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Volumn 26, Issue 8, 2015, Pages 438-448

Targeting endoplasmic reticulum stress in insulin resistance

Author keywords

Apoptosis; Endoplasmic reticulum stress; Inflammation; Insulin resistance; Type 2 diabetes mellitus; Unfolded protein response

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR; CCAAT ENHANCER BINDING PROTEIN; CHAPERONE; CYCLIC AMP; FATTY ACID; GLUCOSE 6 PHOSPHATASE; GUANINE NUCLEOTIDE EXCHANGE FACTOR; HORMONE SENSITIVE LIPASE; I KAPPA B; IMMUNOGLOBULIN BINDING FACTOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INITIATION FACTOR 2ALPHA; INSULIN; INTERLEUKIN 6; PROTEIN DISULFIDE ISOMERASE; PROTEIN IRE1; PROTEIN KINASE B; PROTEIN KINASE R; STEROL REGULATORY ELEMENT BINDING PROTEIN 1C; STRESS ACTIVATED PROTEIN KINASE; THIOREDOXIN INTERACTING PROTEIN; TOLL LIKE RECEPTOR 4; TRANSCRIPTION FACTOR AP 1; TRANSCRIPTION FACTOR FKHR; TRANSCRIPTION FACTOR NRF2; TRIACYLGLYCEROL LIPASE; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; VERY LOW DENSITY LIPOPROTEIN; X BOX BINDING PROTEIN 1;

EID: 84938287688     PISSN: 10432760     EISSN: 18793061     Source Type: Journal    
DOI: 10.1016/j.tem.2015.05.007     Document Type: Review
Times cited : (180)

References (88)
  • 1
    • 84864320585 scopus 로고    scopus 로고
    • New insights into ER stress-induced insulin resistance
    • Flamment M., et al. New insights into ER stress-induced insulin resistance. Trends Endocrinol. Metab. 2012, 23:381-390.
    • (2012) Trends Endocrinol. Metab. , vol.23 , pp. 381-390
    • Flamment, M.1
  • 2
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: from stress pathway to homeostatic regulation
    • Walter P., Ron D. The unfolded protein response: from stress pathway to homeostatic regulation. Science 2011, 334:1081-1086.
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 3
    • 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 S., 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. U.S.A. 2010, 107:19320-19325.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 19320-19325
    • Park, S.1
  • 4
    • 80052366845 scopus 로고    scopus 로고
    • Stressed out about obesity: IRE1a-XBP1 in metabolic disorders
    • Sha H., et al. Stressed out about obesity: IRE1a-XBP1 in metabolic disorders. Trends Endocrinol. Metab. 2011, 22:374-381.
    • (2011) Trends Endocrinol. Metab. , vol.22 , pp. 374-381
    • Sha, H.1
  • 5
    • 84892646801 scopus 로고    scopus 로고
    • Unfolded protein response signaling and metabolic diseases
    • Lee J., Ozcan U. Unfolded protein response signaling and metabolic diseases. J. Biol. Chem. 2014, 289:1203-1211.
    • (2014) J. Biol. Chem. , vol.289 , pp. 1203-1211
    • Lee, J.1    Ozcan, U.2
  • 6
    • 33748069813 scopus 로고    scopus 로고
    • Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes
    • Ozcan U., et al. Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes. Science 2006, 313:1137-1140.
    • (2006) Science , vol.313 , pp. 1137-1140
    • Ozcan, U.1
  • 7
    • 52749091008 scopus 로고    scopus 로고
    • Increase in endoplasmic reticulum stress-related proteins and genes in adipose tissue of obese, insulin-resistant individuals
    • Boden G., et al. Increase in endoplasmic reticulum stress-related 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
  • 8
    • 62749178966 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress is reduced in tissues of obese subjects after weight loss
    • Gregor M.F., 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
  • 9
    • 80053902834 scopus 로고    scopus 로고
    • Endurance exercise training ameliorates insulin resistance and reticulum stress in adipose and hepatic tissue in obese rats
    • da Luz G., et al. Endurance exercise training ameliorates insulin resistance and reticulum stress in adipose and hepatic tissue in obese rats. Eur. J. Appl. Physiol. 2011, 111:2015-2023.
    • (2011) Eur. J. Appl. Physiol. , vol.111 , pp. 2015-2023
    • da Luz, G.1
  • 10
    • 84869184022 scopus 로고    scopus 로고
    • Obesity-induced endoplasmic reticulum stress causes chronic inflammation in adipose tissue
    • Kawasaki N., et al. Obesity-induced endoplasmic reticulum stress causes chronic inflammation in adipose tissue. Sci. Rep. 2012, 2:799.
    • (2012) Sci. Rep. , vol.2 , pp. 799
    • Kawasaki, N.1
  • 11
    • 79952003715 scopus 로고    scopus 로고
    • FFA-induced adipocyte inflammation and insulin resistance: involvement of ER stress and IKKbeta pathways
    • Jiao P., et al. FFA-induced adipocyte inflammation and insulin resistance: involvement of ER stress and IKKbeta pathways. Obesity 2011, 19:483-491.
    • (2011) Obesity , vol.19 , pp. 483-491
    • Jiao, P.1
  • 12
    • 33845768987 scopus 로고    scopus 로고
    • Integrating cell-signalling pathways with NF-kappaB and IKK function
    • Perkins N.D. Integrating cell-signalling pathways with NF-kappaB and IKK function. Nat. Rev. Mol. Cell Biol. 2007, 8:49-62.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 49-62
    • Perkins, N.D.1
  • 13
    • 84864003561 scopus 로고    scopus 로고
    • PERK utilizes intrinsic lipid kinase activity to generate phosphatidic acid, mediate Akt activation, and promote adipocyte differentiation
    • Bobrovnikova-Marjon E., et al. PERK utilizes intrinsic lipid kinase activity to generate phosphatidic acid, mediate Akt activation, and promote adipocyte differentiation. Mol. Cell. Biol. 2012, 32:2268-2278.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 2268-2278
    • Bobrovnikova-Marjon, E.1
  • 14
    • 84863163071 scopus 로고    scopus 로고
    • Lipolysis response to endoplasmic reticulum stress in adipose cells
    • Deng J., et al. Lipolysis response to endoplasmic reticulum stress in adipose cells. J. Biol. Chem. 2012, 287:6240-6249.
    • (2012) J. Biol. Chem. , vol.287 , pp. 6240-6249
    • Deng, J.1
  • 15
    • 77954218373 scopus 로고    scopus 로고
    • Lipopolysaccharide, high glucose and saturated fatty acids induce endoplasmic reticulum stress in cultured primary human adipocytes: Salicylate alleviates this stress
    • Alhusaini S., et al. Lipopolysaccharide, high glucose and saturated fatty acids induce endoplasmic reticulum stress in cultured primary human adipocytes: Salicylate alleviates this stress. Biochem. Biophys. Res. Commun. 2010, 397:472-478.
    • (2010) Biochem. Biophys. Res. Commun. , vol.397 , pp. 472-478
    • Alhusaini, S.1
  • 16
    • 84894465374 scopus 로고    scopus 로고
    • Insulin regulates the unfolded protein response in human adipose tissue
    • Boden G., et al. Insulin regulates the unfolded protein response in human adipose tissue. Diabetes 2014, 63:912-922.
    • (2014) Diabetes , vol.63 , pp. 912-922
    • Boden, G.1
  • 17
    • 84892650136 scopus 로고    scopus 로고
    • Very low density lipoprotein receptor (VLDLR) expression is a determinant factor in adipose tissue inflammation and adipocyte-macrophage interaction
    • Nguyen A., et al. Very low density lipoprotein receptor (VLDLR) expression is a determinant factor in adipose tissue inflammation and adipocyte-macrophage interaction. J. Biol. Chem. 2014, 289:1688-1703.
    • (2014) J. Biol. Chem. , vol.289 , pp. 1688-1703
    • Nguyen, A.1
  • 18
    • 77953196716 scopus 로고    scopus 로고
    • Deletion of the alpha-arrestin protein Txnip in mice promotes adiposity and adipogenesis while preserving insulin sensitivity
    • Chutkow W.A., et al. Deletion of the alpha-arrestin protein Txnip in mice promotes adiposity and adipogenesis while preserving insulin sensitivity. Diabetes 2010, 59:1424-1434.
    • (2010) Diabetes , vol.59 , pp. 1424-1434
    • Chutkow, W.A.1
  • 19
    • 84901825185 scopus 로고    scopus 로고
    • Thioredoxin-interacting protein regulates protein disulfide isomerases and endoplasmic reticulum stress
    • Lee S., et al. Thioredoxin-interacting protein regulates protein disulfide isomerases and endoplasmic reticulum stress. EMBO Mol. Med. 2014, 6:732-743.
    • (2014) EMBO Mol. Med. , vol.6 , pp. 732-743
    • Lee, S.1
  • 20
    • 77950285163 scopus 로고    scopus 로고
    • Regulation of hepatic gluconeogenesis by an ER-bound transcription factor, CREBH
    • Lee M.W., 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
  • 21
    • 79952381078 scopus 로고    scopus 로고
    • Regulation of glucose homeostasis through a XBP-1-FoxO1 interaction
    • Zhou Y., et al. Regulation of glucose homeostasis through a XBP-1-FoxO1 interaction. Nat. Med. 2011, 17:356-365.
    • (2011) Nat. Med. , vol.17 , pp. 356-365
    • Zhou, Y.1
  • 22
    • 84878218164 scopus 로고    scopus 로고
    • Activation of PPARα ameliorates hepatic insulin resistance and steatosis in high fructose-fed mice despite increased endoplasmic reticulum stress
    • Chan S.M.H., et al. Activation of PPARα ameliorates hepatic insulin resistance and steatosis in high fructose-fed mice despite increased endoplasmic reticulum stress. Diabetes 2013, 62:2095-2105.
    • (2013) Diabetes , vol.62 , pp. 2095-2105
    • Chan, S.M.H.1
  • 23
    • 84904514591 scopus 로고    scopus 로고
    • AMPK activation prevents excess nutrient-induced hepatic lipid accumulation by inhibiting mTORC1 signaling and endoplasmic reticulum stress response
    • Li H., et al. AMPK activation prevents excess nutrient-induced hepatic lipid accumulation by inhibiting mTORC1 signaling and endoplasmic reticulum stress response. Biochim. Biophys. Acta 2014, 1842:1844-1854.
    • (2014) Biochim. Biophys. Acta , vol.1842 , pp. 1844-1854
    • Li, H.1
  • 24
    • 84876154662 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induces hepatic steatosis via increased expression of the hepatic very low-density lipoprotein receptor
    • Jo H., et al. Endoplasmic reticulum stress induces hepatic steatosis via increased expression of the hepatic very low-density lipoprotein receptor. Hepatology 2013, 57:1366-1377.
    • (2013) Hepatology , vol.57 , pp. 1366-1377
    • Jo, H.1
  • 25
    • 66449137379 scopus 로고    scopus 로고
    • GRP78 expression inhibits insulin and ER stress-induced SREBP-1c activation and reduces hepatic steatosis in mice
    • Kammoun H.L., 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
  • 26
    • 84862984616 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress is involved in hepatic SREBP-1c activation and lipid accumulation in fructose-fed mice
    • Zhang C., et al. Endoplasmic reticulum stress is involved in hepatic SREBP-1c activation and lipid accumulation in fructose-fed mice. Toxicol. Lett. 2012, 212:229-240.
    • (2012) Toxicol. Lett. , vol.212 , pp. 229-240
    • Zhang, C.1
  • 27
    • 79956292356 scopus 로고    scopus 로고
    • Constitutive role for IRE1α-XBP1 signaling pathway in the insulin-mediated hepatic lipogenic program
    • Ning J., et al. Constitutive role for IRE1α-XBP1 signaling pathway in the insulin-mediated hepatic lipogenic program. Endocrinology 2011, 152:2247-2255.
    • (2011) Endocrinology , vol.152 , pp. 2247-2255
    • Ning, J.1
  • 28
    • 84867038186 scopus 로고    scopus 로고
    • Silencing of lipid metabolism genes through IRE1α-mediated mRNA decay lowers plasma lipids in mice
    • So J.S., et al. Silencing of lipid metabolism genes through IRE1α-mediated mRNA decay lowers plasma lipids in mice. Cell Metab. 2012, 16:487-499.
    • (2012) Cell Metab. , vol.16 , pp. 487-499
    • So, J.S.1
  • 29
    • 84862908245 scopus 로고    scopus 로고
    • Dissociation of inositol-requiring enzyme (IRE1α)-mediated c-Jun N-terminal kinase activation from hepatic insulin resistance in conditional X-box-binding protein-1 (XBP1) knock-out mice
    • Jurczak M.J., et al. Dissociation of inositol-requiring enzyme (IRE1α)-mediated c-Jun N-terminal kinase activation from hepatic insulin resistance in conditional X-box-binding protein-1 (XBP1) knock-out mice. J. Biol. Chem. 2012, 287:2558-2567.
    • (2012) J. Biol. Chem. , vol.287 , pp. 2558-2567
    • Jurczak, M.J.1
  • 30
    • 84862577245 scopus 로고    scopus 로고
    • Deletion of C/EBP homologous protein (Chop) in C57Bl/6 mice dissociates obesity from insulin resistance
    • Maris M., et al. Deletion of C/EBP homologous protein (Chop) in C57Bl/6 mice dissociates obesity from insulin resistance. Diabetologia 2012, 55:1167-1178.
    • (2012) Diabetologia , vol.55 , pp. 1167-1178
    • Maris, M.1
  • 31
    • 84874268065 scopus 로고    scopus 로고
    • ER stress potentiates insulin resistance through PERK-mediated FOXO phosphorylation
    • Zhang W., et al. ER stress potentiates insulin resistance through PERK-mediated FOXO phosphorylation. Genes Dev. 2013, 27:441-449.
    • (2013) Genes Dev. , vol.27 , pp. 441-449
    • Zhang, W.1
  • 32
    • 84908200877 scopus 로고    scopus 로고
    • Fibroblast growth factor 21 is regulated by the IRE1α-XBP1 branch of the unfolded protein response and counteracts endoplasmic reticulum stress-induced hepatic steatosis
    • Jiang S., et al. Fibroblast growth factor 21 is regulated by the IRE1α-XBP1 branch of the unfolded protein response and counteracts endoplasmic reticulum stress-induced hepatic steatosis. J. Biol. Chem. 2014, 289:29751-29765.
    • (2014) J. Biol. Chem. , vol.289 , pp. 29751-29765
    • Jiang, S.1
  • 33
    • 84872057896 scopus 로고    scopus 로고
    • Autophagy deficiency leads to protection from obesity and insulin resistance by inducing Fgf21 as a mitokine
    • Kim K.H., et al. Autophagy deficiency leads to protection from obesity and insulin resistance by inducing Fgf21 as a mitokine. Nat. Med. 2013, 19:83-92.
    • (2013) Nat. Med. , vol.19 , pp. 83-92
    • Kim, K.H.1
  • 34
    • 77956400005 scopus 로고    scopus 로고
    • Defective hepatic autophagy in obesity promotes ER stress and causes insulin resistance
    • Yang L., et al. Defective hepatic autophagy in obesity promotes ER stress and causes insulin resistance. Cell Metab. 2010, 11:467-478.
    • (2010) Cell Metab. , vol.11 , pp. 467-478
    • Yang, L.1
  • 35
    • 84874427117 scopus 로고    scopus 로고
    • Proteasome dysfunction mediates obesity-induced endoplasmic reticulum stress and insulin resistance in the liver
    • Otoda T., et al. Proteasome dysfunction mediates obesity-induced endoplasmic reticulum stress and insulin resistance in the liver. Diabetes 2013, 62:811-824.
    • (2013) Diabetes , vol.62 , pp. 811-824
    • Otoda, T.1
  • 36
    • 84862777165 scopus 로고    scopus 로고
    • Improved insulin sensitivity by rapamycin is associated with reduction of mTOR and S6K1 activities in L6 myotubes
    • Hwang S.L., et al. Improved insulin sensitivity by rapamycin is associated with reduction of mTOR and S6K1 activities in L6 myotubes. Biochem. Biophys. Res. Commun. 2012, 418:402-407.
    • (2012) Biochem. Biophys. Res. Commun. , vol.418 , pp. 402-407
    • Hwang, S.L.1
  • 37
    • 79956326793 scopus 로고    scopus 로고
    • Oleate blocks palmitate-induced abnormal lipid distribution, endoplasmic reticulum expansion and stress, and insulin resistance in skeletal muscle
    • Peng G., et al. Oleate blocks palmitate-induced abnormal lipid distribution, endoplasmic reticulum expansion and stress, and insulin resistance in skeletal muscle. Endocrinology 2011, 152:2206-2218.
    • (2011) Endocrinology , vol.152 , pp. 2206-2218
    • Peng, G.1
  • 38
    • 84877770648 scopus 로고    scopus 로고
    • Oleate prevents saturated-fatty-acid-induced ER stress, inflammation and insulin resistance in skeletal muscle cells through an AMPK-dependent mechanism
    • Salvadó L., et al. Oleate prevents saturated-fatty-acid-induced ER stress, inflammation and insulin resistance in skeletal muscle cells through an AMPK-dependent mechanism. Diabetologia 2013, 56:1372-1382.
    • (2013) Diabetologia , vol.56 , pp. 1372-1382
    • Salvadó, L.1
  • 39
    • 84856737149 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress does not mediate palmitate-induced insulin resistance in mouse and human muscle cells
    • Hage Hassan R., et al. Endoplasmic reticulum stress does not mediate palmitate-induced insulin resistance in mouse and human muscle cells. Diabetologia 2012, 55:204-214.
    • (2012) Diabetologia , vol.55 , pp. 204-214
    • Hage Hassan, R.1
  • 40
    • 27144489669 scopus 로고    scopus 로고
    • AMP-activated protein kinase protects cardiomyocytes against hypoxic injury through attenuation of endoplasmic reticulum stress
    • Terai K., et al. AMP-activated protein kinase protects cardiomyocytes against hypoxic injury through attenuation of endoplasmic reticulum stress. Mol. Cell. Biol. 2005, 25:9554-9575.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 9554-9575
    • Terai, K.1
  • 41
    • 77149134285 scopus 로고    scopus 로고
    • Reduction of AMP-activated protein kinase alpha2 increases endoplasmic reticulum stress and atherosclerosis in vivo
    • Dong Y., 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
  • 42
    • 79953168083 scopus 로고    scopus 로고
    • Involvement of oxygen-regulated protein 150 in AMP-activated protein kinase-mediated alleviation of lipid-induced endoplasmic reticulum stress
    • Wang Y., et al. Involvement of oxygen-regulated protein 150 in AMP-activated protein kinase-mediated alleviation of lipid-induced endoplasmic reticulum stress. J. Biol. Chem. 2011, 286:11119-11131.
    • (2011) J. Biol. Chem. , vol.286 , pp. 11119-11131
    • Wang, Y.1
  • 43
    • 84878706533 scopus 로고    scopus 로고
    • Tribbles 3 mediates endoplasmic reticulum stress-induced insulin resistance in skeletal muscle
    • Koh H.J., et al. Tribbles 3 mediates endoplasmic reticulum stress-induced insulin resistance in skeletal muscle. Nat. Commun. 2013, 4:1871.
    • (2013) Nat. Commun. , vol.4 , pp. 1871
    • Koh, H.J.1
  • 44
    • 84878360717 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress upregulates protein tyrosine phosphatase 1B and impairs glucose uptake in cultured myotubes
    • Panzhinskiy E., et al. Endoplasmic reticulum stress upregulates protein tyrosine phosphatase 1B and impairs glucose uptake in cultured myotubes. Diabetologia 2013, 56:598-607.
    • (2013) Diabetologia , vol.56 , pp. 598-607
    • Panzhinskiy, E.1
  • 45
    • 79952410092 scopus 로고    scopus 로고
    • Sodium phenylbutyrate, a drug with known capacity to reduce endoplasmic reticulum stress, partially alleviates lipid-induced insulin resistance and beta-cell dysfunction in humans
    • Xiao C., et al. Sodium phenylbutyrate, a drug with known capacity to reduce endoplasmic reticulum stress, partially alleviates lipid-induced insulin resistance and beta-cell dysfunction in humans. Diabetes 2011, 60:918-924.
    • (2011) Diabetes , vol.60 , pp. 918-924
    • Xiao, C.1
  • 46
    • 84888832151 scopus 로고    scopus 로고
    • Oleate rescues INS-1E β-cells from palmitate-induced apoptosis by preventing activation of the unfolded protein response
    • Sommerweiss D., et al. Oleate rescues INS-1E β-cells from palmitate-induced apoptosis by preventing activation of the unfolded protein response. Biochem. Biophys. Res. Commun. 2013, 441:770-776.
    • (2013) Biochem. Biophys. Res. Commun. , vol.441 , pp. 770-776
    • Sommerweiss, D.1
  • 47
    • 77957255986 scopus 로고    scopus 로고
    • Fatty acid-induced oxidation and triglyceride formation is higher in insulin producing MIN6 cells exposed to oleate compared to palmitate
    • Thorn K., Bergsten P. Fatty acid-induced oxidation and triglyceride formation is higher in insulin producing MIN6 cells exposed to oleate compared to palmitate. J. Cell Biochem. 2010, 111:497-507.
    • (2010) J. Cell Biochem. , vol.111 , pp. 497-507
    • Thorn, K.1    Bergsten, P.2
  • 48
    • 79951865533 scopus 로고    scopus 로고
    • Stimulation of lipogenesis as well as fatty acid oxidation protects against palmitate-induced INS-1 beta-cell death
    • Choi S.E., et al. Stimulation of lipogenesis as well as fatty acid oxidation protects against palmitate-induced INS-1 beta-cell death. Endocrinology 2011, 152:816-827.
    • (2011) Endocrinology , vol.152 , pp. 816-827
    • Choi, S.E.1
  • 49
    • 42449110310 scopus 로고    scopus 로고
    • Thioredoxin-interacting protein: a critical link between glucose toxicity and beta-cell apoptosis
    • Chen J., et al. Thioredoxin-interacting protein: a critical link between glucose toxicity and beta-cell apoptosis. Diabetes 2008, 57:938-944.
    • (2008) Diabetes , vol.57 , pp. 938-944
    • Chen, J.1
  • 50
    • 84875992503 scopus 로고    scopus 로고
    • Involvement of ASK1-p38 pathway in the pathogenesis of diabetes triggered by pancreatic ss cell exhaustion
    • Yamaguchi K., et al. Involvement of ASK1-p38 pathway in the pathogenesis of diabetes triggered by pancreatic ss cell exhaustion. Biochim. Biophys. Acta 2013, 1830:3656-3663.
    • (2013) Biochim. Biophys. Acta , vol.1830 , pp. 3656-3663
    • Yamaguchi, K.1
  • 51
    • 84917727835 scopus 로고    scopus 로고
    • ATFβ regulates the Wfs1 gene and has a cell survival role in the ER stress response in pancreatic β-cells
    • Odisho T., et al. ATFβ regulates the Wfs1 gene and has a cell survival role in the ER stress response in pancreatic β-cells. Exp. Cell Res. 2015, 330:111-122.
    • (2015) Exp. Cell Res. , vol.330 , pp. 111-122
    • Odisho, T.1
  • 52
    • 77949751415 scopus 로고    scopus 로고
    • Wolfram syndrome 1 gene negatively regulates ER stress signaling in rodent and human cells
    • Fonseca S.G., et al. Wolfram syndrome 1 gene negatively regulates ER stress signaling in rodent and human cells. J. Clin. Invest. 2010, 120:744-755.
    • (2010) J. Clin. Invest. , vol.120 , pp. 744-755
    • Fonseca, S.G.1
  • 53
    • 78049281798 scopus 로고    scopus 로고
    • Proinsulin misfolding and diabetes: mutant INS gene-induced diabetes of youth
    • Liu M., et al. Proinsulin misfolding and diabetes: mutant INS gene-induced diabetes of youth. Trends Endocrinol. Metab. 2010, 21:652-659.
    • (2010) Trends Endocrinol. Metab. , vol.21 , pp. 652-659
    • Liu, M.1
  • 54
    • 84877578475 scopus 로고    scopus 로고
    • ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death
    • Han J., et al. ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death. Nat. Cell Biol. 2013, 15:481-490.
    • (2013) Nat. Cell Biol. , vol.15 , pp. 481-490
    • Han, J.1
  • 55
    • 84904248428 scopus 로고    scopus 로고
    • Chaperones ameliorate beta cell dysfunction associated with human islet amyloid polypeptide overexpression
    • Cadavez L., et al. Chaperones ameliorate beta cell dysfunction associated with human islet amyloid polypeptide overexpression. PLoS ONE 2014, 9:e101797.
    • (2014) PLoS ONE , vol.9 , pp. e101797
    • Cadavez, L.1
  • 56
    • 84925581887 scopus 로고    scopus 로고
    • Glycemic control in diabetes is restored by therapeutic manipulation of cytokines that regulate beta cell stress
    • Hasnain S.Z., et al. Glycemic control in diabetes is restored by therapeutic manipulation of cytokines that regulate beta cell stress. Nat. Med. 2014, 20:1417-1426.
    • (2014) Nat. Med. , vol.20 , pp. 1417-1426
    • Hasnain, S.Z.1
  • 57
    • 84876496860 scopus 로고    scopus 로고
    • GRP78 overproduction in pancreatic beta cells protects against high-fat-diet-induced diabetes in mice
    • Teodoro-Morrison T., et al. GRP78 overproduction in pancreatic beta cells protects against high-fat-diet-induced diabetes in mice. Diabetologia 2013, 56:1057-1067.
    • (2013) Diabetologia , vol.56 , pp. 1057-1067
    • Teodoro-Morrison, T.1
  • 58
    • 22544444513 scopus 로고    scopus 로고
    • Control of mRNA translation preserves endoplasmic reticulum function in beta cells and maintains glucose homeostasis
    • Scheuner D., et al. Control of mRNA translation preserves endoplasmic reticulum function in beta cells and maintains glucose homeostasis. Nat. Med. 2005, 11:757-764.
    • (2005) Nat. Med. , vol.11 , pp. 757-764
    • Scheuner, D.1
  • 59
    • 34248223285 scopus 로고    scopus 로고
    • Biology of incretins: GLP-1 and GIP
    • Baggio L.L., Drucker D.J. Biology of incretins: GLP-1 and GIP. Gastroenterology 2007, 132:2131-2157.
    • (2007) Gastroenterology , vol.132 , pp. 2131-2157
    • Baggio, L.L.1    Drucker, D.J.2
  • 60
    • 84875143788 scopus 로고    scopus 로고
    • Targeting endoplasmic reticulum stress in metabolic disease
    • Cao S.S., Kaufman R.J. Targeting endoplasmic reticulum stress in metabolic disease. Expert Opin. Ther. Targets 2013, 17:437-448.
    • (2013) Expert Opin. Ther. Targets , vol.17 , pp. 437-448
    • Cao, S.S.1    Kaufman, R.J.2
  • 61
    • 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., 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
  • 62
    • 84881478531 scopus 로고    scopus 로고
    • Potential for therapeutic manipulation of the UPR in disease
    • Park S.W., Ozcan U. Potential for therapeutic manipulation of the UPR in disease. Semin. Immunopathol. 2013, 35:351-373.
    • (2013) Semin. Immunopathol. , vol.35 , pp. 351-373
    • Park, S.W.1    Ozcan, U.2
  • 63
    • 0036692295 scopus 로고    scopus 로고
    • The peroxisome proliferator phenylbutyric acid (PBA) protects astrocytes from ts1 MoMuLV-induced oxidative cell death
    • Liu N., et al. The peroxisome proliferator phenylbutyric acid (PBA) protects astrocytes from ts1 MoMuLV-induced oxidative cell death. J. Neurovirol. 2002, 8:318-325.
    • (2002) J. Neurovirol. , vol.8 , pp. 318-325
    • Liu, N.1
  • 64
    • 84859822353 scopus 로고    scopus 로고
    • Regulation of chemokine and chemokine receptor expression by PPARgamma in adipocytes and macrophages
    • Nguyen M.T., et al. Regulation of chemokine and chemokine receptor expression by PPARgamma in adipocytes and macrophages. PLoS ONE 2012, 7:e34976.
    • (2012) PLoS ONE , vol.7 , pp. e34976
    • Nguyen, M.T.1
  • 65
    • 0036299982 scopus 로고    scopus 로고
    • Metformin increases AMP-activated protein kinase activity in skeletal muscle of subjects with type 2 diabetes
    • Musi N., et al. Metformin increases AMP-activated protein kinase activity in skeletal muscle of subjects with type 2 diabetes. Diabetes 2002, 51:2074-2081.
    • (2002) Diabetes , vol.51 , pp. 2074-2081
    • Musi, N.1
  • 66
    • 84902436230 scopus 로고    scopus 로고
    • Metformin attenuates palmitate-induced endoplasmic reticulum stress, serine phosphorylation of IRS-1 and apoptosis in rat insulinoma cells
    • Simon-Szabó L., et al. Metformin attenuates palmitate-induced endoplasmic reticulum stress, serine phosphorylation of IRS-1 and apoptosis in rat insulinoma cells. PLoS ONE 2014, 9:e97868.
    • (2014) PLoS ONE , vol.9 , pp. e97868
    • Simon-Szabó, L.1
  • 67
    • 79953284583 scopus 로고    scopus 로고
    • AMP-activated protein kinase activation during cardioplegia-induced hypoxia/reoxygenation injury attenuates cardiomyocytic apoptosis via reduction of endoplasmic reticulum stress
    • Yeh C.H., et al. AMP-activated protein kinase activation during cardioplegia-induced hypoxia/reoxygenation injury attenuates cardiomyocytic apoptosis via reduction of endoplasmic reticulum stress. Mediators Inflamm. 2010, 2010:130636.
    • (2010) Mediators Inflamm. , vol.2010 , pp. 130636
    • Yeh, C.H.1
  • 68
    • 73249116246 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 agonists protect pancreatic beta-cells from lipotoxic endoplasmic reticulum stress through upregulation of BiP and JunB
    • Cunha D.A., et al. Glucagon-like peptide-1 agonists protect pancreatic beta-cells from lipotoxic endoplasmic reticulum stress through upregulation of BiP and JunB. Diabetes 2009, 58:2851-2862.
    • (2009) Diabetes , vol.58 , pp. 2851-2862
    • Cunha, D.A.1
  • 69
    • 84897398609 scopus 로고    scopus 로고
    • Metformin protects endothelial function in diet-induced obese mice by inhibition of endoplasmic reticulum stress through 5' adenosine monophosphate-activated protein kinase-peroxisome proliferator-activated receptor δ pathway
    • Cheang W.S., et al. Metformin protects endothelial function in diet-induced obese mice by inhibition of endoplasmic reticulum stress through 5' adenosine monophosphate-activated protein kinase-peroxisome proliferator-activated receptor δ pathway. Arterioscler. Thromb. Vasc. Biol. 2014, 34:830-836.
    • (2014) Arterioscler. Thromb. Vasc. Biol. , vol.34 , pp. 830-836
    • Cheang, W.S.1
  • 70
    • 48449094498 scopus 로고    scopus 로고
    • AMPK and PPARδ agonists are exercise mimetics
    • Narkar V.A., et al. AMPK and PPARδ agonists are exercise mimetics. Cell 2008, 134:405-415.
    • (2008) Cell , vol.134 , pp. 405-415
    • Narkar, V.A.1
  • 71
    • 84891792481 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor δ agonist GW1516 attenuates diet-induced aortic inflammation, insulin resistance, and atherosclerosis in low-density lipoprotein receptor knockout mice
    • Bojic L.A., et al. Peroxisome proliferator-activated receptor δ agonist GW1516 attenuates diet-induced aortic inflammation, insulin resistance, and atherosclerosis in low-density lipoprotein receptor knockout mice. Arterioscler. Thromb. Vasc. Biol. 2014, 34:52-60.
    • (2014) Arterioscler. Thromb. Vasc. Biol. , vol.34 , pp. 52-60
    • Bojic, L.A.1
  • 72
    • 84924653266 scopus 로고    scopus 로고
    • PPARβ/δ prevents endoplasmic reticulum stress-associated inflammation and insulin resistance in skeletal muscle cells through an AMPK-dependent mechanism
    • Salvadó L., et al. PPARβ/δ prevents endoplasmic reticulum stress-associated inflammation and insulin resistance in skeletal muscle cells through an AMPK-dependent mechanism. Diabetologia 2014, 57:2126-2135.
    • (2014) Diabetologia , vol.57 , pp. 2126-2135
    • Salvadó, L.1
  • 73
    • 84876215872 scopus 로고    scopus 로고
    • Inhibitory cross-talk between the AMPK and ERK pathways mediates endoplasmic reticulum stress-induced insulin resistance in skeletal muscle
    • Hwang S.L., et al. Inhibitory cross-talk between the AMPK and ERK pathways mediates endoplasmic reticulum stress-induced insulin resistance in skeletal muscle. Br. J. Pharmacol. 2013, 169:69-81.
    • (2013) Br. J. Pharmacol. , vol.169 , pp. 69-81
    • Hwang, S.L.1
  • 74
    • 79957605136 scopus 로고    scopus 로고
    • Aberrant lipid metabolism disrupts calcium homeostasis causing liver endoplasmic reticulum stress in obesity
    • Fu S., et al. Aberrant lipid metabolism disrupts calcium homeostasis causing liver endoplasmic reticulum stress in obesity. Nature 2011, 473:528-531.
    • (2011) Nature , vol.473 , pp. 528-531
    • Fu, S.1
  • 75
    • 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 S.W., 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. U.S.A. 2010, 107:19320-19325.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 19320-19325
    • Park, S.W.1
  • 76
    • 84921901605 scopus 로고    scopus 로고
    • The role of endoplasmic reticulum stress in human pathology
    • Oakes S.A., Papa F.R. The role of endoplasmic reticulum stress in human pathology. Annu. Rev. Pathol. 2015, 10:173-194.
    • (2015) Annu. Rev. Pathol. , vol.10 , pp. 173-194
    • Oakes, S.A.1    Papa, F.R.2
  • 77
    • 84866905708 scopus 로고    scopus 로고
    • Discovery of 7-methyl-5-(1-{[3-(trifluoromethyl)phenyl]acetyl}-2,3-dihydro-1H-indol-5-yl)-7H-p yrrolo[2,3-d]pyrimidin-4-amine (GSK2606414), a potent and selective first-in-class inhibitor of protein kinase R (PKR)-like endoplasmic reticulum kinase (PERK)
    • Axten J.M., et al. Discovery of 7-methyl-5-(1-{[3-(trifluoromethyl)phenyl]acetyl}-2,3-dihydro-1H-indol-5-yl)-7H-p yrrolo[2,3-d]pyrimidin-4-amine (GSK2606414), a potent and selective first-in-class inhibitor of protein kinase R (PKR)-like endoplasmic reticulum kinase (PERK). J. Med. Chem. 2012, 55:7193-7207.
    • (2012) J. Med. Chem. , vol.55 , pp. 7193-7207
    • Axten, J.M.1
  • 78
    • 79953288480 scopus 로고    scopus 로고
    • Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis
    • Tsaytler P., et al. Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis. Science 2011, 332:91-94.
    • (2011) Science , vol.332 , pp. 91-94
    • Tsaytler, P.1
  • 79
    • 84921458749 scopus 로고    scopus 로고
    • Role of islet β cell autophagy in the pathogenesis of diabetes
    • Lee M.S. Role of islet β cell autophagy in the pathogenesis of diabetes. Trends Endocrinol. Metab. 2014, 25:620-627.
    • (2014) Trends Endocrinol. Metab. , vol.25 , pp. 620-627
    • Lee, M.S.1
  • 80
    • 84901237355 scopus 로고    scopus 로고
    • PPARβ/δ attenuates palmitate-induced endoplasmic reticulum stress and induces autophagic markers in human cardiac cells
    • Palomer X., et al. PPARβ/δ attenuates palmitate-induced endoplasmic reticulum stress and induces autophagic markers in human cardiac cells. Int. J. Cardiol. 2014, 174:110-118.
    • (2014) Int. J. Cardiol. , vol.174 , pp. 110-118
    • Palomer, X.1
  • 81
    • 80053985758 scopus 로고    scopus 로고
    • P38 MAPK-mediated regulation of Xbp1s is crucial for glucose homeostasis
    • Lee J., et al. p38 MAPK-mediated regulation of Xbp1s is crucial for glucose homeostasis. Nat. Med. 2011, 17:1251-1260.
    • (2011) Nat. Med. , vol.17 , pp. 1251-1260
    • Lee, J.1
  • 82
    • 84870868447 scopus 로고    scopus 로고
    • Direct association of unfolded proteins with mammalian ER stress sensor, IRE1beta
    • Oikawa D., et al. Direct association of unfolded proteins with mammalian ER stress sensor, IRE1beta. PLoS ONE 2012, 7:e51290.
    • (2012) PLoS ONE , vol.7 , pp. e51290
    • Oikawa, D.1
  • 83
    • 1642442467 scopus 로고    scopus 로고
    • Underglycosylation of ATF6 as a novel sensing mechanism for activation of the unfolded protein response
    • Hong M., et al. Underglycosylation of ATF6 as a novel sensing mechanism for activation of the unfolded protein response. J. Biol. Chem. 2004, 279:11354-11363.
    • (2004) J. Biol. Chem. , vol.279 , pp. 11354-11363
    • Hong, M.1
  • 84
    • 84899937866 scopus 로고    scopus 로고
    • Getting RIDD of RNA: IRE1 in cell fate regulation
    • Maurel M., et al. Getting RIDD of RNA: IRE1 in cell fate regulation. Trends Biochem. Sci. 2014, 39:245-254.
    • (2014) Trends Biochem. Sci. , vol.39 , pp. 245-254
    • Maurel, M.1
  • 85
    • 84868525253 scopus 로고    scopus 로고
    • IRE1alpha cleaves select microRNAs during ER stress to derepress translation of proapoptotic Caspase-2
    • Upton J.P., et al. IRE1alpha cleaves select microRNAs during ER stress to derepress translation of proapoptotic Caspase-2. Science 2012, 338:818-822.
    • (2012) Science , vol.338 , pp. 818-822
    • Upton, J.P.1
  • 86
    • 77950343252 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the inflammatory basis of metabolic disease
    • Hotamisligil G.S. 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
  • 87
    • 84864693470 scopus 로고    scopus 로고
    • Thioredoxin-interacting protein mediates ER stress-induced β cell death through initiation of the inflammasome
    • Oslowski C.M., et al. Thioredoxin-interacting protein mediates ER stress-induced β cell death through initiation of the inflammasome. Cell Metab. 2012, 16:265-273.
    • (2012) Cell Metab. , vol.16 , pp. 265-273
    • Oslowski, C.M.1
  • 88
    • 84864682160 scopus 로고    scopus 로고
    • IRE1α induces thioredoxin-interacting protein to activate the NLRP3 inflammasome and promote programmed cell death under irremediable ER stress
    • Lerner A.G., et al. IRE1α induces thioredoxin-interacting protein to activate the NLRP3 inflammasome and promote programmed cell death under irremediable ER stress. Cell Metab. 2012, 16:250-264.
    • (2012) Cell Metab. , vol.16 , pp. 250-264
    • Lerner, A.G.1


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