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Volumn 62, Issue 3, 2013, Pages 811-824

Proteasome dysfunction mediates obesity-induced endoplasmic reticulum stress and insulin resistance in the liver

Author keywords

[No Author keywords available]

Indexed keywords

BORTEZOMIB; GLUCOSE; INSULIN; PROTEASOME; PROTEIN;

EID: 84874427117     PISSN: 00121797     EISSN: 1939327X     Source Type: Journal    
DOI: 10.2337/db11-1652     Document Type: Article
Times cited : (106)

References (55)
  • 1
    • 30044438426 scopus 로고    scopus 로고
    • Stressed out about obesity and insulin resistance
    • de Luca C, Olefsky JM. Stressed out about obesity and insulin resistance. Nat Med 2006;12:41-42
    • (2006) Nat Med , vol.12 , pp. 41-42
    • De Luca, C.1    Olefsky, J.M.2
  • 2
    • 5644231992 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes
    • Ozcan U, Cao Q, Yilmaz E, et al. Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes. Science 2004;306:457-461
    • (2004) Science , vol.306 , pp. 457-461
    • Ozcan, U.1    Cao, Q.2    Yilmaz, E.3
  • 3
    • 33748069813 scopus 로고    scopus 로고
    • Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes
    • Ozcan U, Yilmaz E, Ozcan L, 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    Yilmaz, E.2    Ozcan, L.3
  • 4
    • 19944430402 scopus 로고    scopus 로고
    • Involvement of endoplasmic reticulum stress in insulin resistance and diabetes
    • Nakatani Y, Kaneto H, Kawamori D, et al. Involvement of endoplasmic reticulum stress in insulin resistance and diabetes. J Biol Chem 2005;280: 847-851
    • (2005) J Biol Chem , vol.280 , pp. 847-851
    • Nakatani, Y.1    Kaneto, H.2    Kawamori, D.3
  • 5
    • 58149316376 scopus 로고    scopus 로고
    • Obesity upregulates genes involved in oxidative phosphorylation in livers of diabetic patients
    • Takamura T, Misu H, Matsuzawa-Nagata N, et al. Obesity upregulates genes involved in oxidative phosphorylation in livers of diabetic patients. Obesity (Silver Spring) 2008;16:2601-2609
    • (2008) Obesity (Silver Spring) , vol.16 , pp. 2601-2609
    • Takamura, T.1    Misu, H.2    Matsuzawa-Nagata, N.3
  • 6
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • Voges D, Zwickl P, Baumeister W. The 26S proteasome: A molecular machine designed for controlled proteolysis. Annu Rev Biochem 1999;68: 1015-1068
    • (1999) Annu Rev Biochem , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 7
    • 0033529596 scopus 로고    scopus 로고
    • The proteasome, a novel protease regulated by multiple mechanisms
    • DeMartino GN, Slaughter CA. The proteasome, a novel protease regulated by multiple mechanisms. J Biol Chem 1999;274:22123-22126
    • (1999) J Biol Chem , vol.274 , pp. 22123-22126
    • DeMartino, G.N.1    Slaughter, C.A.2
  • 8
    • 0034640520 scopus 로고    scopus 로고
    • Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis
    • Tanahashi N, Murakami Y, Minami Y, Shimbara N, Hendil KB, Tanaka K. Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis. J Biol Chem 2000;275:14336-14345
    • (2000) J Biol Chem , vol.275 , pp. 14336-14345
    • Tanahashi, N.1    Murakami, Y.2    Minami, Y.3    Shimbara, N.4    Hendil, K.B.5    Tanaka, K.6
  • 9
    • 0030840661 scopus 로고    scopus 로고
    • Expression and subcellular localization of mouse 20S proteasome activator complex PA28
    • Soza A, Knuehl C, Groettrup M, Henklein P, Tanaka K, Kloetzel PM. Expression and subcellular localization of mouse 20S proteasome activator complex PA28. FEBS Lett 1997;413:27-34
    • (1997) FEBS Lett , vol.413 , pp. 27-34
    • Soza, A.1    Knuehl, C.2    Groettrup, M.3    Henklein, P.4    Tanaka, K.5    Kloetzel, P.M.6
  • 10
    • 3242771511 scopus 로고    scopus 로고
    • Generation of major histocompatibility complex class I antigens: Functional interplay between proteasomes and TPPII
    • Kloetzel PM. Generation of major histocompatibility complex class I antigens: Functional interplay between proteasomes and TPPII. Nat Immunol 2004;5:661-669
    • (2004) Nat Immunol , vol.5 , pp. 661-669
    • Kloetzel, P.M.1
  • 11
    • 0032778516 scopus 로고    scopus 로고
    • Impaired immunoproteasome assembly and immune responses in PA28-/-mice
    • Preckel T, Fung-Leung WP, Cai Z, et al. Impaired immunoproteasome assembly and immune responses in PA28-/-mice. Science 1999;286:2162-2165
    • (1999) Science , vol.286 , pp. 2162-2165
    • Preckel, T.1    Fung-Leung, W.P.2    Cai, Z.3
  • 12
    • 34250342888 scopus 로고    scopus 로고
    • Ubiquitin-independent degradation of cell-cycle inhibitors by the REGgamma proteasome
    • Chen X, Barton LF, Chi Y, Clurman BE, Roberts JM. Ubiquitin-independent degradation of cell-cycle inhibitors by the REGgamma proteasome. Mol Cell 2007;26:843-852
    • (2007) Mol Cell , vol.26 , pp. 843-852
    • Chen, X.1    Barton, L.F.2    Chi, Y.3    Clurman, B.E.4    Roberts, J.M.5
  • 13
    • 80052386730 scopus 로고    scopus 로고
    • Enhancement of proteasomal function protects against cardiac proteinopathy and ischemia/reperfusion injury in mice
    • Li J, Horak KM, Su H, Sanbe A, Robbins J, Wang X. Enhancement of proteasomal function protects against cardiac proteinopathy and ischemia/reperfusion injury in mice. J Clin Invest 2011;121:3689-3700
    • (2011) J Clin Invest , vol.121 , pp. 3689-3700
    • Li, J.1    Horak, K.M.2    Su, H.3    Sanbe, A.4    Robbins, J.5    Wang, X.6
  • 14
    • 67651114144 scopus 로고    scopus 로고
    • Preliminary report: Inhibition of cellular proteasome activity by free fatty acids
    • Hamel FG. Preliminary report: Inhibition of cellular proteasome activity by free fatty acids. Metabolism 2009;58:1047-1049
    • (2009) Metabolism , vol.58 , pp. 1047-1049
    • Hamel, F.G.1
  • 15
    • 4544304395 scopus 로고    scopus 로고
    • Peroxynitrite alters the catalytic activity of rodent liver proteasome in vitro and in vivo
    • Osna NA, Haorah J, Krutik VM, Donohue TM Jr. Peroxynitrite alters the catalytic activity of rodent liver proteasome in vitro and in vivo. Hepatology 2004;40:574-582
    • (2004) Hepatology , vol.40 , pp. 574-582
    • Osna, N.A.1    Haorah, J.2    Krutik, V.M.3    Donohue Jr., T.M.4
  • 16
    • 34247637323 scopus 로고    scopus 로고
    • Genes involved in oxidative phosphorylation are coordinately upregulated with fasting hyperglycaemia in livers of patients with type 2 diabetes
    • Misu H, Takamura T, Matsuzawa N, et al. Genes involved in oxidative phosphorylation are coordinately upregulated with fasting hyperglycaemia in livers of patients with type 2 diabetes. Diabetologia 2007;50:268-277
    • (2007) Diabetologia , vol.50 , pp. 268-277
    • Misu, H.1    Takamura, T.2    Matsuzawa, N.3
  • 17
    • 0037391756 scopus 로고    scopus 로고
    • Predicting hepatitis B virus-positive metastatic hepatocellular carcinomas using gene expression profiling and supervised machine learning
    • Ye QH, Qin LX, Forgues M, et al. Predicting hepatitis B virus-positive metastatic hepatocellular carcinomas using gene expression profiling and supervised machine learning. Nat Med 2003;9:416-423
    • (2003) Nat Med , vol.9 , pp. 416-423
    • Ye, Q.H.1    Qin, L.X.2    Forgues, M.3
  • 18
    • 17944369433 scopus 로고    scopus 로고
    • Immunoproteasome assembly and antigen presentation in mice lacking both PA28alpha and PA28beta
    • Murata S, Udono H, Tanahashi N, et al. Immunoproteasome assembly and antigen presentation in mice lacking both PA28alpha and PA28beta. EMBO J 2001;20:5898-5907
    • (2001) EMBO J , vol.20 , pp. 5898-5907
    • Murata, S.1    Udono, H.2    Tanahashi, N.3
  • 19
    • 0033621341 scopus 로고    scopus 로고
    • Growth retardation in mice lacking the proteasome activator PA28gamma
    • Murata S, Kawahara H, Tohma S, et al. Growth retardation in mice lacking the proteasome activator PA28gamma. J Biol Chem 1999;274:38211-38215
    • (1999) J Biol Chem , vol.274 , pp. 38211-38215
    • Murata, S.1    Kawahara, H.2    Tohma, S.3
  • 20
    • 84555195142 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress inhibits STAT3-dependent suppression of hepatic gluconeogenesis via dephosphorylation and deacetylation
    • Kimura K, Yamada T, Matsumoto M, et al. Endoplasmic reticulum stress inhibits STAT3-dependent suppression of hepatic gluconeogenesis via dephosphorylation and deacetylation. Diabetes 2012;61:61-73
    • (2012) Diabetes , vol.61 , pp. 61-73
    • Kimura, K.1    Yamada, T.2    Matsumoto, M.3
  • 21
    • 60549117283 scopus 로고    scopus 로고
    • The hepatic circadian clock is preserved in a lipid-induced mouse model of non-alcoholic steatohepatitis
    • Ando H, Takamura T, Matsuzawa-Nagata N, et al. The hepatic circadian clock is preserved in a lipid-induced mouse model of non-alcoholic steatohepatitis. Biochem Biophys Res Commun 2009;380:684-688
    • (2009) Biochem Biophys Res Commun , vol.380 , pp. 684-688
    • Ando, H.1    Takamura, T.2    Matsuzawa-Nagata, N.3
  • 22
    • 2442654220 scopus 로고    scopus 로고
    • Genes for systemic vascular complications are differentially expressed in the livers of type 2 diabetic patients
    • Takamura T, Sakurai M, Ota T, Ando H, Honda M, Kaneko S. Genes for systemic vascular complications are differentially expressed in the livers of type 2 diabetic patients. Diabetologia 2004;47:638-647
    • (2004) Diabetologia , vol.47 , pp. 638-647
    • Takamura, T.1    Sakurai, M.2    Ota, T.3    Ando, H.4    Honda, M.5    Kaneko, S.6
  • 23
    • 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
  • 24
    • 1342265394 scopus 로고    scopus 로고
    • Proteasome inhibition increases HuR level, restores heat-inducible HSP72 expression and thermotolerance in WI-38 senescent human fibroblasts
    • Bonelli MA, Alfieri RR, Desenzani S, Petronini PG, Borghetti AF. Proteasome inhibition increases HuR level, restores heat-inducible HSP72 expression and thermotolerance in WI-38 senescent human fibroblasts. Exp Gerontol 2004;39:423-432
    • (2004) Exp Gerontol , vol.39 , pp. 423-432
    • Bonelli, M.A.1    Alfieri, R.R.2    Desenzani, S.3    Petronini, P.G.4    Borghetti, A.F.5
  • 25
    • 78049428301 scopus 로고    scopus 로고
    • A liver-derived secretory protein, selenoprotein P, causes insulin resistance
    • Misu H, Takamura T, Takayama H, et al. A liver-derived secretory protein, selenoprotein P, causes insulin resistance. Cell Metab 2010;12:483-495
    • (2010) Cell Metab , vol.12 , pp. 483-495
    • Misu, H.1    Takamura, T.2    Takayama, H.3
  • 26
    • 38649116056 scopus 로고    scopus 로고
    • Selective versus total insulin resistance: A pathogenic paradox
    • Brown MS, Goldstein JL. Selective versus total insulin resistance: A pathogenic paradox. Cell Metab 2008;7:95-96
    • (2008) Cell Metab , vol.7 , pp. 95-96
    • Brown, M.S.1    Goldstein, J.L.2
  • 27
    • 33845480131 scopus 로고    scopus 로고
    • Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response
    • Bernales S, McDonald KL, Walter P. Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response. PLoS Biol 2006;4:e423
    • (2006) PLoS Biol , vol.4
    • Bernales, S.1    McDonald, K.L.2    Walter, P.3
  • 28
    • 0036437307 scopus 로고    scopus 로고
    • Transcriptional and translational control in the Mammalian unfolded protein response
    • Harding HP, Calfon M, Urano F, Novoa I, Ron D. Transcriptional and translational control in the Mammalian unfolded protein response. Annu Rev Cell Dev Biol 2002;18:575-599
    • (2002) Annu Rev Cell Dev Biol , vol.18 , pp. 575-599
    • Harding, H.P.1    Calfon, M.2    Urano, F.3    Novoa, I.4    Ron, D.5
  • 29
    • 0036086064 scopus 로고    scopus 로고
    • The unfolded protein response in nutrient sensing and differentiation
    • Kaufman RJ, Scheuner D, Schröder M, et al. The unfolded protein response in nutrient sensing and differentiation. Nat Rev Mol Cell Biol 2002;3:411-421
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 411-421
    • Kaufman, R.J.1    Scheuner, D.2    Schröder, M.3
  • 30
    • 69549135927 scopus 로고    scopus 로고
    • Hepatic CYP3A suppression by high concentrations of proteasomal inhibitors: A consequence of endoplasmic reticulum (ER) stress induction, activation of RNA-dependent protein kinase-like ER-bound eukaryotic initiation factor 2alpha (eIF2alpha)-kinase (PERK) and general control nonderepressible-2 eIF2alpha kinase (GCN2), and global translational shutoff
    • Acharya P, Engel JC, Correia MA. Hepatic CYP3A suppression by high concentrations of proteasomal inhibitors: A consequence of endoplasmic reticulum (ER) stress induction, activation of RNA-dependent protein kinase-like ER-bound eukaryotic initiation factor 2alpha (eIF2alpha)-kinase (PERK) and general control nonderepressible-2 eIF2alpha kinase (GCN2), and global translational shutoff. Mol Pharmacol 2009;76:503-515
    • (2009) Mol Pharmacol , vol.76 , pp. 503-515
    • Acharya, P.1    Engel, J.C.2    Correia, M.A.3
  • 31
    • 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
  • 32
    • 18244370762 scopus 로고    scopus 로고
    • Inflammation, stress, and diabetes
    • Wellen KE, Hotamisligil GS. Inflammation, stress, and diabetes. J Clin Invest 2005;115:1111-1119
    • (2005) J Clin Invest , vol.115 , pp. 1111-1119
    • Wellen, K.E.1    Hotamisligil, G.S.2
  • 33
    • 0141706357 scopus 로고    scopus 로고
    • Insulin-induced phosphorylation of FKHR (Foxo1) targets to proteasomal degradation
    • Matsuzaki H, Daitoku H, Hatta M, Tanaka K, Fukamizu A. Insulin-induced phosphorylation of FKHR (Foxo1) targets to proteasomal degradation. Proc Natl Acad Sci USA 2003;100:11285-11290
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 11285-11290
    • Matsuzaki, H.1    Daitoku, H.2    Hatta, M.3    Tanaka, K.4    Fukamizu, A.5
  • 34
    • 4544312844 scopus 로고    scopus 로고
    • Proteasomal degradation of the FoxO1 transcriptional regulator in cells transformed by the P3k and Akt oncoproteins
    • Aoki M, Jiang H, Vogt PK. Proteasomal degradation of the FoxO1 transcriptional regulator in cells transformed by the P3k and Akt oncoproteins. Proc Natl Acad Sci USA 2004;101:13613-13617
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13613-13617
    • Aoki, M.1    Jiang, H.2    Vogt, P.K.3
  • 35
    • 13444252337 scopus 로고    scopus 로고
    • Skp2 inhibits FOXO1 in tumor suppression through ubiquitin-mediated degradation
    • Huang H, Regan KM, Wang F, et al. Skp2 inhibits FOXO1 in tumor suppression through ubiquitin-mediated degradation. Proc Natl Acad Sci USA 2005;102:1649-1654
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 1649-1654
    • Huang, H.1    Regan, K.M.2    Wang, F.3
  • 36
    • 79957605136 scopus 로고    scopus 로고
    • Aberrant lipid metabolism disrupts calcium homeostasis causing liver endoplasmic reticulum stress in obesity
    • Fu S, Yang L, Li P, 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    Yang, L.2    Li, P.3
  • 37
    • 84866184236 scopus 로고    scopus 로고
    • Polysome profiling in liver identifies dynamic regulation of endoplasmic reticulum translatome by obesity and fasting
    • Fu S, Fan J, Blanco J, et al. Polysome profiling in liver identifies dynamic regulation of endoplasmic reticulum translatome by obesity and fasting. PLoS Genet 2012;8:e1002902
    • (2012) PLoS Genet , vol.8
    • Fu, S.1    Fan, J.2    Blanco, J.3
  • 38
    • 77956400005 scopus 로고    scopus 로고
    • Defective hepatic autophagy in obesity promotes ER stress and causes insulin resistance
    • Yang L, Li P, Fu S, Calay ES, Hotamisligil GS. 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    Li, P.2    Fu, S.3    Calay, E.S.4    Hotamisligil, G.S.5
  • 39
    • 77950362951 scopus 로고    scopus 로고
    • Hyperglycemia impairs proteasome function by methylglyoxal
    • Queisser MA, Yao D, Geisler S, et al. Hyperglycemia impairs proteasome function by methylglyoxal. Diabetes 2010;59:670-678
    • (2010) Diabetes , vol.59 , pp. 670-678
    • Queisser, M.A.1    Yao, D.2    Geisler, S.3
  • 40
    • 0032731757 scopus 로고    scopus 로고
    • Diabetes induces an impairment in the proteolytic activity against oxidized proteins and a heterogeneous effect in nonenzymatic protein modifications in the cytosol of rat liver and kidney
    • Portero-Otín M, Pamplona R, Ruiz MC, Cabiscol E, Prat J, Bellmunt MJ. Diabetes induces an impairment in the proteolytic activity against oxidized proteins and a heterogeneous effect in nonenzymatic protein modifications in the cytosol of rat liver and kidney. Diabetes 1999;48: 2215-2220
    • (1999) Diabetes , vol.48 , pp. 2215-2220
    • Portero-Otín, M.1    Pamplona, R.2    Ruiz, M.C.3    Cabiscol, E.4    Prat, J.5    Bellmunt, M.J.6
  • 41
    • 33747619854 scopus 로고    scopus 로고
    • Insulin resistance accelerates muscle protein degradation: Activation of the ubiquitin-proteasome pathway by defects in muscle cell signaling
    • Wang X, Hu Z, Hu J, Du J, Mitch WE. Insulin resistance accelerates muscle protein degradation: Activation of the ubiquitin-proteasome pathway by defects in muscle cell signaling. Endocrinology 2006;147:4160-4168
    • (2006) Endocrinology , vol.147 , pp. 4160-4168
    • Wang, X.1    Hu, Z.2    Hu, J.3    Du, J.4    Mitch, W.E.5
  • 42
    • 57849115277 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress plays a central role in development of leptin resistance
    • Ozcan L, Ergin AS, Lu A, et al. Endoplasmic reticulum stress plays a central role in development of leptin resistance. Cell Metab 2009;9:35-51
    • (2009) Cell Metab , vol.9 , pp. 35-51
    • Ozcan, L.1    Ergin, A.S.2    Lu, A.3
  • 43
    • 84863950705 scopus 로고    scopus 로고
    • Brown rice and its component, g-oryzanol, attenuate the preference for high-fat diet by decreasing hypothalamic endoplasmic reticulum stress in mice
    • Kozuka C, Yabiku K, Sunagawa S, et al. Brown rice and its component, g-oryzanol, attenuate the preference for high-fat diet by decreasing hypothalamic endoplasmic reticulum stress in mice. Diabetes 2012;61:3084-3093
    • (2012) Diabetes , vol.61 , pp. 3084-3093
    • Kozuka, C.1    Yabiku, K.2    Sunagawa, S.3
  • 44
    • 47149115165 scopus 로고    scopus 로고
    • Increased oxidative stress precedes the onset of high-fat diet-induced insulin resistance and obesity
    • Matsuzawa-Nagata N, Takamura T, Ando H, et al. Increased oxidative stress precedes the onset of high-fat diet-induced insulin resistance and obesity. Metabolism 2008;57:1071-1077
    • (2008) Metabolism , vol.57 , pp. 1071-1077
    • Matsuzawa-Nagata, N.1    Takamura, T.2    Ando, H.3
  • 45
    • 67649304876 scopus 로고    scopus 로고
    • Palmitate induces insulin resistance in H4IIEC3 hepatocytes through reactive oxygen species produced by mitochondria
    • Nakamura S, Takamura T, Matsuzawa-Nagata N, et al. Palmitate induces insulin resistance in H4IIEC3 hepatocytes through reactive oxygen species produced by mitochondria. J Biol Chem 2009;284:14809-14818
    • (2009) J Biol Chem , vol.284 , pp. 14809-14818
    • Nakamura, S.1    Takamura, T.2    Matsuzawa-Nagata, N.3
  • 46
    • 79954590790 scopus 로고    scopus 로고
    • Enhancement of proteasome function by PA28α overexpression protects against oxidative stress
    • Li J, Powell SR, Wang X. Enhancement of proteasome function by PA28α overexpression protects against oxidative stress. FASEB J 2011;25:883-893
    • (2011) FASEB J , vol.25 , pp. 883-893
    • Li, J.1    Powell, S.R.2    Wang, X.3
  • 47
    • 77955596988 scopus 로고    scopus 로고
    • Immunoproteasomes preserve protein homeostasis upon interferon-induced oxidative stress
    • Seifert U, Bialy LP, Ebstein F, et al. Immunoproteasomes preserve protein homeostasis upon interferon-induced oxidative stress. Cell 2010;142:613-624
    • (2010) Cell , vol.142 , pp. 613-624
    • Seifert, U.1    Bialy, L.P.2    Ebstein, F.3
  • 49
    • 45849137877 scopus 로고    scopus 로고
    • Regulation of hepatic lipogenesis by the transcription factor XBP1
    • Lee AH, Scapa EF, Cohen DE, Glimcher LH. Regulation of hepatic lipogenesis by the transcription factor XBP1. Science 2008;320:1492-1496
    • (2008) Science , vol.320 , pp. 1492-1496
    • Lee, A.H.1    Scapa, E.F.2    Cohen, D.E.3    Glimcher, L.H.4
  • 50
    • 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
  • 51
    • 0035965231 scopus 로고    scopus 로고
    • Direct demonstration of rapid degradation of nuclear sterol regulatory element-binding proteins by the ubiquitin-proteasome pathway
    • Hirano Y, Yoshida M, Shimizu M, Sato R. Direct demonstration of rapid degradation of nuclear sterol regulatory element-binding proteins by the ubiquitin-proteasome pathway. J Biol Chem 2001;276:36431-36437
    • (2001) J Biol Chem , vol.276 , pp. 36431-36437
    • Hirano, Y.1    Yoshida, M.2    Shimizu, M.3    Sato, R.4
  • 52
    • 79952381078 scopus 로고    scopus 로고
    • Regulation of glucose homeostasis through a XBP-1-FoxO1 interaction
    • Zhou Y, Lee J, Reno CM, 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    Lee, J.2    Reno, C.M.3
  • 53
    • 33744965755 scopus 로고    scopus 로고
    • Essential role of ubiquitinproteasome system in normal regulation of insulin secretion
    • Kawaguchi M, Minami K, Nagashima K, Seino S. Essential role of ubiquitinproteasome system in normal regulation of insulin secretion. J Biol Chem 2006;281:13015-13020
    • (2006) J Biol Chem , vol.281 , pp. 13015-13020
    • Kawaguchi, M.1    Minami, K.2    Nagashima, K.3    Seino, S.4
  • 54
    • 78751490442 scopus 로고    scopus 로고
    • B-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. b-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
  • 55
    • 79952410092 scopus 로고    scopus 로고
    • Sodium phenylbutyrate, a drug with known capacity to reduce endoplasmic reticulum stress, partially alleviates lipidinduced insulin resistance and beta-cell dysfunction in humans
    • Xiao C, Giacca A, Lewis GF. Sodium phenylbutyrate, a drug with known capacity to reduce endoplasmic reticulum stress, partially alleviates lipidinduced insulin resistance and beta-cell dysfunction in humans. Diabetes 2011;60:918-924
    • (2011) Diabetes , vol.60 , pp. 918-924
    • Xiao, C.1    Giacca, A.2    Lewis, G.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.