., Bers, D. M., and, Pogwizd, S. M., (2005) Ca2+/calmodulin-dependent protein kinase modulates cardiac ryanodine receptor phosphorylation and sarcoplasmic reticulum Ca2+ leak in heart failure. Circ. Res. 97, 1314-1322.
    • (2005) Circ. Res. , vol.97 , pp. 1314-1322
    • Ai, X.1    Curran, J.W.2    Shannon, T.R.3    Bers, D.M.4    Pogwizd, S.M.5
  • 18
    • 78650701435 scopus 로고    scopus 로고
    • Ryanodine receptor phosphorylation by calcium/calmodulin-dependent protein kinase II promotes life-threatening ventricular arrhythmias in mice with heart failure
    • van Oort, R. J., McCauley, M. D., Dixit, S. S., Pereira, L., Yang, Y., et al. (2010) Ryanodine receptor phosphorylation by calcium/calmodulin-dependent protein kinase II promotes life-threatening ventricular arrhythmias in mice with heart failure. Circulation 122, 2669-2679.
    • (2010) Circulation , vol.122 , pp. 2669-2679
    • Van Oort, R.J.1    McCauley, M.D.2    Dixit, S.S.3    Pereira, L.4    Yang, Y.5
  • 19
    • 79957481291 scopus 로고    scopus 로고
    • The relationship between arrhythmogenesis and impaired contractility in heart failure: Role of altered ryanodine receptor function
    • Belevych, A. E., Terentyev, D., Terentyeva, R., Nishijima, Y., Sridhar, A., et al. (2011) The relationship between arrhythmogenesis and impaired contractility in heart failure: role of altered ryanodine receptor function. Cardiovasc. Res. 90, 493-502.
    • (2011) Cardiovasc. Res. , vol.90 , pp. 493-502
    • Belevych, A.E.1    Terentyev, D.2    Terentyeva, R.3    Nishijima, Y.4    Sridhar, A.5
  • 20
    • 77956063496 scopus 로고    scopus 로고
    • Late sodium current contributes to diastolic cell Ca2+ accumulation in chronic heart failure
    • Undrovinas, N. A., Maltsev, V. A., Belardinelli, L., Sabbah, H. N., and, Undrovinas, A., (2010) Late sodium current contributes to diastolic cell Ca2+ accumulation in chronic heart failure. J. Physiol. Sci. 60, 245-257.
    • (2010) J. Physiol. Sci. , vol.60 , pp. 245-257
    • Undrovinas, N.A.1    Maltsev, V.A.2    Belardinelli, L.3    Sabbah, H.N.4    Undrovinas, A.5
  • 21
    • 45549105581 scopus 로고    scopus 로고
    • Ranolazine improves diastolic dysfunction in isolated myocardium from failing human hearts - Role of late sodium current and intracellular ion accumulation
    • Sossalla, S., Wagner, S., Rasenack, E. C., Ruff, H., Weber, S. L., et al. (2008) Ranolazine improves diastolic dysfunction in isolated myocardium from failing human hearts - role of late sodium current and intracellular ion accumulation. J. Mol. Cell. Cardiol. 45, 32-43.
    • (2008) J. Mol. Cell. Cardiol. , vol.45 , pp. 32-43
    • Sossalla, S.1    Wagner, S.2    Rasenack, E.C.3    Ruff, H.4    Weber, S.L.5
  • 23
    • 70349610465 scopus 로고    scopus 로고
    • Impaired contractile function and calcium handling in hearts of cardiac-specific calcineurin b1-deficient mice
    • Schaeffer, P. J., Desantiago, J., Yang, J., Flagg, T. P., Kovacs, A., et al. (2009) Impaired contractile function and calcium handling in hearts of cardiac-specific calcineurin b1-deficient mice. Am. J. Physiol. Heart Circ. Physiol. 297, H744-H750.
    • (2009) Am. J. Physiol. Heart Circ. Physiol. , vol.297
    • Schaeffer, P.J.1    Desantiago, J.2    Yang, J.3    Flagg, T.P.4    Kovacs, A.5
  • 24
    • 12844271214 scopus 로고    scopus 로고
    • Direct and indirect interactions between calcineurin-NFAT and MEK1-extracellular signal-regulated kinase 1/2 signaling pathways regulate cardiac gene expression and cellular growth
    • DOI 10.1128/MCB.25.3.865-878.2005
    • Sanna, B., Bueno, O. F., Dai, Y. S., Wilkins, B. J., and, Molkentin, J. D., (2005) Direct and indirect interactions between calcineurin-NFAT and MEK1-extracellular signal-regulated kinase 1/2 signaling pathways regulate cardiac gene expression and cellular growth. Mol. Cell. Biol. 25, 865-878. (Pubitemid 40165796)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.3 , pp. 865-878
    • Sanna, B.1    Bueno, O.F.2    Dai, Y.-S.3    Wilkins, B.J.4    Molkentin, J.D.5
  • 26
    • 0036165434 scopus 로고    scopus 로고
    • MEF2: A calcium-dependent regulator of cell division, differentiation and death
    • DOI 10.1016/S0968-0004(01)02031-X, PII S096800040102031X
    • McKinsey, T. A., Zhang, C. L., and, Olson, E. N., (2002) MEF2: a calcium-dependent regulator of cell division, differentiation and death. Trends Biochem. Sci. 27, 40-47. (Pubitemid 34131624)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.1 , pp. 40-47
    • McKinsey, T.A.1    Zhang, C.L.2    Olson, E.N.3
  • 27
    • 0032437107 scopus 로고    scopus 로고
    • Transcriptional control of muscle development by myocyte enhancer factor-2 (MEF2) proteins
    • DOI 10.1146/annurev.cellbio.14.1.167
    • Black, B. L., and, Olson, E. N., (1998) Transcriptional control of muscle development by myocyte enhancer factor-2 (MEF2) proteins. Annu. Rev. Cell. Dev. Biol. 14, 167-196. (Pubitemid 29001453)
    • (1998) Annual Review of Cell and Developmental Biology , vol.14 , pp. 167-196
    • Black, B.L.1    Olson, E.N.2
  • 28
    • 72649088292 scopus 로고    scopus 로고
    • MEF2 transcriptional activity maintains mitochondrial adaptation in cardiac pressure overload
    • el Azzouzi, H., van Oort, R. J., van der Nagel, R., Sluiter, W., Bergmann, M. W., et al. (2010) MEF2 transcriptional activity maintains mitochondrial adaptation in cardiac pressure overload. Eur. J. Heart Fail. 12, 4-12.
    • (2010) Eur. J. Heart Fail. , vol.12 , pp. 4-12
    • El Azzouzi, H.1    Van Oort, R.J.2    Van Der Nagel, R.3    Sluiter, W.4    Bergmann, M.W.5
  • 30
    • 67650520173 scopus 로고    scopus 로고
    • Protein kinase A-regulated assembly of a MEF2{middle dot}HDAC4 repressor complex controls c-Jun expression in vascular smooth muscle cells
    • Gordon, J. W., Pagiatakis, C., Salma, J., Du, M., Andreucci, J. J., et al. (2009) Protein kinase A-regulated assembly of a MEF2{middle dot}HDAC4 repressor complex controls c-Jun expression in vascular smooth muscle cells. J. Biol. Chem. 284, 19027-19042.
    • (2009) J. Biol. Chem. , vol.284 , pp. 19027-19042
    • Gordon, J.W.1    Pagiatakis, C.2    Salma, J.3    Du, M.4    Andreucci, J.J.5
  • 31
    • 43249121693 scopus 로고    scopus 로고
    • Histone deacetylase 5 acquires calcium/calmodulin-dependent kinase II responsiveness by oligomerization with histone deacetylase 4
    • DOI 10.1128/MCB.01611-07
    • Backs, J., Backs, T., Bezprozvannaya, S., McKinsey, T. A., and, Olson, E. N., (2008) Histone deacetylase 5 acquires calcium/calmodulin-dependent kinase II responsiveness by oligomerization with histone deacetylase 4. Mol. Cell. Biol. 28, 3437-3445. (Pubitemid 351657105)
    • (2008) Molecular and Cellular Biology , vol.28 , Issue.10 , pp. 3437-3445
    • Backs, J.1    Backs, T.2    Bezprozvannaya, S.3    McKinsey, T.A.4    Olson, E.N.5
  • 32
    • 0037705392 scopus 로고    scopus 로고
    • 2+/calmodulin inhibits histone deacetylase 5 repressor core binding to myocyte enhancer factor 2
    • DOI 10.1074/jbc.M301646200
    • Berger, I., Bieniossek, C., Schaffitzel, C., Hassler, M., Santelli, E., et al. (2003) Direct interaction of Ca2+/calmodulin inhibits histone deacetylase 5 repressor core binding to myocyte enhancer factor 2. J. Biol. Chem. 278, 17625-17635. (Pubitemid 36799364)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.20 , pp. 17625-17635
    • Berger, I.1    Bieniossek, C.2    Schaffitzel, C.3    Hassler, M.4    Santelli, E.5    Richmond, T.J.6
  • 34
    • 70349236112 scopus 로고    scopus 로고
    • CaMKII negatively regulates calcineurin-NFAT signaling in cardiac myocytes
    • MacDonnell, S. M., Weisser-Thomas, J., Kubo, H., Hanscome, M., Liu, Q., et al. (2009) CaMKII negatively regulates calcineurin-NFAT signaling in cardiac myocytes. Circ. Res. 105, 316-325.
    • (2009) Circ. Res. , vol.105 , pp. 316-325
    • MacDonnell, S.M.1    Weisser-Thomas, J.2    Kubo, H.3    Hanscome, M.4    Liu, Q.5
  • 36
    • 0033592696 scopus 로고    scopus 로고
    • MEF2 is upregulated during cardiac hypertrophy and is required for normal post-natal growth of the myocardium
    • DOI 10.1016/S0960-9822(00)80027-5
    • Kolodziejczyk, S. M., Wang, L., Balazsi, K., DeRepentigny, Y., Kothary, R., et al. (1999) MEF2 is upregulated during cardiac hypertrophy and is required for normal post-natal growth of the myocardium. Curr. Biol. 9, 1203-1206. (Pubitemid 29527110)
    • (1999) Current Biology , vol.9 , Issue.20 , pp. 1203-1206
    • Kolodziejczyk, S.M.1    Wang, L.2    Balazsi, K.3    Derepentigny, Y.4    Kothary, R.5    Megeney, L.A.6
  • 37
    • 77951790171 scopus 로고    scopus 로고
    • The calcineurin-myocyte enhancer factor 2c pathway mediates cardiac hypertrophy induced by endoplasmic reticulum stress in neonatal rat cardiomyocytes
    • Zhang, Z. Y., Liu, X. H., Hu, W. C., Rong, F., and, Wu, X. D., (2010) The calcineurin-myocyte enhancer factor 2c pathway mediates cardiac hypertrophy induced by endoplasmic reticulum stress in neonatal rat cardiomyocytes. Am. J. Physiol. Heart Circ. Physiol. 298, H744-H750.
    • (2010) Am. J. Physiol. Heart Circ. Physiol. , vol.298
    • Zhang, Z.Y.1    Liu, X.H.2    Hu, W.C.3    Rong, F.4    Wu, X.D.5
  • 38
    • 77954532839 scopus 로고    scopus 로고
    • Epac activation induces histone deacetylase nuclear export via a Ras-dependent signalling pathway
    • Metrich, M., Laurent, A. C., Breckler, M., Duquesnes, N., Hmitou, I., et al. (2010) Epac activation induces histone deacetylase nuclear export via a Ras-dependent signalling pathway. Cell. Signal. 22, 1459-1468.
    • (2010) Cell. Signal. , vol.22 , pp. 1459-1468
    • Metrich, M.1    Laurent, A.C.2    Breckler, M.3    Duquesnes, N.4    Hmitou, I.5
  • 41
    • 64649094112 scopus 로고    scopus 로고
    • MicroRNA-1 negatively regulates expression of the hypertrophy-associated calmodulin and Mef2a genes
    • Ikeda, S., He, A., Kong, S. W., Lu, J., Bejar, R., et al. (2009) MicroRNA-1 negatively regulates expression of the hypertrophy-associated calmodulin and Mef2a genes. Mol. Cell. Biol. 29, 2193-2204.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 2193-2204
    • Ikeda, S.1    He, A.2    Kong, S.W.3    Lu, J.4    Bejar, R.5
  • 42
    • 78649843756 scopus 로고    scopus 로고
    • MicroRNA-199b targets the nuclear kinase Dyrk1a in an auto-amplification loop promoting calcineurin/NFAT signalling
    • da Costa Martins, P. A., Salic, K., Gladka, M. M., Armand, A. S., Leptidis, S., et al. (2010) MicroRNA-199b targets the nuclear kinase Dyrk1a in an auto-amplification loop promoting calcineurin/NFAT signalling. Nat. Cell Biol. 12, 1220-1227.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 1220-1227
    • Da Costa Martins, P.A.1    Salic, K.2    Gladka, M.M.3    Armand, A.S.4    Leptidis, S.5
  • 43
    • 77951225449 scopus 로고    scopus 로고
    • DYRK1A and DYRK3 promote cell survival through phosphorylation and activation of SIRT1
    • Guo, X., Williams, J. G., Schug, T. T., and, Li, X., (2010) DYRK1A and DYRK3 promote cell survival through phosphorylation and activation of SIRT1. J. Biol. Chem. 285, 13223-13232.
    • (2010) J. Biol. Chem. , vol.285 , pp. 13223-13232
    • Guo, X.1    Williams, J.G.2    Schug, T.T.3    Li, X.4
  • 44
    • 80052799903 scopus 로고    scopus 로고
    • Emerging roles of SIRT1 deacetylase in regulating cardiomyocyte survival and hypertrophy
    • Sundaresan, N. R., Pillai, V. B., and, Gupta, M. P., (2011) Emerging roles of SIRT1 deacetylase in regulating cardiomyocyte survival and hypertrophy. J. Mol. Cell. Cardiol.
    • (2011) J. Mol. Cell. Cardiol
    • Sundaresan, N.R.1    Pillai, V.B.2    Gupta, M.P.3
  • 45
    • 77949324001 scopus 로고    scopus 로고
    • Evidence for coregulation of myocardial gene expression by MEF2 and NFAT in human heart failure
    • Putt, M. E., Hannenhalli, S., Lu, Y., Haines, P., Chandrupatla, H. R., et al. (2009) Evidence for coregulation of myocardial gene expression by MEF2 and NFAT in human heart failure. Circ. Cardiovasc. Genet 2, 212-219.
    • (2009) Circ. Cardiovasc. Genet , vol.2 , pp. 212-219
    • Putt, M.E.1    Hannenhalli, S.2    Lu, Y.3    Haines, P.4    Chandrupatla, H.R.5
  • 46
    • 44449101173 scopus 로고    scopus 로고
    • ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum
    • DOI 10.1247/csf.07044
    • Adachi, Y., Yamamoto, K., Okada, T., Yoshida, H., Harada, A., et al. (2008) ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum. Cell Struct. Funct. 33, 75-89. (Pubitemid 351860903)
    • (2008) Cell Structure and Function , vol.33 , Issue.1 , pp. 75-89
    • Adachi, Y.1    Yamamoto, K.2    Okada, T.3    Yoshida, H.4    Harada, A.5    Mori, K.6
  • 47
    • 0033920261 scopus 로고    scopus 로고
    • ATF6 as a transcription activator of the endoplasmic reticulum stress element: Thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1
    • DOI 10.1128/MCB.20.14.5096-5106.2000
    • Li, M., Baumeister, P., Roy, B., Phan, T., Foti, D., et al. (2000) ATF6 as a transcription activator of the endoplasmic reticulum stress element: thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1. Mol. Cell. Biol. 20, 5096-5106. (Pubitemid 30431563)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.14 , pp. 5096-5106
    • Li, M.1    Baumeister, P.2    Roy, B.3    Phan, T.4    Foti, D.5    Luo, S.6    Lee, A.S.7
  • 48
    • 0035930549 scopus 로고    scopus 로고
    • Sarco/endoplasmic reticulum calcium ATPase-2 expression is regulated by ATF6 during the endoplasmic reticulum stress response: Intracellular signaling of calcium stress in a cardiac myocyte model system
    • Thuerauf, D. J., Hoover, H., Meller, J., Hernandez, J., Su, L., et al. (2001) Sarco/endoplasmic reticulum calcium ATPase-2 expression is regulated by ATF6 during the endoplasmic reticulum stress response: intracellular signaling of calcium stress in a cardiac myocyte model system. J. Biol. Chem. 276, 48309-48317.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48309-48317
    • Thuerauf, D.J.1    Hoover, H.2    Meller, J.3    Hernandez, J.4    Su, L.5
  • 49
    • 46649111986 scopus 로고    scopus 로고
    • Coordination of growth and endoplasmic reticulum stress signaling by regulator of calcineurin 1 (RCAN1), a novel ATF6-inducible gene
    • Belmont, P. J., Tadimalla, A., Chen, W. J., Martindale, J. J., Thuerauf, D. J., et al. (2008) Coordination of growth and endoplasmic reticulum stress signaling by regulator of calcineurin 1 (RCAN1), a novel ATF6-inducible gene. J. Biol. Chem. 283, 14012-14021.
    • (2008) J. Biol. Chem. , vol.283 , pp. 14012-14021
    • Belmont, P.J.1    Tadimalla, A.2    Chen, W.J.3    Martindale, J.J.4    Thuerauf, D.J.5
  • 50
    • 3242770548 scopus 로고    scopus 로고
    • Contractile arrest reveals calcium-dependent stimulation of SERCA2a mRNA expression in cultured ventricular cardiomyocytes
    • DOI 10.1016/j.cardiores.2004.04.005, PII S0008636304001646
    • Vlasblom, R., Muller, A., Musters, R. J., Zuidwijk, M. J., Van Hardeveld, C., et al. (2004) Contractile arrest reveals calcium-dependent stimulation of SERCA2a mRNA expression in cultured ventricular cardiomyocytes. Cardiovasc. Res. 63, 537-544. (Pubitemid 38970198)
    • (2004) Cardiovascular Research , vol.63 , Issue.3 , pp. 537-544
    • Vlasblom, R.1    Muller, A.2    Musters, R.J.P.3    Zuidwijk, M.J.4    Van Hardeveld, C.5    Paulus, W.J.6    Simonides, W.S.7
  • 51
    • 61349167808 scopus 로고    scopus 로고
    • Control of muscleryanodine receptor calcium release channels by proteins in the sarcoplasmic reticulum lumen
    • Beard, N. A., Wei, L., and, Dulhunty, A. F., (2009) Control of muscleryanodine receptor calcium release channels by proteins in the sarcoplasmic reticulum lumen. Clin. Exp. Pharmacol. Physiol. 36, 340-345.
    • (2009) Clin. Exp. Pharmacol. Physiol. , vol.36 , pp. 340-345
    • Beard, N.A.1    Wei, L.2    Dulhunty, A.F.3
  • 52
    • 37249028578 scopus 로고    scopus 로고
    • Transcriptional analysis of the human cardiac calsequestrin gene in cardiac and skeletal myocytes
    • DOI 10.1074/jbc.M707788200
    • Reyes-Juarez, J. L., Juarez-Rubi, R., Rodriguez, G., and, Zarain-Herzberg, A., (2007) Transcriptional analysis of the human cardiac calsequestrin gene in cardiac and skeletal myocytes. J. Biol. Chem. 282, 35554-35563. (Pubitemid 350277093)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.49 , pp. 35554-35563
    • Reyes-Juarez, J.L.1    Juarez-Rubi, R.2    Rodriguez, G.3    Zarain-Herzberg, A.4
  • 53
    • 60149089102 scopus 로고    scopus 로고
    • Egr-1 negatively regulates calsequestrin expression and calcium dynamics in ventricular cells
    • Kasneci, A., Kemeny-Suss, N. M., Komarova, S. V., and, Chalifour, L. E., (2009) Egr-1 negatively regulates calsequestrin expression and calcium dynamics in ventricular cells. Cardiovasc. Res. 81, 695-702.
    • (2009) Cardiovasc. Res. , vol.81 , pp. 695-702
    • Kasneci, A.1    Kemeny-Suss, N.M.2    Komarova, S.V.3    Chalifour, L.E.4
  • 54
    • 0029814911 scopus 로고    scopus 로고
    • Modification of sarcoplasmic reticulum gene expression in pressure overload cardiac hypertrophy by etomoxir
    • Zarain-Herzberg, A., Rupp, H., Elimban, V., and, Dhalla, N. S., (1996) Modification of sarcoplasmic reticulum gene expression in pressure overload cardiac hypertrophy by etomoxir. FASEB, J. 10, 1303-1309. (Pubitemid 26307516)
    • (1996) FASEB Journal , vol.10 , Issue.11 , pp. 1303-1309
    • Zarain-Herzberg, A.1    Rupp, H.2    Elimban, V.3    Dhalla, N.S.4
  • 55
    • 0036195453 scopus 로고    scopus 로고
    • Therapeutic potential of CPT I inhibitors: Cardiac gene transcription as a target
    • DOI 10.1517/13543784.11.3.345
    • Zarain-Herzberg, A., and, Rupp, H., (2002) Therapeutic potential of CPT I inhibitors: cardiac gene transcription as a target. Expert Opin. Investig. Drugs 11, 345-356. (Pubitemid 34213389)
    • (2002) Expert Opinion on Investigational Drugs , vol.11 , Issue.3 , pp. 345-356
    • Zarain-Herzberg, A.1    Rupp, H.2
  • 58
    • 77957914859 scopus 로고    scopus 로고
    • Gene delivery of sarcoplasmic reticulum calcium ATPase inhibits ventricular remodeling in ischemic mitral regurgitation
    • Beeri, R., Chaput, M., Guerrero, J. L., Kawase, Y., Yosefy, C., et al. (2010) Gene delivery of sarcoplasmic reticulum calcium ATPase inhibits ventricular remodeling in ischemic mitral regurgitation. Circulation: Heart Fail. 3, 627-634.
    • (2010) Circulation: Heart Fail. , vol.3 , pp. 627-634
    • Beeri, R.1    Chaput, M.2    Guerrero, J.L.3    Kawase, Y.4    Yosefy, C.5
  • 59
    • 77949293432 scopus 로고    scopus 로고
    • Right ventricular beneficial effects of intracoronary SERCA2a gene transfer in an experimental model of heart failure
    • Molina, E. J., Gupta, D., Palma, J., Gaughan, J. P., and, Macha, M., (2010) Right ventricular beneficial effects of intracoronary SERCA2a gene transfer in an experimental model of heart failure. Folia Biol. (Praha) 56, 1-8.
    • (2010) Folia Biol. (Praha) , vol.56 , pp. 1-8
    • Molina, E.J.1    Gupta, D.2    Palma, J.3    Gaughan, J.P.4    MacHa, M.5
  • 60
    • 79951824228 scopus 로고    scopus 로고
    • Augmentation of left ventricular mechanics by recirculation-mediated AAV2/1-SERCA2a gene delivery in experimental heart failure
    • Mariani, J. A., Smolic, A., Preovolos, A., Byrne, M. J., Power, J. M., et al. (2011) Augmentation of left ventricular mechanics by recirculation-mediated AAV2/1-SERCA2a gene delivery in experimental heart failure. Eur. J. Heart Fail. 13, 247-253.
    • (2011) Eur. J. Heart Fail. , vol.13 , pp. 247-253
    • Mariani, J.A.1    Smolic, A.2    Preovolos, A.3    Byrne, M.J.4    Power, J.M.5
  • 61
    • 0035713505 scopus 로고    scopus 로고
    • In vivo myocardial gene transfer: Optimization and evaluation of intracoronary gene delivery in vivo
    • DOI 10.1038/sj.gt.3301614
    • Wright, M. J., Wightman, L. M., Latchman, D. S., and, Marber, M. S., (2001) In vivo myocardial gene transfer: optimization and evaluation of intracoronary gene delivery in vivo. Gene Ther. 8, 1833-1839. (Pubitemid 34141489)
    • (2001) Gene Therapy , vol.8 , Issue.24 , pp. 1833-1839
    • Wright, M.J.1    Wightman, L.M.L.2    Latchman, D.S.3    Marber, M.S.4
  • 63
    • 62649133817 scopus 로고    scopus 로고
    • Calcium upregulation by percutaneous administration of gene therapy in cardiac disease (CUPID Trial), a first-in-human phase 1/2 clinical trial
    • Jaski, B. E., Jessup, M. L., Mancini, D. M., Cappola, T. P., Pauly, D. F., et al. (2009) Calcium upregulation by percutaneous administration of gene therapy in cardiac disease (CUPID Trial), a first-in-human phase 1/2 clinical trial. J. Card. Fail. 15, 171-181.
    • (2009) J. Card. Fail. , vol.15 , pp. 171-181
    • Jaski, B.E.1    Jessup, M.L.2    Mancini, D.M.3    Cappola, T.P.4    Pauly, D.F.5
  • 64
    • 79953168028 scopus 로고    scopus 로고
    • Compromised myocardial energetics in hypertrophied mouse hearts diminish the beneficial effect of overexpressing SERCA2a
    • Pinz, I., Tian, R., Belke, D., Swanson, E., Dillmann, W., et al. (2011) Compromised myocardial energetics in hypertrophied mouse hearts diminish the beneficial effect of overexpressing SERCA2a. J. Biol. Chem. 286, 10163-10168.
    • (2011) J. Biol. Chem. , vol.286 , pp. 10163-10168
    • Pinz, I.1    Tian, R.2    Belke, D.3    Swanson, E.4    Dillmann, W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.