메뉴 건너뛰기




Volumn 14, Issue 4, 2011, Pages 367-373

Endoplasmic reticulum stress and glucose homeostasis

Author keywords

diabetes; insulin resistance; nonalcoholic fatty liver disease; transcription factors; unfolded protein response

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; ACTIVATING TRANSCRIPTION FACTOR 6; BUTYRIC ACID; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; FATTY ACID; GLUCOSE REGULATED PROTEIN 78; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; INITIATION FACTOR 2ALPHA; ORPHAN NUCLEAR RECEPTOR; PHOSPHOENOLPYRUVATE CARBOXYKINASE (GTP); PHOSPHOPROTEIN PHOSPHATASE 2A; PROTEIN IRE1; RECEPTOR FOR ACTIVATED C KINASE 1; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; STEROL REGULATORY ELEMENT BINDING PROTEIN 1; TAUROURSODEOXYCHOLIC ACID; TRANSCRIPTION FACTOR FKHR; VERY LOW DENSITY LIPOPROTEIN; X BOX BINDING PROTEIN 1;

EID: 79959263110     PISSN: 13631950     EISSN: 14736519     Source Type: Journal    
DOI: 10.1097/MCO.0b013e32834778d4     Document Type: Review
Times cited : (27)

References (62)
  • 1
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • DOI 10.1038/nrm2199, PII NRM2199
    • Ron D, Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 2007; 8:519-529. (Pubitemid 46985379)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.7 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 2
    • 77950343252 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the inflammatory basis of metabolic disease
    • Hotamisligil GS. Endoplasmic reticulum stress and the inflammatory basis of metabolic disease. Cell 2010; 140:900-917.
    • (2010) Cell , vol.140 , pp. 900-917
    • Hotamisligil, G.S.1
  • 3
    • 79952708723 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in liver disease
    • Malhi H, Kaufman RJ. Endoplasmic reticulum stress in liver disease. J Hepatol 2011; 54:795-809.
    • (2011) J Hepatol , vol.54 , pp. 795-809
    • Malhi, H.1    Kaufman, R.J.2
  • 4
    • 33645815074 scopus 로고    scopus 로고
    • Autocrine tumor necrosis factor alpha links endoplasmic reticulum stress to the membrane death receptor pathway through IRE1alpha-mediated NF-kappaB activation and down-regulation of TRAF2 expression
    • Hu P, Han Z, Couvillon AD, et al. Autocrine tumor necrosis factor alpha links endoplasmic reticulum stress to the membrane death receptor pathway through IRE1alpha-mediated NF-kappaB activation and down-regulation of TRAF2 expression. Mol Cell Biol 2006; 26:3071-3084.
    • (2006) Mol Cell Biol , vol.26 , pp. 3071-3084
    • Hu, P.1    Han, Z.2    Couvillon, A.D.3
  • 5
    • 0034723235 scopus 로고    scopus 로고
    • Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
    • DOI 10.1126/science.287.5453.664
    • 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. (Pubitemid 30070916)
    • (2000) Science , vol.287 , Issue.5453 , 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
  • 6
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic- reticulum-resident kinase
    • DOI 10.1038/16729
    • Harding HP, Zhang Y, Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 1999; 397:271-274. (Pubitemid 29051178)
    • (1999) Nature , vol.397 , Issue.6716 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 7
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding HP, Novoa I, Zhang Y, et al. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol Cell 2000; 6:1099-1108.
    • (2000) Mol Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3
  • 8
    • 75749108288 scopus 로고    scopus 로고
    • Double-stranded RNA-dependent protein kinase links pathogen sensing with stress and metabolic homeostasis
    • Nakamura T, Furuhashi M, Li P, et al. Double-stranded RNA-dependent protein kinase links pathogen sensing with stress and metabolic homeostasis. Cell 2010; 140:338-348.
    • (2010) Cell , vol.140 , pp. 338-348
    • Nakamura, T.1    Furuhashi, M.2    Li, P.3
  • 9
    • 33751069967 scopus 로고    scopus 로고
    • Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins
    • Rutkowski DT, Arnold SM, Miller CN, et al. Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins. PLoS Biol 2006; 4:e374.
    • (2006) PLoS Biol , vol.4
    • Rutkowski, D.T.1    Arnold, S.M.2    Miller, C.N.3
  • 10
    • 55849096988 scopus 로고    scopus 로고
    • Chop deletion reduces oxidative stress, improves beta cell function, and promotes cell survival in multiple mouse models of diabetes
    • Song B, Scheuner D, Ron D, et al. Chop deletion reduces oxidative stress, improves beta cell function, and promotes cell survival in multiple mouse models of diabetes. J Clin Invest 2008; 118:3378-3389.
    • (2008) J Clin Invest , vol.118 , pp. 3378-3389
    • Song, B.1    Scheuner, D.2    Ron, D.3
  • 12
    • 0043133837 scopus 로고    scopus 로고
    • Phosphorylation of the α subunit of eukaryotic initiation factor 2 is required for activation of NF-κB in response to diverse cellular stresses
    • DOI 10.1128/MCB.23.16.5651-5663.2003
    • Jiang HY, Wek SA, McGrath BC, et al. Phosphorylation of the alpha subunit of eukaryotic initiation factor 2 is required for activation of NF-kappaB in response to diverse cellular stresses. Mol Cell Biol 2003; 23:5651-5663. (Pubitemid 36951330)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.16 , pp. 5651-5663
    • Jiang, H.-Y.1    Wek, S.A.2    McGrath, B.C.3    Scheuner, D.4    Kaufman, R.J.5    Cavener, D.R.6    Wek, R.C.7
  • 13
    • 69849109361 scopus 로고    scopus 로고
    • Activation of the Akt-NF-kappaB pathway by subtilase cytotoxin through the ATF6 branch of the unfolded protein response
    • Yamazaki H, Hiramatsu N, Hayakawa K, et al. Activation of the Akt-NF-kappaB pathway by subtilase cytotoxin through the ATF6 branch of the unfolded protein response. J Immunol 2009; 183:1480-1487.
    • (2009) J Immunol , vol.183 , pp. 1480-1487
    • Yamazaki, H.1    Hiramatsu, N.2    Hayakawa, K.3
  • 17
    • 53849133093 scopus 로고    scopus 로고
    • An update on lipotoxic endoplasmic reticulum stress in pancreatic beta-cells
    • Cnop M, Igoillo-Esteve M, Cunha DA, et al. An update on lipotoxic endoplasmic reticulum stress in pancreatic beta-cells. Biochem Soc Trans 2008; .36. (Pt 5):909-915.
    • (2008) Biochem Soc Trans , vol.36 , Issue.PART 5 , pp. 909-915
    • Cnop, M.1    Igoillo-Esteve, M.2    Cunha, D.A.3
  • 18
    • 33747849846 scopus 로고    scopus 로고
    • Regulation of insulin biosynthesis in pancreatic beta cells by an endoplasmic reticulum-resident protein kinase IRE1
    • DOI 10.1016/j.cmet.2006.07.007, PII S1550413106002701
    • Lipson KL, Fonseca SG, Ishigaki S, et al. Regulation of insulin biosynthesis in pancreatic beta cells by an endoplasmic reticulum-resident protein kinase IRE1. Cell Metab 2006; 4:245-254. (Pubitemid 44283955)
    • (2006) Cell Metabolism , vol.4 , Issue.3 , pp. 245-254
    • Lipson, K.L.1    Fonseca, S.G.2    Ishigaki, S.3    Nguyen, L.X.4    Foss, E.5    Bortell, R.6    Rossini, A.A.7    Urano, F.8
  • 19
    • 77951645463 scopus 로고    scopus 로고
    • A crucial role for RACK1 in the regulation of glucose-stimulated IRE1alpha activation in pancreatic beta cells
    • Qiu Y, Mao T, Zhang Y, et al. A crucial role for RACK1 in the regulation of glucose-stimulated IRE1alpha activation in pancreatic beta cells. Sci Signal 2010; 3:ra7.
    • (2010) Sci Signal , vol.3
    • Qiu, Y.1    Mao, T.2    Zhang, Y.3
  • 20
    • 77958590030 scopus 로고    scopus 로고
    • IRE1alpha disruption causes histological abnormality of exocrine tissues, increase of blood glucose level, and decrease of serum immunoglobulin level
    • Iwawaki T, Akai R, Kohno K. IRE1alpha disruption causes histological abnormality of exocrine tissues, increase of blood glucose level, and decrease of serum immunoglobulin level. PLoS One 2010; 5:e13052.
    • (2010) PLoS One , vol.5
    • Iwawaki, T.1    Akai, R.2    Kohno, K.3
  • 22
    • 45749114525 scopus 로고    scopus 로고
    • The role of IRE1alpha in the degradation of insulin mRNA in pancreatic beta-cells
    • Lipson KL, Ghosh R, Urano F. The role of IRE1alpha in the degradation of insulin mRNA in pancreatic beta-cells. PLoS One 2008; 3:e1648.
    • (2008) PLoS One , vol.3
    • Lipson, K.L.1    Ghosh, R.2    Urano, F.3
  • 23
    • 77955383087 scopus 로고    scopus 로고
    • PERK (EIF2AK3) regulates proinsulin trafficking and quality control in the secretory pathway
    • Gupta S, McGrath B, Cavener DR. PERK (EIF2AK3) regulates proinsulin trafficking and quality control in the secretory pathway. Diabetes 2010; 59:1937-1947.
    • (2010) Diabetes , vol.59 , pp. 1937-1947
    • Gupta, S.1    McGrath, B.2    Cavener, D.R.3
  • 24
    • 0034968330 scopus 로고    scopus 로고
    • Diabetes mellitus and exocrine pancreatic dysfunction in Perk-/- mice reveals a role for translational control in secretory cell survival
    • DOI 10.1016/S1097-2765(01)00264-7
    • Harding HP, Zeng H, Zhang Y, et al. Diabetes mellitus and exocrine pancreatic dysfunction in perk-/-mice reveals a role for translational control in secretory cell survival. Mol Cell 2001; 7:1153-1163. (Pubitemid 32607350)
    • (2001) Molecular Cell , vol.7 , Issue.6 , 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
  • 26
    • 67649450485 scopus 로고    scopus 로고
    • Translation attenuation through eIF2alpha phosphorylation prevents oxidative stress and maintains the differentiated state in beta cells
    • Back SH, Scheuner D, Han J, et al. Translation attenuation through eIF2alpha phosphorylation prevents oxidative stress and maintains the differentiated state in beta cells. Cell Metab 2009; 10:13-26.
    • (2009) Cell Metab , vol.10 , pp. 13-26
    • Back, S.H.1    Scheuner, D.2    Han, J.3
  • 27
    • 0034425698 scopus 로고    scopus 로고
    • EIF2AK3, encoding translation initiation factor 2-α kinase 3, is mutated in patients with Wolcott-Rallison syndrome
    • DOI 10.1038/78085
    • Delepine M, Nicolino M, Barrett T, et al. EIF2AK3, encoding translation initiation factor 2-alpha kinase 3, is mutated in patients with Wolcott-Rallison syndrome. Nat Genet 2000; 25:406-409. (Pubitemid 32983431)
    • (2000) Nature Genetics , vol.25 , Issue.4 , pp. 406-409
    • Delepine, M.1    Nicolino, M.2    Barrett, T.3    Golamaully, M.4    Mark Lathrop, G.5    Julier, C.6
  • 28
    • 28244435870 scopus 로고    scopus 로고
    • WFS1 is a novel component of the unfolded protein response and maintains homeostasis of the endoplasmic reticulum in pacreatic β-cells
    • DOI 10.1074/jbc.M507426200
    • Fonseca SG, Fukuma M, Lipson KL, et al. WFS1 is a novel component of the unfolded protein response and maintains homeostasis of the endoplasmic reticulum in pancreatic beta-cells. J Biol Chem 2005; 280:39609-39615. (Pubitemid 41713920)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.47 , pp. 39609-39615
    • Fonseca, S.G.1    Fukuma, M.2    Lipson, K.L.3    Nguyen, L.X.4    Allen, J.R.5    Oka, Y.6    Urano, F.7
  • 30
    • 33947510911 scopus 로고    scopus 로고
    • Selective inhibition of eukaryotic translation initiation factor 2α dephosphorylation potentiates fatty acid-induced endoplasmic reticulum stress and causes pancreatic β-cell dysfunction and apoptosis
    • DOI 10.1074/jbc.M607627200
    • Cnop M, Ladriere L, Hekerman P, et al. Selective inhibition of eukaryotic translation initiation factor 2 alpha dephosphorylation potentiates fatty acidinduced endoplasmic reticulum stress and causes pancreatic beta-cell dysfunction and apoptosis. J Biol Chem 2007; 282:3989-3997. (Pubitemid 47084497)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.6 , pp. 3989-3997
    • Cnop, M.1    Ladriere, L.2    Hekerman, P.3    Ortis, F.4    Cardozo, A.K.5    Dogusan, Z.6    Flamez, D.7    Boyce, M.8    Yuan, J.9    Eizirik, D.L.10
  • 31
    • 47949127583 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced activation of activating transcription factor 6 decreases insulin gene expression via up-regulation of orphan nuclear receptor small heterodimer partner
    • Seo HY, Kim YD, Lee KM, et al. Endoplasmic reticulum stress-induced activation of activating transcription factor 6 decreases insulin gene expression via up-regulation of orphan nuclear receptor small heterodimer partner. Endocrinology 2008; 149:3832-3841.
    • (2008) Endocrinology , vol.149 , pp. 3832-3841
    • Seo, H.Y.1    Kim, Y.D.2    Lee, K.M.3
  • 33
    • 74949118002 scopus 로고    scopus 로고
    • Ablation of C/EBPbeta alleviates ER stress and pancreatic beta cell failure through the GRP78 chaperone in mice
    • Matsuda T, Kido Y, Asahara S, et al. Ablation of C/EBPbeta alleviates ER stress and pancreatic beta cell failure through the GRP78 chaperone in mice. J Clin Invest 2010; 120:115-126.
    • (2010) J Clin Invest , vol.120 , pp. 115-126
    • Matsuda, T.1    Kido, Y.2    Asahara, S.3
  • 34
    • 79951705219 scopus 로고    scopus 로고
    • PERK activation at low glucose concentration is mediated by SERCA pump inhibition and confers preemptive cytoprotection to pancreatic {beta}-cells
    • Moore CE, Omikorede O, Gomez E, et al. PERK activation at low glucose concentration is mediated by SERCA pump inhibition and confers preemptive cytoprotection to pancreatic {beta}-cells. Mol Endocrinol 2010; 25:315-326.
    • (2010) Mol Endocrinol , vol.25 , pp. 315-326
    • Moore, C.E.1    Omikorede, O.2    Gomez, E.3
  • 35
    • 77956706423 scopus 로고    scopus 로고
    • Phosphorylation of eIF2alpha at serine .51. is an important determinant of cell survival and adaptation to glucose deficiency
    • Muaddi H, Majumder M, Peidis P, et al. Phosphorylation of eIF2alpha at serine .51. is an important determinant of cell survival and adaptation to glucose deficiency. Mol Biol Cell 2010; 21:3220-3231.
    • (2010) Mol Biol Cell , vol.21 , pp. 3220-3231
    • Muaddi, H.1    Majumder, M.2    Peidis, P.3
  • 36
    • 78650615554 scopus 로고    scopus 로고
    • Sarco(endo)plasmic reticulum Ca2\+-ATPase 2b is a major regulator of endoplasmic reticulum stress and glucose homeostasis in obesity
    • Park SW, Zhou Y, Lee J, et al. Sarco(endo)plasmic reticulum Ca2\+-ATPase 2b is a major regulator of endoplasmic reticulum stress and glucose homeostasis in obesity. Proc Natl Acad Sci USA 2010; 107:19320-19325.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 19320-19325
    • Park, S.W.1    Zhou, Y.2    Lee, J.3
  • 38
    • 67749135249 scopus 로고    scopus 로고
    • The CREB coactivator CRTC2 links hepatic ER stress and fasting gluconeogenesis
    • Wang Y, Vera L, Fischer WH, et al. The CREB coactivator CRTC2 links hepatic ER stress and fasting gluconeogenesis. Nature 2009; 460:534-537.
    • (2009) Nature , vol.460 , pp. 534-537
    • Wang, Y.1    Vera, L.2    Fischer, W.H.3
  • 39
    • 74949109735 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced activation of activating transcription factor 6 decreases cAMP-stimulated hepatic gluconeogenesis via inhibition of CREB
    • Seo HY, Kim MK, Min AK, et al. Endoplasmic reticulum stress-induced activation of activating transcription factor 6 decreases cAMP-stimulated hepatic gluconeogenesis via inhibition of CREB. Endocrinology 2008; 151:561-568.
    • (2008) Endocrinology , vol.151 , pp. 561-568
    • Seo, H.Y.1    Kim, M.K.2    Min, A.K.3
  • 40
    • 77649253906 scopus 로고    scopus 로고
    • Targeted disruption of the CREB coactivator Crtc2 increases insulin sensitivity
    • Wang Y, Inoue H, Ravnskjaer K, et al. Targeted disruption of the CREB coactivator Crtc2 increases insulin sensitivity. Proc Natl Acad Sci USA 2010; 107:3087-3092.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 3087-3092
    • Wang, Y.1    Inoue, H.2    Ravnskjaer, K.3
  • 41
    • 44349163999 scopus 로고    scopus 로고
    • Dephosphorylation of Translation Initiation Factor 2α Enhances Glucose Tolerance and Attenuates Hepatosteatosis in Mice
    • DOI 10.1016/j.cmet.2008.04.011, PII S1550413108001435
    • Oyadomari S, Harding HP, Zhang Y, et al. Dephosphorylation of translation initiation factor 2alpha enhances glucose tolerance and attenuates hepatosteatosis in mice. Cell Metab 2008; 7:520-532. (Pubitemid 351729207)
    • (2008) Cell Metabolism , vol.7 , Issue.6 , pp. 520-532
    • Oyadomari, S.1    Harding, H.P.2    Zhang, Y.3    Oyadomari, M.4    Ron, D.5
  • 42
    • 57049111040 scopus 로고    scopus 로고
    • UPR pathways combine to prevent hepatic steatosis caused by ER stress-mediated suppression of transcriptional master regulators
    • Rutkowski DT, Wu J, Back SH, et al. UPR pathways combine to prevent hepatic steatosis caused by ER stress-mediated suppression of transcriptional master regulators. Dev Cell 2008; 15:829-840.
    • (2008) Dev Cell , vol.15 , pp. 829-840
    • Rutkowski, D.T.1    Wu, J.2    Back, S.H.3
  • 43
    • 32044453080 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response
    • DOI 10.1016/j.cell.2005.11.040, PII S0092867406000043
    • Zhang K, Shen X,WuJ, et al. Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response. Cell 2006; 124: 587-599. (Pubitemid 43199443)
    • (2006) Cell , vol.124 , Issue.3 , 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
  • 44
    • 77950285163 scopus 로고    scopus 로고
    • Regulation of hepatic gluconeogenesis by an ER-bound transcription factor, CREBH
    • Lee MW, Chanda D, Yang J, et al. Regulation of hepatic gluconeogenesis by an ER-bound transcription factor, CREBH. Cell Metab 2010; 11:331-339.
    • (2010) Cell Metab , vol.11 , pp. 331-339
    • Lee, M.W.1    Chanda, D.2    Yang, J.3
  • 45
    • 77954949431 scopus 로고    scopus 로고
    • FoxO1 links hepatic insulin action to endoplasmic reticulum stress
    • Kamagate A, Kim DH, Zhang T, et al. FoxO1 links hepatic insulin action to endoplasmic reticulum stress. Endocrinology 2010; 151:3521-3535.
    • (2010) Endocrinology , vol.151 , pp. 3521-3535
    • Kamagate, A.1    Kim, D.H.2    Zhang, T.3
  • 46
    • 77950523710 scopus 로고    scopus 로고
    • The regulatory subunits of PI3K, p85alpha and p85beta, interact with XBP-1 and increase its nuclear translocation
    • Park SW, Zhou Y, Lee J, et al. The regulatory subunits of PI3K, p85alpha and p85beta, interact with XBP-1 and increase its nuclear translocation. Nat Med 2010; 16:429-437.
    • (2010) Nat Med , vol.16 , pp. 429-437
    • Park, S.W.1    Zhou, Y.2    Lee, J.3
  • 47
    • 77950537400 scopus 로고    scopus 로고
    • A regulatory subunit of phosphoinositide 3-kinase increases the nuclear accumulation of X-box-binding protein-1 to modulate the unfolded protein response
    • Winnay JN, Boucher J, Mori MA, et al. A regulatory subunit of phosphoinositide 3-kinase increases the nuclear accumulation of X-box-binding protein-1 to modulate the unfolded protein response. Nat Med 2010; 16:438-445.
    • (2010) Nat Med , vol.16 , pp. 438-445
    • Winnay, J.N.1    Boucher, J.2    Mori, M.A.3
  • 48
    • 78149411370 scopus 로고    scopus 로고
    • C/EBPbeta is AMP kinase sensitive and up-regulates PEPCK in response to ER stress in hepatoma cells
    • Choudhury M, Qadri I, Rahman SM, et al. C/EBPbeta is AMP kinase sensitive and up-regulates PEPCK in response to ER stress in hepatoma cells. Mol Cell Endocrinol 2011; 331:102-108.
    • (2011) Mol Cell Endocrinol , vol.331 , pp. 102-108
    • Choudhury, M.1    Qadri, I.2    Rahman, S.M.3
  • 49
    • 77149134285 scopus 로고    scopus 로고
    • Reduction of AMP-activated protein kinase alpha2 increases endoplasmic reticulum stress and atherosclerosis in vivo
    • Dong Y, Zhang M, Liang B, et al. Reduction of AMP-activated protein kinase alpha2 increases endoplasmic reticulum stress and atherosclerosis in vivo. Circulation 2010; 121:792-803.
    • (2010) Circulation , vol.121 , pp. 792-803
    • Dong, Y.1    Zhang, M.2    Liang, B.3
  • 50
    • 40649104735 scopus 로고    scopus 로고
    • Loss of the tuberous sclerosis complex tumor suppressors triggers the unfolded protein response to regulate insulin signaling and apoptosis
    • DOI 10.1016/j.molcel.2007.12.023, PII S109727650800066X
    • Ozcan U, Ozcan L, Yilmaz E, et al. Loss of the tuberous sclerosis complex tumor suppressors triggers the unfolded protein response to regulate insulin signaling and apoptosis. Mol Cell 2008; 29:541-551. (Pubitemid 351384644)
    • (2008) Molecular Cell , vol.29 , Issue.5 , pp. 541-551
    • Ozcan, U.1    Ozcan, L.2    Yilmaz, E.3    Duvel, K.4    Sahin, M.5    Manning, B.D.6    Hotamisligil, G.S.7
  • 51
    • 45849137877 scopus 로고    scopus 로고
    • Regulation of hepatic lipogenesis by the transcription factor XBP1
    • DOI 10.1126/science.1158042
    • Lee AH, Scapa EF, Cohen DE, et al. Regulation of hepatic lipogenesis by the transcription factor XBP1. Science 2008; 320:1492-1496. (Pubitemid 351929428)
    • (2008) Science , vol.320 , Issue.5882 , pp. 1492-1496
    • Lee, A.-H.1    Scapa, E.F.2    Cohen, D.E.3    Glimcher, L.H.4
  • 52
    • 38149136598 scopus 로고    scopus 로고
    • Inhibition of apolipoprotein B100 secretion by lipid-induced hepatic endoplasmic reticulum stress in rodents
    • Ota T, Gayet C, Ginsberg HN. Inhibition of apolipoprotein B100 secretion by lipid-induced hepatic endoplasmic reticulum stress in rodents. J Clin Invest 2008; 118:316-332.
    • (2008) J Clin Invest , vol.118 , pp. 316-332
    • Ota, T.1    Gayet, C.2    Ginsberg, H.N.3
  • 53
    • 38649124615 scopus 로고    scopus 로고
    • Activation and dysregulation of the unfolded protein response in nonalcoholic fatty liver disease
    • DOI 10.1053/j.gastro.2007.10.039, PII S0016508507019191
    • Puri P, Mirshahi F, Cheung O, et al. Activation and dysregulation of the unfolded protein response in nonalcoholic fatty liver disease. Gastroenterology 2008; 134:568-576. (Pubitemid 351173040)
    • (2008) Gastroenterology , vol.134 , Issue.2 , pp. 568-576
    • Puri, P.1    Mirshahi, F.2    Cheung, O.3    Natarajan, R.4    Maher, J.W.5    Kellum, J.M.6    Sanyal, A.J.7
  • 54
    • 77956232915 scopus 로고    scopus 로고
    • Induction of liver steatosis and lipid droplet formation in ATF6alpha-knockout mice burdened with pharmacological endoplasmic reticulum stress
    • Yamamoto K, Takahara K, Oyadomari S, et al. Induction of liver steatosis and lipid droplet formation in ATF6alpha-knockout mice burdened with pharmacological endoplasmic reticulum stress. Mol Biol Cell 2010; 21: 2975-2986.
    • (2010) Mol Biol Cell , vol.21 , pp. 2975-2986
    • Yamamoto, K.1    Takahara, K.2    Oyadomari, S.3
  • 55
    • 66449137379 scopus 로고    scopus 로고
    • GRP78 expression inhibits insulin and ER stress-induced SREBP-1c activation and reduces hepatic steatosis in mice
    • Kammoun HL, Chabanon H, Hainault I, et al.GRP78 expression inhibits insulin and ER stress-induced SREBP-1c activation and reduces hepatic steatosis in mice. J Clin Invest 2009; 119:1201-1215.
    • (2009) J Clin Invest , vol.119 , pp. 1201-1215
    • Kammoun, H.L.1    Chabanon, H.2    Hainault, I.3
  • 56
    • 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, et al. Association of amino acid variants in the activating transcription factor 6 gene (ATF6) on 1q21-q23 with type 2 diabetes in Pima Indians. Diabetes 2006; 55:839-842. (Pubitemid 43343245)
    • (2006) Diabetes , vol.55 , Issue.3 , pp. 839-842
    • Thameem, F.1    Farook, V.S.2    Bogardus, C.3    Prochazka, M.4
  • 57
    • 52749091008 scopus 로고    scopus 로고
    • Increase in endoplasmic reticulum stressrelated proteins and genes in adipose tissue of obese, insulin-resistant individuals
    • Boden G, Duan X, Homko C, et al. Increase in endoplasmic reticulum stressrelated proteins and genes in adipose tissue of obese, insulin-resistant individuals. Diabetes 2008; 57:2438-2444.
    • (2008) Diabetes , vol.57 , pp. 2438-2444
    • Boden, G.1    Duan, X.2    Homko, C.3
  • 58
    • 62749178966 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress is reduced in tissues of obese subjects after weight loss
    • Gregor MF, Yang L, Fabbrini E, et al. Endoplasmic reticulum stress is reduced in tissues of obese subjects after weight loss. Diabetes 2009; 58:693-700.
    • (2009) Diabetes , vol.58 , pp. 693-700
    • Gregor, M.F.1    Yang, L.2    Fabbrini, E.3
  • 60
    • 77949902607 scopus 로고    scopus 로고
    • 4-Phenyl butyric acid does not generally reduce glucose levels in rodent models of diabetes
    • Xu TY, Chen RH, Wang P, et al. 4-Phenyl butyric acid does not generally reduce glucose levels in rodent models of diabetes. Clin Exp Pharmacol Physiol 2010; 37:441-446.
    • (2010) Clin Exp Pharmacol Physiol , vol.37 , pp. 441-446
    • Xu, T.Y.1    Chen, R.H.2    Wang, P.3
  • 61
    • 71549152580 scopus 로고    scopus 로고
    • Reducing endoplasmic reticulum stress through a macrophage lipid chaperone alleviates atherosclerosis
    • Erbay E, Babaev VR, Mayers JR, et al. Reducing endoplasmic reticulum stress through a macrophage lipid chaperone alleviates atherosclerosis. Nat Med 2009; 15:1383-1391.
    • (2009) Nat Med , vol.15 , pp. 1383-1391
    • Erbay, E.1    Babaev, V.R.2    Mayers, J.R.3
  • 62
    • 77955411159 scopus 로고    scopus 로고
    • Tauroursodeoxycholic Acid may improve liver and muscle but not adipose tissue insulin sensitivity in obese men and women
    • Kars M, Yang L, Gregor MF, et al. Tauroursodeoxycholic Acid may improve liver and muscle but not adipose tissue insulin sensitivity in obese men and women. Diabetes 2010; 59:1899-1905.
    • (2010) Diabetes , vol.59 , pp. 1899-1905
    • Kars, M.1    Yang, L.2    Gregor, M.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.