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Volumn 136, Issue 3, 2013, Pages 926-943

Co-induction of the heat shock response ameliorates disease progression in a mouse model of human spinal and bulbar muscular atrophy: Implications for therapy

Author keywords

heat shock protein; motor neuron disease; neuroprotective agents; polyglutamine expansions; protein aggregation

Indexed keywords

ANDROGEN RECEPTOR; ARIMOCLOMOL; COPPER ZINC SUPEROXIDE DISMUTASE; DRINKING WATER; HEAT SHOCK PROTEIN; VASCULOTROPIN;

EID: 84874901074     PISSN: 00068950     EISSN: 14602156     Source Type: Journal    
DOI: 10.1093/brain/aws343     Document Type: Article
Times cited : (53)

References (87)
  • 1
    • 0035862754 scopus 로고    scopus 로고
    • Expression of expanded repeat androgen receptor produces neurologic disease in transgenic mice
    • Abel A, Walcott J, Woods J, Duda J, Merry DE. Expression of expanded repeat androgen receptor produces neurologic disease in transgenic mice. Hum Mol Genet 2001; 10: 107-16.
    • (2001) Hum Mol Genet , vol.10 , pp. 107-116
    • Abel, A.1    Walcott, J.2    Woods, J.3    Duda, J.4    Merry, D.E.5
  • 2
    • 18344399938 scopus 로고    scopus 로고
    • Transgenic mice with an expanded CAG repeat controlled by the human AR promoter show polyglutamine nuclear inclusions and neuronal dysfunction without neuronal cell death
    • Adachi H, Kume A, Li M, Nakagomi Y, Niwa H, Do J, et al. Transgenic mice with an expanded CAG repeat controlled by the human AR promoter show polyglutamine nuclear inclusions and neuronal dysfunction without neuronal cell death. Hum Mol Genet 2001; 10: 1039-48.
    • (2001) Hum Mol Genet , vol.10 , pp. 1039-1048
    • Adachi, H.1    Kume, A.2    Li, M.3    Nakagomi, Y.4    Niwa, H.5    Do, J.6
  • 3
    • 0037444446 scopus 로고    scopus 로고
    • Heat shock protein 70 chaperone overexpression ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model by reducing nuclear-localized mutant androgen receptor protein
    • Adachi H, Katsuno M, Minamiyama M, Sang C, Pagoulatos G, Angelidis C, et al. Heat shock protein 70 chaperone overexpression ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model by reducing nuclear-localized mutant androgen receptor protein. J Neurosci 2003; 23: 2203-11.
    • (2003) J Neurosci , vol.23 , pp. 2203-2211
    • Adachi, H.1    Katsuno, M.2    Minamiyama, M.3    Sang, C.4    Pagoulatos, G.5    Angelidis, C.6
  • 4
    • 20144362557 scopus 로고    scopus 로고
    • Widespread nuclear and cytoplasmic accumulation of mutant androgen receptor in SBMA patients
    • Adachi H, Katsuno M, Minamiyama M, Waza M, Sang C, Nakagomi Y, et al. Widespread nuclear and cytoplasmic accumulation of mutant androgen receptor in SBMA patients. Brain 2005; 128: 659-70.
    • (2005) Brain , vol.128 , pp. 659-670
    • Adachi, H.1    Katsuno, M.2    Minamiyama, M.3    Waza, M.4    Sang, C.5    Nakagomi, Y.6
  • 5
    • 34248327285 scopus 로고    scopus 로고
    • CHIP overexpression reduces mutant androgen receptor protein and ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model
    • Adachi H, Waza M, Tokui K, Katsuno M, Minamiyama M, Tanaka F, et al. CHIP overexpression reduces mutant androgen receptor protein and ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model. J Neurosci 2007; 27: 5115-26.
    • (2007) J Neurosci , vol.27 , pp. 5115-5126
    • Adachi, H.1    Waza, M.2    Tokui, K.3    Katsuno, M.4    Minamiyama, M.5    Tanaka, F.6
  • 6
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate M, Mitra S, Schweitzer ES, Segal MR, Finkbeiner S. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 2004; 431: 805-10.
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 7
  • 8
    • 0036501074 scopus 로고    scopus 로고
    • Molecular chaperones enhance the degradation of expanded polyglutamine repeat androgen receptor in a cellular model of spinal and bulbar muscular atrophy
    • Bailey CK, Andriola IF, Kampinga HH, Merry DE. Molecular chaperones enhance the degradation of expanded polyglutamine repeat androgen receptor in a cellular model of spinal and bulbar muscular atrophy. Hum Mol Genet 2002; 11: 515-23.
    • (2002) Hum Mol Genet , vol.11 , pp. 515-523
    • Bailey, C.K.1    Andriola, I.F.2    Kampinga, H.H.3    Merry, D.E.4
  • 9
    • 23044441106 scopus 로고    scopus 로고
    • Phase i pharmacokinetic and pharmacodynamic study of 17-allylamino, 17-demethoxygeldanamycin in patients with advanced malignancies
    • Banerji U, O'Donnell A, Scurr M, Pacey S, Stapleton S, Asad Y, et al. Phase I pharmacokinetic and pharmacodynamic study of 17-allylamino, 17-demethoxygeldanamycin in patients with advanced malignancies. J Clin Oncol 2005; 23: 4152-61.
    • (2005) J Clin Oncol , vol.23 , pp. 4152-4161
    • Banerji, U.1    O'Donnell, A.2    Scurr, M.3    Pacey, S.4    Stapleton, S.5    Asad, Y.6
  • 10
    • 63449093208 scopus 로고    scopus 로고
    • Neuropathology and therapeutic intervention in spinal and bulbar muscular atrophy
    • Banno H, Katsuno M, Suzuki K, Tanaka F, Sobue G. Neuropathology and therapeutic intervention in spinal and bulbar muscular atrophy. Int J Mol Sci 2009; 10: 1000-12.
    • (2009) Int J Mol Sci , vol.10 , pp. 1000-1012
    • Banno, H.1    Katsuno, M.2    Suzuki, K.3    Tanaka, F.4    Sobue, G.5
  • 11
    • 66049162280 scopus 로고    scopus 로고
    • Induction of overexpression of the 27-and 70-kDa heat shock proteins by bicyclol attenuates concanavalin A-induced liver injury through suppression of nuclear factor-kappaB in mice
    • Bao XQ, Liu GT. Induction of overexpression of the 27-and 70-kDa heat shock proteins by bicyclol attenuates concanavalin A-induced liver injury through suppression of nuclear factor-kappaB in mice. Mol Pharmacol 2009; 75: 1180-88.
    • (2009) Mol Pharmacol , vol.75 , pp. 1180-1188
    • Bao, X.Q.1    Liu, G.T.2
  • 12
    • 33845683331 scopus 로고    scopus 로고
    • Increasing cannabinoid levels by pharmacological and genetic manipulation delay disease progression in SOD1 mice
    • Bilsland LG, Dick JR, Pryce G, Petrosino S, Di Marzo V, Baker D, et al. Increasing cannabinoid levels by pharmacological and genetic manipulation delay disease progression in SOD1 mice. FASEB J 2006; 20: 1003-5.
    • (2006) FASEB J , vol.20 , pp. 1003-1005
    • Bilsland, L.G.1    Dick, J.R.2    Pryce, G.3    Petrosino, S.4    Di Marzo, V.5    Baker, D.6
  • 13
    • 14644419638 scopus 로고    scopus 로고
    • Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitinproteasome system impairment and inversely correlates with the degree of nuclear inclusion formation
    • Bowman AB, Yoo SY, Dantuma NP, Zoghbi HY. Neuronal dysfunction in a polyglutamine disease model occurs in the absence of ubiquitinproteasome system impairment and inversely correlates with the degree of nuclear inclusion formation. Hum Mol Genet 2005; 14: 679-91.
    • (2005) Hum Mol Genet , vol.14 , pp. 679-691
    • Bowman, A.B.1    Yoo, S.Y.2    Dantuma, N.P.3    Zoghbi, H.Y.4
  • 14
    • 44949250067 scopus 로고    scopus 로고
    • Natural history of spinal-bulbar muscular atrophy
    • Chahin N, Klein C, Mandrekar J, Sorenson E. Natural history of spinal-bulbar muscular atrophy. Neurology 2008; 70: 1967-71.
    • (2008) Neurology , vol.70 , pp. 1967-1971
    • Chahin, N.1    Klein, C.2    Mandrekar, J.3    Sorenson, E.4
  • 15
    • 2442719008 scopus 로고    scopus 로고
    • Castration restores function and neurofilament alterations of aged symptomatic males in a transgenic mouse model of spinal and bulbar muscular atrophy
    • Chevalier-Larsen ES, O'Brien CJ, Wang H, Jenkins SC, Holder L, Lieberman A, et al. Castration restores function and neurofilament alterations of aged symptomatic males in a transgenic mouse model of spinal and bulbar muscular atrophy. J Neurosci 2004; 24: 4778-86.
    • (2004) J Neurosci , vol.24 , pp. 4778-4786
    • Chevalier-Larsen, E.S.1    O'Brien, C.J.2    Wang, H.3    Jenkins, S.C.4    Holder, L.5    Lieberman, A.6
  • 16
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P, Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 1987; 162: 156-159.
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 17
    • 0038039288 scopus 로고    scopus 로고
    • Polyglutamine protein aggregation and toxicity are linked to the cellular stress response
    • Cowan KJ, Diamond MI, Welch WJ. Polyglutamine protein aggregation and toxicity are linked to the cellular stress response. Hum Mol Genet 2003; 12: 1377-91.
    • (2003) Hum Mol Genet , vol.12 , pp. 1377-1391
    • Cowan, K.J.1    Diamond, M.I.2    Welch, W.J.3
  • 18
    • 77955365630 scopus 로고    scopus 로고
    • The small heat shock protein B8 (HspB8) promotes autophagic removal of misfolded proteins involved in amyotrophic lateral sclerosis (ALS)
    • Crippa V, Sau D, Rusmini P, Boncoraglio A, Onesto E, Bolzoni E, et al. The small heat shock protein B8 (HspB8) promotes autophagic removal of misfolded proteins involved in amyotrophic lateral sclerosis (ALS). Hum Mol Genet 2010; 19: 3440-56.
    • (2010) Hum Mol Genet , vol.19 , pp. 3440-3456
    • Crippa, V.1    Sau, D.2    Rusmini, P.3    Boncoraglio, A.4    Onesto, E.5    Bolzoni, E.6
  • 19
    • 46249117510 scopus 로고    scopus 로고
    • Arimoclomol at dosages up to 300 mg/day is well tolerated and safe in amyotrophic lateral sclerosis
    • Cudkowicz ME, Shefner JM, Simpson E, Grasso D, Yu H, Zhang H, et al. Arimoclomol at dosages up to 300 mg/day is well tolerated and safe in amyotrophic lateral sclerosis. Muscle Nerve 2008; 38: 837-44.
    • (2008) Muscle Nerve , vol.38 , pp. 837-844
    • Cudkowicz, M.E.1    Shefner, J.M.2    Simpson, E.3    Grasso, D.4    Yu, H.5    Zhang, H.6
  • 20
    • 81255158083 scopus 로고    scopus 로고
    • Vascular endothelial growth factor ameliorates the ataxic phenotype in a mouse model of spinocerebellar ataxia type 1
    • Cvetanovic M, Patel JM, Marti HH, Kini AR, Opal P. Vascular endothelial growth factor ameliorates the ataxic phenotype in a mouse model of spinocerebellar ataxia type 1. Nat Med 2011; 17: 1445-47.
    • (2011) Nat Med , vol.17 , pp. 1445-1447
    • Cvetanovic, M.1    Patel, J.M.2    Marti, H.H.3    Kini, A.R.4    Opal, P.5
  • 22
    • 0035504919 scopus 로고    scopus 로고
    • Polyglutamine expansion neurodegenerative disease
    • Fischbeck KH. Polyglutamine expansion neurodegenerative disease. Brain Res Bull 2001; 56: 161-3.
    • (2001) Brain Res Bull , vol.56 , pp. 161-163
    • Fischbeck, K.H.1
  • 23
    • 54449101793 scopus 로고    scopus 로고
    • Heat shock transcription factor 1-activating compounds suppress polyglutamine-induced neurodegeneration through induction of multiple molecular chaperones
    • Fujikake N, Nagai Y, Popiel HA, Okamoto Y, Yamaguchi M, Toda T. Heat shock transcription factor 1-activating compounds suppress polyglutamine-induced neurodegeneration through induction of multiple molecular chaperones. J Biol Chem 2008; 283: 26188-97.
    • (2008) J Biol Chem , vol.283 , pp. 26188-26197
    • Fujikake, N.1    Nagai, Y.2    Popiel, H.A.3    Okamoto, Y.4    Yamaguchi, M.5    Toda, T.6
  • 24
    • 0030746053 scopus 로고    scopus 로고
    • Hsp70 prevents activation of stress kinases. A novel pathway of cellular thermotolerance
    • Gabai VL, Meriin AB, Mosser DD, Caron AW, Rits S, Shifrin VI, et al. Hsp70 prevents activation of stress kinases. A novel pathway of cellular thermotolerance. J Biol Chem 1997; 272: 18033-7.
    • (1997) J Biol Chem , vol.272 , pp. 18033-18037
    • Gabai, V.L.1    Meriin, A.B.2    Mosser, D.D.3    Caron, A.W.4    Rits, S.5    Shifrin, V.I.6
  • 25
    • 25844487226 scopus 로고    scopus 로고
    • Diseases of unstable repeat expansion: Mechanisms and common principles
    • Gatchel JR, Zoghbi HY. Diseases of unstable repeat expansion: mechanisms and common principles. Nat Rev Genet 2005; 6: 743-55.
    • (2005) Nat Rev Genet , vol.6 , pp. 743-755
    • Gatchel, J.R.1    Zoghbi, H.Y.2
  • 26
    • 77956184558 scopus 로고    scopus 로고
    • Neurotoxic protein oligomerisation associated with polyglutamine diseases
    • Hands SL, Wyttenbach A. Neurotoxic protein oligomerisation associated with polyglutamine diseases. Acta Neuropathol 2010; 120: 419-37.
    • (2010) Acta Neuropathol , vol.120 , pp. 419-437
    • Hands, S.L.1    Wyttenbach, A.2
  • 27
    • 0042170384 scopus 로고    scopus 로고
    • Bimoclomol, a heat shock protein co-inducer, acts by the prolonged activation of heat shock factor-1
    • Hargitai J, Lewis H, Boros I, Rá cz T, Fiser A, Kurucz I, et al. Bimoclomol, a heat shock protein co-inducer, acts by the prolonged activation of heat shock factor-1. Biochem Biophys Res Commun 2003; 307: 689-95.
    • (2003) Biochem Biophys Res Commun , vol.307 , pp. 689-695
    • Hargitai, J.1    Lewis, H.2    Boros, I.3    Rá Cz, T.4    Fiser, A.5    Kurucz, I.6
  • 28
    • 0035002568 scopus 로고    scopus 로고
    • Role of chaperones in nuclear translocation and transactivation of steroid receptors
    • Heinlein CA, Chang C. Role of chaperones in nuclear translocation and transactivation of steroid receptors. Endocrine 2001; 14: 143-9.
    • (2001) Endocrine , vol.14 , pp. 143-149
    • Heinlein, C.A.1    Chang, C.2
  • 29
    • 58249088475 scopus 로고    scopus 로고
    • Transcriptional upregulation of HSP70-2 by HIF-1 in cancer cells in response to hypoxia
    • Huang WJ, Xia LM, Zhu F, Huang B, Zhou C, Zhu HF, et al. Transcriptional upregulation of HSP70-2 by HIF-1 in cancer cells in response to hypoxia. Int J Cancer 2009; 124: 298-305.
    • (2009) Int J Cancer , vol.124 , pp. 298-305
    • Huang, W.J.1    Xia, L.M.2    Zhu, F.3    Huang, B.4    Zhou, C.5    Zhu, H.F.6
  • 30
    • 0037119415 scopus 로고    scopus 로고
    • Hsp90 regulates a von Hippel Lindau-independent hypoxiainducible factor-1 alpha-degradative pathway
    • Isaacs JS, Jung YJ, Mimnaugh EG, Martinez A, Cuttitta F, Neckers LM. Hsp90 regulates a von Hippel Lindau-independent hypoxiainducible factor-1 alpha-degradative pathway. J Biol Chem 2002; 277: 29936-44.
    • (2002) J Biol Chem , vol.277 , pp. 29936-29944
    • Isaacs, J.S.1    Jung, Y.J.2    Mimnaugh, E.G.3    Martinez, A.4    Cuttitta, F.5    Neckers, L.M.6
  • 31
    • 53149114499 scopus 로고    scopus 로고
    • Late stage treatment with arimoclomol delays disease progression and prevents protein aggregation in the SOD1 mouse model of ALS
    • Kalmar B, Novoselov S, Gray A, Cheetham ME, Margulis B, Greensmith L. Late stage treatment with arimoclomol delays disease progression and prevents protein aggregation in the SOD1 mouse model of ALS. J Neurochem 2008; 107: 339-50.
    • (2008) J Neurochem , vol.107 , pp. 339-350
    • Kalmar, B.1    Novoselov, S.2    Gray, A.3    Cheetham, M.E.4    Margulis, B.5    Greensmith, L.6
  • 32
    • 18644379256 scopus 로고    scopus 로고
    • Testosterone reduction prevents phenotypic expression in a transgenic mouse model of spinal and bulbar muscular atrophy
    • Katsuno M, Adachi H, Kume A, Li M, Nakagomi Y, Niwa H, et al. Testosterone reduction prevents phenotypic expression in a transgenic mouse model of spinal and bulbar muscular atrophy. Neuron 2002; 35: 843-54.
    • (2002) Neuron , vol.35 , pp. 843-854
    • Katsuno, M.1    Adachi, H.2    Kume, A.3    Li, M.4    Nakagomi, Y.5    Niwa, H.6
  • 33
    • 2542483769 scopus 로고    scopus 로고
    • Spinal and bulbar muscular atrophy: Ligand-dependent pathogenesis and therapeutic perspectives
    • Katsuno M, Adachi H, Tanaka F, Sobue G. Spinal and bulbar muscular atrophy: ligand-dependent pathogenesis and therapeutic perspectives. J Mol Med 2004; 82: 298-307.
    • (2004) J Mol Med , vol.82 , pp. 298-307
    • Katsuno, M.1    Adachi, H.2    Tanaka, F.3    Sobue, G.4
  • 34
    • 28044469532 scopus 로고    scopus 로고
    • Pharmacological induction of heat-shock proteins alleviates polyglutamine-mediated motor neuron disease
    • Katsuno M, Sang C, Adachi H, Minamiyama M, Waza M, Tanaka F, et al. Pharmacological induction of heat-shock proteins alleviates polyglutamine- mediated motor neuron disease. Proc Natl Acad Sci U S A 2005; 102: 16801-6.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 16801-16806
    • Katsuno, M.1    Sang, C.2    Adachi, H.3    Minamiyama, M.4    Waza, M.5    Tanaka, F.6
  • 35
    • 33751339785 scopus 로고    scopus 로고
    • Reversible disruption of dynactin 1-mediated retrograde axonaltransport in polyglutamine-induced motor neuron degeneration
    • Katsuno M, Adachi H, Minamiyama M, Waza M, Tokui K, Banno H, et al. Reversible disruption of dynactin 1-mediated retrograde axonaltransport in polyglutamine-induced motor neuron degeneration. J Neurosci 2006; 26: 12106-17.
    • (2006) J Neurosci , vol.26 , pp. 12106-12117
    • Katsuno, M.1    Adachi, H.2    Minamiyama, M.3    Waza, M.4    Tokui, K.5    Banno, H.6
  • 36
    • 77951520909 scopus 로고    scopus 로고
    • Disrupted transforming growth factor-beta signaling in spinal and bulbar muscular atrophy
    • Katsuno M, Adachi H, Minamiyama M, Waza M, Doi H, Kondo N, et al. Disrupted transforming growth factor-beta signaling in spinal and bulbar muscular atrophy. J Neurosci 2010a; 30: 5702-12.
    • J Neurosci 2010a , vol.30 , pp. 5702-5712
    • Katsuno, M.1    Adachi, H.2    Minamiyama, M.3    Waza, M.4    Doi, H.5    Kondo, N.6
  • 37
    • 77955662063 scopus 로고    scopus 로고
    • Efficacy and safety of leuprorelin in patients with spinal and bulbar muscular atrophy (JASMITT Study): A multicentre randomised double-blind placebo-controlled trial
    • Katsuno M, Banno H, Suzuki K, Takeuchi Y, Kawashima M, Yabe I, et al. Efficacy and safety of leuprorelin in patients with spinal and bulbar muscular atrophy (JASMITT study): a multicentre, randomised, double-blind, placebo-controlled trial. Lancet Neurol 2010b; 9: 875-84.
    • (2010) Lancet Neurol , vol.9 , pp. 875-884
    • Katsuno, M.1    Banno, H.2    Suzuki, K.3    Takeuchi, Y.4    Kawashima, M.5    Yabe, I.6
  • 38
    • 1942486792 scopus 로고    scopus 로고
    • Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice
    • Kieran D, Kalmar B, Dick JR, Riddoch-Contreras J, Burnstock G, Greensmith L. Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice. Nat Med 2004; 10: 402-5.
    • (2004) Nat Med , vol.10 , pp. 402-405
    • Kieran, D.1    Kalmar, B.2    Dick, J.R.3    Riddoch-Contreras, J.4    Burnstock, G.5    Greensmith, L.6
  • 39
    • 0034708793 scopus 로고    scopus 로고
    • Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract
    • Kobayashi Y, Kume A, Li M, Doyu M, Hata M, Ohtsuka K, et al. Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract. J Biol Chem 2000; 275: 8772-8.
    • (2000) J Biol Chem , vol.275 , pp. 8772-8778
    • Kobayashi, Y.1    Kume, A.2    Li, M.3    Doyu, M.4    Hata, M.5    Ohtsuka, K.6
  • 40
    • 0025800526 scopus 로고
    • Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy
    • La Spada AR, Wilson EM, Lubahn DB, Harding AE, Fischbeck KH. Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy. Nature 1991; 352: 77-9.
    • (1991) Nature , vol.352 , pp. 77-79
    • La Spada, A.R.1    Wilson, E.M.2    Lubahn, D.B.3    Harding, A.E.4    Fischbeck, K.H.5
  • 41
    • 79961013560 scopus 로고    scopus 로고
    • Altered chromatin architecture underlies progressive impairment of the heat shock response in mouse models of Huntington disease
    • Labbadia J, Cunliffe H, Weiss A, Katsyuba E, Sathasivam K, Seredenina T, et al. Altered chromatin architecture underlies progressive impairment of the heat shock response in mouse models of Huntington disease. J Clin Invest 2011; 121: 3306-19.
    • (2011) J Clin Invest , vol.121 , pp. 3306-3319
    • Labbadia, J.1    Cunliffe, H.2    Weiss, A.3    Katsyuba, E.4    Sathasivam, K.5    Seredenina, T.6
  • 42
    • 0041903805 scopus 로고    scopus 로고
    • VEGF is a modifier of amyotrophic lateral sclerosis in mice and humans and protects motoneurons against ischemic death
    • Lambrechts D, Storkebaum E, Morimoto M, Del-Favero J, Desmet F, Marklund SL, et al. VEGF is a modifier of amyotrophic lateral sclerosis in mice and humans and protects motoneurons against ischemic death. Nat Genet 2003; 34: 383-94.
    • (2003) Nat Genet , vol.34 , pp. 383-394
    • Lambrechts, D.1    Storkebaum, E.2    Morimoto, M.3    Del-Favero, J.4    Desmet, F.5    Marklund, S.L.6
  • 44
    • 34047269594 scopus 로고    scopus 로고
    • Soluble androgen receptor oligomers underlie pathology in a mouse model of spinobulbar muscular atrophy
    • Li M, Chevalier-Larsen ES, Merry DE, Diamond MI. Soluble androgen receptor oligomers underlie pathology in a mouse model of spinobulbar muscular atrophy. J Biol Chem 2007; 282: 3157-64.
    • (2007) J Biol Chem , vol.282 , pp. 3157-3164
    • Li, M.1    Chevalier-Larsen, E.S.2    Merry, D.E.3    Diamond, M.I.4
  • 45
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • Livak KJ, Schmittgen TD. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 2001; 25: 402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 46
    • 41849118025 scopus 로고    scopus 로고
    • Loss of neuronal cell cycle control as a mechanism of neurodegeneration in the presenilin-1 Alzheimer's disease brain
    • Malik B, Currais A, Andres A, Towlson C, Pitsi D, Nunes A, et al. Loss of neuronal cell cycle control as a mechanism of neurodegeneration in the presenilin-1 Alzheimer's disease brain. Cell Cycle 2008a; 7: 637-46.
    • (2008) Cell Cycle , vol.7 , pp. 637-646
    • Malik, B.1    Currais, A.2    Andres, A.3    Towlson, C.4    Pitsi, D.5    Nunes, A.6
  • 47
    • 51649101133 scopus 로고    scopus 로고
    • Cell cycle-driven neuronal apoptosis specifically linked to amyloid peptide Abeta1-42 exposure is not exacerbated in a mouse model of presenilin-1 familial Alzheimer's disease
    • Malik B, Currais A, Soriano S. Cell cycle-driven neuronal apoptosis specifically linked to amyloid peptide Abeta1-42 exposure is not exacerbated in a mouse model of presenilin-1 familial Alzheimer's disease. J Neurochem 2008b; 106: 912-6.
    • (2008) J Neurochem , vol.106 , pp. 912-916
    • Malik, B.1    Currais, A.2    Soriano, S.3
  • 49
    • 84864251377 scopus 로고    scopus 로고
    • Oligomeric amyloid-beta peptide affects the expression of genes involved in steroid and lipid metabolism in primary neurons
    • Malik B, Fernandes C, Killick R, Wroe R, Usardi A, Williamson R, et al. Oligomeric amyloid-beta peptide affects the expression of genes involved in steroid and lipid metabolism in primary neurons. Neurochem Int 2012; 61: 321-33.
    • (2012) Neurochem Int , vol.61 , pp. 321-333
    • Malik, B.1    Fernandes, C.2    Killick, R.3    Wroe, R.4    Usardi, A.5    Williamson, R.6
  • 50
    • 70249105784 scopus 로고    scopus 로고
    • Heat-shock pretreatment inhibits sorbitol-induced apoptosis in K562, U937 and HeLa cells
    • Marfe G, Pucci B, De ML, Fiorito F, Di Stefano C, Indelicato M, et al. Heat-shock pretreatment inhibits sorbitol-induced apoptosis in K562, U937 and HeLa cells. Int J Cancer 2009; 125: 2077-85.
    • (2009) Int J Cancer , vol.125 , pp. 2077-2085
    • Marfe, G.1    Pucci, B.2    De Ml Fiorito, F.3    Di Stefano, C.4    Indelicato, M.5
  • 51
    • 65549163327 scopus 로고    scopus 로고
    • Cytoplasmic retention of polyglutamine-expanded androgen receptor ameliorates disease via autophagy in a mouse model of spinal and bulbar muscular atrophy
    • Montie HL, Cho MS, Holder L, Liu Y, Tsvetkov AS, Finkbeiner S, et al. Cytoplasmic retention of polyglutamine-expanded androgen receptor ameliorates disease via autophagy in a mouse model of spinal and bulbar muscular atrophy. Hum Mol Genet 2009; 18: 1937-50.
    • (2009) Hum Mol Genet , vol.18 , pp. 1937-1950
    • Montie, H.L.1    Cho, M.S.2    Holder, L.3    Liu, Y.4    Tsvetkov, A.S.5    Finkbeiner, S.6
  • 52
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • Muchowski PJ, Wacker JL. Modulation of neurodegeneration by molecular chaperones. Nat Rev Neurosci 2005; 6: 11-22.
    • (2005) Nat Rev Neurosci , vol.6 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 53
    • 33751092252 scopus 로고    scopus 로고
    • Genome-wide analysis of human HSF1 signaling reveals a transcriptional program linked to cellular adaptation and survival
    • Page TJ, Sikder D, Yang L, Pluta L, Wolfinger RD, Kodadek T, et al. Genome-wide analysis of human HSF1 signaling reveals a transcriptional program linked to cellular adaptation and survival. Mol Biosyst 2006; 2: 627-39.
    • (2006) Mol Biosyst , vol.2 , pp. 627-639
    • Page, T.J.1    Sikder, D.2    Yang, L.3    Pluta, L.4    Wolfinger, R.D.5    Kodadek, T.6
  • 54
    • 0028283985 scopus 로고
    • Glutamine repeats as polar zippers: Their possible role in inherited neurodegenerative diseases
    • Perutz MF, Johnson T, Suzuki M, Finch JT. Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc Natl Acad Sci U S A 1994; 91: 5355-8.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 5355-5358
    • Perutz, M.F.1    Johnson, T.2    Suzuki, M.3    Finch, J.T.4
  • 55
    • 0031895351 scopus 로고    scopus 로고
    • The hsp90-based chaperone system: Involvement in signal transduction from a variety of hormone and growth factor receptors
    • Pratt WB. The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors. Proc Soc Exp Biol Med 1998; 217: 420-34.
    • (1998) Proc Soc Exp Biol Med , vol.217 , pp. 420-434
    • Pratt, W.B.1
  • 56
    • 21144432950 scopus 로고    scopus 로고
    • The heat shock protein 90 inhibitor, 17-allylamino-17- demethoxygeldanamycin, enhances osteoclast formation and potentiates bone metastasis of a human breast cancer cell line
    • Price JT, Quinn JM, Sims NA, Vieusseux J, Waldeck K, Docherty SE, et al. The heat shock protein 90 inhibitor, 17-allylamino-17-demethoxygeldanamycin, enhances osteoclast formation and potentiates bone metastasis of a human breast cancer cell line. Cancer Res 2005; 65: 4929-38.
    • (2005) Cancer Res , vol.65 , pp. 4929-4938
    • Price, J.T.1    Quinn, J.M.2    Sims, N.A.3    Vieusseux, J.4    Waldeck, K.5    Docherty, S.E.6
  • 57
    • 78649473387 scopus 로고    scopus 로고
    • An examination of wild-type SOD1 in modulating the toxicity and aggregation of ALS-associated mutant SOD1
    • Prudencio M, Durazo A, Whitelegge JP, Borchelt DR. An examination of wild-type SOD1 in modulating the toxicity and aggregation of ALS-associated mutant SOD1. Hum Mol Genet 2010; 19: 4774-89.
    • (2010) Hum Mol Genet , vol.19 , pp. 4774-4789
    • Prudencio, M.1    Durazo, A.2    Whitelegge, J.P.3    Borchelt, D.R.4
  • 58
    • 78651071860 scopus 로고    scopus 로고
    • Mortalin overexpression attenuates beta-amyloid-induced neurotoxicity in SH-SY5Y cells
    • Qu M, Zhou Z, Xu S, Chen C, Yu Z, Wang D. Mortalin overexpression attenuates beta-amyloid-induced neurotoxicity in SH-SY5Y cells. Brain Res 2011; 1368: 336-45.
    • (2011) Brain Res , vol.1368 , pp. 336-345
    • Qu, M.1    Zhou, Z.2    Xu, S.3    Chen, C.4    Yu, Z.5    Wang, D.6
  • 59
    • 77958150581 scopus 로고    scopus 로고
    • Therapeutic approaches to spinal and bulbar muscular atrophy
    • Ranganathan S, Fischbeck KH. Therapeutic approaches to spinal and bulbar muscular atrophy. Trends Pharmacol Sci 2010; 31: 523-27.
    • (2010) Trends Pharmacol Sci , vol.31 , pp. 523-527
    • Ranganathan, S.1    Fischbeck, K.H.2
  • 61
    • 0037194897 scopus 로고    scopus 로고
    • Polyglutamine pathogenesis: Emergence of unifying mechanisms for Huntington's disease and related disorders
    • Ross CA. Polyglutamine pathogenesis: emergence of unifying mechanisms for Huntington's disease and related disorders. Neuron 2002; 35: 819-22.
    • (2002) Neuron , vol.35 , pp. 819-822
    • Ross, C.A.1
  • 62
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross CA, Poirier MA. Protein aggregation and neurodegenerative disease. Nat Med 2004; 10 (Suppl): S10-17.
    • (2004) Nat Med , vol.10 , Issue.SUPPL.
    • Ross, C.A.1    Poirier, M.A.2
  • 63
    • 27644596641 scopus 로고    scopus 로고
    • Opinion: What is the role of protein aggregation in neurodegeneration?
    • Ross CA, Poirier MA. Opinion: What is the role of protein aggregation in neurodegeneration? Nat Rev Mol Cell Biol 2005; 6: 891-8.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 891-898
    • Ross, C.A.1    Poirier, M.A.2
  • 64
    • 33646384157 scopus 로고    scopus 로고
    • Distinct hsp70 domains mediate apoptosis-inducing factor release and nuclear accumulation
    • Ruchalski K, Mao H, Li Z, Wang Z, Gillers S, Wang Y, et al. Distinct hsp70 domains mediate apoptosis-inducing factor release and nuclear accumulation. J Biol Chem 2006; 281: 7873-80.
    • (2006) J Biol Chem , vol.281 , pp. 7873-7880
    • Ruchalski, K.1    Mao, H.2    Li, Z.3    Wang, Z.4    Gillers, S.5    Wang, Y.6
  • 65
    • 78349309239 scopus 로고    scopus 로고
    • 17-AAG increases autophagic removal of mutant androgen receptor in spinal and bulbar muscular atrophy
    • Rusmini P, Simonini F, Crippa V, Bolzoni E, Onesto E, Cagnin M, et al. 17-AAG increases autophagic removal of mutant androgen receptor in spinal and bulbar muscular atrophy. Neurobiol Dis 2011; 41: 83-95.
    • (2011) Neurobiol Dis , vol.41 , pp. 83-95
    • Rusmini, P.1    Simonini, F.2    Crippa, V.3    Bolzoni, E.4    Onesto, E.5    Cagnin, M.6
  • 66
    • 11844267193 scopus 로고    scopus 로고
    • The effect of peripheral nerve injury on disease progression in the SOD1(G93A) mouse model of amyotrophic lateral sclerosis
    • Sharp PS, Dick JR, Greensmith L. The effect of peripheral nerve injury on disease progression in the SOD1(G93A) mouse model of amyotrophic lateral sclerosis. Neuroscience 2005; 130: 897-910.
    • (2005) Neuroscience , vol.130 , pp. 897-910
    • Sharp, P.S.1    Dick, J.R.2    Greensmith, L.3
  • 67
    • 0034098057 scopus 로고    scopus 로고
    • Motoneuronal cell death is not correlated with aggregate formation of androgen receptors containing an elongated polyglutamine tract
    • Simeoni S, Mancini MA, Stenoien DL, Marcelli M, Weigel NL, Zanisi M, et al. Motoneuronal cell death is not correlated with aggregate formation of androgen receptors containing an elongated polyglutamine tract. Hum Mol Genet 2000; 9: 133-44.
    • (2000) Hum Mol Genet , vol.9 , pp. 133-144
    • Simeoni, S.1    Mancini, M.A.2    Stenoien, D.L.3    Marcelli, M.4    Weigel, N.L.5    Zanisi, M.6
  • 68
    • 12144286872 scopus 로고    scopus 로고
    • Androgen receptor YAC transgenic mice recapitulate SBMA motor neuronopathy and implicate VEGF164 in the motor neuron degeneration
    • Sopher BL, Thomas PS Jr, LaFevre-Bernt MA, Holm IE, Wilke SA, Ware CB, et al. Androgen receptor YAC transgenic mice recapitulate SBMA motor neuronopathy and implicate VEGF164 in the motor neuron degeneration. Neuron 2004; 41: 687-99.
    • (2004) Neuron , vol.41 , pp. 687-699
    • Sopher, B.L.1    Thomas Jr., P.S.2    Lafevre-Bernt, M.A.3    Holm, I.E.4    Wilke, S.A.5    Ware, C.B.6
  • 69
    • 0032945938 scopus 로고    scopus 로고
    • Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone
    • Stenoien DL, Cummings CJ, Adams HP, Mancini MG, Patel K, DeMartino GN, et al. Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone. Hum Mol Genet 1999; 8: 731-41.
    • (1999) Hum Mol Genet , vol.8 , pp. 731-741
    • Stenoien, D.L.1    Cummings, C.J.2    Adams, H.P.3    Mancini, M.G.4    Patel, K.5    Demartino, G.N.6
  • 71
    • 37549036991 scopus 로고    scopus 로고
    • CAG repeat size correlates to electrophysiological motor and sensory phenotypes in SBMA
    • Suzuki K, Katsuno M, Banno H, Takeuchi Y, Atsuta N, Ito M, et al. CAG repeat size correlates to electrophysiological motor and sensory phenotypes in SBMA. Brain 2008; 131: 229-39.
    • (2008) Brain , vol.131 , pp. 229-239
    • Suzuki, K.1    Katsuno, M.2    Banno, H.3    Takeuchi, Y.4    Atsuta, N.5    Ito, M.6
  • 72
    • 38349158062 scopus 로고    scopus 로고
    • Soluble polyglutamine oligomers formed prior to inclusion body formation are cytotoxic
    • Takahashi T, Kikuchi S, Katada S, Nagai Y, Nishizawa M, Onodera O. Soluble polyglutamine oligomers formed prior to inclusion body formation are cytotoxic. Hum Mol Genet 2008; 17: 345-56.
    • (2008) Hum Mol Genet , vol.17 , pp. 345-356
    • Takahashi, T.1    Kikuchi, S.2    Katada, S.3    Nagai, Y.4    Nishizawa, M.5    Onodera, O.6
  • 73
    • 0037194896 scopus 로고    scopus 로고
    • Androgen-dependent neurodegeneration by polyglutamineexpanded human androgen receptor in Drosophila
    • Takeyama K, Ito S, Yamamoto A, Tanimoto H, Furutani T, Kanuka H, et al. Androgen-dependent neurodegeneration by polyglutamineexpanded human androgen receptor in Drosophila. Neuron 2002; 35: 855-64.
    • (2002) Neuron , vol.35 , pp. 855-864
    • Takeyama, K.1    Ito, S.2    Yamamoto, A.3    Tanimoto, H.4    Furutani, T.5    Kanuka, H.6
  • 75
    • 33745592187 scopus 로고    scopus 로고
    • Loss of endogenous androgen receptor protein accelerates motor neuron degeneration and accentuates androgen insensitivity in a mouse model of X-linked spinal and bulbar muscular atrophy
    • Thomas PS Jr, Fraley GS, Damien V, Woodke LB, Zapata F, Sopher BL, et al. Loss of endogenous androgen receptor protein accelerates motor neuron degeneration and accentuates androgen insensitivity in a mouse model of X-linked spinal and bulbar muscular atrophy. Hum Mol Genet 2006; 15: 2225-38.
    • (2006) Hum Mol Genet , vol.15 , pp. 2225-2238
    • Thomas Jr., P.S.1    Fraley, G.S.2    Damien, V.3    Woodke, L.B.4    Zapata, F.5    Sopher, B.L.6
  • 76
    • 60549084901 scopus 로고    scopus 로고
    • 17-DMAG ameliorates polyglutamine-mediated motor neuron degeneration through well-preserved proteasome function in an SBMA model mouse
    • Tokui K, Adachi H, Waza M, Katsuno M, Minamiyama M, Doi H, et al. 17-DMAG ameliorates polyglutamine-mediated motor neuron degeneration through well-preserved proteasome function in an SBMA model mouse. Hum Mol Genet 2009; 18: 898-910.
    • (2009) Hum Mol Genet , vol.18 , pp. 898-910
    • Tokui, K.1    Adachi, H.2    Waza, M.3    Katsuno, M.4    Minamiyama, M.5    Doi, H.6
  • 77
    • 0037129827 scopus 로고    scopus 로고
    • Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes
    • RESEARCH0034
    • Vandesompele J, De PK, Pattyn F, Poppe B, Van Roy N, De Paepe A, et al. Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biol 2002; 3: RESEARCH0034.
    • (2002) Genome Biol , vol.3
    • Vandesompele, J.1    De Pk Pattyn, F.2    Poppe, B.3    Van Roy, N.4    De Paepe, A.5
  • 78
    • 20244367890 scopus 로고    scopus 로고
    • Bimoclomol: A nontoxic, hydroxylamine derivative with stress protein-inducing activity and cytoprotective effects
    • Vigh L, Literati PN, Horvath I, Török Z, Balogh G, Glatz A, et al. Bimoclomol: a nontoxic, hydroxylamine derivative with stress protein-inducing activity and cytoprotective effects. Nat Med 1997; 3: 1150-54.
    • (1997) Nat Med , vol.3 , pp. 1150-1154
    • Vigh, L.1    Literati, P.N.2    Horvath, I.3    Török, Z.4    Balogh, G.5    Glatz, A.6
  • 79
    • 0037184933 scopus 로고    scopus 로고
    • Ligand promotes intranuclear inclusions in a novel cell model of spinal and bulbar muscular atrophy
    • Walcott JL, Merry DE. Ligand promotes intranuclear inclusions in a novel cell model of spinal and bulbar muscular atrophy. J Biol Chem 2002; 277: 50855-9.
    • (2002) J Biol Chem , vol.277 , pp. 50855-50859
    • Walcott, J.L.1    Merry, D.E.2
  • 80
    • 0035664213 scopus 로고    scopus 로고
    • Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues
    • Watanabe M, Dykes-Hoberg M, Culotta VC, Price DL, Wong PC, Rothstein JD. Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues. Neurobiol Dis 2001; 8: 933-41.
    • (2001) Neurobiol Dis , vol.8 , pp. 933-941
    • Watanabe, M.1    Dykes-Hoberg, M.2    Culotta, V.C.3    Price, D.L.4    Wong, P.C.5    Rothstein, J.D.6
  • 81
    • 27144503120 scopus 로고    scopus 로고
    • 17-AAG, an Hsp90 inhibitor, ameliorates polyglutaminemediated motor neuron degeneration
    • Waza M, Adachi H, Katsuno M, Minamiyama M, Sang C, Tanaka F, et al. 17-AAG, an Hsp90 inhibitor, ameliorates polyglutaminemediated motor neuron degeneration. Nat Med 2005; 11: 1088-95.
    • (2005) Nat Med , vol.11 , pp. 1088-1095
    • Waza, M.1    Adachi, H.2    Katsuno, M.3    Minamiyama, M.4    Sang, C.5    Tanaka, F.6
  • 82
    • 52049093169 scopus 로고    scopus 로고
    • Polyglutamine neurodegeneration: Protein misfolding revisited
    • Williams AJ, Paulson HL. Polyglutamine neurodegeneration: protein misfolding revisited. Trends Neurosci 2008; 31: 521-8.
    • (2008) Trends Neurosci , vol.31 , pp. 521-528
    • Williams, A.J.1    Paulson, H.L.2
  • 84
    • 4344674075 scopus 로고    scopus 로고
    • Role of heat shock proteins during polyglutamine neurodegeneration: Mechanisms and hypothesis
    • Wyttenbach A. Role of heat shock proteins during polyglutamine neurodegeneration: mechanisms and hypothesis. J Mol Neurosci 2004; 23: 69-96.
    • (2004) J Mol Neurosci , vol.23 , pp. 69-96
    • Wyttenbach, A.1
  • 85
    • 77955053465 scopus 로고    scopus 로고
    • Hsp105 reduces the protein aggregation and cytotoxicity by expandedpolyglutamine proteins through the induction of Hsp70
    • Yamagishi N, Goto K, Nakagawa S, Saito Y, Hatayama T. Hsp105 reduces the protein aggregation and cytotoxicity by expandedpolyglutamine proteins through the induction of Hsp70. Exp Cell Res 2010; 316: 2424-33.
    • (2010) Exp Cell Res , vol.316 , pp. 2424-2433
    • Yamagishi, N.1    Goto, K.2    Nakagawa, S.3    Saito, Y.4    Hatayama, T.5
  • 86
    • 0037421691 scopus 로고    scopus 로고
    • SCA7 knockin mice model human SCA7 and reveal gradual accumulation of mutant ataxin-7 in neurons and abnormalities in short-term plasticity
    • Yoo SY, Pennesi ME, Weeber EJ, Xu B, Atkinson R, Chen S, et al. SCA7 knockin mice model human SCA7 and reveal gradual accumulation of mutant ataxin-7 in neurons and abnormalities in short-term plasticity. Neuron 2003; 37: 383-401.
    • (2003) Neuron , vol.37 , pp. 383-401
    • Yoo, S.Y.1    Pennesi, M.E.2    Weeber, E.J.3    Xu, B.4    Atkinson, R.5    Chen, S.6
  • 87
    • 33749442673 scopus 로고    scopus 로고
    • Androgen-dependent pathology demonstrates myopathic contribution to the Kennedy disease phenotype in a mouse knock-in model
    • Yu Z, Dadgar N, Albertelli M, Gruis K, Jordan C, Robins DM, et al. Androgen-dependent pathology demonstrates myopathic contribution to the Kennedy disease phenotype in a mouse knock-in model. J Clin Invest 2006; 116: 2663-72.
    • (2006) J Clin Invest , vol.116 , pp. 2663-2672
    • Yu, Z.1    Dadgar, N.2    Albertelli, M.3    Gruis, K.4    Jordan, C.5    Robins, D.M.6


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