메뉴 건너뛰기




Volumn 318, Issue 1-2, 2008, Pages 109-115

Endoplasmic reticulum stress contributes to the cell death induced by UCH-L1 inhibitor

Author keywords

Endoplasmic reticulum stress; Parkinson's disease; Ubiquitin proteasome system; UCH L1 inhibitor; Unfolded protein response

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 6; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; HYDROLASE; HYDROLASE INHIBITOR; ISATIN; PROTEASOME; UBIQUITIN; UBIQUITIN CARBOXYL TERMINAL HYDROLASE L1 PROTEIN INHIBITOR; UNCLASSIFIED DRUG; X BOX BINDING PROTEIN 1;

EID: 54949145341     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-008-9862-x     Document Type: Article
Times cited : (37)

References (27)
  • 1
    • 0024461942 scopus 로고
    • The neuron-specific protein PGP 9.5 is a ubiquitin carboxyl-terminal hydrolase
    • doi: 10.1126/science.2530630
    • Wilkinson KD, Lee KM, Deshpande S et al (1989) The neuron-specific protein PGP 9.5 is a ubiquitin carboxyl-terminal hydrolase. Science 246:670-673. doi: 10.1126/science.2530630
    • (1989) Science , vol.246 , pp. 670-673
    • Wilkinson, K.D.1    Lee, K.M.2    Deshpande, S.3
  • 2
    • 0032190090 scopus 로고    scopus 로고
    • The ubiquitin pathway in Parkinson's disease
    • doi: 10.1038/26652
    • Leroy E, Boyer R, Auburger G et al (1998) The ubiquitin pathway in Parkinson's disease. Nature 395:451-452. doi: 10.1038/26652
    • (1998) Nature , vol.395 , pp. 451-452
    • Leroy, E.1    Boyer, R.2    Auburger, G.3
  • 3
    • 0037466510 scopus 로고    scopus 로고
    • Alterations of structure and hydrolase activity of parkinsonism-associated human ubiquitin carboxyl-terminal hydrolase L1 variants
    • doi: 10.1016/S0006-291X(03)00555-2
    • Nishikawa K, Li H, Kawamura R et al (2003) Alterations of structure and hydrolase activity of parkinsonism-associated human ubiquitin carboxyl-terminal hydrolase L1 variants. Biochem Biophys Res Commun 304:176-183. doi: 10.1016/S0006-291X(03)00555-2
    • (2003) Biochem Biophys Res Commun , vol.304 , pp. 176-183
    • Nishikawa, K.1    Li, H.2    Kawamura, R.3
  • 4
    • 33846605587 scopus 로고    scopus 로고
    • Activation of the unfolded protein response in Parkinson's disease
    • doi: 10.1016/j.bbrc.2007.01.043
    • Hoozemans JJ, van Haastert ES, Eikelenboom P et al (2007) Activation of the unfolded protein response in Parkinson's disease. Biochem Biophys Res Commun 354:707-711. doi: 10.1016/j.bbrc.2007.01.043
    • (2007) Biochem Biophys Res Commun , vol.354 , pp. 707-711
    • Hoozemans, J.J.1    van Haastert, E.S.2    Eikelenboom, P.3
  • 5
    • 0038143287 scopus 로고    scopus 로고
    • Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons
    • doi: 10.1074/jbc.M211821200
    • Holtz WA, O'Malley KL (2003) Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons. J Biol Chem 278:19367-19377. doi: 10.1074/jbc.M211821200
    • (2003) J Biol Chem , vol.278 , pp. 19367-19377
    • Holtz, W.A.1    O'Malley, K.L.2
  • 6
    • 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 et al (2002) Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease. J Neurosci 22:10690-10698
    • (2002) J Neurosci , vol.22 , pp. 10690-10698
    • Ryu, E.J.1    Harding, H.P.2    Angelastro, J.M.3
  • 7
    • 0035967883 scopus 로고    scopus 로고
    • An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin
    • doi: 10.1016/S0092-8674(01)00407-X
    • Imai Y, Soda M, Inoue H et al (2001) An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell 105:891-902. doi: 10.1016/S0092-8674(01)00407-X
    • (2001) Cell , vol.105 , pp. 891-902
    • Imai, Y.1    Soda, M.2    Inoue, H.3
  • 8
    • 33746533924 scopus 로고    scopus 로고
    • Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models
    • doi: 10.1126/science.1129462
    • Cooper AA, Gitler AD, Cashikar A et al (2006) Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models. Science 313:324-328. doi: 10.1126/science.1129462
    • (2006) Science , vol.313 , pp. 324-328
    • Cooper, A.A.1    Gitler, A.D.2    Cashikar, A.3
  • 9
    • 0036316947 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system causes dopaminergic cell death and inclusion body formation in ventral mesencephalic cultures
    • doi: 10.1046/j.1471-4159.2002.00821.x
    • McNaught KS, Mytilineou C, Jnobaptiste R et al (2002) Impairment of the ubiquitin-proteasome system causes dopaminergic cell death and inclusion body formation in ventral mesencephalic cultures. J Neurochem 81:301-306. doi: 10.1046/j.1471-4159.2002.00821.x
    • (2002) J Neurochem , vol.81 , pp. 301-306
    • McNaught, K.S.1    Mytilineou, C.2    Jnobaptiste, R.3
  • 10
    • 12444269118 scopus 로고    scopus 로고
    • Discovery of inhibitors that elucidate the role of UCH-L1 activity in the H1299 lung cancer cell line
    • doi: 10.1016/j.chembiol.2003.08.010
    • Liu Y, Lashuel HA, Choi S et al (2003) Discovery of inhibitors that elucidate the role of UCH-L1 activity in the H1299 lung cancer cell line. Chem Biol 10:837-846. doi: 10.1016/j.chembiol.2003.08.010
    • (2003) Chem Biol , vol.10 , pp. 837-846
    • Liu, Y.1    Lashuel, H.A.2    Choi, S.3
  • 11
    • 33747199933 scopus 로고    scopus 로고
    • Ubiquitin hydrolase Uch-l1 rescues β-Amyloid-induced decreases in synaptic function and contextual memory
    • doi: 10.1016/j.cell.2006.06.046
    • Gong B, Cao ZX, Zheng P (2006) Ubiquitin hydrolase Uch-l1 rescues β-Amyloid-induced decreases in synaptic function and contextual memory. Cell 126:775-788. doi: 10.1016/j.cell.2006.06.046
    • (2006) Cell , vol.126 , pp. 775-788
    • Gong, B.1    Cao, Z.X.2    Zheng, P.3
  • 12
    • 0028070372 scopus 로고
    • Production and characterization of monoclonal antibodies specific to multi-ubiquitin chains of polyubiquitinated proteins
    • doi: 10.1016/0014-5793(94)00647-4
    • Fujimuro M, Sawada H, Yokosawa H (1994) Production and characterization of monoclonal antibodies specific to multi-ubiquitin chains of polyubiquitinated proteins. FEBS Lett 349:173-180. doi: 10.1016/ 0014-5793(94)00647-4
    • (1994) FEBS Lett , vol.349 , pp. 173-180
    • Fujimuro, M.1    Sawada, H.2    Yokosawa, H.3
  • 13
    • 0032509216 scopus 로고    scopus 로고
    • Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors
    • doi: 10.1074/jbc.273.50.33741
    • Yoshida H, Haze K, Yanagi H et al (1998) Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors. J Biol Chem 273:33741-33749. doi: 10.1074/jbc.273.50.33741
    • (1998) J Biol Chem , vol.273 , pp. 33741-33749
    • Yoshida, H.1    Haze, K.2    Yanagi, H.3
  • 14
    • 1342305497 scopus 로고    scopus 로고
    • Caspase-12 and ER-stress-mediated apoptosis: The story so far
    • doi: 10.1196/annals.1299.032
    • Szegezdi E, Fitzgerald U, Samali A (2003) Caspase-12 and ER-stress-mediated apoptosis: The story so far. Ann N Y Acad Sci 1010:186-194. doi: 10.1196/annals.1299.032
    • (2003) Ann N Y Acad Sci , vol.1010 , pp. 186-194
    • Szegezdi, E.1    Fitzgerald, U.2    Samali, A.3
  • 15
    • 0035144493 scopus 로고    scopus 로고
    • Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state
    • doi: 10.1128/MCB.21.4.1249-1259.2001
    • McCullough KD, Martindale JL, Klotz LO et al (2001) Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state. Mol Cell Biol 21:1249-1259. doi: 10.1128/MCB.21.4.1249-1259.2001
    • (2001) Mol Cell Biol , vol.21 , pp. 1249-1259
    • McCullough, K.D.1    Martindale, J.L.2    Klotz, L.O.3
  • 16
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response
    • doi: 10.1128/MCB.23.21.7448-7459.2003
    • Lee AH, Iwakoshi NN, Glimcher LH (2003) XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol Cell Biol 23:7448-7459. doi: 10.1128/ MCB.23.21.7448-7459.2003
    • (2003) Mol Cell Biol , vol.23 , pp. 7448-7459
    • Lee, A.H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 17
    • 33846829603 scopus 로고    scopus 로고
    • Ire1 regulated XBP1 mRNA splicing is essential for the unfolded protein response (unfolded protein response) in Drosophila melanogaster
    • doi: 10.1016/j.bbrc.2007.01.056
    • Plongthongkum N, Kullawong N, Panyim S et al (2007) Ire1 regulated XBP1 mRNA splicing is essential for the unfolded protein response (unfolded protein response) in Drosophila melanogaster. Biochem Biophys Res Commun 354:789-794. doi: 10.1016/j.bbrc.2007.01.056
    • (2007) Biochem Biophys Res Commun , vol.354 , pp. 789-794
    • Plongthongkum, N.1    Kullawong, N.2    Panyim, S.3
  • 18
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • doi: 10.1016/S0092-8674(01)00611-0
    • Yoshida H, Matsui T, Yamamoto A et al (2001) XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 107:881-891. doi: 10.1016/ S0092-8674(01)00611-0
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3
  • 19
    • 0037083755 scopus 로고    scopus 로고
    • IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response
    • doi: 10.1101/gad.964702
    • Lee K, Tirasophon W, Shen X et al (2002) IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response. Genes Dev 16:452-466. doi: 10.1101/gad.964702
    • (2002) Genes Dev , vol.16 , pp. 452-466
    • Lee, K.1    Tirasophon, W.2    Shen, X.3
  • 20
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg
    • doi: 10.1016/S0896-6273(03)00606-8
    • Ciechanover A, Brundin P (2003) The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg. Neuron 40:427-446. doi: 10.1016/S0896-6273(03)00606-8
    • (2003) Neuron , vol.40 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 21
    • 33745070550 scopus 로고    scopus 로고
    • Involvement of endoplasmic reticulum stress on cell death induced by 6-OHDA
    • doi: 10.1007/s11064-006-9062-6
    • Akiko Y, Yasuhiro Y, Kiyokazu O et al (2006) Involvement of endoplasmic reticulum stress on cell death induced by 6-OHDA. Neurochem Res 31:657-664. doi: 10.1007/s11064-006-9062-6
    • (2006) Neurochem Res , vol.31 , pp. 657-664
    • Akiko, Y.1    Yasuhiro, Y.2    Kiyokazu, O.3
  • 22
    • 0347285295 scopus 로고    scopus 로고
    • A trip to the ER: Coping with stress
    • doi: 10.1016/j.tcb.2003.11.001
    • Rutkowski DT, Kaufman RJ (2004) A trip to the ER: Coping with stress. Trends Cell Biol 14:20-28. doi: 10.1016/j.tcb.2003.11.001
    • (2004) Trends Cell Biol , vol.14 , pp. 20-28
    • Rutkowski, D.T.1    Kaufman, R.J.2
  • 23
    • 0024427039 scopus 로고
    • Control of protein exit from the endoplasmic reticulum
    • doi: 10.1146/annurev.cb.05.110189.000245
    • Pelham HR (1989) Control of protein exit from the endoplasmic reticulum. Annu Rev Cell Biol 5:1-23. doi: 10.1146/annurev.cb.05.110189.000245
    • (1989) Annu Rev Cell Biol , vol.5 , pp. 1-23
    • Pelham, H.R.1
  • 24
    • 0032127493 scopus 로고    scopus 로고
    • Identification of novel stress-induced genes downstream of chop
    • doi: 10.1093/emboj/17.13.3619
    • Wang XZ, Kuroda M, Sok J et al (1998) Identification of novel stress-induced genes downstream of chop. EMBO J 17:3619-3630. doi: 10.1093/emboj/17.13.3619
    • (1998) EMBO J , vol.17 , pp. 3619-3630
    • Wang, X.Z.1    Kuroda, M.2    Sok, J.3
  • 25
    • 0033607801 scopus 로고    scopus 로고
    • Degradation of alpha-synuclein by proteasome
    • doi: 10.1074/jbc.274.48.33855
    • Bennett MC, Bishop JF, Leng Y et al (1999) Degradation of alpha-synuclein by proteasome. J Biol Chem 274:33855-33858. doi: 10.1074/ jbc.274.48.33855
    • (1999) J Biol Chem , vol.274 , pp. 33855-33858
    • Bennett, M.C.1    Bishop, J.F.2    Leng, Y.3
  • 26
    • 0034884622 scopus 로고    scopus 로고
    • Proteasomal inhibition leads to formation of ubiquitin/ alpha-synuclein-immunoreactive inclusions in PC12 cells
    • doi: 10.1046/j.1471-4159.2001.00474.x
    • Rideout HJ, Larsen KE, Sulzer D et al (2001) Proteasomal inhibition leads to formation of ubiquitin/alpha-synuclein-immunoreactive inclusions in PC12 cells. J Neurochem 78:899-908. doi: 10.1046/ j.1471-4159.2001.00474.x
    • (2001) J Neurochem , vol.78 , pp. 899-908
    • Rideout, H.J.1    Larsen, K.E.2    Sulzer, D.3
  • 27
    • 44749083979 scopus 로고    scopus 로고
    • Assembly-dependent endocytosis and clearance of extracellular alpha-synuclein
    • Epub ahead of print
    • Lee HJ, Suk JE, Bae EJ et al (2008) Assembly-dependent endocytosis and clearance of extracellular alpha-synuclein. Int J Biochem Cell Biol; Epub ahead of print
    • (2008) Int J Biochem Cell Biol
    • Lee, H.J.1    Suk, J.E.2    Bae, E.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.