메뉴 건너뛰기




Volumn 9, Issue 5, 2007, Pages 553-561

Expanding insights on the involvement of endoplasmic reticulum stress in Parkinson's disease

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE;

EID: 34247172998     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2006.1524     Document Type: Review
Times cited : (101)

References (59)
  • 1
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease
    • Auluck PK, Chan HY, Trojanowski JQ, Lee VM, and Bonini NM. Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease. Science 295: 865-868, 2002.
    • (2002) Science , vol.295 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.2    Trojanowski, J.Q.3    Lee, V.M.4    Bonini, N.M.5
  • 2
    • 15944369290 scopus 로고    scopus 로고
    • ER stress signaling by regulated splicing: IRE1/HAC1/XBP1
    • Back SH, Schroder M, Lee K, Zhang K, and Kaufman RJ. ER stress signaling by regulated splicing: IRE1/HAC1/XBP1. Methods 35: 395-416, 2005.
    • (2005) Methods , vol.35 , pp. 395-416
    • Back, S.H.1    Schroder, M.2    Lee, K.3    Zhang, K.4    Kaufman, R.J.5
  • 3
    • 17644365438 scopus 로고    scopus 로고
    • Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability
    • Beilina A, Van Der Brug M, Ahmad R, Kesavapany S, Miller DW, Petsko GA, and Cookson MR. Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability. Proc Natl Acad Sci USA 102: 5703-5708, 2005.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 5703-5708
    • Beilina, A.1    Van Der Brug, M.2    Ahmad, R.3    Kesavapany, S.4    Miller, D.W.5    Petsko, G.A.6    Cookson, M.R.7
  • 4
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence NF, Sampat RM, and Kopito RR. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292: 1552-1555, 2001.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 5
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • Bertolotti A, Zhang Y, Hendershot LM, Harding HP, and Ron D. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat Cell Biol 2: 326-332, 2000.
    • (2000) Nat Cell Biol , vol.2 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 10
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • Cuervo AM, Stefanis L, Fredenburg R, Lansbury PT, and Sulzer D. Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 305: 1292-1295, 2004.
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 11
    • 27144469287 scopus 로고    scopus 로고
    • Small interfering RNA targeting the PINK1 induces apoptosis in dopaminergic cells SH-SY5Y
    • Deng H, Jankovic J, Guo Y, Xie W, and Le W. Small interfering RNA targeting the PINK1 induces apoptosis in dopaminergic cells SH-SY5Y. Biochem Biophys Res Commun 337: 1133-1138, 2005.
    • (2005) Biochem Biophys Res Commun , vol.337 , pp. 1133-1138
    • Deng, H.1    Jankovic, J.2    Guo, Y.3    Xie, W.4    Le, W.5
  • 12
    • 5144234034 scopus 로고    scopus 로고
    • Fernagut PO and Chesselet ME Alpha-synuclein and transgenic mouse models. Neurobiol Dis 17: 123-130, 2004.
    • Fernagut PO and Chesselet ME Alpha-synuclein and transgenic mouse models. Neurobiol Dis 17: 123-130, 2004.
  • 13
    • 0033780610 scopus 로고    scopus 로고
    • A regulatory link between ER-associated protein degradation and the unfolded-protein response
    • Friedlander R, Jarosch E, Urban J, Volkwein C, and Sommer T. A regulatory link between ER-associated protein degradation and the unfolded-protein response. Nat Cell Biol 2: 379-384, 2000.
    • (2000) Nat Cell Biol , vol.2 , pp. 379-384
    • Friedlander, R.1    Jarosch, E.2    Urban, J.3    Volkwein, C.4    Sommer, T.5
  • 14
    • 0024535437 scopus 로고
    • Intermediates in the aerobic autoxidation of 6-hydroxydopamine: Relative importance under different reaction conditions
    • Gee P and Davison AJ. Intermediates in the aerobic autoxidation of 6-hydroxydopamine: relative importance under different reaction conditions. Free Radic Biol Med 6: 271-284, 1989.
    • (1989) Free Radic Biol Med , vol.6 , pp. 271-284
    • Gee, P.1    Davison, A.J.2
  • 15
    • 0033788434 scopus 로고    scopus 로고
    • Rat alpha-synuclein interacts with Tat binding protein 1, a component of the 26S proteasomal complex
    • Ghee M, Fournier A, and Mallet J. Rat alpha-synuclein interacts with Tat binding protein 1, a component of the 26S proteasomal complex. J Neurochem 75: 2221-2224, 2000.
    • (2000) J Neurochem , vol.75 , pp. 2221-2224
    • Ghee, M.1    Fournier, A.2    Mallet, J.3
  • 16
    • 0038143287 scopus 로고    scopus 로고
    • Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons
    • Holtz WA and O'Malley KL. Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons. J Biol Chem 278: 19367-19377, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 19367-19377
    • Holtz, W.A.1    O'Malley, K.L.2
  • 17
    • 0036345454 scopus 로고    scopus 로고
    • CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity
    • Imai Y, Soda M, Hatakeyama S, Akagi T, Hashikawa T, Nakayama KI, and Takahashi R. CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Mol Cell 10: 55-67, 2002.
    • (2002) Mol Cell , vol.10 , pp. 55-67
    • Imai, Y.1    Soda, M.2    Hatakeyama, S.3    Akagi, T.4    Hashikawa, T.5    Nakayama, K.I.6    Takahashi, R.7
  • 18
    • 0035967883 scopus 로고    scopus 로고
    • An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin
    • Imai Y, Soda M, Inoue H, Hattori N, Mizuno Y, and Takahashi R. An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell 105: 891-902, 2001.
    • (2001) Cell , vol.105 , pp. 891-902
    • Imai, Y.1    Soda, M.2    Inoue, H.3    Hattori, N.4    Mizuno, Y.5    Takahashi, R.6
  • 19
    • 0034680913 scopus 로고    scopus 로고
    • Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity
    • Imai Y, Soda M, and Takahashi R. Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity. J Biol Chem 275: 35661-35664, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 35661-35664
    • Imai, Y.1    Soda, M.2    Takahashi, R.3
  • 25
    • 0036902707 scopus 로고    scopus 로고
    • Astrocytic but not neuronal increased expression and redistribution of parkin during unfolded protein stress
    • Ledesma MD, Galvan C, Hellias B, Dotti C, and Jensen PH. Astrocytic but not neuronal increased expression and redistribution of parkin during unfolded protein stress. J Neurochem 83: 1431-1440, 2002.
    • (2002) J Neurochem , vol.83 , pp. 1431-1440
    • Ledesma, M.D.1    Galvan, C.2    Hellias, B.3    Dotti, C.4    Jensen, P.H.5
  • 26
  • 27
    • 10644281090 scopus 로고    scopus 로고
    • Lentiviral vector delivery of parkin prevents dopaminergic degeneration in an alpha-synuclein rat model of Parkinson's disease
    • Lo Bianco C, Schneider BL, Bauer M, Sajadi A, Brice A, Iwatsubo T, and Aebischer P. Lentiviral vector delivery of parkin prevents dopaminergic degeneration in an alpha-synuclein rat model of Parkinson's disease. Proc Natl Acad Sci USA 101: 17510-17515, 2004.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 17510-17515
    • Lo Bianco, C.1    Schneider, B.L.2    Bauer, M.3    Sajadi, A.4    Brice, A.5    Iwatsubo, T.6    Aebischer, P.7
  • 29
    • 0034716887 scopus 로고    scopus 로고
    • Tripartite management of unfolded proteins in the endoplasmic reticulum
    • Mori K. Tripartite management of unfolded proteins in the endoplasmic reticulum. Cell 101: 451-454, 2000.
    • (2000) Cell , vol.101 , pp. 451-454
    • Mori, K.1
  • 30
    • 0037154184 scopus 로고    scopus 로고
    • Recent advances in the genetics and pathogenesis of Parkinson disease
    • Mouradian MM. Recent advances in the genetics and pathogenesis of Parkinson disease. Neurology 58: 179-185, 2002.
    • (2002) Neurology , vol.58 , pp. 179-185
    • Mouradian, M.M.1
  • 31
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
    • Murata S, Minami Y, Minami M, Chiba T, and Tanaka K. CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein. EMBO Rep 2: 1133-1138, 2001.
    • (2001) EMBO Rep , vol.2 , pp. 1133-1138
    • Murata, S.1    Minami, Y.2    Minami, M.3    Chiba, T.4    Tanaka, K.5
  • 32
    • 20944445990 scopus 로고    scopus 로고
    • Tisp40, a spermatid specific bZip transcription factor, functions by binding to the unfolded protein response element via the Rip pathway
    • Nagamori I, Yabuta N, Fujii T, Tanaka H, Yomogida K, Nishimune Y, and Nojima H. Tisp40, a spermatid specific bZip transcription factor, functions by binding to the unfolded protein response element via the Rip pathway. Genes Cells 10: 575-594, 2005.
    • (2005) Genes Cells , vol.10 , pp. 575-594
    • Nagamori, I.1    Yabuta, N.2    Fujii, T.3    Tanaka, H.4    Yomogida, K.5    Nishimune, Y.6    Nojima, H.7
  • 33
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • Nishitoh H, Matsuzawa A, Tobiume K, Saegusa K, Takeda K, Inoue K, Hori S, Kakizuka A, and Ichijo H. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev 16: 1345-1355, 2002.
    • (2002) Genes Dev , vol.16 , pp. 1345-1355
    • Nishitoh, H.1    Matsuzawa, A.2    Tobiume, K.3    Saegusa, K.4    Takeda, K.5    Inoue, K.6    Hori, S.7    Kakizuka, A.8    Ichijo, H.9
  • 36
    • 0033031194 scopus 로고    scopus 로고
    • Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species
    • Plemper RK, Deak PM, Otto RT, and Wolf DH. Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species. FEBS Lett 443: 241-245, 1999.
    • (1999) FEBS Lett , vol.443 , pp. 241-245
    • Plemper, R.K.1    Deak, P.M.2    Otto, R.T.3    Wolf, D.H.4
  • 37
    • 0033118448 scopus 로고    scopus 로고
    • Endoplasmic reticulum degradation. Reverse protein transport and its end in the proteasome
    • Plemper RK and Wolf DH. Endoplasmic reticulum degradation. Reverse protein transport and its end in the proteasome. Mol Biol Rep 26: 125-130, 1999.
    • (1999) Mol Biol Rep , vol.26 , pp. 125-130
    • Plemper, R.K.1    Wolf, D.H.2
  • 38
    • 0033168382 scopus 로고    scopus 로고
    • Retrograde protein translocation: ERADication of secretory proteins in health and disease
    • Plemper RK and Wolf DH. Retrograde protein translocation: ERADication of secretory proteins in health and disease. Trends Biochem Sci 24: 266-270, 1999.
    • (1999) Trends Biochem Sci , vol.24 , pp. 266-270
    • Plemper, R.K.1    Wolf, D.H.2
  • 40
    • 7744232493 scopus 로고    scopus 로고
    • Misfolded proteins, endoplasmic reticulum stress and neurodegeneration
    • Rao RV and Bredesen DE. Misfolded proteins, endoplasmic reticulum stress and neurodegeneration. Curr Opin Cell Biol 16: 653-662, 2004.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 653-662
    • Rao, R.V.1    Bredesen, D.E.2
  • 41
    • 0034194227 scopus 로고    scopus 로고
    • Differential impairment of 20S and 26S proteasome activities in human hematopoietic K562 cells during oxidative stress
    • Reinheckel T, Ullrich O, Sitte N, and Grune T. Differential impairment of 20S and 26S proteasome activities in human hematopoietic K562 cells during oxidative stress. Arch Biochem Biophys 377: 65-68, 2000.
    • (2000) Arch Biochem Biophys , vol.377 , pp. 65-68
    • Reinheckel, T.1    Ullrich, O.2    Sitte, N.3    Grune, T.4
  • 42
    • 0037114971 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease
    • Ryu EJ, Harding HP, Angelastro JM, Vitolo OV, Ron D, and Greene LA. Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease. J Neurosci 22: 10690-10698, 2002.
    • (2002) J Neurosci , vol.22 , pp. 10690-10698
    • Ryu, E.J.1    Harding, H.P.2    Angelastro, J.M.3    Vitolo, O.V.4    Ron, D.5    Greene, L.A.6
  • 43
    • 10444226462 scopus 로고    scopus 로고
    • ER stress and the unfolded protein response
    • Schroder M and Kaufman RJ. ER stress and the unfolded protein response. Mutat Res 569: 29-63, 2005.
    • (2005) Mutat Res , vol.569 , pp. 29-63
    • Schroder, M.1    Kaufman, R.J.2
  • 44
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schroder M and Kaufman RJ. The mammalian unfolded protein response. Annu Rev Biochem 74: 739-789, 2005.
    • (2005) Annu Rev Biochem , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 45
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe DJ. Folding proteins in fatal ways. Nature 426: 900-904, 2003.
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 47
    • 29644434199 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha-synuclein-induced toxicity
    • Smith WW, Jiang H, Pei Z, Tanaka Y, Morita H, Sawa A, Dawson VL, Dawson TM, and Ross CA. Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha-synuclein-induced toxicity. Hum Mol Genet 14: 3801-3811, 2005.
    • (2005) Hum Mol Genet , vol.14 , pp. 3801-3811
    • Smith, W.W.1    Jiang, H.2    Pei, Z.3    Tanaka, Y.4    Morita, H.5    Sawa, A.6    Dawson, V.L.7    Dawson, T.M.8    Ross, C.A.9
  • 49
    • 33749027475 scopus 로고    scopus 로고
    • Mechanisms and models of alpha-synuclein-related neurodegeneration
    • Springer W and Kahle PJ. Mechanisms and models of alpha-synuclein-related neurodegeneration. Curr Neurol Neurosci Rep 6: 432-436, 2006.
    • (2006) Curr Neurol Neurosci Rep , vol.6 , pp. 432-436
    • Springer, W.1    Kahle, P.J.2
  • 50
    • 0035894855 scopus 로고    scopus 로고
    • Expression of A53T mutant but not wild-type alpha-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death
    • Stefanis L, Larsen KE, Rideout HJ, Sulzer D, and Greene LA. Expression of A53T mutant but not wild-type alpha-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death. J Neurosci 21: 9549-9560, 2001.
    • (2001) J Neurosci , vol.21 , pp. 9549-9560
    • Stefanis, L.1    Larsen, K.E.2    Rideout, H.J.3    Sulzer, D.4    Greene, L.A.5
  • 51
    • 0035870881 scopus 로고    scopus 로고
    • Inducible expression of mutant alpha-synuclein decreases proteasome activity and increases sensitivity to mitochondria- dependent apoptosis
    • Tanaka Y, Engelender S, Igarashi S, Rao RK, Wanner T, Tanzi RE, Sawa A, V LD, Dawson TM, and Ross CA. Inducible expression of mutant alpha-synuclein decreases proteasome activity and increases sensitivity to mitochondria- dependent apoptosis. Hum Mol Genet 10: 919-926, 2001.
    • (2001) Hum Mol Genet , vol.10 , pp. 919-926
    • Tanaka, Y.1    Engelender, S.2    Igarashi, S.3    Rao, R.K.4    Wanner, T.5    Tanzi, R.E.6    Sawa, A.7    LD, V.8    Dawson, T.M.9    Ross, C.A.10
  • 54
    • 33745070550 scopus 로고    scopus 로고
    • Involvement of endoplasmic reticulum stress on the cell death induced by 6-hydroxydopamine in human neuroblastoma SH-SY5Y cells
    • Yamamuro A, Yoshioka Y, Ogita K, and Maeda S. Involvement of endoplasmic reticulum stress on the cell death induced by 6-hydroxydopamine in human neuroblastoma SH-SY5Y cells. Neurochem Res 31: 657-664, 2006.
    • (2006) Neurochem Res , vol.31 , pp. 657-664
    • Yamamuro, A.1    Yoshioka, Y.2    Ogita, K.3    Maeda, S.4
  • 55
    • 0037468831 scopus 로고    scopus 로고
    • Parkin suppresses dopaminergic neuron-selective neurotoxicity induced by Pael-R in Drosophila
    • Yang Y, Nishimura I, Imai Y, Takahashi R, and Lu B. Parkin suppresses dopaminergic neuron-selective neurotoxicity induced by Pael-R in Drosophila. Neuron 37: 911-924, 2003.
    • (2003) Neuron , vol.37 , pp. 911-924
    • Yang, Y.1    Nishimura, I.2    Imai, Y.3    Takahashi, R.4    Lu, B.5
  • 57
    • 32044453080 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response
    • Zhang K, Shen X, Wu J, Sakaki K, Saunders T, Rutkowski DT, Back SH, and Kaufman RJ. Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response. Cell 124: 587-599, 2006.
    • (2006) Cell , vol.124 , pp. 587-599
    • Zhang, K.1    Shen, X.2    Wu, J.3    Sakaki, K.4    Saunders, T.5    Rutkowski, D.T.6    Back, S.H.7    Kaufman, R.J.8
  • 58
    • 33745844503 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in health and disease
    • Zhao L and Ackerman SL. Endoplasmic reticulum stress in health and disease. Curr Opin Cell Biol 18: 444-452, 2006.
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 444-452
    • Zhao, L.1    Ackerman, S.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.