메뉴 건너뛰기




Volumn 1604, Issue , 2015, Pages 15-24

Intracellular translocation of histone deacetylase 5 regulates neuronal cell apoptosis

Author keywords

Apoptosis; CaMKII; HDAC5; Histone acetylation; Neuron; NMDA

Indexed keywords

CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II ALPHA; HISTONE DEACETYLASE 5; N METHYL DEXTRO ASPARTIC ACID; N [2 [[N [3 (4 CHLOROPHENYL) 2 PROPENYL] N METHYLAMINO]METHYL]PHENYL] N (2 HYDROXYETHYL) 4 METHOXYBENZENESULFONAMIDE; TRICHOSTATIN A; UNCLASSIFIED DRUG; BENZYLAMINE DERIVATIVE; HDAC5 PROTEIN, RAT; HISTONE DEACETYLASE; HISTONE DEACETYLASE INHIBITOR; N METHYLASPARTIC ACID; SULFONAMIDE;

EID: 84925689137     PISSN: 00068993     EISSN: 18726240     Source Type: Journal    
DOI: 10.1016/j.brainres.2015.01.043     Document Type: Article
Times cited : (11)

References (39)
  • 2
    • 79953043596 scopus 로고    scopus 로고
    • Excitotoxic neuroprotection and vulnerability with CaMKII inhibition
    • N.M. Ashpole, and A. Hudmon Excitotoxic neuroprotection and vulnerability with CaMKII inhibition Mol. Cell Neurosci. 46 2011 720 730
    • (2011) Mol. Cell Neurosci. , vol.46 , pp. 720-730
    • Ashpole, N.M.1    Hudmon, A.2
  • 3
    • 26844518082 scopus 로고    scopus 로고
    • Intracellular trafficking of histone deacetylase 4 regulates neuronal cell death
    • T.A. Bolger, and T.P. Yao Intracellular trafficking of histone deacetylase 4 regulates neuronal cell death J. Neurosci. 25 2005 9544 9553
    • (2005) J. Neurosci. , vol.25 , pp. 9544-9553
    • Bolger, T.A.1    Yao, T.P.2
  • 4
    • 34247385039 scopus 로고    scopus 로고
    • Novelty stress induces phospho-acetylation of histone H3 in rat dentate gyrus granule neurons through coincident signalling via the N-methyl-d-aspartate receptor and the glucocorticoid receptor: Relevance for c-fos induction
    • Y. Chandramohan, S.K. Droste, and J.M. Reul Novelty stress induces phospho-acetylation of histone H3 in rat dentate gyrus granule neurons through coincident signalling via the N-methyl-d-aspartate receptor and the glucocorticoid receptor: relevance for c-fos induction J. Neurochem. 101 2007 815 828
    • (2007) J. Neurochem. , vol.101 , pp. 815-828
    • Chandramohan, Y.1    Droste, S.K.2    Reul, J.M.3
  • 5
    • 58149389397 scopus 로고    scopus 로고
    • HDAC4 regulates neuronal survival in normal and diseased retinas
    • B. Chen, and C.L. Cepko HDAC4 regulates neuronal survival in normal and diseased retinas Science 323 2009 256 259
    • (2009) Science , vol.323 , pp. 256-259
    • Chen, B.1    Cepko, C.L.2
  • 6
    • 84879026413 scopus 로고    scopus 로고
    • Neuroprotective activities of catalpol against CaMKII-dependent apoptosis induced by LPS in PC12 cells
    • W. Chen, X. Li, L.Q. Jia, J. Wang, L. Zhang, D. Hou, J. Wang, and L. Ren Neuroprotective activities of catalpol against CaMKII-dependent apoptosis induced by LPS in PC12 cells Br. J. Pharmacol. 169 2013 1140 1152
    • (2013) Br. J. Pharmacol. , vol.169 , pp. 1140-1152
    • Chen, W.1    Li, X.2    Jia, L.Q.3    Wang, J.4    Zhang, L.5    Hou, D.6    Wang, J.7    Ren, L.8
  • 8
    • 0037426839 scopus 로고    scopus 로고
    • Rhythmic histone acetylation underlies transcription in the mammalian circadian clock
    • J.P. Etchegaray, C. Lee, P.A. Wade, and S.M. Reppert Rhythmic histone acetylation underlies transcription in the mammalian circadian clock Nature 421 2003 177 182
    • (2003) Nature , vol.421 , pp. 177-182
    • Etchegaray, J.P.1    Lee, C.2    Wade, P.A.3    Reppert, S.M.4
  • 10
    • 66649086928 scopus 로고    scopus 로고
    • Mechanism of differential control of NMDA receptor activity by NR2 subunits
    • M. Gielen, B. Siegler Retchless, L. Mony, J.W. Johnson, and P. Paoletti Mechanism of differential control of NMDA receptor activity by NR2 subunits Nature 459 2009 703 707
    • (2009) Nature , vol.459 , pp. 703-707
    • Gielen, M.1    Siegler Retchless, B.2    Mony, L.3    Johnson, J.W.4    Paoletti, P.5
  • 11
    • 0034608955 scopus 로고    scopus 로고
    • Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization
    • C.M. Grozinger, and S.L. Schreiber Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization Proc. Natl. Acad. Sci. USA 97 2000 7835 7840
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7835-7840
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 12
    • 77957261983 scopus 로고    scopus 로고
    • PKA phosphorylates histone deacetylase 5 and prevents its nuclear export, leading to the inhibition of gene transcription and cardiomyocyte hypertrophy
    • C.H. Ha, J.Y. Kim, J. Zhao, W. Wang, B.S. Jhun, C. Wong, and Z.G. Jin PKA phosphorylates histone deacetylase 5 and prevents its nuclear export, leading to the inhibition of gene transcription and cardiomyocyte hypertrophy Proc. Natl. Acad. Sci. USA 107 2010 15467 15472
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 15467-15472
    • Ha, C.H.1    Kim, J.Y.2    Zhao, J.3    Wang, W.4    Jhun, B.S.5    Wong, C.6    Jin, Z.G.7
  • 13
    • 33746341792 scopus 로고    scopus 로고
    • Activity-dependent gating of CaMKII autonomous activity by Drosophila CASK
    • J.J. Hodge, P. Mullasseril, and L.C. Griffith Activity-dependent gating of CaMKII autonomous activity by Drosophila CASK Neuron 51 2006 327 337
    • (2006) Neuron , vol.51 , pp. 327-337
    • Hodge, J.J.1    Mullasseril, P.2    Griffith, L.C.3
  • 14
    • 5444244267 scopus 로고    scopus 로고
    • Epigenetic control of neural stem cell fate
    • J. Hsieh, and F.H. Gage Epigenetic control of neural stem cell fate Curr. Opin. Genet. Dev. 14 2004 461 469
    • (2004) Curr. Opin. Genet. Dev. , vol.14 , pp. 461-469
    • Hsieh, J.1    Gage, F.H.2
  • 16
    • 53249130741 scopus 로고    scopus 로고
    • Therapeutic application of histone deacetylase inhibitors for central nervous system disorders
    • A.G. Kazantsev, and L.M. Thompson Therapeutic application of histone deacetylase inhibitors for central nervous system disorders Nat. Rev. Drug Discov. 7 2008 854 868
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 854-868
    • Kazantsev, A.G.1    Thompson, L.M.2
  • 17
    • 0035914462 scopus 로고    scopus 로고
    • Caspase-mediated cleavage of the Ca2+/calmodulin-dependent protein kinase-like kinase facilitates neuronal apoptosis
    • M. Kruidering, T. Schouten, G.I. Evan, and E. Vreugdenhil Caspase-mediated cleavage of the Ca2+/calmodulin-dependent protein kinase-like kinase facilitates neuronal apoptosis J. Biol. Chem. 276 2001 38417 38425
    • (2001) J. Biol. Chem. , vol.276 , pp. 38417-38425
    • Kruidering, M.1    Schouten, T.2    Evan, G.I.3    Vreugdenhil, E.4
  • 18
    • 20844438031 scopus 로고    scopus 로고
    • Remodeling chromatin and stress resistance in the central nervous system: Histone deacetylase inhibitors as novel and broadly effective neuroprotective agents
    • B. Langley, J.M. Gensert, M.F. Beal, and R.R. Ratan Remodeling chromatin and stress resistance in the central nervous system: histone deacetylase inhibitors as novel and broadly effective neuroprotective agents Curr. Drug Targets CNS Neurol. Disord. 4 2005 41 50
    • (2005) Curr. Drug Targets CNS Neurol. Disord. , vol.4 , pp. 41-50
    • Langley, B.1    Gensert, J.M.2    Beal, M.F.3    Ratan, R.R.4
  • 20
    • 84954358195 scopus 로고    scopus 로고
    • Necroptosis contributes to the NMDA-induced excitotoxicity in rats cultured cortical neurons
    • Y. Li, X. Yang, C. Ma, J. Qiao, and C. Zhang Necroptosis contributes to the NMDA-induced excitotoxicity in rats cultured cortical neurons Neurosci. Lett. 447 2008 120 123
    • (2008) Neurosci. Lett. , vol.447 , pp. 120-123
    • Li, Y.1    Yang, X.2    Ma, C.3    Qiao, J.4    Zhang, C.5
  • 21
    • 33947389277 scopus 로고    scopus 로고
    • Cadmium activates CaMK-II and initiates CaMK-II-dependent apoptosis in mesangial cells
    • Y. Liu, and D.M. Templeton Cadmium activates CaMK-II and initiates CaMK-II-dependent apoptosis in mesangial cells FEBS Lett. 581 2007 1481 1486
    • (2007) FEBS Lett. , vol.581 , pp. 1481-1486
    • Liu, Y.1    Templeton, D.M.2
  • 22
    • 78049278342 scopus 로고    scopus 로고
    • Alterations of NMDA receptor subunits NR1, NR2A and NR2B mRNA expression and their relationship to apoptosis following transient forebrain ischemia
    • Z. Liu, W. Zhao, T. Xu, D. Pei, and Y. Peng Alterations of NMDA receptor subunits NR1, NR2A and NR2B mRNA expression and their relationship to apoptosis following transient forebrain ischemia Brain Res. 1361 2010 133 139
    • (2010) Brain Res. , vol.1361 , pp. 133-139
    • Liu, Z.1    Zhao, W.2    Xu, T.3    Pei, D.4    Peng, Y.5
  • 23
    • 79551532277 scopus 로고    scopus 로고
    • Neuroprotection by histone deacetylase-7 (HDAC7) occurs by inhibition of c-jun expression through a deacetylase-independent mechanism
    • C. Ma, and S.R. DMello Neuroprotection by histone deacetylase-7 (HDAC7) occurs by inhibition of c-jun expression through a deacetylase-independent mechanism J. Biol. Chem. 286 2011 4819 4828
    • (2011) J. Biol. Chem. , vol.286 , pp. 4819-4828
    • Ma, C.1    Dmello, S.R.2
  • 24
    • 38449085572 scopus 로고    scopus 로고
    • Class IIA HDACs in the regulation of neurodegeneration
    • N. Majdzadeh, B.E. Morrison, and S.R. DMello Class IIA HDACs in the regulation of neurodegeneration Front. Biosci. 13 2008 1072 1082
    • (2008) Front. Biosci. , vol.13 , pp. 1072-1082
    • Majdzadeh, N.1    Morrison, B.E.2    Dmello, S.R.3
  • 25
    • 0034597816 scopus 로고    scopus 로고
    • Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation
    • T.A. McKinsey, C.L. Zhang, J. Lu, and E.N. Olson Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation Nature 408 2000 106 111
    • (2000) Nature , vol.408 , pp. 106-111
    • McKinsey, T.A.1    Zhang, C.L.2    Lu, J.3    Olson, E.N.4
  • 26
    • 0034687741 scopus 로고    scopus 로고
    • Activation of the myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase 5
    • T.A. McKinsey, C.L. Zhang, and E.N. Olson Activation of the myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase 5 Proc. Natl. Acad. Sci. USA 97 2000 14400 14405
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14400-14405
    • McKinsey, T.A.1    Zhang, C.L.2    Olson, E.N.3
  • 30
    • 84887161736 scopus 로고    scopus 로고
    • HDAC5, a key component in temporal regulation of p53-mediated transactivation in response to genotoxic stress
    • N. Sen, R. Kumari, M.I. Singh, and S. Das HDAC5, a key component in temporal regulation of p53-mediated transactivation in response to genotoxic stress Mol. Cell 52 2013 406 420
    • (2013) Mol. Cell , vol.52 , pp. 406-420
    • Sen, N.1    Kumari, R.2    Singh, M.I.3    Das, S.4
  • 31
    • 67649619244 scopus 로고    scopus 로고
    • Putting the 'HAT' back on survival signalling: The promises and challenges of HDAC inhibition in the treatment of neurological conditions
    • S.F. Sleiman, M. Basso, L. Mahishi, A.P. Kozikowski, M.E. Donohoe, B. Langley, and R.R. Ratan Putting the 'HAT' back on survival signalling: the promises and challenges of HDAC inhibition in the treatment of neurological conditions Expert Opin. Investig. Drugs 18 2009 573 584
    • (2009) Expert Opin. Investig. Drugs , vol.18 , pp. 573-584
    • Sleiman, S.F.1    Basso, M.2    Mahishi, L.3    Kozikowski, A.P.4    Donohoe, M.E.5    Langley, B.6    Ratan, R.R.7
  • 32
    • 3242765335 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors - A new tool to treat cancer
    • R. Somech, S. Izraeli, and J.S. A Histone deacetylase inhibitors - a new tool to treat cancer Cancer Treat. Rev. 30 2004 461 472
    • (2004) Cancer Treat. Rev. , vol.30 , pp. 461-472
    • Somech, R.1    Izraeli, S.2
  • 33
    • 82455199274 scopus 로고    scopus 로고
    • Paraquat induces epigenetic changes by promoting histone acetylation in cell culture models of dopaminergic degeneration
    • C. Song, A. Kanthasamy, H. Jin, V. Anantharam, and A.G. Kanthasamy Paraquat induces epigenetic changes by promoting histone acetylation in cell culture models of dopaminergic degeneration Neurotoxicology 32 2011 586 595
    • (2011) Neurotoxicology , vol.32 , pp. 586-595
    • Song, C.1    Kanthasamy, A.2    Jin, H.3    Anantharam, V.4    Kanthasamy, A.G.5
  • 34
    • 66449102444 scopus 로고    scopus 로고
    • Role of histone acetylation in the activity-dependent regulation of sulfiredoxin and sestrin 2
    • F.X. Soriano, S. Papadia, K.F. Bell, and G.E. Hardingham Role of histone acetylation in the activity-dependent regulation of sulfiredoxin and sestrin 2 Epigenetics 4 2009 152 158
    • (2009) Epigenetics , vol.4 , pp. 152-158
    • Soriano, F.X.1    Papadia, S.2    Bell, K.F.3    Hardingham, G.E.4
  • 36
    • 0028175464 scopus 로고
    • Ca2+ ionophore-induced apoptosis on cultured embryonic rat cortical neurons
    • N. Takei, and Y. Endo Ca2+ ionophore-induced apoptosis on cultured embryonic rat cortical neurons Brain Res. 652 1994 65 70
    • (1994) Brain Res. , vol.652 , pp. 65-70
    • Takei, N.1    Endo, Y.2
  • 37
    • 70449518179 scopus 로고    scopus 로고
    • HDAC inhibitor trichostatin A-inhibited survival of dopaminergic neuronal cells
    • Y. Wang, X. Wang, L. Liu, and X. Wang HDAC inhibitor trichostatin A-inhibited survival of dopaminergic neuronal cells Neurosci. Lett. 467 2009 212 216
    • (2009) Neurosci. Lett. , vol.467 , pp. 212-216
    • Wang, Y.1    Wang, X.2    Liu, L.3    Wang, X.4
  • 38
    • 0029800074 scopus 로고    scopus 로고
    • Calcium influx via the NMDA receptor induces immediate early gene transcription by a MAP kinase/ERK-dependent mechanism
    • Z. Xia, H. Dudek, C.K. Miranti, and M.E. Greenberg Calcium influx via the NMDA receptor induces immediate early gene transcription by a MAP kinase/ERK-dependent mechanism J. Neurosci. 16 1996 5425 5436
    • (1996) J. Neurosci. , vol.16 , pp. 5425-5436
    • Xia, Z.1    Dudek, H.2    Miranti, C.K.3    Greenberg, M.E.4
  • 39
    • 79960679247 scopus 로고    scopus 로고
    • Receptor-independent protein kinase C alpha (PKCalpha) signaling by calpain-generated free catalytic domains induces HDAC5 nuclear export and regulates cardiac transcription
    • Y. Zhang, S.J. Matkovich, X. Duan, A. Diwan, M.Y. Kang, and G.W. Dorn 2nd Receptor-independent protein kinase C alpha (PKCalpha) signaling by calpain-generated free catalytic domains induces HDAC5 nuclear export and regulates cardiac transcription J. Biol. Chem. 286 2011 26943 26951
    • (2011) J. Biol. Chem. , vol.286 , pp. 26943-26951
    • Zhang, Y.1    Matkovich, S.J.2    Duan, X.3    Diwan, A.4    Kang, M.Y.5    Dorn, G.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.