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Volumn 29, Issue 3, 2008, Pages 317-333

The unfolded protein response: A pathway that links insulin demand with β-cell failure and diabetes

Author keywords

[No Author keywords available]

Indexed keywords

INSULIN; POLYPEPTIDE;

EID: 43549105167     PISSN: 0163769X     EISSN: 0163769X     Source Type: Journal    
DOI: 10.1210/er.2007-0039     Document Type: Review
Times cited : (464)

References (173)
  • 2
    • 4444318357 scopus 로고    scopus 로고
    • ER chaperone functions during normal and stress conditions
    • Ma Y, Hendershot LM 2004 ER chaperone functions during normal and stress conditions. J Chem Neuroanat 28:51-65
    • (2004) J Chem Neuroanat , vol.28 , pp. 51-65
    • Ma, Y.1    Hendershot, L.M.2
  • 3
    • 3142587059 scopus 로고    scopus 로고
    • Protein folding and quality control in the endoplasmic reticulum
    • Kleizen B, Braakman I 2004 Protein folding and quality control in the endoplasmic reticulum. Curr Opin Cell Biol 16:343-349
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 343-349
    • Kleizen, B.1    Braakman, I.2
  • 4
    • 8744302265 scopus 로고    scopus 로고
    • Catalysis of disulphide bond formation in the endoplasmic reticulum
    • Ellgaard L 2004 Catalysis of disulphide bond formation in the endoplasmic reticulum. Biochem Soc Trans 32:663-667
    • (2004) Biochem Soc Trans , vol.32 , pp. 663-667
    • Ellgaard, L.1
  • 5
    • 33745861722 scopus 로고    scopus 로고
    • Conservation and diversity of the cellular disulfide bond formation pathways
    • Sevier CS, Kaiser CA 2006 Conservation and diversity of the cellular disulfide bond formation pathways. Antioxid Redox Signal 8:797-811
    • (2006) Antioxid Redox Signal , vol.8 , pp. 797-811
    • Sevier, C.S.1    Kaiser, C.A.2
  • 6
    • 0037683407 scopus 로고    scopus 로고
    • Signals for COPII-dependent export from the ER: What's the ticket out?
    • Barlowe C 2003 Signals for COPII-dependent export from the ER: what's the ticket out? Trends Cell Biol 13:295-300
    • (2003) Trends Cell Biol , vol.13 , pp. 295-300
    • Barlowe, C.1
  • 8
    • 34248997838 scopus 로고    scopus 로고
    • N-Glycan structure dictates extension of protein folding or onset of disposal
    • Molinari M 2007 N-Glycan structure dictates extension of protein folding or onset of disposal. Nat Chem Biol 3:313-320
    • (2007) Nat Chem Biol , vol.3 , pp. 313-320
    • Molinari, M.1
  • 9
    • 33846821651 scopus 로고    scopus 로고
    • Misfolded proteins traffic from the endoplasmic reticulum (ER) due to ER export signals
    • Kincaid MM, Cooper AA 2007 Misfolded proteins traffic from the endoplasmic reticulum (ER) due to ER export signals. Mol Biol Cell 18:455-463
    • (2007) Mol Biol Cell , vol.18 , pp. 455-463
    • Kincaid, M.M.1    Cooper, A.A.2
  • 10
    • 0346331895 scopus 로고    scopus 로고
    • Stressed-out B cells? Plasma-cell differentiation and the unfolded protein response
    • Gass JN, Gunn KE, Sriburi R, Brewer JW 2004 Stressed-out B cells? Plasma-cell differentiation and the unfolded protein response. Trends Immunol 25:17-24
    • (2004) Trends Immunol , vol.25 , pp. 17-24
    • Gass, J.N.1    Gunn, K.E.2    Sriburi, R.3    Brewer, J.W.4
  • 11
    • 29244448729 scopus 로고    scopus 로고
    • XBP-1 is required for biogenesis of cellular secretory machinery of exocrine glands
    • Lee AH, Chu GC, Iwakoshi NN, Glimcher LH 2005 XBP-1 is required for biogenesis of cellular secretory machinery of exocrine glands. EMBO J 24:4368-4380
    • (2005) EMBO J , vol.24 , pp. 4368-4380
    • Lee, A.H.1    Chu, G.C.2    Iwakoshi, N.N.3    Glimcher, L.H.4
  • 12
    • 0026511824 scopus 로고
    • Overexpression of GRP78 mitigates stress induction of glucose regulated proteins and blocks secretion of selective proteins in Chinese hamster ovary cells
    • Dorner AJ, Wasley LC, Kaufman RJ 1992 Overexpression of GRP78 mitigates stress induction of glucose regulated proteins and blocks secretion of selective proteins in Chinese hamster ovary cells. EMBO J 11:1563-1571
    • (1992) EMBO J , vol.11 , pp. 1563-1571
    • Dorner, A.J.1    Wasley, L.C.2    Kaufman, R.J.3
  • 14
    • 0342506459 scopus 로고    scopus 로고
    • Differential fate of glycoproteins carrying a monoglucosylated form of truncated N-glycan in a new CHO line, MadIA214214, selected for a thermosensitive secretory defect
    • Ermonval M, Cacan R, Gorgas K, Haas IG, Verbert A, Buttin G 1997 Differential fate of glycoproteins carrying a monoglucosylated form of truncated N-glycan in a new CHO line, MadIA214214, selected for a thermosensitive secretory defect. J Cell Sci 110 (Pt 3):323-336
    • (1997) J Cell Sci , vol.110 , Issue.PART 3 , pp. 323-336
    • Ermonval, M.1    Cacan, R.2    Gorgas, K.3    Haas, I.G.4    Verbert, A.5    Buttin, G.6
  • 15
    • 0034968330 scopus 로고    scopus 로고
    • Diabetes mellitus and exocrine pancreatic dysfunction in perk-/- mice reveals a role for translational control in secretory cell survival
    • Harding HP, Zeng H, Zhang Y, Jungries R, Chung P, Plesken H, Sabatini DD, Ron D 2001 Diabetes mellitus and exocrine pancreatic dysfunction in perk-/- mice reveals a role for translational control in secretory cell survival. Mol Cell 7:1153-1163
    • (2001) Mol Cell , vol.7 , pp. 1153-1163
    • Harding, H.P.1    Zeng, H.2    Zhang, Y.3    Jungries, R.4    Chung, P.5    Plesken, H.6    Sabatini, D.D.7    Ron, D.8
  • 17
    • 0030820146 scopus 로고    scopus 로고
    • Accumulation of misfolded protein aggregates leads to the formation of Russell body-like dilated endoplasmic reticulum in yeast
    • Umebayashi K, Hirata A, Fukuda R, Horiuchi H, Ohta A, Takagi M 1997 Accumulation of misfolded protein aggregates leads to the formation of Russell body-like dilated endoplasmic reticulum in yeast. Yeast 13:1009-1020
    • (1997) Yeast , vol.13 , pp. 1009-1020
    • Umebayashi, K.1    Hirata, A.2    Fukuda, R.3    Horiuchi, H.4    Ohta, A.5    Takagi, M.6
  • 18
    • 34248187585 scopus 로고    scopus 로고
    • Dominant-negative effects of a novel mutated Ins2 allele causes early-onset diabetes and severe β-cell loss in Munich Ins2C95S mutant mice
    • Herbach N, Rathkolb B, Kemter E, Pichl L, Klaften M, de Angelis MH, Halban PA, Wolf E, Aigner B, Wanke R 2007 Dominant-negative effects of a novel mutated Ins2 allele causes early-onset diabetes and severe β-cell loss in Munich Ins2C95S mutant mice. Diabetes 56:1268-1276
    • (2007) Diabetes , vol.56 , pp. 1268-1276
    • Herbach, N.1    Rathkolb, B.2    Kemter, E.3    Pichl, L.4    Klaften, M.5    de Angelis, M.H.6    Halban, P.A.7    Wolf, E.8    Aigner, B.9    Wanke, R.10
  • 19
    • 0042318739 scopus 로고    scopus 로고
    • Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD)
    • McCracken AA, Brodsky JL 2003 Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD). Bioessays 25:868-877
    • (2003) Bioessays , vol.25 , pp. 868-877
    • McCracken, A.A.1    Brodsky, J.L.2
  • 21
    • 34247113888 scopus 로고    scopus 로고
    • Two endoplasmic reticulum-associated degradation (ERAD) systems for the novel variant of the mutant dysferlin: Ubiquitin/proteasome ERAD(I) and autophagy/ lysosome ERAD(II)
    • Fujita E, Kouroku Y, Isoai A, Kumagai H, Misutani A, Matsuda C, Hayashi YK, Momoi T 2007 Two endoplasmic reticulum-associated degradation (ERAD) systems for the novel variant of the mutant dysferlin: ubiquitin/proteasome ERAD(I) and autophagy/ lysosome ERAD(II). Hum Mol Genet 16:618-629
    • (2007) Hum Mol Genet , vol.16 , pp. 618-629
    • Fujita, E.1    Kouroku, Y.2    Isoai, A.3    Kumagai, H.4    Misutani, A.5    Matsuda, C.6    Hayashi, Y.K.7    Momoi, T.8
  • 22
    • 34047179973 scopus 로고    scopus 로고
    • Ubiquitinated-protein aggregates form in pancreatic β-cells during diabetes-induced oxidative stress and are regulated by autophagy
    • Kaniuk NA, Kiraly M, Bates H, Vranic M, Volchuk A, Brumell JH 2007 Ubiquitinated-protein aggregates form in pancreatic β-cells during diabetes-induced oxidative stress and are regulated by autophagy. Diabetes 56:930-939
    • (2007) Diabetes , vol.56 , pp. 930-939
    • Kaniuk, N.A.1    Kiraly, M.2    Bates, H.3    Vranic, M.4    Volchuk, A.5    Brumell, J.H.6
  • 24
    • 33646171699 scopus 로고    scopus 로고
    • Divergent roles of IRE1α and PERK in the unfolded protein response
    • Schroder M, Kaufman RJ 2006 Divergent roles of IRE1α and PERK in the unfolded protein response. Curr Mol Med 6:5-36
    • (2006) Curr Mol Med , vol.6 , pp. 5-36
    • Schroder, M.1    Kaufman, R.J.2
  • 25
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D, Walter P 2007 Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 8:519-529
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 26
    • 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, Ron D 2000 Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat Cell Biol 2:326-332
    • (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
  • 27
    • 0034637605 scopus 로고    scopus 로고
    • Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum
    • Liu CY, Schroder M, Kaufman RJ 2000 Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum. J Biol Chem 275:24881-24885
    • (2000) J Biol Chem , vol.275 , pp. 24881-24885
    • Liu, C.Y.1    Schroder, M.2    Kaufman, R.J.3
  • 28
    • 0036069980 scopus 로고    scopus 로고
    • ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals
    • Shen J, Chen X, Hendershot L, Prywes R 2002 ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev Cell 3:99-111
    • (2002) Dev Cell , vol.3 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 30
    • 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, Kaufman RJ 2006 Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response. Cell 124:587-599
    • (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
  • 32
    • 33745590436 scopus 로고    scopus 로고
    • Intrinsic capacities of molecular sensors of the unfolded protein response to sense alternate forms of endoplasmic reticulum stress
    • DuRose JB, Tam AB, Niwa M 2006 Intrinsic capacities of molecular sensors of the unfolded protein response to sense alternate forms of endoplasmic reticulum stress. Mol Biol Cell 17:3095-3107
    • (2006) Mol Biol Cell , vol.17 , pp. 3095-3107
    • DuRose, J.B.1    Tam, A.B.2    Niwa, M.3
  • 33
    • 26444442450 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress: Cell life and death decisions
    • Xu C, Bailly-Maitre B, Reed JC 2005 Endoplasmic reticulum stress: cell life and death decisions. J Clin Invest 115:2656-2664
    • (2005) J Clin Invest , vol.115 , pp. 2656-2664
    • Xu, C.1    Bailly-Maitre, B.2    Reed, J.C.3
  • 34
    • 0027324844 scopus 로고
    • Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
    • Cox JS, Shamu CE, Walter P 1993 Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 73:1197-1206
    • (1993) Cell , vol.73 , pp. 1197-1206
    • Cox, J.S.1    Shamu, C.E.2    Walter, P.3
  • 36
    • 18244405070 scopus 로고    scopus 로고
    • Shen X, Ellis RE, Lee K, Liu CY, Yang K, Solomon A, Yoshida H, Morimoto R, Kurnit DM, Mori K, Kaufman RJ 2001 Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development. Cell 107:893-903
    • Shen X, Ellis RE, Lee K, Liu CY, Yang K, Solomon A, Yoshida H, Morimoto R, Kurnit DM, Mori K, Kaufman RJ 2001 Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development. Cell 107:893-903
  • 37
    • 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
    • Yoshida H, Matsui T, Yamamoto A, Okada T, Mori K 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
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 39
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response
    • 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
    • (2003) Mol Cell Biol , vol.23 , pp. 7448-7459
    • Lee, A.H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 40
    • 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
    • Lee K, Tirasophon W, Shen X, Michalak M, Prywes R, Okada T, Yoshida H, Mori K, Kaufman RJ 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
    • (2002) Genes Dev , vol.16 , pp. 452-466
    • Lee, K.1    Tirasophon, W.2    Shen, X.3    Michalak, M.4    Prywes, R.5    Okada, T.6    Yoshida, H.7    Mori, K.8    Kaufman, R.J.9
  • 41
    • 31944450850 scopus 로고    scopus 로고
    • Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation
    • Oda Y, Okada T, Yoshida H, Kaufman RJ, Nagata K, Mori K 2006 Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation. J Cell Biol 172:383-393
    • (2006) J Cell Biol , vol.172 , pp. 383-393
    • Oda, Y.1    Okada, T.2    Yoshida, H.3    Kaufman, R.J.4    Nagata, K.5    Mori, K.6
  • 42
    • 30344434977 scopus 로고    scopus 로고
    • The secretory capacity of a cell depends on the efficiency of endoplasmic reticulum-associated degradation
    • Molinari M, Sitia R 2005 The secretory capacity of a cell depends on the efficiency of endoplasmic reticulum-associated degradation. Curr Top Microbiol Immunol 300:1-15
    • (2005) Curr Top Microbiol Immunol , vol.300 , pp. 1-15
    • Molinari, M.1    Sitia, R.2
  • 43
    • 33745893809 scopus 로고    scopus 로고
    • Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response
    • Hollien J, Weissman JS 2006 Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response. Science 313:104-107
    • (2006) Science , vol.313 , pp. 104-107
    • Hollien, J.1    Weissman, J.S.2
  • 44
    • 34147106529 scopus 로고    scopus 로고
    • Global profiling of genes modified by endoplasmic reticulum stress in pancreatic β cells reveals the early degradation of insulin mRNAs
    • Pirot P, Naamane N, Libert F, Magnusson NE, Orntoft TF, Cardozo AK, Eizirik DL 2007 Global profiling of genes modified by endoplasmic reticulum stress in pancreatic β cells reveals the early degradation of insulin mRNAs. Diabetologia 50:1006-1014
    • (2007) Diabetologia , vol.50 , pp. 1006-1014
    • Pirot, P.1    Naamane, N.2    Libert, F.3    Magnusson, N.E.4    Orntoft, T.F.5    Cardozo, A.K.6    Eizirik, D.L.7
  • 45
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • Haze K, Yoshida H, Yanagi H, Yura T, Mori K 1999 Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol Biol Cell 10:3787-3799
    • (1999) Mol Biol Cell , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 46
    • 33846223428 scopus 로고    scopus 로고
    • Role of disulfide bridges formed in the luminal domain of ATF6 in sensing endoplasmic reticulum stress
    • Nadanaka S, Okada T, Yoshida H, Mori K 2007 Role of disulfide bridges formed in the luminal domain of ATF6 in sensing endoplasmic reticulum stress. Mol Cell Biol 27:1027-1043
    • (2007) Mol Cell Biol , vol.27 , pp. 1027-1043
    • Nadanaka, S.1    Okada, T.2    Yoshida, H.3    Mori, K.4
  • 48
    • 34548172495 scopus 로고    scopus 로고
    • Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6α and XBP1
    • Yamamoto K, Sato T, Matsui T, Sato M, Okada T, Yoshida H, Harada A, Mori K 2007 Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6α and XBP1. Dev Cell 13:365-376
    • (2007) Dev Cell , vol.13 , pp. 365-376
    • Yamamoto, K.1    Sato, T.2    Matsui, T.3    Sato, M.4    Okada, T.5    Yoshida, H.6    Harada, A.7    Mori, K.8
  • 49
    • 9144228073 scopus 로고    scopus 로고
    • Differential contributions of ATF6 and XBP1 to the activation of endoplasmic reticulum stress-responsive cis-acting elements ERSE, UPRE and ERSE-II
    • Yamamoto K, Yoshida H, Kokame K, Kaufman RJ, Mori K 2004 Differential contributions of ATF6 and XBP1 to the activation of endoplasmic reticulum stress-responsive cis-acting elements ERSE, UPRE and ERSE-II. J Biochem (Tokyo) 136:343-350
    • (2004) J Biochem (Tokyo) , vol.136 , pp. 343-350
    • Yamamoto, K.1    Yoshida, H.2    Kokame, K.3    Kaufman, R.J.4    Mori, K.5
  • 50
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • Harding HP, Zhang Y, Ron D 1999 Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 397:271-274
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 51
    • 0033005366 scopus 로고    scopus 로고
    • Eukaryotic initiation factor eIF2
    • Kimball SR 1999 Eukaryotic initiation factor eIF2. Int J Biochem Cell Biol 31:25-29
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 25-29
    • Kimball, S.R.1
  • 52
    • 35848935017 scopus 로고    scopus 로고
    • Translational control and the unfolded protein response
    • Wek RC, Cavener DR 2007 Translational control and the unfolded protein response. Antioxid Redox Signal 9:2357-2371
    • (2007) Antioxid Redox Signal , vol.9 , pp. 2357-2371
    • Wek, R.C.1    Cavener, D.R.2
  • 53
    • 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
  • 56
    • 3843117589 scopus 로고    scopus 로고
    • Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells
    • Vattem KM, Wek RC 2004 Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells. Proc Natl Acad Sci USA 101:11269-11274
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 11269-11274
    • Vattem, K.M.1    Wek, R.C.2
  • 57
    • 0036713724 scopus 로고    scopus 로고
    • Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response
    • Okada T, Yoshida H, Akazawa R, Negishi M, Mori K 2002 Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response. Biochem J 366:585-594
    • (2002) Biochem J , vol.366 , pp. 585-594
    • Okada, T.1    Yoshida, H.2    Akazawa, R.3    Negishi, M.4    Mori, K.5
  • 58
    • 0033118409 scopus 로고    scopus 로고
    • Complexes containing activating transcription factor (ATF)/ cAMP-responsive- element-binding protein (CREB) interact with the CCAAT/enhancer-binding protein (C/EBP)-ATF composite site to regulate Gadd153 expression during the stress response
    • Fawcett TW, Martindale JL, Guyton KZ, Hai T, Holbrook NJ 1999 Complexes containing activating transcription factor (ATF)/ cAMP-responsive- element-binding protein (CREB) interact with the CCAAT/enhancer-binding protein (C/EBP)-ATF composite site to regulate Gadd153 expression during the stress response. Biochem J 339 (Pt 1):135-141
    • (1999) Biochem J , vol.339 , Issue.PART 1 , pp. 135-141
    • Fawcett, T.W.1    Martindale, J.L.2    Guyton, K.Z.3    Hai, T.4    Holbrook, N.J.5
  • 59
    • 0036314984 scopus 로고    scopus 로고
    • Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response
    • Ma Y, Brewer JW, Diehl JA, Hendershot LM 2002 Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response. J Mol Biol 318: 1351-1365
    • (2002) J Mol Biol , vol.318 , pp. 1351-1365
    • Ma, Y.1    Brewer, J.W.2    Diehl, J.A.3    Hendershot, L.M.4
  • 64
    • 0036175128 scopus 로고    scopus 로고
    • Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes
    • Oyadomari S, Koizumi A, Takeda K, Gotoh T, Akira S, Araki E, Mori M 2002 Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes. J Clin Invest 109:525-532
    • (2002) J Clin Invest , vol.109 , pp. 525-532
    • Oyadomari, S.1    Koizumi, A.2    Takeda, K.3    Gotoh, T.4    Akira, S.5    Araki, E.6    Mori, M.7
  • 66
    • 0035947778 scopus 로고    scopus 로고
    • Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2α
    • Novoa I, Zeng H, Harding HP, Ron D 2001 Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2α. J Cell Biol 153:1011-1022
    • (2001) J Cell Biol , vol.153 , pp. 1011-1022
    • Novoa, I.1    Zeng, H.2    Harding, H.P.3    Ron, D.4
  • 67
    • 0037416211 scopus 로고    scopus 로고
    • Stress-induced gene expression requires programmed recovery from translational repression
    • Novoa I, Zhang Y, Zeng H, Jungreis R, Harding HP, Ron D 2003 Stress-induced gene expression requires programmed recovery from translational repression. EMBO J 22:1180-1187
    • (2003) EMBO J , vol.22 , pp. 1180-1187
    • Novoa, I.1    Zhang, Y.2    Zeng, H.3    Jungreis, R.4    Harding, H.P.5    Ron, D.6
  • 68
    • 0041703031 scopus 로고    scopus 로고
    • The function of GADD34 is a recovery from a shutoff of protein synthesis induced by ER stress: Elucidation by GADD34-deficient mice
    • Kojima E, Takeuchi A, Haneda M, Yagi A, Hasegawa T, Yamaki K, Takeda K, Akira S, Shimokata K, Isobe K 2003 The function of GADD34 is a recovery from a shutoff of protein synthesis induced by ER stress: elucidation by GADD34-deficient mice. FASEB J 17: 1573-1575
    • (2003) FASEB J , vol.17 , pp. 1573-1575
    • Kojima, E.1    Takeuchi, A.2    Haneda, M.3    Yagi, A.4    Hasegawa, T.5    Yamaki, K.6    Takeda, K.7    Akira, S.8    Shimokata, K.9    Isobe, K.10
  • 69
    • 8544283103 scopus 로고    scopus 로고
    • CHOP is involved in endoplasmic reticulum stress-induced apoptosis by enhancing DR5 expression in human carcinoma cells
    • Yamaguchi H, Wang HG 2004 CHOP is involved in endoplasmic reticulum stress-induced apoptosis by enhancing DR5 expression in human carcinoma cells. J Biol Chem 279:45495-45502
    • (2004) J Biol Chem , vol.279 , pp. 45495-45502
    • Yamaguchi, H.1    Wang, H.G.2
  • 70
    • 17144417669 scopus 로고    scopus 로고
    • TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death
    • Ohoka N, Yoshii S, Hattori T, Onozaki K, Hayashi H 2005 TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death. EMBO J 24:1243-1255
    • (2005) EMBO J , vol.24 , pp. 1243-1255
    • Ohoka, N.1    Yoshii, S.2    Hattori, T.3    Onozaki, K.4    Hayashi, H.5
  • 71
    • 34250758642 scopus 로고    scopus 로고
    • Puthalakath H, O'Reilly LA, Gunn P, Lee L, Kelly PN, Huntington ND, Hughes PD, Michalak EM, McKimm-Breschkin J, Motoyama N, Gotoh T, Akira S, Bouillet P, Strasser A 2007 ER stress triggers apoptosis by activating BH3-only protein Bim. Cell 129: 1337-1349
    • Puthalakath H, O'Reilly LA, Gunn P, Lee L, Kelly PN, Huntington ND, Hughes PD, Michalak EM, McKimm-Breschkin J, Motoyama N, Gotoh T, Akira S, Bouillet P, Strasser A 2007 ER stress triggers apoptosis by activating BH3-only protein Bim. Cell 129: 1337-1349
  • 73
    • 0032940099 scopus 로고    scopus 로고
    • CHOP-dependent stress-inducible expression of a novel form of carbonic anhydrase VI
    • Sok J, Wang XZ, Batchvarova N, Kuroda M, Harding H, Ron D 1999 CHOP-dependent stress-inducible expression of a novel form of carbonic anhydrase VI. Mol Cell Biol 19:495-504
    • (1999) Mol Cell Biol , vol.19 , pp. 495-504
    • Sok, J.1    Wang, X.Z.2    Batchvarova, N.3    Kuroda, M.4    Harding, H.5    Ron, D.6
  • 74
    • 0035144493 scopus 로고    scopus 로고
    • Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state
    • McCullough KD, Martindale JL, Klotz LO, Aw TY, Holbrook NJ 2001 Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state. Mol Cell Biol 21:1249-1259
    • (2001) Mol Cell Biol , vol.21 , pp. 1249-1259
    • McCullough, K.D.1    Martindale, J.L.2    Klotz, L.O.3    Aw, T.Y.4    Holbrook, N.J.5
  • 75
    • 0034723235 scopus 로고    scopus 로고
    • Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
    • Urano F, Wang X, Bertolotti A, Zhang Y, Chung P, Harding HP, Ron D 2000 Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 287:664-666
    • (2000) Science , vol.287 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3    Zhang, Y.4    Chung, P.5    Harding, H.P.6    Ron, D.7
  • 76
    • 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, Ichijo H 2002 ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev 16:1345-1355
    • (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
  • 78
    • 0034001070 scopus 로고    scopus 로고
    • Activation of apoptosis signal-regulating kinase 1 (ASK1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin
    • Liu H, Nishitoh H, Ichijo H, Kyriakis JM 2000 Activation of apoptosis signal-regulating kinase 1 (ASK1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin. Mol Cell Biol 20:2198-2208
    • (2000) Mol Cell Biol , vol.20 , pp. 2198-2208
    • Liu, H.1    Nishitoh, H.2    Ichijo, H.3    Kyriakis, J.M.4
  • 79
    • 0036193169 scopus 로고    scopus 로고
    • Activation of apoptosis signal-regulating kinase 1 by the stress-induced activating phosphorylation of pre-formed oligomer
    • Tobiume K, Saitoh M, Ichijo H 2002 Activation of apoptosis signal-regulating kinase 1 by the stress-induced activating phosphorylation of pre-formed oligomer. J Cell Physiol 191:95-104
    • (2002) J Cell Physiol , vol.191 , pp. 95-104
    • Tobiume, K.1    Saitoh, M.2    Ichijo, H.3
  • 80
    • 33744800561 scopus 로고    scopus 로고
    • Tumour necrosis factor receptor 1 mediates endoplasmic reticulum stress-induced activation of the MAP kinase JNK
    • Yang Q, Kim YS, Lin Y, Lewis J, Neckers L, Liu ZG 2006 Tumour necrosis factor receptor 1 mediates endoplasmic reticulum stress-induced activation of the MAP kinase JNK. EMBO Rep 7:622-627
    • (2006) EMBO Rep , vol.7 , pp. 622-627
    • Yang, Q.1    Kim, Y.S.2    Lin, Y.3    Lewis, J.4    Neckers, L.5    Liu, Z.G.6
  • 81
    • 33645815074 scopus 로고    scopus 로고
    • Autocrine tumor necrosis factor α links endoplasmic reticulum stress to the membrane death receptor pathway through IRE1α-mediated NF-κB activation and down-regulation of TRAF2 expression
    • Hu P, Han Z, Couvillon AD, Kaufman RJ, Exton JH 2006 Autocrine tumor necrosis factor α links endoplasmic reticulum stress to the membrane death receptor pathway through IRE1α-mediated NF-κB activation and down-regulation of TRAF2 expression. Mol Cell Biol 26:3071-3084
    • (2006) Mol Cell Biol , vol.26 , pp. 3071-3084
    • Hu, P.1    Han, Z.2    Couvillon, A.D.3    Kaufman, R.J.4    Exton, J.H.5
  • 82
    • 26644450729 scopus 로고    scopus 로고
    • Tumor necrosis factor α (TNFα) induces the unfolded protein response (UPR) in a reactive oxygen species (ROS)-dependent fashion, and the UPR counteracts ROS accumulation by TNFα
    • Xue X, Piao JH, Nakajima A, Sakon-Komazawa S, Kojima Y, Mori K, Yagita H, Okumura K, Harding H, Nakano H 2005 Tumor necrosis factor α (TNFα) induces the unfolded protein response (UPR) in a reactive oxygen species (ROS)-dependent fashion, and the UPR counteracts ROS accumulation by TNFα. J Biol Chem 280:33917-33925
    • (2005) J Biol Chem , vol.280 , pp. 33917-33925
    • Xue, X.1    Piao, J.H.2    Nakajima, A.3    Sakon-Komazawa, S.4    Kojima, Y.5    Mori, K.6    Yagita, H.7    Okumura, K.8    Harding, H.9    Nakano, H.10
  • 83
    • 33748789479 scopus 로고    scopus 로고
    • Mediators of endoplasmic reticulum stress-induced apoptosis
    • Szegezdi E, Logue SE, Gorman AM, Samali A 2006 Mediators of endoplasmic reticulum stress-induced apoptosis. EMBO Rep 7:880-885
    • (2006) EMBO Rep , vol.7 , pp. 880-885
    • Szegezdi, E.1    Logue, S.E.2    Gorman, A.M.3    Samali, A.4
  • 84
    • 27744603772 scopus 로고    scopus 로고
    • Hayden MR, Tyagi SC, Kerklo MM, Nicolls MR 2005 Type 2 diabetes mellitus as a conformational disease. Jop 6:287-302
    • Hayden MR, Tyagi SC, Kerklo MM, Nicolls MR 2005 Type 2 diabetes mellitus as a conformational disease. Jop 6:287-302
  • 86
    • 2542581025 scopus 로고    scopus 로고
    • Diabetes due to a progressive defect in β-cell mass in rats transgenic for human islet amyloid polypeptide (HIP Rat): A new model for type 2 diabetes
    • Butler AE, Jang J, Gurlo T, Carty MD, Soeller WC, Butler PC 2004 Diabetes due to a progressive defect in β-cell mass in rats transgenic for human islet amyloid polypeptide (HIP Rat): a new model for type 2 diabetes. Diabetes 53:1509-1516
    • (2004) Diabetes , vol.53 , pp. 1509-1516
    • Butler, A.E.1    Jang, J.2    Gurlo, T.3    Carty, M.D.4    Soeller, W.C.5    Butler, P.C.6
  • 87
    • 33745586536 scopus 로고    scopus 로고
    • Islet amyloid polypeptide (IAPP) transgenic rodents as models for type 2 diabetes
    • Matveyenko AV, Butler PC 2006 Islet amyloid polypeptide (IAPP) transgenic rodents as models for type 2 diabetes. ILAR J 47:225-233
    • (2006) ILAR J , vol.47 , pp. 225-233
    • Matveyenko, A.V.1    Butler, P.C.2
  • 88
    • 37149012111 scopus 로고    scopus 로고
    • Induction of endoplasmic reticulum stress induced β cell apoptosis and accumulation of polyubiquitinated proteins by human islet amyloid polypeptide
    • Huang CJ, Haataja L, Gurlo T, Butler AE, Wu X, Soeller W, Butler PC 2007 Induction of endoplasmic reticulum stress induced β cell apoptosis and accumulation of polyubiquitinated proteins by human islet amyloid polypeptide. Am J Physiol Endocrinol Metab 293:E1656-E1662
    • (2007) Am J Physiol Endocrinol Metab , vol.293
    • Huang, C.J.1    Haataja, L.2    Gurlo, T.3    Butler, A.E.4    Wu, X.5    Soeller, W.6    Butler, P.C.7
  • 89
    • 34547638958 scopus 로고    scopus 로고
    • High expression rates of human islet amyloid polypeptide induce endoplasmic reticulum stress mediated β-cell apoptosis, a characteristic of humans with type 2 but not type 1 diabetes
    • Huang CJ, Lin CY, Haataja L, Gurlo T, Butler AE, Rizza RA, Butler PC 2007 High expression rates of human islet amyloid polypeptide induce endoplasmic reticulum stress mediated β-cell apoptosis, a characteristic of humans with type 2 but not type 1 diabetes. Diabetes 56:2016-2027
    • (2007) Diabetes , vol.56 , pp. 2016-2027
    • Huang, C.J.1    Lin, C.Y.2    Haataja, L.3    Gurlo, T.4    Butler, A.E.5    Rizza, R.A.6    Butler, P.C.7
  • 90
    • 0036091476 scopus 로고    scopus 로고
    • The PERK eukaryotic initiation factor 2 α kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreas
    • Zhang P, McGrath B, Li S, Frank A, Zambito F, Reinert J, Gannon M, Ma K, McNaughton K, Cavener DR 2002 The PERK eukaryotic initiation factor 2 α kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreas. Mol Cell Biol 22:3864-3874
    • (2002) Mol Cell Biol , vol.22 , pp. 3864-3874
    • Zhang, P.1    McGrath, B.2    Li, S.3    Frank, A.4    Zambito, F.5    Reinert, J.6    Gannon, M.7    Ma, K.8    McNaughton, K.9    Cavener, D.R.10
  • 91
    • 33751430251 scopus 로고    scopus 로고
    • PERK EIF2AK3 control of pancreatic β cell differentiation and proliferation is required for postnatal glucose homeostasis
    • Zhang W, Feng D, Li Y, Iida K, McGrath B, Cavener DR 2006 PERK EIF2AK3 control of pancreatic β cell differentiation and proliferation is required for postnatal glucose homeostasis. Cell Metab 4:491-497
    • (2006) Cell Metab , vol.4 , pp. 491-497
    • Zhang, W.1    Feng, D.2    Li, Y.3    Iida, K.4    McGrath, B.5    Cavener, D.R.6
  • 92
    • 0842266604 scopus 로고    scopus 로고
    • Oxidative protein folding in eukaryotes: Mechanisms and consequences
    • Tu BP, Weissman JS 2004 Oxidative protein folding in eukaryotes: mechanisms and consequences. J Cell Biol 164:341-346
    • (2004) J Cell Biol , vol.164 , pp. 341-346
    • Tu, B.P.1    Weissman, J.S.2
  • 93
    • 35848957485 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and oxidative stress: A vicious cycle or a double-edged sword
    • Malhotra J, Kaufman R 2007 Endoplasmic reticulum stress and oxidative stress: a vicious cycle or a double-edged sword. Antioxid Redox Signal 9:2277-2293
    • (2007) Antioxid Redox Signal , vol.9 , pp. 2277-2293
    • Malhotra, J.1    Kaufman, R.2
  • 94
    • 38049155818 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induces calcium-dependent permeability transition, mitochondrial outer membrane permeabilization and apoptosis
    • Deniaud A, Sharaf El Dein O, Maillier E, Poncet D, Kroemer G, Lemaire C, Brenner C 2007 Endoplasmic reticulum stress induces calcium-dependent permeability transition, mitochondrial outer membrane permeabilization and apoptosis. Oncogene 27:285-299
    • (2007) Oncogene , vol.27 , pp. 285-299
    • Deniaud, A.1    Sharaf, E.2    Dein, O.3    Maillier, E.4    Poncet, D.5    Kroemer, G.6    Lemaire, C.7    Brenner, C.8
  • 95
    • 26444593029 scopus 로고    scopus 로고
    • Mitochondria and endoplasmic reticulum: The lethal interorganelle cross-talk
    • Walter L, Hajnoczky G 2005 Mitochondria and endoplasmic reticulum: the lethal interorganelle cross-talk. J Bioenerg Biomembr 37:191-206
    • (2005) J Bioenerg Biomembr , vol.37 , pp. 191-206
    • Walter, L.1    Hajnoczky, G.2
  • 96
    • 34547607269 scopus 로고    scopus 로고
    • Bax inhibitor-1 regulates endoplasmic reticulum stress-associated reactive oxygen species and heme oxygenase-1 expression
    • Lee GH, Kim HK, Chae SW, Kim DS, Ha KC, Cuddy M, Kress C, Reed JC, Kim HR, Chae HJ 2007 Bax inhibitor-1 regulates endoplasmic reticulum stress-associated reactive oxygen species and heme oxygenase-1 expression. J Biol Chem 282:21618-21628
    • (2007) J Biol Chem , vol.282 , pp. 21618-21628
    • Lee, G.H.1    Kim, H.K.2    Chae, S.W.3    Kim, D.S.4    Ha, K.C.5    Cuddy, M.6    Kress, C.7    Reed, J.C.8    Kim, H.R.9    Chae, H.J.10
  • 97
    • 0029984682 scopus 로고    scopus 로고
    • Low antioxidant enzyme gene expression in pancreatic islets compared with various other mouse tissues
    • Lenzen S, Drinkgern J, Tiedge M 1996 Low antioxidant enzyme gene expression in pancreatic islets compared with various other mouse tissues. Free Radic Biol Med 20:463-466
    • (1996) Free Radic Biol Med , vol.20 , pp. 463-466
    • Lenzen, S.1    Drinkgern, J.2    Tiedge, M.3
  • 98
    • 0018831212 scopus 로고
    • Translational control of proinsulin synthesis by glucose
    • Itoh N, Okamoto H 1980 Translational control of proinsulin synthesis by glucose. Nature 283:100-102
    • (1980) Nature , vol.283 , pp. 100-102
    • Itoh, N.1    Okamoto, H.2
  • 99
    • 0039829851 scopus 로고
    • Glucose stimulates proinsulin biosynthesis by a dose-dependent recruitment of pancreatic β cells
    • Schuit FC, In't Veld PA, Pipeleers DG 1988 Glucose stimulates proinsulin biosynthesis by a dose-dependent recruitment of pancreatic β cells. Proc Natl Acad Sci USA 85:3865-3869
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 3865-3869
    • Schuit, F.C.1    In't Veld, P.A.2    Pipeleers, D.G.3
  • 100
    • 0142149134 scopus 로고    scopus 로고
    • Glucose-induced translational control of proinsulin biosynthesis is proportional to preproinsulin mRNA levels in islet β-cells but not regulated via a positive feedback of secreted insulin
    • Wicksteed B, Alarcon C, Briaud I, Lingohr MK, Rhodes CJ 2003 Glucose-induced translational control of proinsulin biosynthesis is proportional to preproinsulin mRNA levels in islet β-cells but not regulated via a positive feedback of secreted insulin. J Biol Chem 278:42080-42090
    • (2003) J Biol Chem , vol.278 , pp. 42080-42090
    • Wicksteed, B.1    Alarcon, C.2    Briaud, I.3    Lingohr, M.K.4    Rhodes, C.J.5
  • 101
    • 33847402319 scopus 로고    scopus 로고
    • A cis-element in the 5′ untranslated region of the preproinsulin mRNA (ppIGE) is required for glucose regulation of proinsulin translation
    • Wicksteed B, Uchizono Y, Alarcon C, McCuaig JF, Shalev A, Rhodes CJ 2007 A cis-element in the 5′ untranslated region of the preproinsulin mRNA (ppIGE) is required for glucose regulation of proinsulin translation. Cell Metab 5:221-227
    • (2007) Cell Metab , vol.5 , pp. 221-227
    • Wicksteed, B.1    Uchizono, Y.2    Alarcon, C.3    McCuaig, J.F.4    Shalev, A.5    Rhodes, C.J.6
  • 102
    • 0029071517 scopus 로고
    • Metabolic coupling factors in pancreatic β-cell signal transduction
    • Newgard CB, McGarry JD 1995 Metabolic coupling factors in pancreatic β-cell signal transduction. Annu Rev Biochem 64:689-719
    • (1995) Annu Rev Biochem , vol.64 , pp. 689-719
    • Newgard, C.B.1    McGarry, J.D.2
  • 103
    • 0026051640 scopus 로고
    • Measuring the balance between insulin synthesis and insulin release
    • Schuit FC, Kiekens R, Pipeleers DG 1991 Measuring the balance between insulin synthesis and insulin release. Biochem Biophys Res Commun 178:1182-1187
    • (1991) Biochem Biophys Res Commun , vol.178 , pp. 1182-1187
    • Schuit, F.C.1    Kiekens, R.2    Pipeleers, D.G.3
  • 105
    • 0032548831 scopus 로고    scopus 로고
    • Insulin mediates glucose-stimulated phosphorylation of PHAS-I by pancreatic β cells. An insulin-receptor mechanism for autoregulation of protein synthesis by translation
    • Xu G, Marshall CA, Lin TA, Kwon G, Munivenkatappa RB, Hill JR, Lawrence Jr JC, McDaniel ML 1998 Insulin mediates glucose-stimulated phosphorylation of PHAS-I by pancreatic β cells. An insulin-receptor mechanism for autoregulation of protein synthesis by translation. J Biol Chem 273:4485-4491
    • (1998) J Biol Chem , vol.273 , pp. 4485-4491
    • Xu, G.1    Marshall, C.A.2    Lin, T.A.3    Kwon, G.4    Munivenkatappa, R.B.5    Hill, J.R.6    Lawrence Jr, J.C.7    McDaniel, M.L.8
  • 106
    • 11144222577 scopus 로고    scopus 로고
    • Glucose-stimulated protein synthesis in pancreatic β-cells parallels an increase in the availability of the translational ternary complex (eIF2-GTP.Met-tRNAi) and the dephosphorylation of eIF2α
    • Gomez E, Powell ML, Greenman IC, Herbert TP 2004 Glucose-stimulated protein synthesis in pancreatic β-cells parallels an increase in the availability of the translational ternary complex (eIF2-GTP.Met-tRNAi) and the dephosphorylation of eIF2α. J Biol Chem 279:53937-53946
    • (2004) J Biol Chem , vol.279 , pp. 53937-53946
    • Gomez, E.1    Powell, M.L.2    Greenman, I.C.3    Herbert, T.P.4
  • 108
    • 34249933087 scopus 로고    scopus 로고
    • Acute nutrient regulation of the unfolded protein response and integrated stress response in cultured rat pancreatic islets
    • Elouil H, Bensellam M, Guiot Y, Vander Mierde D, Pascal SM, Schuit FC, Jonas JC 2007 Acute nutrient regulation of the unfolded protein response and integrated stress response in cultured rat pancreatic islets. Diabetologia 50:1442-1452
    • (2007) Diabetologia , vol.50 , pp. 1442-1452
    • Elouil, H.1    Bensellam, M.2    Guiot, Y.3    Vander Mierde, D.4    Pascal, S.M.5    Schuit, F.C.6    Jonas, J.C.7
  • 110
    • 34548317416 scopus 로고    scopus 로고
    • Chronic oxidative stress as a mechanism for glucose toxicity of the β cell in type 2 diabetes
    • Robertson R, Zhou H, Zhang T, Harmon JS 2007 Chronic oxidative stress as a mechanism for glucose toxicity of the β cell in type 2 diabetes. Cell Biochem Biophys 48:139-146
    • (2007) Cell Biochem Biophys , vol.48 , pp. 139-146
    • Robertson, R.1    Zhou, H.2    Zhang, T.3    Harmon, J.S.4
  • 112
    • 5644248079 scopus 로고    scopus 로고
    • Chronic oxidative stress as a central mechanism for glucose toxicity in pancreatic islet β cells in diabetes
    • Robertson RP 2004 Chronic oxidative stress as a central mechanism for glucose toxicity in pancreatic islet β cells in diabetes. J Biol Chem 279:42351-42354
    • (2004) J Biol Chem , vol.279 , pp. 42351-42354
    • Robertson, R.P.1
  • 114
    • 0031831420 scopus 로고    scopus 로고
    • Reconstitution of glucotoxic HIT-T15 cells with somatostatin transcription factor-1 partially restores insulin promoter activity
    • Harmon JS, Tanaka Y, Olson LK, Robertson RP 1998 Reconstitution of glucotoxic HIT-T15 cells with somatostatin transcription factor-1 partially restores insulin promoter activity. Diabetes 47: 900-904
    • (1998) Diabetes , vol.47 , pp. 900-904
    • Harmon, J.S.1    Tanaka, Y.2    Olson, L.K.3    Robertson, R.P.4
  • 115
  • 116
    • 15744379018 scopus 로고    scopus 로고
    • Oxidative stress-mediated, post-translational loss of MafA protein as a contributing mechanism to loss of insulin gene expression in glucotoxic β cells
    • Harmon JS, Stein R, Robertson RP 2005 Oxidative stress-mediated, post-translational loss of MafA protein as a contributing mechanism to loss of insulin gene expression in glucotoxic β cells. J Biol Chem 280:11107-11113
    • (2005) J Biol Chem , vol.280 , pp. 11107-11113
    • Harmon, J.S.1    Stein, R.2    Robertson, R.P.3
  • 117
    • 0348230942 scopus 로고    scopus 로고
    • Glutaredoxins: Glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system
    • Fernandes AP, Holmgren A 2004 Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system. Antioxid Redox Signal 6:63-74
    • (2004) Antioxid Redox Signal , vol.6 , pp. 63-74
    • Fernandes, A.P.1    Holmgren, A.2
  • 118
    • 21344456969 scopus 로고    scopus 로고
    • Ivarsson R, Quintens R, Dejonghe S, Tsukamoto K, in't Veld P, Renstrom E, Schuit FC 2005 Redox control of exocytosis: regulatory role of NADPH, thioredoxin, and glutaredoxin. Diabetes 54: 2132-2142
    • Ivarsson R, Quintens R, Dejonghe S, Tsukamoto K, in't Veld P, Renstrom E, Schuit FC 2005 Redox control of exocytosis: regulatory role of NADPH, thioredoxin, and glutaredoxin. Diabetes 54: 2132-2142
  • 119
    • 9244231766 scopus 로고    scopus 로고
    • Free fatty acids and cytokines induce pancreatic β-cell apoptosis by different mechanisms: Role of nuclear factor-κB and endoplasmic reticulum stress
    • Kharroubi I, Ladriere L, Cardozo AK, Dogusan Z, Cnop M, Eizirik DL 2004 Free fatty acids and cytokines induce pancreatic β-cell apoptosis by different mechanisms: role of nuclear factor-κB and endoplasmic reticulum stress. Endocrinology 145:5087-5096
    • (2004) Endocrinology , vol.145 , pp. 5087-5096
    • Kharroubi, I.1    Ladriere, L.2    Cardozo, A.K.3    Dogusan, Z.4    Cnop, M.5    Eizirik, D.L.6
  • 120
    • 19944432792 scopus 로고    scopus 로고
    • Cytokines downregulate the sarcoendoplasmic reticulum pump Ca2+ ATPase 2b and deplete endoplasmic reticulum Ca2+, leading to induction of endoplasmic reticulum stress in pancreatic β-cells
    • Cardozo AK, Ortis F, Storling J, Feng YM, Rasschaert J, Tonnesen M, Van Eylen F, Mandrup-Poulsen T, Herchuelz A, Eizirik DL 2005 Cytokines downregulate the sarcoendoplasmic reticulum pump Ca2+ ATPase 2b and deplete endoplasmic reticulum Ca2+, leading to induction of endoplasmic reticulum stress in pancreatic β-cells. Diabetes 54:452-461
    • (2005) Diabetes , vol.54 , pp. 452-461
    • Cardozo, A.K.1    Ortis, F.2    Storling, J.3    Feng, Y.M.4    Rasschaert, J.5    Tonnesen, M.6    Van Eylen, F.7    Mandrup-Poulsen, T.8    Herchuelz, A.9    Eizirik, D.L.10
  • 122
    • 33646533330 scopus 로고    scopus 로고
    • Interferon-γ potentiates endoplasmic reticulum stress-induced death by reducing pancreatic β cell defense mechanisms
    • Pirot P, Eizirik DL, Cardozo AK 2006 Interferon-γ potentiates endoplasmic reticulum stress-induced death by reducing pancreatic β cell defense mechanisms. Diabetologia 49:1229-1236
    • (2006) Diabetologia , vol.49 , pp. 1229-1236
    • Pirot, P.1    Eizirik, D.L.2    Cardozo, A.K.3
  • 123
    • 38449122843 scopus 로고    scopus 로고
    • The role of nitric oxide and the unfolded protein response in cytokine induced β-cell death
    • Chambers KT, Unverferth JA, Weber SM, Wek RC, Urano F, Corbett JA 2008 The role of nitric oxide and the unfolded protein response in cytokine induced β-cell death. Diabetes 57:124-132
    • (2008) Diabetes , vol.57 , pp. 124-132
    • Chambers, K.T.1    Unverferth, J.A.2    Weber, S.M.3    Wek, R.C.4    Urano, F.5    Corbett, J.A.6
  • 125
  • 127
    • 0015288961 scopus 로고
    • Infancy-onset diabetes mellitus and multiple epiphyseal dysplasia
    • Wolcott CD, Rallison ML 1972 Infancy-onset diabetes mellitus and multiple epiphyseal dysplasia. J Pediatr 80:292-297
    • (1972) J Pediatr , vol.80 , pp. 292-297
    • Wolcott, C.D.1    Rallison, M.L.2
  • 128
    • 0020030070 scopus 로고
    • Wolcott-Rallison syndrome: Diabetes mellitus and spondyloepiphyseal dysplasia
    • Stoss H, Pesch HJ, Pontz B, Otten A, Spranger J 1982 Wolcott-Rallison syndrome: diabetes mellitus and spondyloepiphyseal dysplasia. Eur J Pediatr 138:120-129
    • (1982) Eur J Pediatr , vol.138 , pp. 120-129
    • Stoss, H.1    Pesch, H.J.2    Pontz, B.3    Otten, A.4    Spranger, J.5
  • 130
    • 0033914612 scopus 로고    scopus 로고
    • Wolcott-Rallison syndrome: A case with endocrine and exocrine pancreatic deficiency and pancreatic hypotrophy
    • Castelnau P, Le Merrer M, Diatloff-Zito C, Marquis E, Tete MJ, Robert JJ 2000 Wolcott-Rallison syndrome: a case with endocrine and exocrine pancreatic deficiency and pancreatic hypotrophy. Eur J Pediatr 159:631-633
    • (2000) Eur J Pediatr , vol.159 , pp. 631-633
    • Castelnau, P.1    Le Merrer, M.2    Diatloff-Zito, C.3    Marquis, E.4    Tete, M.J.5    Robert, J.J.6
  • 131
    • 0034425698 scopus 로고    scopus 로고
    • EIF2AK3, encoding translation initiation factor 2-α kinase 3, is mutated in patients with Wolcott-Rallison syndrome
    • Delepine M, Nicolino M, Barrett T, Golamaully M, Lathrop GM, Julier C 2000 EIF2AK3, encoding translation initiation factor 2-α kinase 3, is mutated in patients with Wolcott-Rallison syndrome. Nat Genet 25:406-409
    • (2000) Nat Genet , vol.25 , pp. 406-409
    • Delepine, M.1    Nicolino, M.2    Barrett, T.3    Golamaully, M.4    Lathrop, G.M.5    Julier, C.6
  • 134
    • 0027949937 scopus 로고
    • The 58,000-dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteins
    • Lee TG, Tang N, Thompson S, Miller J, Katze MG 1994 The 58,000-dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteins. Mol Cell Biol 14:2331-2342
    • (1994) Mol Cell Biol , vol.14 , pp. 2331-2342
    • Lee, T.G.1    Tang, N.2    Thompson, S.3    Miller, J.4    Katze, M.G.5
  • 135
    • 0037058574 scopus 로고    scopus 로고
    • Control of PERK eIF2α kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK
    • Yan W, Frank CL, Korth MJ, Sopher BL, Novoa I, Ron D, Katze MG 2002 Control of PERK eIF2α kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK. Proc Natl Acad Sci USA 99:15920-15925
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 15920-15925
    • Yan, W.1    Frank, C.L.2    Korth, M.J.3    Sopher, B.L.4    Novoa, I.5    Ron, D.6    Katze, M.G.7
  • 139
  • 140
    • 0035032066 scopus 로고    scopus 로고
    • WFS1/wolframin mutations, Wolfram syndrome, and associated diseases
    • Khanim F, Kirk J, Latif F, Barrett TG 2001 WFS1/wolframin mutations, Wolfram syndrome, and associated diseases. Hum Mutat 17:357-367
    • (2001) Hum Mutat , vol.17 , pp. 357-367
    • Khanim, F.1    Kirk, J.2    Latif, F.3    Barrett, T.G.4
  • 146
    • 14944371187 scopus 로고    scopus 로고
    • The unfolded protein response sensor IRE1α is required at two distinct steps in B cell lymphopoiesis
    • Zhang K, Wong HN, Song B, Miller CN, Scheuner D, Kaufman RJ 2005 The unfolded protein response sensor IRE1α is required at two distinct steps in B cell lymphopoiesis. J Clin Invest 115:268-281
    • (2005) J Clin Invest , vol.115 , pp. 268-281
    • Zhang, K.1    Wong, H.N.2    Song, B.3    Miller, C.N.4    Scheuner, D.5    Kaufman, R.J.6
  • 150
    • 42449104952 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and inflammation in obesity and type 2 diabetes
    • discussion 94-98, 162-163
    • Hotamisligi GS 2007 Endoplasmic reticulum stress and inflammation in obesity and type 2 diabetes. Novartis Foundation Symp. 286:86-94; discussion 94-98, 162-163, 196-203
    • (2007) Novartis Foundation Symp , vol.286
    • Hotamisligi, G.S.1
  • 151
    • 33644774734 scopus 로고    scopus 로고
    • Association of amino acid variants in the activating transcription factor 6 gene (ATF6) on 1q21-q23 with type 2 diabetes in Pima Indians
    • Thameem F, Farook VS, Bogardus C, Prochazka M 2006 Association of amino acid variants in the activating transcription factor 6 gene (ATF6) on
    • (2006) Diabetes , vol.55 , pp. 839-842
    • Thameem, F.1    Farook, V.S.2    Bogardus, C.3    Prochazka, M.4
  • 156
    • 33749233991 scopus 로고    scopus 로고
    • The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response
    • Zhou J, Liu CY, Back SH, Clark RL, Peisach D, Xu Z, Kaufman RJ 2006 The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response. Proc Natl Acad Sci USA 103:14343-14348
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 14343-14348
    • Zhou, J.1    Liu, C.Y.2    Back, S.H.3    Clark, R.L.4    Peisach, D.5    Xu, Z.6    Kaufman, R.J.7
  • 157
    • 37649004940 scopus 로고    scopus 로고
    • Structure of the dual enzyme ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing
    • Lee KP, Dey M, Neculai D, Cao C, Dever TE, Sicheri F 2008 Structure of the dual enzyme ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing. Cell 132:89-100
    • (2008) Cell , vol.132 , pp. 89-100
    • Lee, K.P.1    Dey, M.2    Neculai, D.3    Cao, C.4    Dever, T.E.5    Sicheri, F.6
  • 158
    • 33846265304 scopus 로고    scopus 로고
    • Isofagomine-and 2,5-anhydro-2,5-imino-D-glucitol-based glucocerebrosidase pharmacological chaperones for Gaucher disease intervention
    • Yu Z, Sawkar AR, Whalen LJ, Wong CH, Kelly JW 2007 Isofagomine-and 2,5-anhydro-2,5-imino-D-glucitol-based glucocerebrosidase pharmacological chaperones for Gaucher disease intervention. J Med Chem 50:94-100
    • (2007) J Med Chem , vol.50 , pp. 94-100
    • Yu, Z.1    Sawkar, A.R.2    Whalen, L.J.3    Wong, C.H.4    Kelly, J.W.5
  • 159
    • 33745167938 scopus 로고    scopus 로고
    • Protein-misfolding diseases and chaperone-based therapeutic approaches
    • Chaudhuri TK, Paul S 2006 Protein-misfolding diseases and chaperone-based therapeutic approaches. FEBS J 273:1331-1349
    • (2006) FEBS J , vol.273 , pp. 1331-1349
    • Chaudhuri, T.K.1    Paul, S.2
  • 160
    • 34347218245 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced death of mouse embryonic fibroblasts requires the intrinsic pathway of apoptosis
    • Masud A, Mohapatra A, Lakhani SA, Ferrandino A, Hakem R, Flavell RA 2007 Endoplasmic reticulum stress-induced death of mouse embryonic fibroblasts requires the intrinsic pathway of apoptosis. J Biol Chem 282:14132-14139
    • (2007) J Biol Chem , vol.282 , pp. 14132-14139
    • Masud, A.1    Mohapatra, A.2    Lakhani, S.A.3    Ferrandino, A.4    Hakem, R.5    Flavell, R.A.6
  • 161
    • 33750914846 scopus 로고    scopus 로고
    • Exendin 4 controls insulin production in rat islet β cells predominantly by potentiation of glucose-stimulated proinsulin biosynthesis at the translational level
    • Alarcon C, Wicksteed B, Rhodes CJ 2006 Exendin 4 controls insulin production in rat islet β cells predominantly by potentiation of glucose-stimulated proinsulin biosynthesis at the translational level. Diabetologia 49:2920-2929
    • (2006) Diabetologia , vol.49 , pp. 2920-2929
    • Alarcon, C.1    Wicksteed, B.2    Rhodes, C.J.3
  • 162
    • 0036113116 scopus 로고    scopus 로고
    • Vitamin C supplementation decreases insulin glycation and improves glucose homeostasis in obese hyperglycemic (ob/ob) mice
    • Abdel-Wahab YH, O'Harte FP, Mooney MH, Barnett CR, Flatt PR 2002 Vitamin C supplementation decreases insulin glycation and improves glucose homeostasis in obese hyperglycemic (ob/ob) mice. Metabolism 51:514-517
    • (2002) Metabolism , vol.51 , pp. 514-517
    • Abdel-Wahab, Y.H.1    O'Harte, F.P.2    Mooney, M.H.3    Barnett, C.R.4    Flatt, P.R.5
  • 164
    • 14844327760 scopus 로고    scopus 로고
    • Reactive oxygen species promote TNFα-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases
    • Kamata H, Honda S, Maeda S, Chang L, Hirata H, Karin M 2005 Reactive oxygen species promote TNFα-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases. Cell 120:649-661
    • (2005) Cell , vol.120 , pp. 649-661
    • Kamata, H.1    Honda, S.2    Maeda, S.3    Chang, L.4    Hirata, H.5    Karin, M.6
  • 166
    • 0347683430 scopus 로고    scopus 로고
    • Metallothionein protects islets from hypoxia and extends islet graft survival by scavenging most kinds of reactive oxygen species
    • Li X, Chen H, Epstein PN 2004 Metallothionein protects islets from hypoxia and extends islet graft survival by scavenging most kinds of reactive oxygen species. J Biol Chem 279:765-771
    • (2004) J Biol Chem , vol.279 , pp. 765-771
    • Li, X.1    Chen, H.2    Epstein, P.N.3
  • 168
    • 0037315583 scopus 로고    scopus 로고
    • Gene transfer of manganese superoxide dismutase extends islet graft function in a mouse model of autoimmune diabetes
    • Bertera S, Crawford ML, Alexander AM, Papworth GD, Watkins SC, Robbins PD, Trucco M 2003 Gene transfer of manganese superoxide dismutase extends islet graft function in a mouse model of autoimmune diabetes. Diabetes 52:387-393
    • (2003) Diabetes , vol.52 , pp. 387-393
    • Bertera, S.1    Crawford, M.L.2    Alexander, A.M.3    Papworth, G.D.4    Watkins, S.C.5    Robbins, P.D.6    Trucco, M.7
  • 169
    • 35448946819 scopus 로고    scopus 로고
    • Role of Endoplasmic reticulum calcium disequilibria in the mechanism of homocysteineinduced ER stress
    • Dickhout JG, Sood SK, Austin RC 2007 Role of Endoplasmic reticulum calcium disequilibria in the mechanism of homocysteineinduced ER stress. Antioxid Redox Signal 9:1863-1874
    • (2007) Antioxid Redox Signal , vol.9 , pp. 1863-1874
    • Dickhout, J.G.1    Sood, S.K.2    Austin, R.C.3
  • 171
    • 40549093016 scopus 로고    scopus 로고
    • Ethanol promotes endoplasmic reticulum stress-induced neuronal death: Involvement of oxidative stress
    • Chen G, Ma C, Bower KA, Shi X, Ke Z, Luo J 2008 Ethanol promotes endoplasmic reticulum stress-induced neuronal death: Involvement of oxidative stress. J Neurosci Res 86:937-946
    • (2008) J Neurosci Res , vol.86 , pp. 937-946
    • Chen, G.1    Ma, C.2    Bower, K.A.3    Shi, X.4    Ke, Z.5    Luo, J.6
  • 173
    • 0036319579 scopus 로고    scopus 로고
    • Polymorphisms in the oxygen-regulated protein 150 gene (ORP150) are associated with insulin resistance in Pima Indians
    • Kovacs P, Yang X, Permana PA, Bogardus C, Baier LJ 2002 Polymorphisms in the oxygen-regulated protein 150 gene (ORP150) are associated with insulin resistance in Pima Indians. Diabetes 51:1618-1621
    • (2002) Diabetes , vol.51 , pp. 1618-1621
    • Kovacs, P.1    Yang, X.2    Permana, P.A.3    Bogardus, C.4    Baier, L.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.