메뉴 건너뛰기




Volumn 30, Issue 4, 2016, Pages 446-454

CHOP contributes to, but is not the only mediator of, IAPP induced β-cell apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; AMYLIN; BIM PROTEIN; CCAAT ENHANCER BINDING PROTEIN HOMOLOGOUS PROTEIN; INOSITOL REQUIRING ENZYME 1 PHOSPHORYLATED TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; PROTEIN; PROTEIN BCL 2; STRESS ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG; DDIT3 PROTEIN, MOUSE; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153;

EID: 84964294550     PISSN: 08888809     EISSN: 19449917     Source Type: Journal    
DOI: 10.1210/me.2015-1255     Document Type: Article
Times cited : (38)

References (40)
  • 2
    • 0025287442 scopus 로고
    • Effects of meal ingestion on plasma amylin concentration in NIDDM and nondiabetic humans
    • Butler PC, Chou J, Carter WB, et al. Effects of meal ingestion on plasma amylin concentration in NIDDM and nondiabetic humans. Diabetes. 1990;39:752-756.
    • (1990) Diabetes , vol.39 , pp. 752-756
    • Butler, P.C.1    Chou, J.2    Carter, W.B.3
  • 4
    • 0029901739 scopus 로고    scopus 로고
    • Spontaneous diabetes mellitus in transgenic mice expressing human islet amyloid polypeptide
    • Janson J, Soeller WC, Roche PC, et al. Spontaneous diabetes mellitus in transgenic mice expressing human islet amyloid polypeptide. Proc Natl Acad Sci USA. 1996;93:7283-7288.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7283-7288
    • Janson, J.1    Soeller, W.C.2    Roche, P.C.3
  • 5
    • 0042822112 scopus 로고    scopus 로고
    • Increased β-Cell apoptosis prevents adaptive increase in β-Cell mass in mouse model of type 2 diabetes: Evidence for role of islet amyloid formation rather than direct action of amyloid
    • Butler AE, Janson J, Soeller WC, Butler PC. Increased β-Cell apoptosis prevents adaptive increase in β-Cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes. 2003;52:2304-2314.
    • (2003) Diabetes , vol.52 , pp. 2304-2314
    • Butler, A.E.1    Janson, J.2    Soeller, W.C.3    Butler, P.C.4
  • 6
    • 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. 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. 2004;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
  • 7
    • 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, et al. Induction of endoplasmic reticulum stress-induced β-Cell apoptosis and accumulation of polyubiquitinated proteins by human islet amyloid polypeptide. Am J Physiol Endocrinol Metab. 2007;293:E1656-E1662.
    • (2007) Am J Physiol Endocrinol Metab , vol.293 , pp. E1656-E1662
    • Huang, C.J.1    Haataja, L.2    Gurlo, T.3
  • 8
    • 76149102617 scopus 로고    scopus 로고
    • Evidence for proteotoxicity in β cells in type 2 diabetes: Toxic islet amyloid polypeptide oligomers form intracellularly in the secretory pathway
    • Gurlo T, Ryazantsev S, Huang CJ, et al. Evidence for proteotoxicity in β cells in type 2 diabetes: toxic islet amyloid polypeptide oligomers form intracellularly in the secretory pathway. Am J Pathol. 2010;176:861-869.
    • (2010) Am J Pathol , vol.176 , pp. 861-869
    • Gurlo, T.1    Ryazantsev, S.2    Huang, C.J.3
  • 9
    • 34248160486 scopus 로고    scopus 로고
    • Toxic human islet amyloid polypeptide (H-IAPP) oligomers are intracellular, and vaccination to induce anti-toxic oligomer antibodies does not prevent h-IAPP-induced β-Cell apoptosis in h-IAPP transgenic mice
    • Lin CY, Gurlo T, Kayed R, et al. Toxic human islet amyloid polypeptide (h-IAPP) oligomers are intracellular, and vaccination to induce anti-toxic oligomer antibodies does not prevent h-IAPP-induced β-Cell apoptosis in h-IAPP transgenic mice. Diabetes. 2007; 56:1324-13
    • (2007) Diabetes , vol.56 , pp. 1324-1413
    • Lin, C.Y.1    Gurlo, T.2    Kayed, R.3
  • 10
    • 61449123871 scopus 로고    scopus 로고
    • Oxidative stress is induced by islet amyloid formation and time-dependently mediates amyloid-induced β cell apoptosis
    • Zraika S, Hull RL, Udayasankar J, et al. Oxidative stress is induced by islet amyloid formation and time-dependently mediates amyloid-induced β cell apoptosis. Diabetologia. 2009;52:626-635.
    • (2009) Diabetologia , vol.52 , pp. 626-635
    • Zraika, S.1    Hull, R.L.2    Udayasankar, J.3
  • 11
    • 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, et al. 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. 2007;56:2016-2027.
    • (2007) Diabetes , vol.56 , pp. 2016-2027
    • Huang, C.J.1    Lin, C.Y.2    Haataja, L.3
  • 12
    • 84861905329 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and type 2 diabetes
    • Back SH, Kaufman RJ. Endoplasmic reticulum stress and type 2 diabetes. Annu Rev Biochem. 2012;81:767-793.
    • (2012) Annu Rev Biochem , vol.81 , pp. 767-793
    • Back, S.H.1    Kaufman, R.J.2
  • 13
    • 0036175128 scopus 로고    scopus 로고
    • Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes
    • Oyadomari S, Koizumi A, Takeda K, et al. Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes. J Clin Invest. 2002;109:525-532.
    • (2002) J Clin Invest , vol.109 , pp. 525-532
    • Oyadomari, S.1    Koizumi, A.2    Takeda, K.3
  • 14
    • 79951672803 scopus 로고    scopus 로고
    • Human-IAPP disrupts the autophagy/ lysosomal pathway in pancreatic β-Cells: Protective role of p62-positive cytoplasmic inclusions
    • Rivera JF, Gurlo T, Daval M, et al. Human-IAPP disrupts the autophagy/ lysosomal pathway in pancreatic β-Cells: protective role of p62-positive cytoplasmic inclusions. Cell Death Differ. 2011;18: 415-426.
    • (2011) Cell Death Differ , vol.18 , pp. 415-426
    • Rivera, J.F.1    Gurlo, T.2    Daval, M.3
  • 15
    • 84905460021 scopus 로고    scopus 로고
    • Human IAPP-induced pancreatic β cell toxicity and its regulation by autophagy
    • Shigihara N, Fukunaka A, Hara A, et al. Human IAPP-induced pancreatic β cell toxicity and its regulation by autophagy. J Clin Invest. 2014;124:3634-3644.
    • (2014) J Clin Invest , vol.124 , pp. 3634-3644
    • Shigihara, N.1    Fukunaka, A.2    Hara, A.3
  • 16
    • 84905492806 scopus 로고    scopus 로고
    • Amyloidogenic peptide oligomer accumulation in autophagy-deficient _ cells induces diabetes
    • Kim J, Cheon H, Jeong YT, et al. Amyloidogenic peptide oligomer accumulation in autophagy-deficient _ cells induces diabetes. J Clin Invest. 2014;124:3311-3324.
    • (2014) J Clin Invest , vol.124 , pp. 3311-3324
    • Kim, J.1    Cheon, H.2    Jeong, Y.T.3
  • 17
    • 84905460026 scopus 로고    scopus 로고
    • Autophagy defends pancreatic β cells from human islet amyloid polypeptideinduced toxicity
    • Rivera JF, Costes S, Gurlo T, Glabe CG, Butler PC. Autophagy defends pancreatic β cells from human islet amyloid polypeptideinduced toxicity. J Clin Invest. 2014;124:3489-3500.
    • (2014) J Clin Invest , vol.124 , pp. 3489-3500
    • Rivera, J.F.1    Costes, S.2    Gurlo, T.3    Glabe, C.G.4    Butler, P.C.5
  • 18
    • 84897052585 scopus 로고    scopus 로고
    • Dual role forCHOPin the crosstalk between autophagy and apoptosis to determine cell fate in response to amino acid deprivation
    • B’chir W, Chaveroux C, Carraro V, et al. Dual role forCHOPin the crosstalk between autophagy and apoptosis to determine cell fate in response to amino acid deprivation. Cell Signal. 2014;26:1385-1391.
    • (2014) Cell Signal , vol.26 , pp. 1385-1391
    • B’Chir, W.1    Chaveroux, C.2    Carraro, V.3
  • 19
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D, Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol. 2007;8:519-529.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 20
    • 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. Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2α. J Cell Biol. 2001;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
  • 21
    • 0041315834 scopus 로고    scopus 로고
    • Delineation of a negative feedback regulatory loop that controls protein translation during endoplasmic reticulum stress
    • Ma Y, Hendershot LM. Delineation of a negative feedback regulatory loop that controls protein translation during endoplasmic reticulum stress. J Biol Chem. 2003;278:34864-34873.
    • (2003) J Biol Chem , vol.278 , pp. 34864-34873
    • Ma, Y.1    Hendershot, L.M.2
  • 22
    • 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, et al. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science. 2000;287:664-666.
    • (2000) Science , vol.287 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3
  • 23
    • 84873038379 scopus 로고    scopus 로고
    • β-Cell failure in type 2 diabetes: A case of asking too much of too few?
    • Costes S, Langen R, Gurlo T, Matveyenko AV, Butler PC. β-Cell failure in type 2 diabetes: a case of asking too much of too few? Diabetes. 2013;62:327-335.
    • (2013) Diabetes , vol.62 , pp. 327-335
    • Costes, S.1    Langen, R.2    Gurlo, T.3    Matveyenko, A.V.4    Butler, P.C.5
  • 24
    • 84873527000 scopus 로고    scopus 로고
    • Aggregation of islet amyloid polypeptide: From physical chemistry to cell biology
    • Cao P, Abedini A, Raleigh DP. Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology. Curr Opin Struct Biol. 2013;23:82-89.
    • (2013) Curr Opin Struct Biol , vol.23 , pp. 82-89
    • Cao, P.1    Abedini, A.2    Raleigh, D.P.3
  • 26
    • 0025881320 scopus 로고
    • Sequences of islet amyloid polypeptide precursors of an Old World monkey, the pig-tailed macaque (Macaca nemestrina), and the dog (Canis familiaris)
    • Ohagi S, Nishi M, Bell GI, Ensinck JW, Steiner DF. Sequences of islet amyloid polypeptide precursors of an Old World monkey, the pig-tailed macaque (Macaca nemestrina), and the dog (Canis familiaris). Diabetologia. 1991;34:555-558.
    • (1991) Diabetologia , vol.34 , pp. 555-558
    • Ohagi, S.1    Nishi, M.2    Bell, G.I.3    Ensinck, J.W.4    Steiner, D.F.5
  • 27
    • 0029818742 scopus 로고    scopus 로고
    • Missense mutation of amylin gene (S20G) in Japanese NIDDM patients
    • Sakagashira S, Sanke T, Hanabusa T, et al. Missense mutation of amylin gene (S20G) in Japanese NIDDM patients. Diabetes. 1996; 45:1279-1281.
    • (1996) Diabetes , vol.45 , pp. 1279-1281
    • Sakagashira, S.1    Sanke, T.2    Hanabusa, T.3
  • 30
    • 26244456414 scopus 로고    scopus 로고
    • ER stress and SREBP-1 activation are implicated in β-Cell glucolipotoxicity
    • Wang H, Kouri G, Wollheim CB. ER stress and SREBP-1 activation are implicated in β-Cell glucolipotoxicity. J Cell Sci. 2005;118: 3905-3915.
    • (2005) J Cell Sci , vol.118 , pp. 3905-3915
    • Wang, H.1    Kouri, G.2    Wollheim, C.B.3
  • 31
    • 84938739110 scopus 로고    scopus 로고
    • High-fat diet increases autophagic flux in pancreatic β cells in vivo and ex vivo in mice
    • Chu KY, O’Reilly L, Ramm G, Biden TJ. High-fat diet increases autophagic flux in pancreatic β cells in vivo and ex vivo in mice. Diabetologia. 2015;58:2074-2078.
    • (2015) Diabetologia , vol.58 , pp. 2074-2078
    • Chu, K.Y.1    O’Reilly, L.2    Ramm, G.3    Biden, T.J.4
  • 32
    • 84999488593 scopus 로고    scopus 로고
    • Targeting molecules to medicine with mTOR, autophagy, and neurodegenerative disorders
    • Oct 15, [Epub ahead of print]
    • Maiese K. Targeting molecules to medicine with mTOR, autophagy, and neurodegenerative disorders. Br J Clin Pharmacol. 2015 Oct 15. doi: 10.1111/bcp.12804. [Epub ahead of print].
    • (2015) Br J Clin Pharmacol
    • Maiese, K.1
  • 33
    • 84856735212 scopus 로고    scopus 로고
    • CJUN N-terminal kinase (JNK) activation mediates islet amyloid-induced β cell apoptosis in cultured human islet amyloid polypeptide transgenic mouse islets
    • Subramanian SL, Hull RL, Zraika S, Aston-Mourney K, Udayasankar J, Kahn SE. cJUN N-terminal kinase (JNK) activation mediates islet amyloid-induced β cell apoptosis in cultured human islet amyloid polypeptide transgenic mouse islets. Diabetologia. 2012;55: 166-174.
    • (2012) Diabetologia , vol.55 , pp. 166-174
    • Subramanian, S.L.1    Hull, R.L.2    Zraika, S.3    Aston-Mourney, K.4    Udayasankar, J.5    Kahn, S.E.6
  • 34
    • 84863484585 scopus 로고    scopus 로고
    • Perk-dependent repression of miR-106b-25 cluster is required for ER stress-induced apoptosis
    • Gupta S, Read DE, Deepti A, et al. Perk-dependent repression of miR-106b-25 cluster is required for ER stress-induced apoptosis. Cell Death Dis. 2012;3:e333.
    • (2012) Cell Death Dis , vol.3
    • Gupta, S.1    Read, D.E.2    Deepti, A.3
  • 35
    • 78751490442 scopus 로고    scopus 로고
    • β-Cell dysfunctional ERAD/ ubiquitin/proteasome system in type 2 diabetes mediated by islet amyloid polypeptide-induced UCH-L1 deficiency
    • Costes S, Huang CJ, Gurlo T, et al. β-Cell dysfunctional ERAD/ ubiquitin/proteasome system in type 2 diabetes mediated by islet amyloid polypeptide-induced UCH-L1 deficiency. Diabetes. 2011; 60:227-238.
    • (2011) Diabetes , vol.60 , pp. 227-238
    • Costes, S.1    Huang, C.J.2    Gurlo, T.3
  • 36
    • 84903635601 scopus 로고    scopus 로고
    • UCHL1 deficiency exacerbates human islet amyloid polypeptide toxicity in β-Cells: Evidence of interplay between the ubiquitin/proteasome system and autophagy
    • Costes S, Gurlo T, Rivera JF, Butler PC. UCHL1 deficiency exacerbates human islet amyloid polypeptide toxicity in β-Cells: evidence of interplay between the ubiquitin/proteasome system and autophagy. Autophagy. 2014;10:1004-1014.
    • (2014) Autophagy , vol.10 , pp. 1004-1014
    • Costes, S.1    Gurlo, T.2    Rivera, J.F.3    Butler, P.C.4
  • 37
    • 84939152599 scopus 로고    scopus 로고
    • Transcription factor ATF4 induces NLRP1 inflammasome expression during endoplasmic reticulum stress
    • D’Osualdo A, Anania VG, Yu K, et al. Transcription factor ATF4 induces NLRP1 inflammasome expression during endoplasmic reticulum stress. PLoS One. 2015;10:e0130635.
    • (2015) Plos One , vol.10
    • D’Osualdo, A.1    Anania, V.G.2    Yu, K.3
  • 38
    • 77956958947 scopus 로고    scopus 로고
    • Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1β in type 2 diabetes
    • Masters SL, Dunne A, Subramanian SL, et al. Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1β in type 2 diabetes. Nat Immunol. 2010;11:897-904.
    • (2010) Nat Immunol , vol.11 , pp. 897-904
    • Masters, S.L.1    Dunne, A.2    Subramanian, S.L.3
  • 40
    • 84940557532 scopus 로고    scopus 로고
    • Antioxidants complement the requirement for protein chaperone function to maintain β-Cell function and glucose homeostasis
    • Han J, Song B, Kim J, et al. Antioxidants complement the requirement for protein chaperone function to maintain β-Cell function and glucose homeostasis. Diabetes. 2015;64:2892-2904.
    • (2015) Diabetes , vol.64 , pp. 2892-2904
    • Han, J.1    Song, B.2    Kim, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.