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Volumn 5, Issue 6, 2014, Pages

Tissue-specific deregulation of selected HDACs characterizes ALS progression in mouse models: Pharmacological characterization of SIRT1 and SIRT2 pathways

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE DEACETYLASE; HISTONE DEACETYLASE 11; HISTONE DEACETYLASE 5; MESSENGER RNA; PROTEIN P53; SIRTUIN 1; SIRTUIN 2; TUBULIN; UNCLASSIFIED DRUG; COPPER ZINC SUPEROXIDE DISMUTASE; ENZYME INHIBITOR; SIRT1 PROTEIN, MOUSE; SIRT2 PROTEIN, MOUSE; SUPEROXIDE DISMUTASE;

EID: 84903792981     PISSN: None     EISSN: 20414889     Source Type: Journal    
DOI: 10.1038/cddis.2014.247     Document Type: Article
Times cited : (40)

References (40)
  • 1
    • 84865654196 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis: New insights into underlying molecular mechanisms and opportunities for therapeutic intervention
    • Cozzolino M, Pesaresi MG, Gerbino V, Grosskreutz J, Carrì MT. Amyotrophic lateral sclerosis: new insights into underlying molecular mechanisms and opportunities for therapeutic intervention. Antioxid Redox Signal 2012; 17: 1277-1330.
    • (2012) Antioxid Redox Signal , vol.17 , pp. 1277-1330
    • Cozzolino, M.1    Pesaresi, M.G.2    Gerbino, V.3    Grosskreutz, J.4    Carrì, M.T.5
  • 2
    • 77954325417 scopus 로고    scopus 로고
    • Histone deacetylation and motor neuron degeneration
    • Schmalbach S, Petri S. Histone deacetylation and motor neuron degeneration. CNS Neurol Disord Drug Targets 2010; 9: 279-284.
    • (2010) CNS Neurol Disord Drug Targets , vol.9 , pp. 279-284
    • Schmalbach, S.1    Petri, S.2
  • 3
    • 33644946604 scopus 로고    scopus 로고
    • HATs and HDACs in neurodegeneration: A tale of disconcerted acetylation homeostasis
    • Saha RN, Pahan K. HATs and HDACs in neurodegeneration: a tale of disconcerted acetylation homeostasis. Cell Death Differ 2006; 13: 539-550.
    • (2006) Cell Death Differ , vol.13 , pp. 539-550
    • Saha, R.N.1    Pahan, K.2
  • 4
    • 0347624644 scopus 로고    scopus 로고
    • Critical loss of CBP/p300 histone acetylase activity by caspase-6 during neurodegeneration
    • Rouaux C, Jokic N, Mbebi C, Boutillier S, Loeffler JP, Boutillier AL. Critical loss of CBP/p300 histone acetylase activity by caspase-6 during neurodegeneration. EMBO J 2003; 22: 6537-6549.
    • (2003) EMBO J , vol.22 , pp. 6537-6549
    • Rouaux, C.1    Jokic, N.2    Mbebi, C.3    Boutillier, S.4    Loeffler, J.P.5    Boutillier, A.L.6
  • 5
    • 34250612194 scopus 로고    scopus 로고
    • Sodium valproate exerts neuroprotective effects in vivo through CREB-binding proteindependent mechanisms but does not improve survival in an amyotrophic lateral sclerosis mouse model
    • Rouaux C, Panteleeva I, RenéF, Gonzalez de Aguilar JL, Echaniz-Laguna A, Dupuis L et al. Sodium valproate exerts neuroprotective effects in vivo through CREB-binding proteindependent mechanisms but does not improve survival in an amyotrophic lateral sclerosis mouse model. J Neurosci 2007; 27: 5535-5545.
    • (2007) J Neurosci , vol.27 , pp. 5535-5545
    • Rouaux, C.1    Panteleeva, I.2    Renéf3    Gonzalez De Aguilar, J.L.4    Echaniz-Laguna, A.5    Dupuis, L.6
  • 6
    • 4143141116 scopus 로고    scopus 로고
    • Targeting CREB-binding protein (CBP) loss of function as a therapeutic strategy in neurological disorders
    • Rouaux C, Loeffler JP, Boutillier AL. Targeting CREB-binding protein (CBP) loss of function as a therapeutic strategy in neurological disorders. Biochem Pharmacol 2004; 68: 1157-1164.
    • (2004) Biochem Pharmacol , vol.68 , pp. 1157-1164
    • Rouaux, C.1    Loeffler, J.P.2    Boutillier, A.L.3
  • 7
    • 20144385858 scopus 로고    scopus 로고
    • Sodium phenylbutyrate prolongs survival and regulates expression of anti-apoptotic genes in transgenic amyotrophic lateral sclerosis mice
    • Ryu H, Smith K, Camelo SI, Carreras I, Lee J, Iglesias AH et al. Sodium phenylbutyrate prolongs survival and regulates expression of anti-apoptotic genes in transgenic amyotrophic lateral sclerosis mice. J Neurochem 2005; 93: 1087-1098.
    • (2005) J Neurochem , vol.93 , pp. 1087-1098
    • Ryu, H.1    Smith, K.2    Camelo, S.I.3    Carreras, I.4    Lee, J.5    Iglesias, A.H.6
  • 8
    • 10844284615 scopus 로고    scopus 로고
    • Benefit of valproic acid in suppressing disease progression of ALS model mice
    • Sugai F, Yamamoto Y, Miyaguchi K, Zhou Z, Sumi H, Hamasaki T et al. Benefit of valproic acid in suppressing disease progression of ALS model mice. Eur J Neurosci 2004; 20: 3179-3183.
    • (2004) Eur J Neurosci , vol.20 , pp. 3179-3183
    • Sugai, F.1    Yamamoto, Y.2    Miyaguchi, K.3    Zhou, Z.4    Sumi, H.5    Hamasaki, T.6
  • 10
    • 79961028733 scopus 로고    scopus 로고
    • Treatment with trichostatin A initiated after disease onset delays disease progression and increases survival in a mouse model of amyotrophic lateral sclerosis
    • Yoo YE, Ko CP. Treatment with trichostatin A initiated after disease onset delays disease progression and increases survival in a mouse model of amyotrophic lateral sclerosis. Exp Neurol 2011; 231: 147-159.
    • (2011) Exp Neurol , vol.231 , pp. 147-159
    • Yoo, Y.E.1    Ko, C.P.2
  • 11
    • 84881323192 scopus 로고    scopus 로고
    • Histone acetylation as a potential therapeutic target in motor neuron degenerative diseases
    • Garbes L, Riessland M, Wirth B. Histone acetylation as a potential therapeutic target in motor neuron degenerative diseases. Curr Pharm Des 2013; 19: 5093-5104.
    • (2013) Curr Pharm des , vol.19 , pp. 5093-5104
    • Garbes, L.1    Riessland, M.2    Wirth, B.3
  • 13
    • 72149131804 scopus 로고    scopus 로고
    • MicroRNA-206 delays ALS progression and promotes regeneration of neuromuscular synapses in mice
    • Williams AH, Valdez G, Moresi V, Qi X, McAnally J, Elliott JL et al. MicroRNA-206 delays ALS progression and promotes regeneration of neuromuscular synapses in mice. Science 2009; 326: 1549-1554.
    • (2009) Science , vol.326 , pp. 1549-1554
    • Williams, A.H.1    Valdez, G.2    Moresi, V.3    Qi, X.4    McAnally, J.5    Elliott, J.L.6
  • 14
    • 84880960483 scopus 로고    scopus 로고
    • Muscle histone deacetylase 4 upregulation in amyotrophic lateral sclerosis: Potential role in reinnervation ability and disease progression
    • Bruneteau G, Simonet T, BauchéS, Mandjee N, Malfatti E, Girard E et al. Muscle histone deacetylase 4 upregulation in amyotrophic lateral sclerosis: potential role in reinnervation ability and disease progression. Brain 2013; 136(Pt 8): 2359-2368.
    • (2013) Brain , vol.136 , Issue.PART 8 , pp. 2359-2368
    • Bruneteau, G.1    Simonet, T.2    Bauché, S.3    Mandjee, N.4    Malfatti, E.5    Girard, E.6
  • 15
    • 84860915669 scopus 로고    scopus 로고
    • HDAC6 at the intersection of neuroprotection and neurodegeneration
    • d'Ydewalle C, Bogaert E, Van Den Bosch L. HDAC6 at the intersection of neuroprotection and neurodegeneration. Traffic 2012; 13: 771-779.
    • (2012) Traffic , vol.13 , pp. 771-779
    • D'ydewalle, C.1    Bogaert, E.2    Van Den Bosch, L.3
  • 16
    • 80052136588 scopus 로고    scopus 로고
    • TDP-43 knockdown impairs neurite outgrowth dependent on its target histone deacetylase
    • Fiesel FC, Schurr C, Weber SS, Kahle PJ. TDP-43 knockdown impairs neurite outgrowth dependent on its target histone deacetylase. Mol Neurodegener 2011; 6: 76.
    • (2011) Mol Neurodegener , vol.6 , pp. 76
    • Fiesel, F.C.1    Schurr, C.2    Weber, S.S.3    Kahle, P.J.4
  • 18
    • 84878243123 scopus 로고    scopus 로고
    • HDAC6 regulates mutant SOD1 aggregation through two SMIR motifs and tubulin acetylation
    • Gal J, Chen J, Barnett KR, Yang L, Brumley E, Zhu H. HDAC6 regulates mutant SOD1 aggregation through two SMIR motifs and tubulin acetylation. J Biol Chem 2013; 288: 15035-15045.
    • (2013) J Biol Chem , vol.288 , pp. 15035-15045
    • Gal, J.1    Chen, J.2    Barnett, K.R.3    Yang, L.4    Brumley, E.5    Zhu, H.6
  • 19
    • 34447308268 scopus 로고    scopus 로고
    • SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis
    • Kim D, Nguyen MD, Dobbin MM, Fischer A, Sananbenesi F, Rodgers JT et al. SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis. EMBO J 2007; 26: 3169-3179.
    • (2007) EMBO J , vol.26 , pp. 3169-3179
    • Kim, D.1    Nguyen, M.D.2    Dobbin, M.M.3    Fischer, A.4    Sananbenesi, F.5    Rodgers, J.T.6
  • 20
    • 84855200886 scopus 로고    scopus 로고
    • Region-specific changes in the immunoreactivity of SIRT1 expression in the central nervous system of SOD1(G93A) transgenic mice as an in vivo model of amyotrophic lateral sclerosis
    • Lee JC, Shin JH, Park BW, Kim GS, Kim JC, Kang KS et al. Region-specific changes in the immunoreactivity of SIRT1 expression in the central nervous system of SOD1(G93A) transgenic mice as an in vivo model of amyotrophic lateral sclerosis. Brain Res 2012; 1433: 20-28.
    • (2012) Brain Res , vol.1433 , pp. 20-28
    • Lee, J.C.1    Shin, J.H.2    Park, B.W.3    Kim, G.S.4    Kim, J.C.5    Kang, K.S.6
  • 21
    • 84873096554 scopus 로고    scopus 로고
    • Differential sirtuin expression patterns in amyotrophic lateral sclerosis (ALS) postmortem tissue: Neuroprotective or neurotoxic properties of sirtuins in ALS?
    • Körner S, Böselt S, Thau N, Rath KJ, Dengler R, Petri S. Differential sirtuin expression patterns in amyotrophic lateral sclerosis (ALS) postmortem tissue: neuroprotective or neurotoxic properties of sirtuins in ALS? Neurodegener Dis 2013; 11: 141-152.
    • (2013) Neurodegener Dis , vol.11 , pp. 141-152
    • KöRner, S.1    BöSelt, S.2    Thau, N.3    Rath, K.J.4    Dengler, R.5    Petri, S.6
  • 22
    • 84872683148 scopus 로고    scopus 로고
    • Mutant SOD1G93A triggers mitochondrial fragmentation in spinal cord motor neurons: Neuroprotection by SIRT3 and PGC-1a
    • Song W, Song Y, Kincaid B, Bossy B, Bossy-Wetzel E. Mutant SOD1G93A triggers mitochondrial fragmentation in spinal cord motor neurons: neuroprotection by SIRT3 and PGC-1a. Neurobiol Dis 2013; 51: 72-81.
    • (2013) Neurobiol Dis , vol.51 , pp. 72-81
    • Song, W.1    Song, Y.2    Kincaid, B.3    Bossy, B.4    Bossy-Wetzel, E.5
  • 23
    • 84874709843 scopus 로고    scopus 로고
    • SIRT1 and SIRT2: Emerging targets in neurodegeneration
    • Donmez G, Outeiro TF. SIRT1 and SIRT2: emerging targets in neurodegeneration. EMBO Mol Med 2013; 5: 344-352.
    • (2013) EMBO Mol Med , vol.5 , pp. 344-352
    • Donmez, G.1    Outeiro, T.F.2
  • 24
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai S, Armstrong CM, Kaeberlein M, Guarente L. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 2000; 403: 795-800.
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 25
    • 4944245398 scopus 로고    scopus 로고
    • Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin
    • Vaquero A, Scher M, Lee D, Erdjument-Bromage H, Tempst P, Reinberg D. Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin. Mol Cell 2004; 16: 93-105.
    • (2004) Mol Cell , vol.16 , pp. 93-105
    • Vaquero, A.1    Scher, M.2    Lee, D.3    Erdjument-Bromage, H.4    Tempst, P.5    Reinberg, D.6
  • 27
    • 79952806932 scopus 로고    scopus 로고
    • Sirtuins at a glance
    • Nakagawa T, Guarente L. Sirtuins at a glance. J Cell Sci 2011; 124(Pt 6): 833-838.
    • (2011) J Cell Sci , vol.124 , Issue.PART 6 , pp. 833-838
    • Nakagawa, T.1    Guarente, L.2
  • 28
  • 29
    • 84867380741 scopus 로고    scopus 로고
    • Janus-faced role of SIRT1 in tumorigenesis
    • Song NY, Surh YJ. Janus-faced role of SIRT1 in tumorigenesis. Ann N Y Acad Sci 2012; 1271: 10-19.
    • (2012) Ann N y Acad Sci , vol.1271 , pp. 10-19
    • Song, N.Y.1    Surh, Y.J.2
  • 31
    • 84879364137 scopus 로고    scopus 로고
    • Aging well with a little wine and a good clock
    • Belden WJ, Dunlap JC. Aging well with a little wine and a good clock. Cell 2013; 153: 1421-1422.
    • (2013) Cell , vol.153 , pp. 1421-1422
    • Belden, W.J.1    Dunlap, J.C.2
  • 32
    • 84865274411 scopus 로고    scopus 로고
    • The neurobiology of sirtuins and their role in neurodegeneration
    • Donmez G. The neurobiology of sirtuins and their role in neurodegeneration. Trends Pharmacol Sci 2012; 33: 494-501.
    • (2012) Trends Pharmacol Sci , vol.33 , pp. 494-501
    • Donmez, G.1
  • 33
    • 84884158350 scopus 로고    scopus 로고
    • New role of silent information regulator 1 in cerebral ischemia
    • Yang Y, Duan W, Li Y, Yan J, Yi W, Liang Z et al. New role of silent information regulator 1 in cerebral ischemia. Neurobiol Aging 2013; 34: 2879-2888.
    • (2013) Neurobiol Aging , vol.34 , pp. 2879-2888
    • Yang, Y.1    Duan, W.2    Li, Y.3    Yan, J.4    Yi, W.5    Liang, Z.6
  • 34
    • 84883447356 scopus 로고    scopus 로고
    • Sirtuins as therapeutic targets of caprylic triglyceride in ALS therapy
    • Pasinetti GM, Bilski AE, Zhao W. Sirtuins as therapeutic targets of caprylic triglyceride in ALS therapy. Cell Res 2013; 23: 1073-1074.
    • (2013) Cell Res , vol.23 , pp. 1073-1074
    • Pasinetti, G.M.1    Bilski, A.E.2    Zhao, W.3
  • 35
    • 79952805074 scopus 로고    scopus 로고
    • Astroglial inhibition of NF-kB does not ameliorate disease onset and progression in a mouse model for amyotrophic lateral sclerosis (ALS)
    • Crosio C, Valle C, Casciati A, Iaccarino C, Carrì MT. Astroglial inhibition of NF-kB does not ameliorate disease onset and progression in a mouse model for amyotrophic lateral sclerosis (ALS). PLoS One 2011; 6: e17187.
    • (2011) PLoS One , vol.6
    • Crosio, C.1    Valle, C.2    Casciati, A.3    Iaccarino, C.4    Carrì, M.T.5
  • 36
    • 0028888945 scopus 로고
    • Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis
    • Ripps ME, Huntley GW, Hof PR, Morrison JH, Gordon JW. Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis. Proc Natl Acad Sci USA 1995; 92: 689-693.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 689-693
    • Ripps, M.E.1    Huntley, G.W.2    Hof, P.R.3    Morrison, J.H.4    Gordon, J.W.5
  • 37
    • 80053959138 scopus 로고    scopus 로고
    • Mitochondrial redox signalling by p66Shc mediates ALS-like disease through Rac1 inactivation
    • Pesaresi MG, Amori I, Giorgi C, Ferri A, Fiorenzo P, Gabanella F et al. Mitochondrial redox signalling by p66Shc mediates ALS-like disease through Rac1 inactivation. Hum Mol Genet 2011; 20: 4196-4208.
    • (2011) Hum Mol Genet , vol.20 , pp. 4196-4208
    • Pesaresi, M.G.1    Amori, I.2    Giorgi, C.3    Ferri, A.4    Fiorenzo, P.5    Gabanella, F.6
  • 38
    • 0033844835 scopus 로고    scopus 로고
    • Sequential treatment of SH-SY5Y cells with retinoic acid and brain-derived neurotrophic factor gives rise to fully differentiated, neurotrophic factor-dependent, human neuron-like cells
    • Encinas M, Iglesias M, Liu Y, Wang H, Muhaisen A, Ceña V et al. Sequential treatment of SH-SY5Y cells with retinoic acid and brain-derived neurotrophic factor gives rise to fully differentiated, neurotrophic factor-dependent, human neuron-like cells. J Neurochem 2000; 75: 991-1003.
    • (2000) J Neurochem , vol.75 , pp. 991-1003
    • Encinas, M.1    Iglesias, M.2    Liu, Y.3    Wang, H.4    Muhaisen, A.5    Ceña, V.6
  • 40
    • 0030060941 scopus 로고    scopus 로고
    • Molecular cloning of caveolin-3, a novel member of the caveolin gene family expressed predominantly in muscle
    • Tang Z, Scherer PE, Okamoto T, Song K, Chu C, Kohtz DS et al. Molecular cloning of caveolin-3, a novel member of the caveolin gene family expressed predominantly in muscle. J Biol Chem 1996; 271: 2255-2261.
    • (1996) J Biol Chem , vol.271 , pp. 2255-2261
    • Tang, Z.1    Scherer, P.E.2    Okamoto, T.3    Song, K.4    Chu, C.5    Kohtz, D.S.6


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