메뉴 건너뛰기




Volumn 6, Issue 1, 2011, Pages

Reduction of mutant huntingtin accumulation and toxicity by lysosomal cathepsins D and B in neurons

Author keywords

autophagy; cathepsin; huntingtin; lysosome

Indexed keywords

CATHEPSIN B; CATHEPSIN D; HUNTINGTIN; MUTANT PROTEIN; PROTEINASE;

EID: 79957643515     PISSN: None     EISSN: 17501326     Source Type: Journal    
DOI: 10.1186/1750-1326-6-37     Document Type: Article
Times cited : (59)

References (38)
  • 1
    • 77953417539 scopus 로고    scopus 로고
    • Basic mechanisms of neurodegeneration: A critical update
    • 20070435
    • Basic mechanisms of neurodegeneration: a critical update. KA Jellinger, J Cell Mol Med 2010 14 457 487 20070435
    • (2010) J Cell Mol Med , vol.14 , pp. 457-487
    • Jellinger, K.A.1
  • 2
    • 34247161367 scopus 로고    scopus 로고
    • Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and α-synuclein
    • DOI 10.1074/jbc.M609532200
    • Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein. S Sarkar JE Davies Z Huang A Tunnacl (Pubitemid 47093730)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.8 , pp. 5641-5652
    • Sarkar, S.1    Davies, J.E.2    Huang, Z.3    Tunnacliffe, A.4    Rubinsztein, D.C.5
  • 4
    • 49049096562 scopus 로고    scopus 로고
    • Autophagy induction and autophagosome clearance in neurons: Relationship to autophagic pathology in Alzheimer's disease
    • 10.1523/JNEUROSCI.0800-08.2008. 18596167
    • Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer's disease. B Boland A Kumar S Lee FM Platt J Wegiel WH Yu,, et al. J Neurosci 2008 28 6926 6937 10.1523/JNEUROSCI.0800-08. 2008 18596167
    • (2008) J Neurosci , vol.28 , pp. 6926-6937
    • Boland, B.1    Kumar, A.2    Lee, S.3    Platt, F.M.4    Wegiel, J.5    Yu, W.H.6
  • 5
    • 77955291545 scopus 로고    scopus 로고
    • Inhibiting the ubiquitin-proteasome system leads to preferential accumulation of toxic N-terminal mutant huntingtin fragments
    • 10.1093/hmg/ddq127. 20354076
    • Inhibiting the ubiquitin-proteasome system leads to preferential accumulation of toxic N-terminal mutant huntingtin fragments. X Li CE Wang S Huang X Xu XJ Li H Li,, et al. Hum Mol Genet 2010 19 2445 2455 10.1093/hmg/ddq127 20354076
    • (2010) Hum Mol Genet , vol.19 , pp. 2445-2455
    • Li, X.1    Wang, C.E.2    Huang, S.3    Xu, X.4    Li, X.J.5    Li, H.6
  • 6
    • 77955447356 scopus 로고    scopus 로고
    • Clearance of mutant huntingtin
    • Clearance of mutant huntingtin. XJ Li H Li S Li, Autophagy 2010 6
    • (2010) Autophagy , vol.6
    • Li, X.J.1    Li, H.2    Li, S.3
  • 7
    • 77950672979 scopus 로고    scopus 로고
    • Lysosomal function in macromolecular homeostasis and bioenergetics in Parkinson's disease
    • 10.1186/1750-1326-5-14. 20388210
    • Lysosomal function in macromolecular homeostasis and bioenergetics in Parkinson's disease. L Schneider J Zhang, Mol Neurodegener 2010 5 14 10.1186/1750-1326-5-14 20388210
    • (2010) Mol Neurodegener , vol.5 , pp. 14
    • Schneider, L.1    Zhang, J.2
  • 8
    • 33748433101 scopus 로고    scopus 로고
    • Lysosomal chat maintains the balance
    • Lysosomal chat maintains the balance. AC Massey S Kaushik AM Cuervo, Autophagy 2006 2 325 327 16874078 (Pubitemid 44342384)
    • (2006) Autophagy , vol.2 , Issue.4 , pp. 325-327
    • Massey, A.C.1    Kaushik, S.2    Cuervo, A.M.3
  • 9
    • 24644437419 scopus 로고    scopus 로고
    • Protein degradation and aging
    • DOI 10.1016/j.exger.2005.07.005, PII S0531556505001518
    • Protein degradation and aging. M Martinez-Vicente G Sovak AM Cuervo, Exp Gerontol 2005 40 622 633 10.1016/j.exger.2005.07.005 16125351 (Pubitemid 41265812)
    • (2005) Experimental Gerontology , vol.40 , Issue.8-9 , pp. 622-633
    • Martinez-Vicente, M.1    Sovak, G.2    Cuervo, A.M.3
  • 10
    • 0034113064 scopus 로고    scopus 로고
    • When lysosomes get old
    • DOI 10.1016/S0531-5565(00)00075-9, PII S0531556500000759
    • When lysosomes get old. AM Cuervo JF Dice, Exp Gerontol 2000 35 119 131 10.1016/S0531-5565(00)00075-9 10767573 (Pubitemid 30190079)
    • (2000) Experimental Gerontology , vol.35 , Issue.2 , pp. 119-131
    • Cuervo, A.M.1    Dice, J.F.2
  • 11
    • 0031883733 scopus 로고    scopus 로고
    • Lysosomes, a meeting point of proteins, chaperones, and proteases
    • Lysosomes, a meeting point of proteins, chaperones, and proteases. AM Cuervo JF Dice, J Mol Med 1998 76 6 12 10.1007/s109-1998-8099-y 9462863 (Pubitemid 28085056)
    • (1998) Journal of Molecular Medicine , vol.76 , Issue.1 , pp. 6-12
    • Cuervo, A.M.1    Dice, J.F.2
  • 12
    • 0028797005 scopus 로고
    • Degradation of proteasomes by lysosomes in rat liver
    • 10.1111/j.1432-1033.1995.tb20203.x. 7867640
    • Degradation of proteasomes by lysosomes in rat liver. AM Cuervo A Palmer AJ Rivett E Knecht, Eur J Biochem 1995 227 792 800 10.1111/j.1432-1033.1995. tb20203.x 7867640
    • (1995) Eur J Biochem , vol.227 , pp. 792-800
    • Cuervo, A.M.1    Palmer, A.2    Rivett, A.J.3    Knecht, E.4
  • 13
    • 33745862719 scopus 로고    scopus 로고
    • Potential compensatory responses through autophagic/lysosomal pathways in neurodegenerative diseases
    • Potential compensatory responses through autophagic/lysosomal pathways in neurodegenerative diseases. D Butler RA Nixon BA Bahr, Autophagy 2006 2 234 237 16874061 (Pubitemid 44030894)
    • (2006) Autophagy , vol.2 , Issue.3 , pp. 234-237
    • Butler, D.1    Nixon, R.A.2    Bahr, B.A.3
  • 15
    • 34250171697 scopus 로고    scopus 로고
    • Autophagy Induction Rescues Toxicity Mediated by Proteasome Inhibition
    • DOI 10.1016/j.neuron.2007.06.005, PII S089662730700414X
    • Autophagy induction rescues toxicity mediated by proteasome inhibition. DC Rubinsztein, Neuron 2007 54 854 856 10.1016/j.neuron.2007.06.005 17582326 (Pubitemid 46907509)
    • (2007) Neuron , vol.54 , Issue.6 , pp. 854-856
    • Rubinsztein, D.C.1
  • 18
    • 33748524564 scopus 로고    scopus 로고
    • Antiamyloidogenic and Neuroprotective Functions of Cathepsin B: Implications for Alzheimer's Disease
    • DOI 10.1016/j.neuron.2006.07.027, PII S0896627306005976
    • Antiamyloidogenic and neuroprotective functions of cathepsin B: implications for Alzheimer's disease. S Mueller-Steiner Y Zhou H Arai ED Roberson B Sun J Chen,, et al. Neuron 2006 51 703 714 10.1016/j.neuron.2006.07. 027 16982417 (Pubitemid 44374903)
    • (2006) Neuron , vol.51 , Issue.6 , pp. 703-714
    • Mueller-Steiner, S.1    Zhou, Y.2    Arai, H.3    Roberson, E.D.4    Sun, B.5    Chen, J.6    Wang, X.7    Yu, G.8    Esposito, L.9    Mucke, L.10    Gan, L.11
  • 19
    • 79955694568 scopus 로고    scopus 로고
    • Lysosomal enzyme cathepsin D protects against alpha-synuclein aggregation and toxicity
    • 10.1186/1756-6606-1-17. 19021916
    • Lysosomal enzyme cathepsin D protects against alpha-synuclein aggregation and toxicity. L Qiao S Hamamichi KA Caldwell GA Caldwell TA Yacoubian S Wilson,, et al. Mol Brain 2008 1 17 10.1186/1756-6606-1-17 19021916
    • (2008) Mol Brain , vol.1 , pp. 17
    • Qiao, L.1    Hamamichi, S.2    Caldwell, K.A.3    Caldwell, G.A.4    Yacoubian, T.A.5    Wilson, S.6
  • 20
    • 64949185378 scopus 로고    scopus 로고
    • Cathepsin D expression level affects alpha-synuclein processing, aggregation, and toxicity in vivo
    • 10.1186/1756-6606-2-5. 19203374
    • Cathepsin D expression level affects alpha-synuclein processing, aggregation, and toxicity in vivo. V Cullen M Lindfors J Ng A Paetau E Swinton P Kolodziej,, et al. Mol Brain 2009 2 5 10.1186/1756-6606-2-5 19203374
    • (2009) Mol Brain , vol.2 , pp. 5
    • Cullen, V.1    Lindfors, M.2    Ng, J.3    Paetau, A.4    Swinton, E.5    Kolodziej, P.6
  • 21
    • 20744435383 scopus 로고    scopus 로고
    • Molecular pathophysiology of Parkinson's disease
    • DOI 10.1146/annurev.neuro.28.061604.135718
    • Molecular pathophysiology of Parkinson's disease. DJ Moore AB West VL Dawson TM Dawson, Annu Rev Neurosci 2005 28 57 87 10.1146/annurev.neuro.28. 061604.135718 16022590 (Pubitemid 41098899)
    • (2005) Annual Review of Neuroscience , vol.28 , pp. 57-87
    • Moore, D.J.1    West, A.B.2    Dawson, V.L.3    Dawson, T.M.4
  • 22
    • 84993912315 scopus 로고
    • Increased apoptosis and early embryonic lethality in mice nullizygous for the Huntington's disease gene homologue
    • 10.1038/ng1095-155. 7550343
    • Increased apoptosis and early embryonic lethality in mice nullizygous for the Huntington's disease gene homologue. S Zeitlin JP Liu DL Chapman VE Papaioannou A Efstratiadis, Nat Genet 1995 11 155 163 10.1038/ng1095-155 7550343
    • (1995) Nat Genet , vol.11 , pp. 155-163
    • Zeitlin, S.1    Liu, J.P.2    Chapman, D.L.3    Papaioannou, V.E.4    Efstratiadis, A.5
  • 24
    • 0141891952 scopus 로고    scopus 로고
    • 2-terminal fragment complexes that are promoted by the age-dependent decrease in proteasome activity
    • DOI 10.1083/jcb.200306038
    • Huntingtin forms toxic NH2-terminal fragment complexes that are promoted by the age-dependent decrease in proteasome activity. H Zhou F Cao Z Wang ZX Yu HP Nguyen J Evans,, et al. J Cell Biol 2003 163 109 118 10.1083/jcb.200306038 14557250 (Pubitemid 37271438)
    • (2003) Journal of Cell Biology , vol.163 , Issue.1 , pp. 109-118
    • Zhou, H.1    Cao, F.2    Wang, Z.3    Yu, Z.-X.4    Nguyen, H.-P.5    Evans, J.6    Li, S.-H.7    Li, X.-J.8
  • 25
    • 0033324248 scopus 로고    scopus 로고
    • The early cellular pathology of Huntington's disease
    • 10.1007/BF02742437. 10966117
    • The early cellular pathology of Huntington's disease. XJ Li, Mol Neurobiol 1999 20 111 124 10.1007/BF02742437 10966117
    • (1999) Mol Neurobiol , vol.20 , pp. 111-124
    • Li, X.J.1
  • 26
  • 28
    • 33646121970 scopus 로고    scopus 로고
    • Lysosomal proteases are involved in generation of N-terminal huntingtin fragments
    • 10.1016/j.nbd.2005.11.012. 16423528
    • Lysosomal proteases are involved in generation of N-terminal huntingtin fragments. YJ Kim E Sapp BG Cuiffo L Sobin J Yoder KB Kegel,, et al. Neurobiol Dis 2006 22 346 356 10.1016/j.nbd.2005.11.012 16423528
    • (2006) Neurobiol Dis , vol.22 , pp. 346-356
    • Kim, Y.J.1    Sapp, E.2    Cuiffo, B.G.3    Sobin, L.4    Yoder, J.5    Kegel, K.B.6
  • 29
    • 78650035000 scopus 로고    scopus 로고
    • Huntingtin cleavage product A forms in neurons and is reduced by gamma-secretase inhibitors
    • 10.1186/1750-1326-5-58. 21156064
    • Huntingtin cleavage product A forms in neurons and is reduced by gamma-secretase inhibitors. KB Kegel E Sapp J Alexander P Reeves D Bleckmann L Sobin,, et al. Mol Neurodegener 2010 5 58 10.1186/1750-1326-5-58 21156064
    • (2010) Mol Neurodegener , vol.5 , pp. 58
    • Kegel, K.B.1    Sapp, E.2    Alexander, J.3    Reeves, P.4    Bleckmann, D.5    Sobin, L.6
  • 30
    • 65249141171 scopus 로고    scopus 로고
    • Mutant huntingtin impairs post-Golgi trafficking to lysosomes by delocalizing optineurin/Rab8 complex from the Golgi apparatus
    • 10.1091/mbc.E08-07-0726. 19144827
    • Mutant huntingtin impairs post-Golgi trafficking to lysosomes by delocalizing optineurin/Rab8 complex from the Golgi apparatus. TD del J Alberch F Lazaro-Dieguez R Martin-Ibanez X Xifro G Egea,, et al. Mol Biol Cell 2009 20 1478 1492 10.1091/mbc.E08-07-0726 19144827
    • (2009) Mol Biol Cell , vol.20 , pp. 1478-1492
    • Del, T.D.1    Alberch, J.2    Lazaro-Dieguez, F.3    Martin-Ibanez, R.4    Xifro, X.5    Egea, G.6
  • 31
    • 37849042536 scopus 로고    scopus 로고
    • A rational mechanism for combination treatment of Huntington's disease using lithium and rapamycin
    • 17921520
    • A rational mechanism for combination treatment of Huntington's disease using lithium and rapamycin. S Sarkar G Krishna S Imarisio S Saiki CJ O'Kane DC Rubinsztein, Hum Mol Genet 2008 17 170 178 17921520
    • (2008) Hum Mol Genet , vol.17 , pp. 170-178
    • Sarkar, S.1    Krishna, G.2    Imarisio, S.3    Saiki, S.4    O'Kane, C.J.5    Rubinsztein, D.C.6
  • 32
    • 0034754875 scopus 로고    scopus 로고
    • Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation
    • Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation. S Waelter A Boeddrich R Lurz E Scherzinger G Lueder H Lehrach,, et al. Mol Biol Cell 2001 12 1393 1407 11359930 (Pubitemid 33044419)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.5 , pp. 1393-1407
    • Waelter, S.1    Boeddrich, A.2    Lurz, R.3    Scherzinger, E.4    Lueder, G.5    Lehrach, H.6    Wanker, E.E.7
  • 35
    • 68149123529 scopus 로고    scopus 로고
    • Alterations in lysosomal and proteasomal markers in Parkinson's disease: Relationship to alpha-synuclein inclusions
    • Alterations in lysosomal and proteasomal markers in Parkinson's disease: Relationship to alpha-synuclein inclusions. Y Chu H Dodiya P Aebischer CW Olanow JH Kordower, Neurobiol Dis 2009
    • (2009) Neurobiol Dis
    • Chu, Y.1    Dodiya, H.2    Aebischer, P.3    Olanow, C.W.4    Kordower, J.H.5
  • 37
    • 77951768486 scopus 로고    scopus 로고
    • Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids
    • 10.1016/j.cell.2010.02.024. 20381137
    • Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Y Sancak L Bar-Peled R Zoncu AL Markhard S Nada DM Sabatini, Cell 2010 141 290 303 10.1016/j.cell.2010.02.024 20381137
    • (2010) Cell , vol.141 , pp. 290-303
    • Sancak, Y.1    Bar-Peled, L.2    Zoncu, R.3    Markhard, A.L.4    Nada, S.5    Sabatini, D.M.6
  • 38
    • 0034737299 scopus 로고    scopus 로고
    • Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease
    • 10.1016/S0092-8674(00)80623-6. 10778856
    • Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease. A Yamamoto JJ Lucas R Hen, Cell 2000 101 57 66 10.1016/S0092-8674(00)80623-6 10778856
    • (2000) Cell , vol.101 , pp. 57-66
    • Yamamoto, A.1    Lucas, J.J.2    Hen, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.