메뉴 건너뛰기




Volumn 83, Issue , 2015, Pages 14-20

Non-sirtuin histone deacetylases in the control of cardiac aging

Author keywords

Aging; Heart failure; Histone deacetylase

Indexed keywords

CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE; CYCLIN DEPENDENT KINASE INHIBITOR 1C; ENTINOSTAT; HEAT SHOCK PROTEIN 90; HISTONE DEACETYLASE; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 10; HISTONE DEACETYLASE 11; HISTONE DEACETYLASE 2; HISTONE DEACETYLASE 3; HISTONE DEACETYLASE 4; HISTONE DEACETYLASE 5; HISTONE DEACETYLASE 6; HISTONE DEACETYLASE 7; HISTONE DEACETYLASE 8; HISTONE DEACETYLASE 9; HISTONE DEACETYLASE INHIBITOR; MANGANESE SUPEROXIDE DISMUTASE; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MOCETINOSTAT; PROTEIN KINASE D; PROTEIN P15; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 2; TUBASTATIN A; UNCLASSIFIED DRUG; UNINDEXED DRUG; VALPROIC ACID; VORINOSTAT; HISTONE; ISOENZYME;

EID: 84937966754     PISSN: 00222828     EISSN: 10958584     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2015.03.010     Document Type: Review
Times cited : (46)

References (80)
  • 1
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., et al. Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 2009, 325:834-840.
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3    Nielsen, M.L.4    Rehman, M.5    Walther, T.C.6
  • 2
    • 84865726581 scopus 로고    scopus 로고
    • Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns
    • Lundby A., Lage K., Weinert B.T., Bekker-Jensen D.B., Secher A., Skovgaard T., et al. Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Cell Rep 2012, 2:419-431.
    • (2012) Cell Rep , vol.2 , pp. 419-431
    • Lundby, A.1    Lage, K.2    Weinert, B.T.3    Bekker-Jensen, D.B.4    Secher, A.5    Skovgaard, T.6
  • 3
    • 1842578986 scopus 로고    scopus 로고
    • Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis
    • Gregoretti I.V., Lee Y.M., Goodson H.V. Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. J Mol Biol 2004, 338:17-31.
    • (2004) J Mol Biol , vol.338 , pp. 17-31
    • Gregoretti, I.V.1    Lee, Y.M.2    Goodson, H.V.3
  • 5
    • 84855875719 scopus 로고    scopus 로고
    • Therapeutic potential for HDAC inhibitors in the heart
    • McKinsey T.A. Therapeutic potential for HDAC inhibitors in the heart. Annu Rev Pharmacol Toxicol 2012, 52:303-319.
    • (2012) Annu Rev Pharmacol Toxicol , vol.52 , pp. 303-319
    • McKinsey, T.A.1
  • 6
    • 79952775153 scopus 로고    scopus 로고
    • Histone deacetylase (HDAC) inhibitors attenuate cardiac hypertrophy by suppressing autophagy
    • Cao D.J., Wang Z.V., Battiprolu P.K., Jiang N., Morales C.R., Kong Y., et al. Histone deacetylase (HDAC) inhibitors attenuate cardiac hypertrophy by suppressing autophagy. Proc Natl Acad Sci U S A 2011, 108:4123-4128.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 4123-4128
    • Cao, D.J.1    Wang, Z.V.2    Battiprolu, P.K.3    Jiang, N.4    Morales, C.R.5    Kong, Y.6
  • 7
    • 33644861578 scopus 로고    scopus 로고
    • Inhibition of histone deacetylation blocks cardiac hypertrophy induced by angiotensin II infusion and aortic banding
    • Kee H.J., Sohn I.S., Nam K.I., Park J.E., Qian Y.R., Yin Z., et al. Inhibition of histone deacetylation blocks cardiac hypertrophy induced by angiotensin II infusion and aortic banding. Circulation 2006, 113:51-59.
    • (2006) Circulation , vol.113 , pp. 51-59
    • Kee, H.J.1    Sohn, I.S.2    Nam, K.I.3    Park, J.E.4    Qian, Y.R.5    Yin, Z.6
  • 8
    • 84895923936 scopus 로고    scopus 로고
    • Histone deacetylase inhibition blunts ischemia/reperfusion injury by inducing cardiomyocyte autophagy
    • Xie M., Kong Y., Tan W., May H., Battiprolu P.K., Pedrozo Z., et al. Histone deacetylase inhibition blunts ischemia/reperfusion injury by inducing cardiomyocyte autophagy. Circulation 2014, 129:1139-1151.
    • (2014) Circulation , vol.129 , pp. 1139-1151
    • Xie, M.1    Kong, Y.2    Tan, W.3    May, H.4    Battiprolu, P.K.5    Pedrozo, Z.6
  • 9
    • 84860210734 scopus 로고    scopus 로고
    • Autophagy as a therapeutic target for ischaemia/reperfusion injury? Concepts, controversies, and challenges
    • Przyklenk K., Dong Y., Undyala V.V., Whittaker P. Autophagy as a therapeutic target for ischaemia/reperfusion injury? Concepts, controversies, and challenges. Cardiovasc Res 2012, 94:197-205.
    • (2012) Cardiovasc Res , vol.94 , pp. 197-205
    • Przyklenk, K.1    Dong, Y.2    Undyala, V.V.3    Whittaker, P.4
  • 10
    • 84901375234 scopus 로고    scopus 로고
    • Selective inhibition of class I but not class IIb histone deacetylases exerts cardiac protection from ischemia reperfusion
    • Aune S.E., Herr D.J., Mani S.K., Menick D.R. Selective inhibition of class I but not class IIb histone deacetylases exerts cardiac protection from ischemia reperfusion. J Mol Cell Cardiol 2014, 72:138-145.
    • (2014) J Mol Cell Cardiol , vol.72 , pp. 138-145
    • Aune, S.E.1    Herr, D.J.2    Mani, S.K.3    Menick, D.R.4
  • 11
    • 84899061619 scopus 로고    scopus 로고
    • Targeting cardiac fibroblasts to treat fibrosis of the heart: focus on HDACs
    • Schuetze K.B., McKinsey T.A., Long C.S. Targeting cardiac fibroblasts to treat fibrosis of the heart: focus on HDACs. J Mol Cell Cardiol 2014, 70:100-107.
    • (2014) J Mol Cell Cardiol , vol.70 , pp. 100-107
    • Schuetze, K.B.1    McKinsey, T.A.2    Long, C.S.3
  • 13
    • 84903411670 scopus 로고    scopus 로고
    • HDAC class I inhibitor, Mocetinostat, reverses cardiac fibrosis in heart failure and diminishes CD90+ cardiac myofibroblast activation
    • Nural-Guvener H.F., Zakharova L., Nimlos J., Popovic S., Mastroeni D., Gaballa M.A. HDAC class I inhibitor, Mocetinostat, reverses cardiac fibrosis in heart failure and diminishes CD90+ cardiac myofibroblast activation. Fibrogenesis Tissue Repair 2014, 7:10.
    • (2014) Fibrogenesis Tissue Repair , vol.7 , pp. 10
    • Nural-Guvener, H.F.1    Zakharova, L.2    Nimlos, J.3    Popovic, S.4    Mastroeni, D.5    Gaballa, M.A.6
  • 15
    • 84900851026 scopus 로고    scopus 로고
    • Wrestling with heart failure: SUMO-1 to the rescue
    • Vejpongsa P., Yeh E.T. Wrestling with heart failure: SUMO-1 to the rescue. Circ Res 2014, 114:1561-1563.
    • (2014) Circ Res , vol.114 , pp. 1561-1563
    • Vejpongsa, P.1    Yeh, E.T.2
  • 16
    • 84895464034 scopus 로고    scopus 로고
    • Epigenetic regulation of fibrocyte differentiation?
    • Lishnevsky M., Haudek S.B. Epigenetic regulation of fibrocyte differentiation?. J Mol Cell Cardiol 2014, 69:85-87.
    • (2014) J Mol Cell Cardiol , vol.69 , pp. 85-87
    • Lishnevsky, M.1    Haudek, S.B.2
  • 17
    • 77953544771 scopus 로고    scopus 로고
    • Fibrocytes in health and disease
    • Herzog E.L., Bucala R. Fibrocytes in health and disease. Exp Hematol 2010, 38:548-556.
    • (2010) Exp Hematol , vol.38 , pp. 548-556
    • Herzog, E.L.1    Bucala, R.2
  • 18
    • 78650820594 scopus 로고    scopus 로고
    • Immune-inflammatory dysregulation modulates the incidence of progressive fibrosis and diastolic stiffness in the aging heart
    • Cieslik K.A., Taffet G.E., Carlson S., Hermosillo J., Trial J., Entman M.L. Immune-inflammatory dysregulation modulates the incidence of progressive fibrosis and diastolic stiffness in the aging heart. J Mol Cell Cardiol 2011, 50:248-256.
    • (2011) J Mol Cell Cardiol , vol.50 , pp. 248-256
    • Cieslik, K.A.1    Taffet, G.E.2    Carlson, S.3    Hermosillo, J.4    Trial, J.5    Entman, M.L.6
  • 19
    • 56049120057 scopus 로고    scopus 로고
    • Eloquent silence: developmental functions of Class I histone deacetylases
    • Cunliffe V.T. Eloquent silence: developmental functions of Class I histone deacetylases. Curr Opin Genet Dev 2008, 18:404-410.
    • (2008) Curr Opin Genet Dev , vol.18 , pp. 404-410
    • Cunliffe, V.T.1
  • 20
    • 84878273525 scopus 로고    scopus 로고
    • The physiological roles of histone deacetylase (HDAC) 1 and 2: complex co-stars with multiple leading parts
    • Kelly R.D., Cowley S.M. The physiological roles of histone deacetylase (HDAC) 1 and 2: complex co-stars with multiple leading parts. Biochem Soc Trans 2013, 41:741-749.
    • (2013) Biochem Soc Trans , vol.41 , pp. 741-749
    • Kelly, R.D.1    Cowley, S.M.2
  • 21
    • 33746578975 scopus 로고    scopus 로고
    • Histone deacetylase 3 localizes to the plasma membrane and is a substrate of Src
    • Longworth M.S., Laimins L.A. Histone deacetylase 3 localizes to the plasma membrane and is a substrate of Src. Oncogene 2006, 25:4495-4500.
    • (2006) Oncogene , vol.25 , pp. 4495-4500
    • Longworth, M.S.1    Laimins, L.A.2
  • 22
    • 79953133501 scopus 로고    scopus 로고
    • HDAC3-dependent reversible lysine acetylation of cardiac myosin heavy chain isoforms modulates their enzymatic and motor activity
    • Samant S.A., Courson D.S., Sundaresan N.R., Pillai V.B., Tan M., Zhao Y., et al. HDAC3-dependent reversible lysine acetylation of cardiac myosin heavy chain isoforms modulates their enzymatic and motor activity. J Biol Chem 2011, 286:5567-5577.
    • (2011) J Biol Chem , vol.286 , pp. 5567-5577
    • Samant, S.A.1    Courson, D.S.2    Sundaresan, N.R.3    Pillai, V.B.4    Tan, M.5    Zhao, Y.6
  • 23
    • 84937991609 scopus 로고    scopus 로고
    • The role of histone deacetylase 2 and its posttranslational modifications in cardiac hypertrophy
    • [Epub ahead of print]
    • Eom G.H., Kook H. The role of histone deacetylase 2 and its posttranslational modifications in cardiac hypertrophy. BMB Rep 2014, [Epub ahead of print].
    • (2014) BMB Rep
    • Eom, G.H.1    Kook, H.2
  • 24
    • 84897567792 scopus 로고    scopus 로고
    • Regulation of acetylation of histone deacetylase 2 by p300/CBP-associated factor/histone deacetylase 5 in the development of cardiac hypertrophy
    • Eom G.H., Nam Y.S., Oh J.G., Choe N., Min H.K., Yoo E.K., et al. Regulation of acetylation of histone deacetylase 2 by p300/CBP-associated factor/histone deacetylase 5 in the development of cardiac hypertrophy. Circ Res 2014, 114:1133-1143.
    • (2014) Circ Res , vol.114 , pp. 1133-1143
    • Eom, G.H.1    Nam, Y.S.2    Oh, J.G.3    Choe, N.4    Min, H.K.5    Yoo, E.K.6
  • 26
    • 80052992257 scopus 로고    scopus 로고
    • Diet-induced lethality due to deletion of the HDAC3 gene in heart and skeletal muscle
    • Sun Z., Singh N., Mullican S.E., Everett L.J., Li L., Yuan L., et al. Diet-induced lethality due to deletion of the HDAC3 gene in heart and skeletal muscle. J Biol Chem 2011, 286:33301-33309.
    • (2011) J Biol Chem , vol.286 , pp. 33301-33309
    • Sun, Z.1    Singh, N.2    Mullican, S.E.3    Everett, L.J.4    Li, L.5    Yuan, L.6
  • 27
  • 28
    • 84891073800 scopus 로고    scopus 로고
    • Deacetylase-independent function of HDAC3 in transcription and metabolism requires nuclear receptor corepressor
    • Sun Z., Feng D., Fang B., Mullican S.E., You S.H., Lim H.W., et al. Deacetylase-independent function of HDAC3 in transcription and metabolism requires nuclear receptor corepressor. Mol Cell 2013, 52:769-782.
    • (2013) Mol Cell , vol.52 , pp. 769-782
    • Sun, Z.1    Feng, D.2    Fang, B.3    Mullican, S.E.4    You, S.H.5    Lim, H.W.6
  • 29
    • 84878991183 scopus 로고    scopus 로고
    • Signal-dependent repression of DUSP5 by class I HDACs controls nuclear ERK activity and cardiomyocyte hypertrophy
    • Ferguson B.S., Harrison B.C., Jeong M.Y., Reid B.G., Wempe M.F., Wagner F.F., et al. Signal-dependent repression of DUSP5 by class I HDACs controls nuclear ERK activity and cardiomyocyte hypertrophy. Proc Natl Acad Sci U S A 2013, 110:9806-9811.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 9806-9811
    • Ferguson, B.S.1    Harrison, B.C.2    Jeong, M.Y.3    Reid, B.G.4    Wempe, M.F.5    Wagner, F.F.6
  • 30
    • 58149351369 scopus 로고    scopus 로고
    • A new type of ERK1/2 autophosphorylation causes cardiac hypertrophy
    • Lorenz K., Schmitt J.P., Schmitteckert E.M., Lohse M.J. A new type of ERK1/2 autophosphorylation causes cardiac hypertrophy. Nat Med 2009, 15:75-83.
    • (2009) Nat Med , vol.15 , pp. 75-83
    • Lorenz, K.1    Schmitt, J.P.2    Schmitteckert, E.M.3    Lohse, M.J.4
  • 31
    • 84876924477 scopus 로고    scopus 로고
    • Interference with ERK(Thr188) phosphorylation impairs pathological but not physiological cardiac hypertrophy
    • Ruppert C., Deiss K., Herrmann S., Vidal M., Oezkur M., Gorski A., et al. Interference with ERK(Thr188) phosphorylation impairs pathological but not physiological cardiac hypertrophy. Proc Natl Acad Sci U S A 2013, 110:7440-7445.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 7440-7445
    • Ruppert, C.1    Deiss, K.2    Herrmann, S.3    Vidal, M.4    Oezkur, M.5    Gorski, A.6
  • 32
    • 79958033203 scopus 로고    scopus 로고
    • Acetylation of a conserved lysine residue in the ATP binding pocket of p38 augments its kinase activity during hypertrophy of cardiomyocytes
    • Pillai V.B., Sundaresan N.R., Samant S.A., Wolfgeher D., Trivedi C.M., Gupta M.P. Acetylation of a conserved lysine residue in the ATP binding pocket of p38 augments its kinase activity during hypertrophy of cardiomyocytes. Mol Cell Biol 2011, 31:2349-2363.
    • (2011) Mol Cell Biol , vol.31 , pp. 2349-2363
    • Pillai, V.B.1    Sundaresan, N.R.2    Samant, S.A.3    Wolfgeher, D.4    Trivedi, C.M.5    Gupta, M.P.6
  • 33
    • 35548942629 scopus 로고    scopus 로고
    • Inhibition of histone deacetylases triggers pharmacologic preconditioning effects against myocardial ischemic injury
    • Zhao T.C., Cheng G., Zhang L.X., Tseng Y.T., Padbury J.F. Inhibition of histone deacetylases triggers pharmacologic preconditioning effects against myocardial ischemic injury. Cardiovasc Res 2007, 76:473-481.
    • (2007) Cardiovasc Res , vol.76 , pp. 473-481
    • Zhao, T.C.1    Cheng, G.2    Zhang, L.X.3    Tseng, Y.T.4    Padbury, J.F.5
  • 34
    • 84880183268 scopus 로고    scopus 로고
    • HDAC inhibition suppresses cardiac hypertrophy and fibrosis in DOCA-salt hypertensive rats via regulation of HDAC6/HDAC8 enzyme activity
    • Kee H.J., Bae E.H., Park S., Lee K.E., Suh S.H., Kim S.W., et al. HDAC inhibition suppresses cardiac hypertrophy and fibrosis in DOCA-salt hypertensive rats via regulation of HDAC6/HDAC8 enzyme activity. Kidney Blood Press Res 2013, 37:229-239.
    • (2013) Kidney Blood Press Res , vol.37 , pp. 229-239
    • Kee, H.J.1    Bae, E.H.2    Park, S.3    Lee, K.E.4    Suh, S.H.5    Kim, S.W.6
  • 37
    • 20444487771 scopus 로고    scopus 로고
    • Histone deacetylase HDAC8 associates with smooth muscle alpha-actin and is essential for smooth muscle cell contractility
    • Waltregny D., Glenisson W., Tran S.L., North B.J., Verdin E., Colige A., et al. Histone deacetylase HDAC8 associates with smooth muscle alpha-actin and is essential for smooth muscle cell contractility. FASEB J 2005, 19:966-968.
    • (2005) FASEB J , vol.19 , pp. 966-968
    • Waltregny, D.1    Glenisson, W.2    Tran, S.L.3    North, B.J.4    Verdin, E.5    Colige, A.6
  • 38
    • 80053195080 scopus 로고    scopus 로고
    • Acetylation of heat shock protein 20 (Hsp20) regulates human myometrial activity
    • Karolczak-Bayatti M., Sweeney M., Cheng J., Edey L., Robson S.C., Ulrich S.M., et al. Acetylation of heat shock protein 20 (Hsp20) regulates human myometrial activity. J Biol Chem 2011, 286:34346-34355.
    • (2011) J Biol Chem , vol.286 , pp. 34346-34355
    • Karolczak-Bayatti, M.1    Sweeney, M.2    Cheng, J.3    Edey, L.4    Robson, S.C.5    Ulrich, S.M.6
  • 39
    • 84921767210 scopus 로고    scopus 로고
    • Specific inhibition of histone deacetylase 8 reduces gene expression and production of proinflammatory cytokines in vitro and in vivo
    • Li S., Fossati G., Marchetti C., Modena D., Pozzi P., Reznikov L.L., et al. Specific inhibition of histone deacetylase 8 reduces gene expression and production of proinflammatory cytokines in vitro and in vivo. J Biol Chem 2014, 290:2368-2378.
    • (2014) J Biol Chem , vol.290 , pp. 2368-2378
    • Li, S.1    Fossati, G.2    Marchetti, C.3    Modena, D.4    Pozzi, P.5    Reznikov, L.L.6
  • 40
    • 33846889551 scopus 로고    scopus 로고
    • Derepression of pathological cardiac genes by members of the CaM kinase superfamily
    • McKinsey T.A. Derepression of pathological cardiac genes by members of the CaM kinase superfamily. Cardiovasc Res 2007, 73:667-677.
    • (2007) Cardiovasc Res , vol.73 , pp. 667-677
    • McKinsey, T.A.1
  • 41
    • 40849086606 scopus 로고    scopus 로고
    • Probing the elusive catalytic activity of vertebrate class IIa histone deacetylases
    • Jones P., Altamura S., De F.R., Gallinari P., Lahm A., Neddermann P., et al. Probing the elusive catalytic activity of vertebrate class IIa histone deacetylases. Bioorg Med Chem Lett 2008, 18:1814-1819.
    • (2008) Bioorg Med Chem Lett , vol.18 , pp. 1814-1819
    • Jones, P.1    Altamura, S.2    De, F.R.3    Gallinari, P.4    Lahm, A.5    Neddermann, P.6
  • 43
    • 0036787922 scopus 로고    scopus 로고
    • Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation
    • Zhang C.L., McKinsey T.A., Olson E.N. Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation. Mol Cell Biol 2002, 22:7302-7312.
    • (2002) Mol Cell Biol , vol.22 , pp. 7302-7312
    • Zhang, C.L.1    McKinsey, T.A.2    Olson, E.N.3
  • 46
    • 84893126165 scopus 로고    scopus 로고
    • Activation of histone deacetylase-6 induces contractile dysfunction through derailment of alpha-tubulin proteostasis in experimental and human atrial fibrillation
    • Zhang D., Wu C.T., Qi X., Meijering R.A., Hoogstra-Berends F., Tadevosyan A., et al. Activation of histone deacetylase-6 induces contractile dysfunction through derailment of alpha-tubulin proteostasis in experimental and human atrial fibrillation. Circulation 2014, 129:346-358.
    • (2014) Circulation , vol.129 , pp. 346-358
    • Zhang, D.1    Wu, C.T.2    Qi, X.3    Meijering, R.A.4    Hoogstra-Berends, F.5    Tadevosyan, A.6
  • 48
    • 77955355838 scopus 로고    scopus 로고
    • Rational design and simple chemistry yield a superior, neuroprotective HDAC6 inhibitor, tubastatin A
    • Butler K.V., Kalin J., Brochier C., Vistoli G., Langley B., Kozikowski A.P. Rational design and simple chemistry yield a superior, neuroprotective HDAC6 inhibitor, tubastatin A. J Am Chem Soc 2010, 132:10842-10846.
    • (2010) J Am Chem Soc , vol.132 , pp. 10842-10846
    • Butler, K.V.1    Kalin, J.2    Brochier, C.3    Vistoli, G.4    Langley, B.5    Kozikowski, A.P.6
  • 51
    • 77955711544 scopus 로고    scopus 로고
    • Role of autophagy in heart failure associated with aging
    • De Meyer G.R., De Keulenaer G.W., Martinet W. Role of autophagy in heart failure associated with aging. Heart Fail Rev 2010, 15:423-430.
    • (2010) Heart Fail Rev , vol.15 , pp. 423-430
    • De Meyer, G.R.1    De Keulenaer, G.W.2    Martinet, W.3
  • 53
    • 84902975038 scopus 로고    scopus 로고
    • Heart failure with preserved ejection fraction: mechanisms, clinical features, and therapies
    • Sharma K., Kass D.A. Heart failure with preserved ejection fraction: mechanisms, clinical features, and therapies. Circ Res 2014, 115:79-96.
    • (2014) Circ Res , vol.115 , pp. 79-96
    • Sharma, K.1    Kass, D.A.2
  • 54
    • 79952829685 scopus 로고    scopus 로고
    • Heart failure with preserved ejection fraction: pathophysiology, diagnosis, and treatment
    • Borlaug B.A., Paulus W.J. Heart failure with preserved ejection fraction: pathophysiology, diagnosis, and treatment. Eur Heart J 2011, 32:670-679.
    • (2011) Eur Heart J , vol.32 , pp. 670-679
    • Borlaug, B.A.1    Paulus, W.J.2
  • 55
    • 80054686672 scopus 로고    scopus 로고
    • Why are women more likely than men to develop heart failure with preserved ejection fraction?
    • Scantlebury D.C., Borlaug B.A. Why are women more likely than men to develop heart failure with preserved ejection fraction?. Curr Opin Cardiol 2011, 26:562-568.
    • (2011) Curr Opin Cardiol , vol.26 , pp. 562-568
    • Scantlebury, D.C.1    Borlaug, B.A.2
  • 56
    • 33746033433 scopus 로고    scopus 로고
    • Outcome of heart failure with preserved ejection fraction in a population-based study
    • Bhatia R.S., Tu J.V., Lee D.S., Austin P.C., Fang J., Haouzi A., et al. Outcome of heart failure with preserved ejection fraction in a population-based study. N Engl J Med 2006, 355:260-269.
    • (2006) N Engl J Med , vol.355 , pp. 260-269
    • Bhatia, R.S.1    Tu, J.V.2    Lee, D.S.3    Austin, P.C.4    Fang, J.5    Haouzi, A.6
  • 59
    • 47849087223 scopus 로고    scopus 로고
    • Heart failure with preserved ejection fraction: treat now by treating comorbidities
    • Shah S.J., Gheorghiade M. Heart failure with preserved ejection fraction: treat now by treating comorbidities. JAMA 2008, 300:431-433.
    • (2008) JAMA , vol.300 , pp. 431-433
    • Shah, S.J.1    Gheorghiade, M.2
  • 60
    • 77951264436 scopus 로고    scopus 로고
    • Cardiac aging in mice and humans: the role of mitochondrial oxidative stress
    • Dai D.F., Rabinovitch P.S. Cardiac aging in mice and humans: the role of mitochondrial oxidative stress. Trends Cardiovasc Med 2009, 19:213-220.
    • (2009) Trends Cardiovasc Med , vol.19 , pp. 213-220
    • Dai, D.F.1    Rabinovitch, P.S.2
  • 62
    • 14644417749 scopus 로고    scopus 로고
    • Age-associated increases in oxidative stress and antioxidant enzyme activities in cardiac interfibrillar mitochondria: implications for the mitochondrial theory of aging
    • Judge S., Jang Y.M., Smith A., Hagen T., Leeuwenburgh C. Age-associated increases in oxidative stress and antioxidant enzyme activities in cardiac interfibrillar mitochondria: implications for the mitochondrial theory of aging. FASEB J 2005, 19:419-421.
    • (2005) FASEB J , vol.19 , pp. 419-421
    • Judge, S.1    Jang, Y.M.2    Smith, A.3    Hagen, T.4    Leeuwenburgh, C.5
  • 63
    • 84923365528 scopus 로고    scopus 로고
    • The role of oxidative stress and inflammation in cardiovascular aging
    • Wu J., Xia S., Kalionis B., Wan W., Sun T. The role of oxidative stress and inflammation in cardiovascular aging. Biomed Res Int 2014, 2014:615312.
    • (2014) Biomed Res Int , vol.2014 , pp. 615312
    • Wu, J.1    Xia, S.2    Kalionis, B.3    Wan, W.4    Sun, T.5
  • 64
    • 79957964666 scopus 로고    scopus 로고
    • Targeting inflammation in heart failure with histone deacetylase inhibitors
    • McKinsey T.A. Targeting inflammation in heart failure with histone deacetylase inhibitors. Mol Med 2011, 17:434-441.
    • (2011) Mol Med , vol.17 , pp. 434-441
    • McKinsey, T.A.1
  • 65
    • 77955984513 scopus 로고    scopus 로고
    • HDAC inhibition attenuates inflammatory, hypertrophic, and hypertensive responses in spontaneously hypertensive rats
    • Cardinale J.P., Sriramula S., Pariaut R., Guggilam A., Mariappan N., Elks C.M., et al. HDAC inhibition attenuates inflammatory, hypertrophic, and hypertensive responses in spontaneously hypertensive rats. Hypertension 2010, 56:437-444.
    • (2010) Hypertension , vol.56 , pp. 437-444
    • Cardinale, J.P.1    Sriramula, S.2    Pariaut, R.3    Guggilam, A.4    Mariappan, N.5    Elks, C.M.6
  • 66
    • 78651470146 scopus 로고    scopus 로고
    • Effect of inhibiting histone deacetylase with short-chain carboxylic acids and their hydroxamic acid analogs on vertebrate development and neuronal chromatin
    • Fass D.M., Shah R., Ghosh B., Hennig K., Norton S., Zhao W.N., et al. Effect of inhibiting histone deacetylase with short-chain carboxylic acids and their hydroxamic acid analogs on vertebrate development and neuronal chromatin. ACS Med Chem Lett 2010, 2:39-42.
    • (2010) ACS Med Chem Lett , vol.2 , pp. 39-42
    • Fass, D.M.1    Shah, R.2    Ghosh, B.3    Hennig, K.4    Norton, S.5    Zhao, W.N.6
  • 68
    • 84882766696 scopus 로고    scopus 로고
    • Age-dependent mitochondrial energy dynamics in the mice heart: role of superoxide dismutase-2
    • Das K.C., Muniyappa H. Age-dependent mitochondrial energy dynamics in the mice heart: role of superoxide dismutase-2. Exp Gerontol 2013, 48:947-959.
    • (2013) Exp Gerontol , vol.48 , pp. 947-959
    • Das, K.C.1    Muniyappa, H.2
  • 69
    • 67649204729 scopus 로고    scopus 로고
    • Overexpression of catalase targeted to mitochondria attenuates murine cardiac aging
    • Dai D.F., Santana L.F., Vermulst M., Tomazela D.M., Emond M.J., MacCoss M.J., et al. Overexpression of catalase targeted to mitochondria attenuates murine cardiac aging. Circulation 2009, 119:2789-2797.
    • (2009) Circulation , vol.119 , pp. 2789-2797
    • Dai, D.F.1    Santana, L.F.2    Vermulst, M.3    Tomazela, D.M.4    Emond, M.J.5    MacCoss, M.J.6
  • 72
    • 84896532784 scopus 로고    scopus 로고
    • Microtubule acetylation amplifies p38 kinase signalling and anti-inflammatory IL-10 production
    • Wang B., Rao Y.H., Inoue M., Hao R., Lai C.H., Chen D., et al. Microtubule acetylation amplifies p38 kinase signalling and anti-inflammatory IL-10 production. Nat Commun 2014, 5:3479.
    • (2014) Nat Commun , vol.5 , pp. 3479
    • Wang, B.1    Rao, Y.H.2    Inoue, M.3    Hao, R.4    Lai, C.H.5    Chen, D.6
  • 73
    • 79956094244 scopus 로고    scopus 로고
    • Histone deacetylase 6 and heat shock protein 90 control the functions of Foxp3(+) T-regulatory cells
    • de Zoeten E.F., Wang L., Butler K., Beier U.H., Akimova T., Sai H., et al. Histone deacetylase 6 and heat shock protein 90 control the functions of Foxp3(+) T-regulatory cells. Mol Cell Biol 2011, 31:2066-2078.
    • (2011) Mol Cell Biol , vol.31 , pp. 2066-2078
    • de Zoeten, E.F.1    Wang, L.2    Butler, K.3    Beier, U.H.4    Akimova, T.5    Sai, H.6
  • 74
    • 76349122643 scopus 로고    scopus 로고
    • Protein acetylation in the cardiorenal axis: the promise of histone deacetylase inhibitors
    • Bush E.W., McKinsey T.A. Protein acetylation in the cardiorenal axis: the promise of histone deacetylase inhibitors. Circ Res 2010, 106:272-284.
    • (2010) Circ Res , vol.106 , pp. 272-284
    • Bush, E.W.1    McKinsey, T.A.2
  • 75
    • 84902996282 scopus 로고    scopus 로고
    • Heart failure with preserved ejection fraction: molecular pathways of the aging myocardium
    • Loffredo F.S., Nikolova A.P., Pancoast J.R., Lee R.T. Heart failure with preserved ejection fraction: molecular pathways of the aging myocardium. Circ Res 2014, 115:97-107.
    • (2014) Circ Res , vol.115 , pp. 97-107
    • Loffredo, F.S.1    Nikolova, A.P.2    Pancoast, J.R.3    Lee, R.T.4
  • 76
    • 80052814243 scopus 로고    scopus 로고
    • Isoform-selective HDAC inhibitors: closing in on translational medicine for the heart
    • McKinsey T.A. Isoform-selective HDAC inhibitors: closing in on translational medicine for the heart. J Mol Cell Cardiol 2011, 51:491-496.
    • (2011) J Mol Cell Cardiol , vol.51 , pp. 491-496
    • McKinsey, T.A.1
  • 78
    • 84875168737 scopus 로고    scopus 로고
    • Toxicological and metabolic considerations for histone deacetylase inhibitors
    • Fraczek J., Vanhaecke T., Rogiers V. Toxicological and metabolic considerations for histone deacetylase inhibitors. Expert Opin Drug Metab Toxicol 2013, 9:441-457.
    • (2013) Expert Opin Drug Metab Toxicol , vol.9 , pp. 441-457
    • Fraczek, J.1    Vanhaecke, T.2    Rogiers, V.3
  • 80
    • 77955712605 scopus 로고    scopus 로고
    • Modulation of sarcoplasmic reticulum Ca(2+) cycling in systolic and diastolic heart failure associated with aging
    • Janczewski A.M., Lakatta E.G. Modulation of sarcoplasmic reticulum Ca(2+) cycling in systolic and diastolic heart failure associated with aging. Heart Fail Rev 2010, 15:431-445.
    • (2010) Heart Fail Rev , vol.15 , pp. 431-445
    • Janczewski, A.M.1    Lakatta, E.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.