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Volumn 6, Issue , 2016, Pages

Insulin enhanced leptin-induced STAT3 signaling by inducing GRP78

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EID: 84989288330     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep34312     Document Type: Article
Times cited : (11)

References (46)
  • 1
    • 51849146897 scopus 로고    scopus 로고
    • Global burden of obesity in 2005 and projections to 2030
    • Kelly, T., Yang, W., Chen, C. S., Reynolds, K. & He, J. Global burden of obesity in 2005 and projections to 2030. Int J Obes (Lond). 32, 1431-7 (2008).
    • (2008) Int J Obes (Lond) , vol.32 , pp. 1431-1437
    • Kelly, T.1    Yang, W.2    Chen, C.S.3    Reynolds, K.4    He, J.5
  • 2
    • 84920108541 scopus 로고    scopus 로고
    • Recent prevalence of child and adolescent overweight and obesity in France and abroad
    • Castetbon, K. Recent prevalence of child and adolescent overweight and obesity in France and abroad. Arch Pediatr. 22, 111-5 (2015).
    • (2015) Arch Pediatr , vol.22 , pp. 111-115
    • Castetbon, K.1
  • 3
    • 0034611791 scopus 로고    scopus 로고
    • Obesity as a medical problem
    • Kopelman, P. G. Obesity as a medical problem. Nature. 404, 635-43 (2000).
    • (2000) Nature , vol.404 , pp. 635-643
    • Kopelman, P.G.1
  • 4
    • 0029739826 scopus 로고    scopus 로고
    • Leptin activation of Stat3 in the hypothalamus of wild-type and ob/ob mice but not db/db mice
    • Vaisse, C., Halaas, J. L., Horvath, C. M., Darnell, J. E. Jr., Stoffel, M. & Friedman, J. M. Leptin activation of Stat3 in the hypothalamus of wild-type and ob/ob mice but not db/db mice. Nat Genet 14, 95-7 (1996).
    • (1996) Nat Genet , vol.14 , pp. 95-97
    • Vaisse, C.1    Halaas, J.L.2    Horvath, C.M.3    Darnell, J.E.4    Stoffel, M.5    Friedman, J.M.6
  • 5
    • 0036720939 scopus 로고    scopus 로고
    • Brain stem is a direct target for leptins action in the central nervous system
    • Hosoi, T., Kawagishi, T., Okuma, Y., Tanaka, J. & Nomura, Y. Brain stem is a direct target for leptins action in the central nervous system. Endocrinology 143, 3498-504 (2002).
    • (2002) Endocrinology , vol.143 , pp. 3498-3504
    • Hosoi, T.1    Kawagishi, T.2    Okuma, Y.3    Tanaka, J.4    Nomura, Y.5
  • 6
    • 79957896666 scopus 로고    scopus 로고
    • Sixteen years and counting: An update on leptin in energy balance
    • Gautron, L. & Elmquist J. K. Sixteen years and counting: an update on leptin in energy balance. J Clin Invest 121, 2087-93 (2011).
    • (2011) J Clin Invest , vol.121 , pp. 2087-2093
    • Gautron, L.1    Elmquist, J.K.2
  • 7
    • 0018621289 scopus 로고
    • Chronic intracerebroventricular infusion of insulin reduces food intake and body weight of baboons
    • Woods, S. C., Lotter, E. C., McKay, L. D. & Porte, D. Jr. Chronic intracerebroventricular infusion of insulin reduces food intake and body weight of baboons. Nature. 282, 503-5 (1979).
    • (1979) Nature , vol.282 , pp. 503-505
    • Woods, S.C.1    Lotter, E.C.2    McKay, L.D.3    Porte, D.4
  • 8
    • 0842324779 scopus 로고    scopus 로고
    • Obesity wars: Molecular progress confronts an expanding epidemic
    • Flier, J. S. Obesity wars: molecular progress confronts an expanding epidemic. Cell. 116, 337-50 (2004).
    • (2004) Cell , vol.116 , pp. 337-350
    • Flier, J.S.1
  • 9
    • 0037315042 scopus 로고    scopus 로고
    • Insulin activation of phosphatidylinositol 3-kinase in the hypothalamic arcuate nucleus: A key mediator of insulin-induced anorexia
    • Niswender, K. D. et al. Insulin activation of phosphatidylinositol 3-kinase in the hypothalamic arcuate nucleus: a key mediator of insulin-induced anorexia. Diabetes. 52, 227-31 (2003).
    • (2003) Diabetes , vol.52 , pp. 227-231
    • Niswender, K.D.1
  • 10
    • 33645071314 scopus 로고    scopus 로고
    • Insulin action in the brain contributes to glucose lowering during insulin treatment of diabetes
    • Gelling, R. W. et al. Insulin action in the brain contributes to glucose lowering during insulin treatment of diabetes. Cell Metab. 3, 67-73 (2006).
    • (2006) Cell Metab , vol.3 , pp. 67-73
    • Gelling, R.W.1
  • 11
    • 0034703229 scopus 로고    scopus 로고
    • Role of brain insulin receptor in control of body weight and reproduction
    • Bruning, J. C. et al. Role of brain insulin receptor in control of body weight and reproduction. Science. 289, 2122-5 (2000).
    • (2000) Science , vol.289 , pp. 2122-2125
    • Bruning, J.C.1
  • 12
    • 0034776770 scopus 로고    scopus 로고
    • Selective deletion of leptin receptor in neurons leads to obesity
    • Cohen, P. et al. Selective deletion of leptin receptor in neurons leads to obesity. J Clin Invest. 108, 1113-21 (2001).
    • (2001) J Clin Invest , vol.108 , pp. 1113-1121
    • Cohen, P.1
  • 13
    • 20644434143 scopus 로고    scopus 로고
    • Cross-talk between the insulin and leptin signaling systems in rat hypothalamus
    • Carvalheira, J. B. et al. Cross-talk between the insulin and leptin signaling systems in rat hypothalamus. Obes Res. 13, 48-57 (2005).
    • (2005) Obes Res , vol.13 , pp. 48-57
    • Carvalheira, J.B.1
  • 14
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls
    • Kaufman, R. J. Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev. 13, 1211-33 (1999).
    • (1999) Genes Dev , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 15
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • Harding, H. P., Zhang, Y. & Ron, D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature. 397, 271-4 (1999).
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 16
    • 0034716887 scopus 로고    scopus 로고
    • Tripartite management of unfolded proteins in the endoplasmic reticulum
    • Mori, K. Tripartite management of unfolded proteins in the endoplasmic reticulum. Cell. 101, 451-4 (2000).
    • (2000) Cell , vol.101 , pp. 451-454
    • Mori, K.1
  • 17
    • 0033780610 scopus 로고    scopus 로고
    • A regulatory link between ER-associated protein degradation and the unfolded-protein response
    • Friedlander, R., Jarosch, E., Urban, J., Volkwein, C. & Sommer, T. A regulatory link between ER-associated protein degradation and the unfolded-protein response. Nat Cell Biol. 2, 379-84 (2000).
    • (2000) Nat Cell Biol , vol.2 , pp. 379-384
    • Friedlander, R.1    Jarosch, E.2    Urban, J.3    Volkwein, C.4    Sommer, T.5
  • 18
    • 18344388462 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program: Role of the ER chaperone GRP78
    • Rao, R. V. et al. Coupling endoplasmic reticulum stress to the cell death program: role of the ER chaperone GRP78. FEBS Lett. 514, 122-8 (2002).
    • (2002) FEBS Lett , vol.514 , pp. 122-128
    • Rao, R.V.1
  • 19
    • 15944366885 scopus 로고    scopus 로고
    • The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress
    • Lee, A. S. The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress. Methods. 35, 373-81 (2005).
    • (2005) Methods , vol.35 , pp. 373-381
    • Lee, A.S.1
  • 20
    • 33645141853 scopus 로고    scopus 로고
    • ER stress and neurodegenerative diseases
    • Lindholm, D., Wootz, H. & Korhonen, L. ER stress and neurodegenerative diseases. Cell Death Differ. 13, 385-92 (2006).
    • (2006) Cell Death Differ , vol.13 , pp. 385-392
    • Lindholm, D.1    Wootz, H.2    Korhonen, L.3
  • 21
    • 7744232493 scopus 로고    scopus 로고
    • Misfolded proteins, endoplasmic reticulum stress and neurodegeneration
    • Rao, R. V. & Bredesen, D. E. Misfolded proteins, endoplasmic reticulum stress and neurodegeneration. Curr Opin Cell Biol. 16, 653-62 (2004).
    • (2004) Curr Opin Cell Biol. , vol.16 , pp. 653-662
    • Rao, R.V.1    Bredesen, D.E.2
  • 22
    • 0036895383 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the development of diabetes: A review
    • Harding, H. P. & Ron, D. Endoplasmic reticulum stress and the development of diabetes: a review. Diabetes. 51 Suppl 3, S455-61 (2002).
    • (2002) Diabetes , vol.51 , pp. S455-S461
    • Harding, H.P.1    Ron, D.2
  • 23
    • 10344222124 scopus 로고    scopus 로고
    • The role of the unfolded protein response in tumour development: Friend or foe?
    • Ma, Y. & Hendershot, L. M. The role of the unfolded protein response in tumour development: friend or foe? Nat Rev Cancer. 4, 966-77 (2004).
    • (2004) Nat Rev Cancer. , vol.4 , pp. 966-977
    • Ma, Y.1    Hendershot, L.M.2
  • 24
    • 56749112559 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induces leptin resistance
    • Hosoi, T. et al. Endoplasmic reticulum stress induces leptin resistance. Mol Pharmacol 74, 1610-9 (2008).
    • (2008) Mol Pharmacol , vol.74 , pp. 1610-1619
    • Hosoi, T.1
  • 25
    • 5644231992 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes
    • Ozcan, U. et al. Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes. Science. 306, 457-61 (2004).
    • (2004) Science , vol.306 , pp. 457-461
    • Ozcan, U.1
  • 26
    • 52949096557 scopus 로고    scopus 로고
    • Hypothalamic IKKbeta/NF-kappaB and ER stress link overnutrition to energy imbalance and obesity
    • Zhang, X. et al. Hypothalamic IKKbeta/NF-kappaB and ER stress link overnutrition to energy imbalance and obesity. Cell 135, 61-73 (2008).
    • (2008) Cell , vol.135 , pp. 61-73
    • Zhang, X.1
  • 27
    • 17844401180 scopus 로고    scopus 로고
    • Molecular and anatomical determinants of central leptin resistance
    • Munzberg, H. & Myers, M. G. Jr. Molecular and anatomical determinants of central leptin resistance. Nat Neurosci 8, 566-70 (2005).
    • (2005) Nat Neurosci , vol.8 , pp. 566-570
    • Munzberg, H.1    Myers, M.G.2
  • 28
    • 77955661055 scopus 로고    scopus 로고
    • Insulin modulates induction of glucose-regulated protein 78 during endoplasmic reticulum stress via augmentation of ATF4 expression in human neuroblastoma cells
    • Inageda, K. Insulin modulates induction of glucose-regulated protein 78 during endoplasmic reticulum stress via augmentation of ATF4 expression in human neuroblastoma cells. FEBS Lett. 584, 3649-54 (2010).
    • (2010) FEBS Lett , vol.584 , pp. 3649-3654
    • Inageda, K.1
  • 29
    • 0033593461 scopus 로고    scopus 로고
    • Signaling mechanisms that regulate glucose transport
    • Czech, M. P. & Corvera, S. Signaling mechanisms that regulate glucose transport. J Biol Chem. 274, 1865-8 (1999).
    • (1999) J Biol Chem , vol.274 , pp. 1865-1868
    • Czech, M.P.1    Corvera, S.2
  • 30
    • 0034947869 scopus 로고    scopus 로고
    • Mammalian target of rapamycin pathway regulates insulin signaling via subcellular redistribution of insulin receptor substrate 1 and integrates nutritional signals and metabolic signals of insulin
    • Takano, A. et al. Mammalian target of rapamycin pathway regulates insulin signaling via subcellular redistribution of insulin receptor substrate 1 and integrates nutritional signals and metabolic signals of insulin. Mol Cell Biol. 21, 5050-62 (2001).
    • (2001) Mol Cell Biol , vol.21 , pp. 5050-5062
    • Takano, A.1
  • 31
    • 53149105150 scopus 로고    scopus 로고
    • Phosphoinositides in insulin action on GLUT4 dynamics: Not just PtdIns(3,4,5)P3
    • Shisheva, A. Phosphoinositides in insulin action on GLUT4 dynamics: not just PtdIns(3,4,5)P3. Am J Physiol Endocrinol Metab. 295, E536-44 (2008).
    • (2008) Am J Physiol Endocrinol Metab , vol.295 , pp. E536-E544
    • Shisheva, A.1
  • 32
    • 0030013326 scopus 로고    scopus 로고
    • Stimulation of protein synthesis eukaryotic translation initiation factor 4E phosphorylation, and PHAS-I phosphorylation by insulin requires insulin receptor substrate 1 and phosphatidylinositol 3-kinase
    • Mendez, R., Myers, M. G. Jr., White, M. F. & Rhoads, R. E. Stimulation of protein synthesis, eukaryotic translation initiation factor 4E phosphorylation, and PHAS-I phosphorylation by insulin requires insulin receptor substrate 1 and phosphatidylinositol 3-kinase. Mol Cell Biol. 16, 2857-64 (1996).
    • (1996) Mol Cell Biol , vol.16 , pp. 2857-2864
    • Mendez, R.1    Myers, M.G.2    White, M.F.3    Rhoads, R.E.4
  • 33
    • 0035816407 scopus 로고    scopus 로고
    • Insulin modulates leptin-induced STAT3 activation in rat hypothalamus
    • Carvalheira, J. B. et al. Insulin modulates leptin-induced STAT3 activation in rat hypothalamus. FEBS Lett. 500, 119-24 (2001).
    • (2001) FEBS Lett , vol.500 , pp. 119-124
    • Carvalheira, J.B.1
  • 34
    • 30044447631 scopus 로고    scopus 로고
    • Leptin regulates insulin sensitivity via phosphatidylinositol-3-OH kinase signaling in mediobasal hypothalamic neurons
    • Morton, G. J., Gelling, R. W., Niswender, K. D., Morrison, C. D., Rhodes, C. J. & Schwartz, M. W. Leptin regulates insulin sensitivity via phosphatidylinositol-3-OH kinase signaling in mediobasal hypothalamic neurons. Cell Metab. 2, 411-20 (2005).
    • (2005) Cell Metab , vol.2 , pp. 411-420
    • Morton, G.J.1    Gelling, R.W.2    Niswender, K.D.3    Morrison, C.D.4    Rhodes, C.J.5    Schwartz, M.W.6
  • 35
    • 84865421678 scopus 로고    scopus 로고
    • GRP78/BiP is a novel downstream target of IGF-1 receptor mediated signaling
    • Pfaffenbach, K. T. et al. GRP78/BiP is a novel downstream target of IGF-1 receptor mediated signaling. J Cell Physiol. 227, 3803-11 (2012).
    • (2012) J Cell Physiol , vol.227 , pp. 3803-3811
    • Pfaffenbach, K.T.1
  • 36
    • 0029896530 scopus 로고    scopus 로고
    • Role of leptin in the neuroendocrine response to fasting
    • Ahima, R. S. et al. Role of leptin in the neuroendocrine response to fasting. Nature. 382, 250-2 (1996).
    • (1996) Nature , vol.382 , pp. 250-252
    • Ahima, R.S.1
  • 37
    • 84877877476 scopus 로고    scopus 로고
    • Cellular insulin resistance disrupts leptin-mediated control of neuronal signaling and transcription
    • Nazarians-Armavil, A., Menchella, J. A. & Belsham, D. D. Cellular insulin resistance disrupts leptin-mediated control of neuronal signaling and transcription. Mol Endocrinol. 27, 990-1003 (2013).
    • (2013) Mol Endocrinol , vol.27 , pp. 990-1003
    • Nazarians-Armavil, A.1    Menchella, J.A.2    Belsham, D.D.3
  • 38
    • 0029881125 scopus 로고    scopus 로고
    • Cerebrospinal fluid leptin levels: Relationship to plasma levels and to adiposity in humans
    • Schwartz, M. W., Peskind, E., Raskind, M., Boyko, E. J. & Porte, D. Jr. Cerebrospinal fluid leptin levels: relationship to plasma levels and to adiposity in humans. Nat Med. 2, 589-93 (1996).
    • (1996) Nat Med. , vol.2 , pp. 589-593
    • Schwartz, M.W.1    Peskind, E.2    Raskind, M.3    Boyko, E.J.4    Porte, D.5
  • 39
    • 0014142582 scopus 로고
    • The significance of basal insulin levels in the evaluation of the insulin response to glucose in diabetic and nondiabetic subjects
    • Bagdade, J. D., Bierman, E. L. & Porte, D. Jr. The significance of basal insulin levels in the evaluation of the insulin response to glucose in diabetic and nondiabetic subjects. J Clin Invest. 46, 1549-57 (1967).
    • (1967) J Clin Invest. , vol.46 , pp. 1549-1557
    • Bagdade, J.D.1    Bierman, E.L.2    Porte, D.3
  • 40
    • 0028825577 scopus 로고
    • Recombinant ob protein reduces feeding and body weight in the ob/ob mouse
    • Weigle, D. S. et al. Recombinant ob protein reduces feeding and body weight in the ob/ob mouse. J Clin Invest. 96, 2065-70 (1995).
    • (1995) J Clin Invest , vol.96 , pp. 2065-2070
    • Weigle, D.S.1
  • 41
    • 70350203976 scopus 로고    scopus 로고
    • Central leptin action improves skeletal muscle AKT AMPK and PGC1 alpha activation by hypothalamic PI3Kdependent mechanism
    • Roman, E. A. et al. Central leptin action improves skeletal muscle AKT, AMPK, and PGC1 alpha activation by hypothalamic PI3Kdependent mechanism. Mol Cell Endocrinol. 314, 62-9 (2010).
    • (2010) Mol Cell Endocrinol , vol.314 , pp. 62-69
    • Roman, E.A.1
  • 42
    • 0035950093 scopus 로고    scopus 로고
    • Intracellular signalling. Key enzyme in leptin-induced anorexia
    • Niswender, K. D. et al. Intracellular signalling. Key enzyme in leptin-induced anorexia. Nature. 413, 794-5 (2001).
    • (2001) Nature , vol.413 , pp. 794-795
    • Niswender, K.D.1
  • 43
    • 57849115277 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress plays a central role in development of leptin resistance
    • Ozcan, L. et al. Endoplasmic reticulum stress plays a central role in development of leptin resistance. Cell Metab. 9, 35-51 (2009).
    • (2009) Cell Metab , vol.9 , pp. 35-51
    • Ozcan, L.1
  • 44
    • 84923347695 scopus 로고    scopus 로고
    • Leptin induced GRP78 expression through the PI3K-mTOR pathway in neuronal cells
    • Thon, M., Hosoi, T., Yoshii, M. & Ozawa, K. Leptin induced GRP78 expression through the PI3K-mTOR pathway in neuronal cells. Sci Rep. 4, 7096 (2014).
    • (2014) Sci Rep , vol.4 , pp. 7096
    • Thon, M.1    Hosoi, T.2    Yoshii, M.3    Ozawa, K.4
  • 45
    • 33751181217 scopus 로고    scopus 로고
    • 2-Aminopurine inhibits leptin receptor signal transduction
    • Hosoi, T. et al. 2-Aminopurine inhibits leptin receptor signal transduction. Eur J Pharmacol. 553, 61-6 (2006).
    • (2006) Eur J Pharmacol , vol.553 , pp. 61-66
    • Hosoi, T.1
  • 46
    • 0035014266 scopus 로고    scopus 로고
    • Homocysteine-induced endoplasmic reticulum stress causes dysregulation of the cholesterol and triglyceride biosynthetic pathways
    • Werstuck, G. H. et al. Homocysteine-induced endoplasmic reticulum stress causes dysregulation of the cholesterol and triglyceride biosynthetic pathways. J Clin Invest. 107, 1263-73 (2001).
    • (2001) J Clin Invest , vol.107 , pp. 1263-1273
    • Werstuck, G.H.1


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