메뉴 건너뛰기




Volumn 25, Issue 11, 2005, Pages 2793-2802

The disulfide isomerase Grp58 is a protective factor against prion neurotoxicity

Author keywords

Apoptosis; Caspase 12; Endoplasmic reticulum stress; Grp58; Prion; Scrapie; Transmissible spongiform encephalopathy

Indexed keywords

CASPASE 12; CHAPERONE; DISULFIDE; GLUCOSE REGULATED PROTEIN; GLUCOSE REGULATED PROTEIN 58; ISOMERASE; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 15244361681     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.4090-04.2005     Document Type: Article
Times cited : (188)

References (37)
  • 2
    • 0037064026 scopus 로고    scopus 로고
    • Stimulation of PrP(C) retrograde transport toward the endoplasmic reticulum increases accumulation of PrP(Sc) in prion-infected cells
    • Beranger F, Mange A, Goud B, Lehmann S (2002) Stimulation of PrP(C) retrograde transport toward the endoplasmic reticulum increases accumulation of PrP(Sc) in prion-infected cells. J Biol Chem 277:38972-38977.
    • (2002) J Biol Chem , vol.277 , pp. 38972-38977
    • Beranger, F.1    Mange, A.2    Goud, B.3    Lehmann, S.4
  • 7
    • 0242492706 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress is a determinant of retrovirus-induced spongiform neurodegeneration
    • Dimcheff DE, Askovic S, Baker AH, Johnson-Fowler C, Portis JL (2003b) Endoplasmic reticulum stress is a determinant of retrovirus-induced spongiform neurodegeneration. J Virol 77:12617-12629.
    • (2003) J Virol , vol.77 , pp. 12617-12629
    • Dimcheff, D.E.1    Askovic, S.2    Baker, A.H.3    Johnson-Fowler, C.4    Portis, J.L.5
  • 8
    • 0035736259 scopus 로고    scopus 로고
    • Organelle-specific initiation of cell death pathways
    • Ferri KF, Kroemer G (2001) Organelle-specific initiation of cell death pathways. Nat Cell Biol 3:E255-E263.
    • (2001) Nat Cell Biol , vol.3
    • Ferri, K.F.1    Kroemer, G.2
  • 10
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding HP, Novoa I, Zhang Y, Zeng H, Wek R, Schapira M, Ron D (2000) Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol Cell 6:1099-1108.
    • (2000) Mol Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5    Schapira, M.6    Ron, D.7
  • 11
    • 0142105406 scopus 로고    scopus 로고
    • Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein
    • Hetz C, Russelakis-Carneiro M, Maundrell K, Castilla J, Soto C (2003) Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein. EMBO J 22:5435-5445.
    • (2003) EMBO J , vol.22 , pp. 5435-5445
    • Hetz, C.1    Russelakis-Carneiro, M.2    Maundrell, K.3    Castilla, J.4    Soto, C.5
  • 12
    • 0038143287 scopus 로고    scopus 로고
    • Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons
    • 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.
    • (2003) J Biol Chem , vol.278 , pp. 19367-19377
    • Holtz, W.A.1    O'Malley, K.L.2
  • 13
    • 0035838390 scopus 로고    scopus 로고
    • Thy-1 binds to integrin beta(3) on astrocytes and triggers formation of focal contact sites
    • Leyton L, Schneider P, Labra CV, Ruegg C, Hetz CA, Quest AF, Bron C (2001) Thy-1 binds to integrin beta(3) on astrocytes and triggers formation of focal contact sites. Curr Biol 11:1028-1038.
    • (2001) Curr Biol , vol.11 , pp. 1028-1038
    • Leyton, L.1    Schneider, P.2    Labra, C.V.3    Ruegg, C.4    Hetz, C.A.5    Quest, A.F.6    Bron, C.7
  • 14
    • 0347753252 scopus 로고    scopus 로고
    • 2+-dependent redox modulation of SERCA 2b by ERp57
    • 2+-dependent redox modulation of SERCA 2b by ERp57. J Cell Biol 164:35-46.
    • (2004) J Cell Biol , vol.164 , pp. 35-46
    • Li, Y.1    Camacho, P.2
  • 16
    • 0037446508 scopus 로고    scopus 로고
    • In vitro amplification of protease-resistant prion protein requires free sulfhydryl groups
    • Lucassen R, Nishina K, Supattapone S (2003) In vitro amplification of protease-resistant prion protein requires free sulfhydryl groups. Biochemistry 42:4127-4135.
    • (2003) Biochemistry , vol.42 , pp. 4127-4135
    • Lucassen, R.1    Nishina, K.2    Supattapone, S.3
  • 17
    • 0033203242 scopus 로고    scopus 로고
    • De novo generation of a PrPSc-like conformation in living cells
    • Ma J, Lindquist S (1999) De novo generation of a PrPSc-like conformation in living cells. Nat Cell Biol 1:358-361.
    • (1999) Nat Cell Biol , vol.1 , pp. 358-361
    • Ma, J.1    Lindquist, S.2
  • 19
    • 0034610792 scopus 로고    scopus 로고
    • Caspases find a new place to hide
    • Mehmet H (2000) Caspases find a new place to hide. Nature 403:29-30.
    • (2000) Nature , vol.403 , pp. 29-30
    • Mehmet, H.1
  • 20
    • 0036877146 scopus 로고    scopus 로고
    • 2+ signaling and calcium binding chaperones of the endoplasmic reticulum
    • 2+ signaling and calcium binding chaperones of the endoplasmic reticulum. Cell Calcium 32:269-278.
    • (2002) Cell Calcium , vol.32 , pp. 269-278
    • Michalak, M.1    Robert Parker, J.M.2    Opas, M.3
  • 21
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa T, Zhu H, Morishima N, Li E, Xu J, Yankner BA, Yuan J (2000) Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 403:98-103.
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 24
    • 0033214088 scopus 로고    scopus 로고
    • 2+-binding and antiapoptotic properties is a novel proteolytic target of calpain during etoposide-induced apoptosis
    • 2+-binding and antiapoptotic properties is a novel proteolytic target of calpain during etoposide-induced apoptosis. J Biol Chem 274:28476-28483.
    • (1999) J Biol Chem , vol.274 , pp. 28476-28483
    • Reddy, R.K.1    Lu, J.2    Lee, A.S.3
  • 25
    • 0037184107 scopus 로고    scopus 로고
    • Changes in the glycosylation pattern of prion protein in murine scrapie. Implications for the mechanism of neurodegeneration in prion diseases
    • Russelakis-Carneiro M, Saborio GP, Anderes L, Soto C (2002) Changes in the glycosylation pattern of prion protein in murine scrapie. Implications for the mechanism of neurodegeneration in prion diseases. J Biol Chem 277:36872-36877.
    • (2002) J Biol Chem , vol.277 , pp. 36872-36877
    • Russelakis-Carneiro, M.1    Saborio, G.P.2    Anderes, L.3    Soto, C.4
  • 26
    • 0037010141 scopus 로고    scopus 로고
    • Transport of protein toxins into cells: Pathways used by ricin, cholera toxin and Shiga toxin
    • Sandvig K, van Deurs B (2002) Transport of protein toxins into cells: pathways used by ricin, cholera toxin and Shiga toxin. FEBS Lett 529:49-53.
    • (2002) FEBS Lett , vol.529 , pp. 49-53
    • Sandvig, K.1    Van Deurs, B.2
  • 27
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum protein factory
    • Sitia R, Braakman I (2003) Quality control in the endoplasmic reticulum protein factory. Nature 426:891-894.
    • (2003) Nature , vol.426 , pp. 891-894
    • Sitia, R.1    Braakman, I.2
  • 28
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • Soto C (2003) Unfolding the role of protein misfolding in neurodegenerative diseases. Nat Rev Neurosci 4:49-60.
    • (2003) Nat Rev Neurosci , vol.4 , pp. 49-60
    • Soto, C.1
  • 30
    • 0344443678 scopus 로고    scopus 로고
    • EndoPDI, a novel protein-disulfide isomerase-like protein that is preferentially expressed in endothelial cells acts as a stress survival factor
    • Sullivan DC, Huminiecki L, Moore JW, Boyle JJ, Poulsom R, Creamer D, Barker J, Bicknell R (2003) EndoPDI, a novel protein-disulfide isomerase-like protein that is preferentially expressed in endothelial cells acts as a stress survival factor. J Biol Chem 278:47079-47088.
    • (2003) J Biol Chem , vol.278 , pp. 47079-47088
    • Sullivan, D.C.1    Huminiecki, L.2    Moore, J.W.3    Boyle, J.J.4    Poulsom, R.5    Creamer, D.6    Barker, J.7    Bicknell, R.8
  • 31
    • 0034615941 scopus 로고    scopus 로고
    • Up-regulation of protein-disulfide isomerase in response to hypoxia/brain ischemia and its protective effect against apoptotic cell death
    • Tanaka S, Uehara T, Nomura Y (2000) Up-regulation of protein-disulfide isomerase in response to hypoxia/brain ischemia and its protective effect against apoptotic cell death. J Biol Chem 275:10388-10393.
    • (2000) J Biol Chem , vol.275 , pp. 10388-10393
    • Tanaka, S.1    Uehara, T.2    Nomura, Y.3
  • 32
  • 33
    • 0037191074 scopus 로고    scopus 로고
    • Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Erol
    • Tsai B, Rapoport TA (2002) Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Erol. J Cell Biol 159:207-216.
    • (2002) J Cell Biol , vol.159 , pp. 207-216
    • Tsai, B.1    Rapoport, T.A.2
  • 34
    • 0036836665 scopus 로고    scopus 로고
    • Proteins of the PDI family: Unpredicted non-ER locations and functions
    • Turano C, Coppari S, Altieri F, Ferraro A (2002) Proteins of the PDI family: unpredicted non-ER locations and functions. J Cell Physiol 193:154-163.
    • (2002) J Cell Physiol , vol.193 , pp. 154-163
    • Turano, C.1    Coppari, S.2    Altieri, F.3    Ferraro, A.4
  • 36
    • 0035957929 scopus 로고    scopus 로고
    • Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress
    • Yoneda T, Imaizumi K, Oono K, Yui D, Gomi F, Katayama T, Tohyama M (2001) Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress. J Biol Chem 276:13935-13940.
    • (2001) J Biol Chem , vol.276 , pp. 13935-13940
    • Yoneda, T.1    Imaizumi, K.2    Oono, K.3    Yui, D.4    Gomi, F.5    Katayama, T.6    Tohyama, M.7
  • 37
    • 0037121618 scopus 로고    scopus 로고
    • Overexpressed protein disulfide isomerase in brains of patients with sporadic Creutzfeldt-Jakob disease
    • Yoo BC, Krapfenbauer K, Cairns N, Belay G, Bajo M, Lubec G (2002) Overexpressed protein disulfide isomerase in brains of patients with sporadic Creutzfeldt-Jakob disease. Neurosci Lett 334:196-200.
    • (2002) Neurosci Lett , vol.334 , pp. 196-200
    • Yoo, B.C.1    Krapfenbauer, K.2    Cairns, N.3    Belay, G.4    Bajo, M.5    Lubec, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.