메뉴 건너뛰기




Volumn 34, Issue 1, 2014, Pages 24-34

Geldanamycin attenuates 3-nitropropionic acid-induced apoptosis and JNK activation through the expression of HSP 70 in striatal cells

Author keywords

3 nitropropionic acid; Geldanamycin; Heat shock protein 70; Huntington's disease; Reactive oxygen species

Indexed keywords

3 NITROPROPIONIC ACID; GELDANAMYCIN; HEAT SHOCK PROTEIN 70; I KAPPA B ALPHA; LACTATE DEHYDROGENASE; REACTIVE OXYGEN METABOLITE; STRESS ACTIVATED PROTEIN KINASE; TRIPTOLIDE; 3-NITROPROPIONIC ACID; BENZOQUINONE DERIVATIVE; DITERPENE; EPOXIDE; MACROCYCLIC LACTAM; NITRO DERIVATIVE; PHENANTHRENE DERIVATIVE; PROPIONIC ACID DERIVATIVE;

EID: 84902675831     PISSN: 11073756     EISSN: 1791244X     Source Type: Journal    
DOI: 10.3892/ijmm.2014.1747     Document Type: Article
Times cited : (11)

References (56)
  • 3
    • 25444474703 scopus 로고    scopus 로고
    • Mitochondria take center stage in aging and neurodegeneration
    • Beal MF: Mitochondria take center stage in aging and neurodegeneration. Ann Neurol 58: 495-505, 2005.
    • (2005) Ann Neurol , vol.58 , pp. 495-505
    • Beal, M.F.1
  • 5
    • 0037088935 scopus 로고    scopus 로고
    • The mitochondrial toxin 3-nitropropionic acid induces striatal neurodegeneration via a c-Jun N-terminal kinase/c-Jun module
    • Garcia M, Vanhoutte P, Pages C, Besson MJ, Brouillet E and Caboche J: The mitochondrial toxin 3-nitropropionic acid induces striatal neurodegeneration via a c -Jun N -terminal kinase/c-Jun module. J Neurosci 22: 2174-2184, 2002. (Pubitemid 35386517)
    • (2002) Journal of Neuroscience , vol.22 , Issue.6 , pp. 2174-2184
    • Garcia, M.1    Vanhoutte, P.2    Pages, C.3    Besson, M.-J.4    Brouillet, E.5    Caboche, J.6
  • 6
    • 0032815680 scopus 로고    scopus 로고
    • Replicating Huntington's disease phenotype in experimental animals
    • DOI 10.1016/S0301-0082(99)00005-2, PII S0301008299000052
    • Brouillet E, Condé F, Beal MF and Hantraye P: Replicating Huntington's disease phenotype in experimental animals. Prog Neurobiol 59: 427-468, 1999. (Pubitemid 29392967)
    • (1999) Progress in Neurobiology , vol.59 , Issue.5 , pp. 427-468
    • Brouillet, E.1    Conde, F.2    Beal, M.F.3    Hantraye, P.4
  • 7
    • 84873055636 scopus 로고    scopus 로고
    • Heat shock transcription factor-1 suppresses apoptotic cell death and ROS generation in 3-nitropropionic acid-stimulated striatal cells
    • Choi YJ, Om JY, Kim NH, et al: Heat shock transcription factor-1 suppresses apoptotic cell death and ROS generation in 3-nitropropionic acid-stimulated striatal cells. Mol Cell Biochem 375: 59-67, 2013.
    • (2013) Mol Cell Biochem , vol.375 , pp. 59-67
    • Choi, Y.J.1    Om, J.Y.2    Kim, N.H.3
  • 8
    • 0036315706 scopus 로고    scopus 로고
    • Mice overexpressing 70-kDa heat shock protein show increased resistance to malonate and 3-nitropropionic acid
    • DOI 10.1006/exnr.2002.7933
    • Dedeoglu A, Ferrante RJ, Andreassen OA, Dillmann WH and Beal MF: Mice overexpressing 70-kDa heat shock protein show increased resistance to malonate and 3-nitropropionic acid. Exp Neurol 176: 262-265, 2002. (Pubitemid 34762127)
    • (2002) Experimental Neurology , vol.176 , Issue.1 , pp. 262-265
    • Dedeoglu, A.1    Ferrante, R.J.2    Andreassen, O.A.3    Dillmann, W.H.4    Beal M.Flint5
  • 9
    • 1642471825 scopus 로고    scopus 로고
    • Heat-shock proteins as regulators of apoptosis
    • DOI 10.1038/sj.onc.1207114, Apoptosis - Part 2
    • Takayama S, Reed JC and Homma S: Heat-shock proteins as regulators of apoptosis. Oncogene 22: 9041-9047, 2003. (Pubitemid 38121704)
    • (2003) Oncogene , vol.22 , Issue.56 REV. ISS. 8 , pp. 9041-9047
    • Takayama, S.1    Reed, J.C.2    Homma, S.3
  • 10
    • 0034253533 scopus 로고    scopus 로고
    • Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome
    • Beere HM, Wolf BB, Cain K, et al: Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome. Nat Cell Biol 2: 469-475, 2000.
    • (2000) Nat Cell Biol , vol.2 , pp. 469-475
    • Beere, H.M.1    Wolf, B.B.2    Cain, K.3
  • 11
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • DOI 10.1038/502
    • Cummings CJ, Mancini MA, Antalffy B, DeFranco DB, Orr HT and Zoghbi HY: Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nat Genet 19: 148-154, 1998. (Pubitemid 28248795)
    • (1998) Nature Genetics , vol.19 , Issue.2 , pp. 148-154
    • Cummings, C.J.1    Mancini, M.A.2    Antalffy, B.3    DeFranco, D.B.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 12
    • 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
    • DOI 10.1074/jbc.275.12.8772
    • Kobayashi Y, Kume A, Li M, 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 275: 8772-8778, 2000. (Pubitemid 30180231)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.12 , pp. 8772-8778
    • Kobayashi, Y.1    Kume, A.2    Li, M.3    Doyu, M.4    Hata, M.5    Ohtsuka, K.6    Sobue, G.7
  • 15
    • 0032476668 scopus 로고    scopus 로고
    • Hsp7O exerts its anti-apoptotic function downstream of caspase-3-like proteases
    • DOI 10.1093/emboj/17.21.6124
    • Jäättelä M, Wissing D, Kokholm K, Kallunki T and Egeblad M: Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases. EMBO J 17: 6124-6134, 1998. (Pubitemid 28497786)
    • (1998) EMBO Journal , vol.17 , Issue.21 , pp. 6124-6134
    • Jaattela, M.1    Wissing, D.2    Kokholm, K.3    Kallunki, T.4    Egeblad, M.5
  • 16
    • 0033830374 scopus 로고    scopus 로고
    • The chaperone function of hsp70 is required for protection against stress-induced apoptosis
    • Mosser DD, Caron AW, Bourget L, et al: The chaperone function of hsp70 is required for protection against stress-induced apoptosis. Mol Cell Biol 20: 7146-7159, 2000.
    • (2000) Mol Cell Biol , vol.20 , pp. 7146-7159
    • Mosser, D.D.1    Caron, A.W.2    Bourget, L.3
  • 20
    • 0031844350 scopus 로고    scopus 로고
    • Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin
    • DOI 10.1379/1466-1268(1998)003<0100:ARBTTN>2.3.
    • Schulte TW, Akinaga S, Soga S, et al: Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin. Cell Stress Chaperones 3: 100-108, 1998. (Pubitemid 28327422)
    • (1998) Cell Stress and Chaperones , vol.3 , Issue.2 , pp. 100-108
    • Schulte, T.W.1    Akinaga, S.2    Soga, S.3    Sullivan, W.4    Stensgard, B.5    Toft, D.6    Neckers, L.M.7
  • 21
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
    • Zou J, Guo Y, Guettouche T, Smith DF and Voellmy R: Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 94: 471-480, 1998. (Pubitemid 28391863)
    • (1998) Cell , vol.94 , Issue.4 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5
  • 24
    • 0035966071 scopus 로고    scopus 로고
    • NF-kappa B activation mediates doxorubicin-induced cell death in N-type neuroblastoma cells
    • Bian X, McAllister-Lucas LM, Shao F, et al: NF-kappa B activation mediates doxorubicin-induced cell death in N-type neuroblastoma cells. J Biol Chem 276: 48921-48929, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 48921-48929
    • Bian, X.1    McAllister-Lucas, L.M.2    Shao, F.3
  • 26
    • 0033590630 scopus 로고    scopus 로고
    • Hydrogen peroxide-induced apoptosis is CD95-independent, requires the release of mitochondria-derived reactive oxygen species and the activation of NF-kappaB
    • DOI 10.1038/sj.onc.1202325
    • Dumont A, Hehner SP, Hofmann TG, Ueffing M, Dröge W and Schmitz ML: Hydrogen peroxide-induced apoptosis is CD95-independent, requires the release of mitochondria-derived reactive oxygen species and the activation of NF-kappaB. Oncogene 18: 747-757, 1999. (Pubitemid 29080332)
    • (1999) Oncogene , vol.18 , Issue.3 , pp. 747-757
    • Dumont, A.1    Hehner, S.P.2    Hofmann, T.G.3    Ueffing, M.4    Droge, W.5    Schmitz, M.L.6
  • 27
    • 33646900838 scopus 로고    scopus 로고
    • Triptolide, an inhibitor of the human heat shock response that enhances stress-induced cell death
    • DOI 10.1074/jbc.M512044200
    • Westerheide SD, Kawahara TL, Orton K and Morimoto RI: Triptolide, an inhibitor of the human heat shock response that enhances stress-induced cell death. J Biol Chem 281: 9616-9622, 2006. (Pubitemid 43864680)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.14 , pp. 9616-9622
    • Westerheide, S.D.1    Kawahara, T.L.A.2    Orton, K.3    Morimoto, R.I.4
  • 28
    • 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 23: 69-96, 2004.
    • (2004) J Mol Neurosci , vol.23 , pp. 69-96
    • Wyttenbach, A.1
  • 29
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • DOI 10.1038/nrn1587
    • Muchowski PJ and Wacker JL: Modulation of neurodegeneration by molecular chaperones. Nat Rev Neurosci 6: 11-22, 2005. (Pubitemid 40052135)
    • (2005) Nature Reviews Neuroscience , vol.6 , Issue.1 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 31
    • 0025880971 scopus 로고
    • Drug-target interactions: Only the first step in the commitment to a programmed cell death?
    • Dive C and Hickman JA: Drug-target interactions: only the first step in the commitment to a programmed cell death? Br J Cancer 64: 192-196, 1991.
    • (1991) Br J Cancer , vol.64 , pp. 192-196
    • Dive, C.1    Hickman, J.A.2
  • 32
    • 0030054050 scopus 로고    scopus 로고
    • T cell lymphoma in transgenic mice expressing the human Hsp70 gene
    • Seo JS, Park YM, Kim JI, et al: T cell lymphoma in transgenic mice expressing the human Hsp70 gene. Biochem Biophys Res Commun 218: 582-587, 1996.
    • (1996) Biochem Biophys Res Commun , vol.218 , pp. 582-587
    • Seo, J.S.1    Park, Y.M.2    Kim, J.I.3
  • 33
    • 0028919063 scopus 로고
    • Inhibition of proliferation and induction of apoptosis by abrogation of heat-shock protein (HSP) 70 expression in tumor cells
    • Wei YQ, Zhao X, Kariya Y, Teshigawara K and Uchida A: Inhibition of proliferation and induction of apoptosis by abrogation of heat-shock protein (HSP) 70 expression in tumor cells. Cancer Immunol Immunother 40: 73-78, 1995.
    • (1995) Cancer Immunol Immunother , vol.40 , pp. 73-78
    • Wei, Y.Q.1    Zhao, X.2    Kariya, Y.3    Teshigawara, K.4    Uchida, A.5
  • 34
    • 79956311279 scopus 로고    scopus 로고
    • The novel hydroxylamine derivative NG-094 suppresses polyglutamine protein toxicity in Caenorhabditis elegans
    • Haldimann P, Muriset M, Vigh L and Goloubinoff P: The novel hydroxylamine derivative NG-094 suppresses polyglutamine protein toxicity in Caenorhabditis elegans. J Biol Chem 286: 18784-18794.
    • J Biol Chem , vol.286 , pp. 18784-18794
    • Haldimann, P.1    Muriset, M.2    Vigh, L.3    Goloubinoff, P.4
  • 35
    • 0036219609 scopus 로고    scopus 로고
    • Hsp90 inhibitors as novel cancer chemotherapeutic agents
    • Neckers L: Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol Med 8: S55-S61, 2002.
    • (2002) Trends Mol Med , vol.8
    • Neckers, L.1
  • 36
    • 0032541344 scopus 로고    scopus 로고
    • ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
    • DOI 10.1093/emboj/17.16.4829
    • Panaretou B, Prodromou C, Roe SM, et al: ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J 17: 4829-4836, 1998. (Pubitemid 28377183)
    • (1998) EMBO Journal , vol.17 , Issue.16 , pp. 4829-4836
    • Panaretou, B.1    Prodromou, C.2    Roe, S.M.3    O'Brien, R.4    Ladbury, J.E.5    Piper, P.W.6    Pearl, L.H.7
  • 37
    • 0033581021 scopus 로고    scopus 로고
    • The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes
    • Grenert JP, Johnson BD and Toft DO: The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes. J Biol Chem 274: 17525-17533, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 17525-17533
    • Grenert, J.P.1    Johnson, B.D.2    Toft, D.O.3
  • 40
    • 0036789884 scopus 로고    scopus 로고
    • Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu
    • Xu W, Marcu M, Yuan X, Mimnaugh E, Patterson C and Neckers L: Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu. Proc Natl Acad Sci USA 99: 12847-12852, 2002.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 12847-12852
    • Xu, W.1    Marcu, M.2    Yuan, X.3    Mimnaugh, E.4    Patterson, C.5    Neckers, L.6
  • 41
    • 67650745109 scopus 로고    scopus 로고
    • Loss of Hsp70 exacerbates pathogenesis but not levels of fibrillar aggregates in a mouse model of Huntington's disease
    • Wacker JL, Huang SY, Steele AD, et al: Loss of Hsp70 exacerbates pathogenesis but not levels of fibrillar aggregates in a mouse model of Huntington's disease. J Neurosci 29: 9104-9114, 2009.
    • (2009) J Neurosci , vol.29 , pp. 9104-9114
    • Wacker, J.L.1    Huang, S.Y.2    Steele, A.D.3
  • 42
    • 28844451001 scopus 로고    scopus 로고
    • Geldanamycin induces heat shock protein 70 and protects against MPTP-induced dopaminergic neurotoxicity in mice
    • DOI 10.1074/jbc.M505524200
    • Shen HY, He JC, Wang Y, Huang QY and Chen JF: Geldanamycin induces heat shock protein 70 and protects against MPTP-induced dopaminergic neurotoxicity in mice. J Biol Chem 280: 39962-39969, 2005. (Pubitemid 41779131)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.48 , pp. 39962-39969
    • Shen, H.-Y.1    He, J.-C.2    Wang, Y.3    Huang, Q.-Y.4    Chen, J.-F.5
  • 43
    • 0034237719 scopus 로고    scopus 로고
    • Energetics in the pathogenesis of neurodegenerative diseases
    • Beal MF: Energetics in the pathogenesis of neurodegenerative diseases. Trends Neurosci 23: 298-304, 2000.
    • (2000) Trends Neurosci , vol.23 , pp. 298-304
    • Beal, M.F.1
  • 48
    • 0023118066 scopus 로고
    • Nature and distribution of brain lesions in rats intoxicated with 3-nitropropionic acid: A type of hypoxic (energy deficient) brain damage
    • DOI 10.1007/BF00691103
    • Hamilton BF and Gould DH: Nature and distribution of brain lesions in rats intoxicated with 3-nitropropionic acid: a type of hypoxic (energy deficient) brain damage. Acta Neuropathol 72: 286-297, 1987. (Pubitemid 17006851)
    • (1987) Acta Neuropathologica , vol.72 , Issue.3 , pp. 286-297
    • Hamilton, B.F.1    Gould, D.H.2
  • 49
    • 0029118136 scopus 로고
    • Chronic mitochondrial energy impairment produces selective striatal degeneration and abnormal choreiform movements in primates
    • Brouillet E, Hantraye P, Ferrante RJ, et al: Chronic mitochondrial energy impairment produces selective striatal degeneration and abnormal choreiform movements in primates. Proc Natl Acad Sci USA 92: 7105-7109, 1995.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7105-7109
    • Brouillet, E.1    Hantraye, P.2    Ferrante, R.J.3
  • 51
    • 0032582562 scopus 로고    scopus 로고
    • Role of Hsp70 in regulation of stress-kinase JNK: Implications in apoptosis and aging
    • DOI 10.1016/S0014-5793(98)01242-3, PII S0014579398012423
    • Gabai VL, Meriin AB, Yaglom JA, Volloch VZ and Sherman MY: Role of Hsp70 in regulation of stress-kinase JNK: implications in apoptosis and aging. FEBS Lett 438: 1-4, 1998. (Pubitemid 28517824)
    • (1998) FEBS Letters , vol.438 , Issue.1-2 , pp. 1-4
    • Gabai, V.L.1    Meriin, A.B.2    Yaglom, J.A.3    Volloch, V.Z.4    Sherman, M.Y.5
  • 52
    • 0032932192 scopus 로고    scopus 로고
    • Protein-damaging stresses activate c-Jun N-terminal kinase via inhibition of its dephosphorylation: A novel pathway controlled by HSP72
    • Meriin AB, Yaglom JA, Gabai VL, et al: Protein-damaging stresses activate c-Jun N-terminal kinase via inhibition of its dephosphorylation: a novel pathway controlled by HSP72. Mol Cell Biol 19: 2547-2555, 1999. (Pubitemid 29144498)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.4 , pp. 2547-2555
    • Meriin, A.B.1    Yaglom, J.A.2    Gabai, V.L.3    Mosser, D.D.4    Zon, L.5    Sherman, M.Y.6
  • 53
    • 0030198344 scopus 로고    scopus 로고
    • Protein kinase cascades activated by stress and inflammatory cytokines
    • Kyriakis JM and Avruch J: Protein kinase cascades activated by stress and inflammatory cytokines. Bioessays 18: 567-577, 1996. (Pubitemid 26311096)
    • (1996) BioEssays , vol.18 , Issue.7 , pp. 567-577
    • Kyriakis, J.M.1    Avruch, J.2
  • 54
    • 0035254227 scopus 로고    scopus 로고
    • Hsp72 functions as a natural inhibitory protein of c-Jun N-terminal kinase
    • Park HS, Lee JS, Huh SH, Seo JS and Choi EJ: Hsp72 functions as a natural inhibitory protein of c-Jun N-terminal kinase. EMBO J 20: 446-456, 2001.
    • (2001) EMBO J , vol.20 , pp. 446-456
    • Park, H.S.1    Lee, J.S.2    Huh, S.H.3    Seo, J.S.4    Choi, E.J.5
  • 55
    • 14844307612 scopus 로고    scopus 로고
    • HSP70 deficiency results in activation of c-Jun N-terminal Kinase, extracellular signal-regulated kinase, and caspase-3 in hyperosmolarity-induced apoptosis
    • Lee JS, Lee JJ and Seo JS: HSP70 deficiency results in activation of c-Jun N-terminal Kinase, extracellular signal-regulated kinase, and caspase-3 in hyperosmolarity-induced apoptosis. J Biol Chem 280: 6634-6641, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 6634-6641
    • Lee, J.S.1    Lee, J.J.2    Seo, J.S.3
  • 56
    • 78249266912 scopus 로고    scopus 로고
    • Inhibition of the JNK/Bim pathway by Hsp70 prevents Bax activation in UV?Induced apoptosis
    • Li H, Liu L, Xing D and Chen WR: Inhibition of the JNK/Bim pathway by Hsp70 prevents Bax activation in UV?induced apoptosis. FEBS Lett 584: 4672-4678, 2010.
    • (2010) FEBS Lett , vol.584 , pp. 4672-4678
    • Li, H.1    Liu, L.2    Xing, D.3    Chen, W.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.