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Volumn 71, Issue 6, 2009, Pages 576-591

Glucotoxicity and pancreatic proteomics

Author keywords

Diabetes; Glucotoxicity; Mass spectrometry; Proteomics

Indexed keywords

GLUCAGON; GLUCOSE; GLUCOSE TRANSPORTER; INSULIN;

EID: 58249137655     PISSN: 18743919     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jprot.2008.10.002     Document Type: Review
Times cited : (52)

References (189)
  • 1
    • 0036084280 scopus 로고    scopus 로고
    • Role of human liver, kidney, and skeletal muscle in postprandial glucose homeostasis
    • Meyer C., Dostou J.M., Welle S.L., and Gerich J.E. Role of human liver, kidney, and skeletal muscle in postprandial glucose homeostasis. Am J Physiol Endocrinol Metab 282 (2002) E419-427
    • (2002) Am J Physiol Endocrinol Metab , vol.282
    • Meyer, C.1    Dostou, J.M.2    Welle, S.L.3    Gerich, J.E.4
  • 2
    • 0029050595 scopus 로고
    • Insulin and insulin-like growth factors in diabetes mellitus
    • Dunger D.B. Insulin and insulin-like growth factors in diabetes mellitus. Arch Dis Child 72 (1995) 469-471
    • (1995) Arch Dis Child , vol.72 , pp. 469-471
    • Dunger, D.B.1
  • 3
    • 0023837574 scopus 로고
    • Overview of counterregulation and its abnormalities in diabetes mellitus and other conditions
    • Gerich J.E., and Campbell P.J. Overview of counterregulation and its abnormalities in diabetes mellitus and other conditions. Diabetes Metab Rev 4 (1988) 93-111
    • (1988) Diabetes Metab Rev , vol.4 , pp. 93-111
    • Gerich, J.E.1    Campbell, P.J.2
  • 6
    • 0034078910 scopus 로고    scopus 로고
    • Reduced glucose uptake precedes insulin signaling defects in adipocytes from heterozygous GLUT4 knockout mice
    • Li J., Houseknecht K.L., Stenbit A.E., Katz E.B., and Charron M.J. Reduced glucose uptake precedes insulin signaling defects in adipocytes from heterozygous GLUT4 knockout mice. FASEB J 14 (2000) 1117-1125
    • (2000) FASEB J , vol.14 , pp. 1117-1125
    • Li, J.1    Houseknecht, K.L.2    Stenbit, A.E.3    Katz, E.B.4    Charron, M.J.5
  • 8
    • 0023736417 scopus 로고
    • The insulin receptor and the molecular mechanism of insulin action
    • Kahn C.R., and White M.F. The insulin receptor and the molecular mechanism of insulin action. J Clin Invest 82 (1988) 1151-1156
    • (1988) J Clin Invest , vol.82 , pp. 1151-1156
    • Kahn, C.R.1    White, M.F.2
  • 10
    • 0028152377 scopus 로고
    • Facilitative glucose transporters
    • Mueckler M. Facilitative glucose transporters. Eur J Biochem 219 (1994) 713-725
    • (1994) Eur J Biochem , vol.219 , pp. 713-725
    • Mueckler, M.1
  • 12
    • 0027420730 scopus 로고
    • The glucose transporter family: structure, function and tissue-specific expression
    • Gould G.W., and Holman G.D. The glucose transporter family: structure, function and tissue-specific expression. Biochem J 295 Pt 2 (1993) 329-341
    • (1993) Biochem J , vol.295 , Issue.PART 2 , pp. 329-341
    • Gould, G.W.1    Holman, G.D.2
  • 13
    • 0035686071 scopus 로고    scopus 로고
    • GLUT2 in pancreatic and extra-pancreatic gluco-detection (review)
    • Thorens B. GLUT2 in pancreatic and extra-pancreatic gluco-detection (review). Mol Membr Biol 18 (2001) 265-273
    • (2001) Mol Membr Biol , vol.18 , pp. 265-273
    • Thorens, B.1
  • 14
    • 0031238676 scopus 로고    scopus 로고
    • Glucose transporter proteins in brain: delivery of glucose to neurons and glia
    • Vannucci S.J., Maher F., and Simpson I.A. Glucose transporter proteins in brain: delivery of glucose to neurons and glia. Glia 21 (1997) 2-21
    • (1997) Glia , vol.21 , pp. 2-21
    • Vannucci, S.J.1    Maher, F.2    Simpson, I.A.3
  • 15
    • 0035787305 scopus 로고    scopus 로고
    • Intracellular organization of insulin signaling and GLUT4 translocation
    • Watson R.T., and Pessin J.E. Intracellular organization of insulin signaling and GLUT4 translocation. Recent Prog Horm Res 56 (2001) 175-193
    • (2001) Recent Prog Horm Res , vol.56 , pp. 175-193
    • Watson, R.T.1    Pessin, J.E.2
  • 16
    • 0016771971 scopus 로고
    • Glucagon and insulin control of gluconeogenesis in the perfused isolated rat liver
    • Parrilla R., Jimenez I., and Ayuso-Parrilla M.S. Glucagon and insulin control of gluconeogenesis in the perfused isolated rat liver. Eur J Biochem 56 (1975) 375-383
    • (1975) Eur J Biochem , vol.56 , pp. 375-383
    • Parrilla, R.1    Jimenez, I.2    Ayuso-Parrilla, M.S.3
  • 17
    • 2942729543 scopus 로고    scopus 로고
    • Insulin regulation of hepatic gluconeogenesis through phosphorylation of CREB-binding protein
    • Zhou X.Y., Shibusawa N., Naik K., Porras D., Temple K., Ou H., et al. Insulin regulation of hepatic gluconeogenesis through phosphorylation of CREB-binding protein. Nat Med 10 (2004) 633-637
    • (2004) Nat Med , vol.10 , pp. 633-637
    • Zhou, X.Y.1    Shibusawa, N.2    Naik, K.3    Porras, D.4    Temple, K.5    Ou, H.6
  • 19
    • 33947216862 scopus 로고    scopus 로고
    • The effect of food composition on serum testosterone levels after oral administration of Andriol Testocaps
    • Schnabel P.G., Bagchus W., Lass H., Thomsen T., and Geurts T.B. The effect of food composition on serum testosterone levels after oral administration of Andriol Testocaps. Clin Endocrinol (Oxf) 66 (2007) 579-585
    • (2007) Clin Endocrinol (Oxf) , vol.66 , pp. 579-585
    • Schnabel, P.G.1    Bagchus, W.2    Lass, H.3    Thomsen, T.4    Geurts, T.B.5
  • 21
    • 0035038782 scopus 로고    scopus 로고
    • Mechanisms of nutritional and hormonal regulation of lipogenesis
    • Kersten S. Mechanisms of nutritional and hormonal regulation of lipogenesis. EMBO Rep 2 (2001) 282-286
    • (2001) EMBO Rep , vol.2 , pp. 282-286
    • Kersten, S.1
  • 22
    • 0018633068 scopus 로고
    • Insulin inhibition of lipolysis of human adipocytes: the role of cyclic adenosine monophosphate
    • Burns T.W., Terry B.E., Langley P.E., and Robison G.A. Insulin inhibition of lipolysis of human adipocytes: the role of cyclic adenosine monophosphate. Diabetes 28 (1979) 957-961
    • (1979) Diabetes , vol.28 , pp. 957-961
    • Burns, T.W.1    Terry, B.E.2    Langley, P.E.3    Robison, G.A.4
  • 23
    • 33646462136 scopus 로고    scopus 로고
    • Defective lipolysis and altered energy metabolism in mice lacking adipose triglyceride lipase
    • Haemmerle G., Lass A., Zimmermann R., Gorkiewicz G., Meyer C., Rozman J., et al. Defective lipolysis and altered energy metabolism in mice lacking adipose triglyceride lipase. Science 312 (2006) 734-737
    • (2006) Science , vol.312 , pp. 734-737
    • Haemmerle, G.1    Lass, A.2    Zimmermann, R.3    Gorkiewicz, G.4    Meyer, C.5    Rozman, J.6
  • 24
    • 2942731789 scopus 로고    scopus 로고
    • Muscle glycogen and metabolic regulation
    • Hargreaves M. Muscle glycogen and metabolic regulation. Proc Nutr Soc 63 (2004) 217-220
    • (2004) Proc Nutr Soc , vol.63 , pp. 217-220
    • Hargreaves, M.1
  • 25
    • 42249107130 scopus 로고    scopus 로고
    • Brain insulin, energy and glucose homeostasis; genes, environment and metabolic pathologies
    • Gerozissis K. Brain insulin, energy and glucose homeostasis; genes, environment and metabolic pathologies. Eur J Pharmacol 585 (2008) 38-49
    • (2008) Eur J Pharmacol , vol.585 , pp. 38-49
    • Gerozissis, K.1
  • 26
    • 12344277552 scopus 로고    scopus 로고
    • Diabetes, obesity, and the brain
    • Schwartz M.W., and Porte Jr. D. Diabetes, obesity, and the brain. Science 307 (2005) 375-379
    • (2005) Science , vol.307 , pp. 375-379
    • Schwartz, M.W.1    Porte Jr., D.2
  • 27
    • 34548207654 scopus 로고    scopus 로고
    • Brain glucose sensing, counterregulation, and energy homeostasis
    • Marty N., Dallaporta M., and Thorens B. Brain glucose sensing, counterregulation, and energy homeostasis. Physiology (Bethesda) 22 (2007) 241-251
    • (2007) Physiology (Bethesda) , vol.22 , pp. 241-251
    • Marty, N.1    Dallaporta, M.2    Thorens, B.3
  • 29
    • 0242380324 scopus 로고    scopus 로고
    • Diabetes, microvascular complications, and cardiovascular complications: what is it about glucose?
    • Reusch J.E. Diabetes, microvascular complications, and cardiovascular complications: what is it about glucose?. J Clin Invest 112 (2003) 986-988
    • (2003) J Clin Invest , vol.112 , pp. 986-988
    • Reusch, J.E.1
  • 30
    • 0037191135 scopus 로고    scopus 로고
    • Beta-cell dysfunction and insulin resistance in type 2 diabetes: role of metabolic and genetic abnormalities
    • LeRoith D. Beta-cell dysfunction and insulin resistance in type 2 diabetes: role of metabolic and genetic abnormalities. Am J Med 113 Suppl 6A (2002) 3S-11S
    • (2002) Am J Med , vol.113 , Issue.SUPPL. 6A
    • LeRoith, D.1
  • 32
    • 4143110556 scopus 로고    scopus 로고
    • Oxidative stress in the pathogenesis of diabetic neuropathy
    • Vincent A.M., Russell J.W., Low P., and Feldman E.L. Oxidative stress in the pathogenesis of diabetic neuropathy. Endocr Rev 25 (2004) 612-628
    • (2004) Endocr Rev , vol.25 , pp. 612-628
    • Vincent, A.M.1    Russell, J.W.2    Low, P.3    Feldman, E.L.4
  • 33
    • 0032913309 scopus 로고    scopus 로고
    • Role of oxidative stress in diabetic complications: a new perspective on an old paradigm
    • Baynes J.W., and Thorpe S.R. Role of oxidative stress in diabetic complications: a new perspective on an old paradigm. Diabetes 48 (1999) 1-9
    • (1999) Diabetes , vol.48 , pp. 1-9
    • Baynes, J.W.1    Thorpe, S.R.2
  • 36
    • 33750502270 scopus 로고    scopus 로고
    • Oxidative stress and impaired insulin secretion in type 2 diabetes
    • Robertson R.P. Oxidative stress and impaired insulin secretion in type 2 diabetes. Curr Opin Pharmacol 6 (2006) 615-619
    • (2006) Curr Opin Pharmacol , vol.6 , pp. 615-619
    • Robertson, R.P.1
  • 37
    • 20044390365 scopus 로고    scopus 로고
    • Functional and molecular defects of pancreatic islets in human type 2 diabetes
    • Del Guerra S., Lupi R., Marselli L., Masini M., Bugliani M., Sbrana S., et al. Functional and molecular defects of pancreatic islets in human type 2 diabetes. Diabetes 54 (2005) 727-735
    • (2005) Diabetes , vol.54 , pp. 727-735
    • Del Guerra, S.1    Lupi, R.2    Marselli, L.3    Masini, M.4    Bugliani, M.5    Sbrana, S.6
  • 38
    • 34447625413 scopus 로고    scopus 로고
    • Metabolic stress in insulin's target cells leads to ROS accumulation - a hypothetical common pathway causing insulin resistance
    • Eriksson J.W. Metabolic stress in insulin's target cells leads to ROS accumulation - a hypothetical common pathway causing insulin resistance. FEBS Lett 581 (2007) 3734-3742
    • (2007) FEBS Lett , vol.581 , pp. 3734-3742
    • Eriksson, J.W.1
  • 39
    • 0035929553 scopus 로고    scopus 로고
    • Enhanced sensitivity of insulin-resistant adipocytes to vanadate is associated with oxidative stress and decreased reduction of vanadate (+5) to vanadyl (+4)
    • Lu B., Ennis D., Lai R., Bogdanovic E., Nikolov R., and Salamon L. Enhanced sensitivity of insulin-resistant adipocytes to vanadate is associated with oxidative stress and decreased reduction of vanadate (+5) to vanadyl (+4). J Biol Chem 276 (2001) 35589-35598
    • (2001) J Biol Chem , vol.276 , pp. 35589-35598
    • Lu, B.1    Ennis, D.2    Lai, R.3    Bogdanovic, E.4    Nikolov, R.5    Salamon, L.6
  • 40
    • 0031683542 scopus 로고    scopus 로고
    • Prolonged oxidative stress impairs insulin-induced GLUT4 translocation in 3T3-L1 adipocytes
    • Rudich A., Tirosh A., Potashnik R., Hemi R., Kanety H., Bashan N., et al. Prolonged oxidative stress impairs insulin-induced GLUT4 translocation in 3T3-L1 adipocytes. Diabetes 47 (1998) 1562-1569
    • (1998) Diabetes , vol.47 , pp. 1562-1569
    • Rudich, A.1    Tirosh, A.2    Potashnik, R.3    Hemi, R.4    Kanety, H.5    Bashan, N.6
  • 41
    • 0043092304 scopus 로고    scopus 로고
    • Hyperglycemia induced by glucose infusion causes hepatic oxidative stress and systemic inflammation, but not STAT3 or MAP kinase activation in liver in rats
    • Ling P.R., Mueller C., Smith R.J., and Bistrian B.R. Hyperglycemia induced by glucose infusion causes hepatic oxidative stress and systemic inflammation, but not STAT3 or MAP kinase activation in liver in rats. Metabolism 52 (2003) 868-874
    • (2003) Metabolism , vol.52 , pp. 868-874
    • Ling, P.R.1    Mueller, C.2    Smith, R.J.3    Bistrian, B.R.4
  • 44
    • 8644267972 scopus 로고    scopus 로고
    • Hyperglycemia-induced oxidative stress in diabetic complications
    • King G.L., and Loeken M.R. Hyperglycemia-induced oxidative stress in diabetic complications. Histochem Cell Biol 122 (2004) 333-338
    • (2004) Histochem Cell Biol , vol.122 , pp. 333-338
    • King, G.L.1    Loeken, M.R.2
  • 45
    • 34247394257 scopus 로고    scopus 로고
    • Oxidative stress and diabetic retinopathy
    • Kowluru R.A., and Chan P.S. Oxidative stress and diabetic retinopathy. Exp Diabetes Res 2007 (2007) 43603
    • (2007) Exp Diabetes Res , vol.2007 , pp. 43603
    • Kowluru, R.A.1    Chan, P.S.2
  • 46
    • 0344012015 scopus 로고    scopus 로고
    • Hyperglycemia increases mitochondrial superoxide in retina and retinal cells
    • Du Y., Miller C.M., and Kern T.S. Hyperglycemia increases mitochondrial superoxide in retina and retinal cells. Free Radic Biol Med 35 (2003) 1491-1499
    • (2003) Free Radic Biol Med , vol.35 , pp. 1491-1499
    • Du, Y.1    Miller, C.M.2    Kern, T.S.3
  • 47
    • 0033621686 scopus 로고    scopus 로고
    • Somogyi-Mann, M., Grant, M.B., Increased H2O2, vascular endothelial growth factor and receptors in the retina of the BBZ/Wor diabetic rat
    • Ellis E.A., and Guberski D.L. Somogyi-Mann, M., Grant, M.B., Increased H2O2, vascular endothelial growth factor and receptors in the retina of the BBZ/Wor diabetic rat. Free Radic Biol Med 28 (2000) 91-101
    • (2000) Free Radic Biol Med , vol.28 , pp. 91-101
    • Ellis, E.A.1    Guberski, D.L.2
  • 48
    • 0037342855 scopus 로고    scopus 로고
    • Effect of reinstitution of good glycemic control on retinal oxidative stress and nitrative stress in diabetic rats
    • Kowluru R.A. Effect of reinstitution of good glycemic control on retinal oxidative stress and nitrative stress in diabetic rats. Diabetes 52 (2003) 818-823
    • (2003) Diabetes , vol.52 , pp. 818-823
    • Kowluru, R.A.1
  • 49
    • 0035985234 scopus 로고    scopus 로고
    • Oxidative stress and diabetic neuropathy: pathophysiological mechanisms and treatment perspectives
    • van Dam P.S. Oxidative stress and diabetic neuropathy: pathophysiological mechanisms and treatment perspectives. Diabetes Metab Res Rev 18 (2002) 176-184
    • (2002) Diabetes Metab Res Rev , vol.18 , pp. 176-184
    • van Dam, P.S.1
  • 50
    • 0032837106 scopus 로고    scopus 로고
    • Alpha-lipoic acid: effect on glucose uptake, sorbitol pathway, and energy metabolism in experimental diabetic neuropathy
    • Kishi Y., Schmelzer J.D., Yao J.K., Zollman P.J., Nickander K.K., Tritschler H.J., et al. Alpha-lipoic acid: effect on glucose uptake, sorbitol pathway, and energy metabolism in experimental diabetic neuropathy. Diabetes 48 (1999) 2045-2051
    • (1999) Diabetes , vol.48 , pp. 2045-2051
    • Kishi, Y.1    Schmelzer, J.D.2    Yao, J.K.3    Zollman, P.J.4    Nickander, K.K.5    Tritschler, H.J.6
  • 51
    • 0042668303 scopus 로고    scopus 로고
    • The sensory symptoms of diabetic polyneuropathy are improved with alpha-lipoic acid: the SYDNEY trial
    • Ametov A.S., Barinov A., Dyck P.J., Hermann R., Kozlova N., Litchy W.J., et al. The sensory symptoms of diabetic polyneuropathy are improved with alpha-lipoic acid: the SYDNEY trial. Diabetes Care 26 (2003) 770-776
    • (2003) Diabetes Care , vol.26 , pp. 770-776
    • Ametov, A.S.1    Barinov, A.2    Dyck, P.J.3    Hermann, R.4    Kozlova, N.5    Litchy, W.J.6
  • 52
    • 0036317040 scopus 로고    scopus 로고
    • Accumulation of 8-hydroxy-2'-deoxyguanosine and mitochondrial DNA deletion in kidney of diabetic rats
    • Kakimoto M., Inoguchi T., Sonta T., Yu H.Y., Imamura M., Etoh T., et al. Accumulation of 8-hydroxy-2'-deoxyguanosine and mitochondrial DNA deletion in kidney of diabetic rats. Diabetes 51 (2002) 1588-1595
    • (2002) Diabetes , vol.51 , pp. 1588-1595
    • Kakimoto, M.1    Inoguchi, T.2    Sonta, T.3    Yu, H.Y.4    Imamura, M.5    Etoh, T.6
  • 53
    • 35848956112 scopus 로고    scopus 로고
    • Diabetic nephropathy is associated with oxidative stress and decreased renal nitric oxide production
    • Prabhakar S., Starnes J., Shi S., Lonis B., and Tran R. Diabetic nephropathy is associated with oxidative stress and decreased renal nitric oxide production. J Am Soc Nephrol 18 (2007) 2945-2952
    • (2007) J Am Soc Nephrol , vol.18 , pp. 2945-2952
    • Prabhakar, S.1    Starnes, J.2    Shi, S.3    Lonis, B.4    Tran, R.5
  • 54
    • 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 (2000) 451-454
    • (2000) Cell , vol.101 , pp. 451-454
    • Mori, K.1
  • 55
    • 0036022403 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-mediated apoptosis in pancreatic beta-cells
    • Oyadomari S., Araki E., and Mori M. Endoplasmic reticulum stress-mediated apoptosis in pancreatic beta-cells. Apoptosis 7 (2002) 335-345
    • (2002) Apoptosis , vol.7 , pp. 335-345
    • Oyadomari, S.1    Araki, E.2    Mori, M.3
  • 56
    • 35848963392 scopus 로고    scopus 로고
    • The endoplasmic reticulum in pancreatic beta cells of type 2 diabetes patients
    • Marchetti P., Bugliani M., Lupi R., Marselli L., Masini M., Boggi U., et al. The endoplasmic reticulum in pancreatic beta cells of type 2 diabetes patients. Diabetologia 50 (2007) 2486-2494
    • (2007) Diabetologia , vol.50 , pp. 2486-2494
    • Marchetti, P.1    Bugliani, M.2    Lupi, R.3    Marselli, L.4    Masini, M.5    Boggi, U.6
  • 57
    • 39149104320 scopus 로고    scopus 로고
    • The role for endoplasmic reticulum stress in diabetes mellitus
    • Eizirik D.L., Cardozo A.K., and Cnop M. The role for endoplasmic reticulum stress in diabetes mellitus. Endocr Rev 29 (2008) 42-61
    • (2008) Endocr Rev , vol.29 , pp. 42-61
    • Eizirik, D.L.1    Cardozo, A.K.2    Cnop, M.3
  • 58
    • 0242609973 scopus 로고    scopus 로고
    • Impact of endoplasmic reticulum stress pathway on pancreatic beta-cells and diabetes mellitus
    • Araki E., Oyadomari S., and Mori M. Impact of endoplasmic reticulum stress pathway on pancreatic beta-cells and diabetes mellitus. Exp Biol Med (Maywood) 228 (2003) 1213-1217
    • (2003) Exp Biol Med (Maywood) , vol.228 , pp. 1213-1217
    • Araki, E.1    Oyadomari, S.2    Mori, M.3
  • 59
    • 35848957485 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and oxidative stress: a vicious cycle or a double-edged sword?
    • Malhotra J.D., and Kaufman R.J. Endoplasmic reticulum stress and oxidative stress: a vicious cycle or a double-edged sword?. Antioxid Redox Signal 9 (2007) 2277-2293
    • (2007) Antioxid Redox Signal , vol.9 , pp. 2277-2293
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 60
    • 34249933087 scopus 로고    scopus 로고
    • Acute nutrient regulation of the unfolded protein response and integrated stress response in cultured rat pancreatic islets
    • Elouil H., Bensellam M., Guiot Y., Vander Mierde D., Pascal S.M., Schuit F.C., et al. Acute nutrient regulation of the unfolded protein response and integrated stress response in cultured rat pancreatic islets. Diabetologia 50 (2007) 1442-1452
    • (2007) Diabetologia , vol.50 , pp. 1442-1452
    • Elouil, H.1    Bensellam, M.2    Guiot, Y.3    Vander Mierde, D.4    Pascal, S.M.5    Schuit, F.C.6
  • 61
    • 0032054744 scopus 로고    scopus 로고
    • CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum
    • Zinszner H., Kuroda M., Wang X., Batchvarova N., Ligthfoot R.T., Remotti H., et al. CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum. Genes Dev 12 (1998) 982-995
    • (1998) Genes Dev , vol.12 , pp. 982-995
    • Zinszner, H.1    Kuroda, M.2    Wang, X.3    Batchvarova, N.4    Ligthfoot, R.T.5    Remotti, H.6
  • 62
    • 0030971097 scopus 로고    scopus 로고
    • Mammalian GADD34, an apoptosis- and DNA damage-inducible gene
    • Hollander M.C., Zhan Q., Bae I., and Fornace Jr. A.J. Mammalian GADD34, an apoptosis- and DNA damage-inducible gene. J Biol Chem 272 (1997) 13731-13737
    • (1997) J Biol Chem , vol.272 , pp. 13731-13737
    • Hollander, M.C.1    Zhan, Q.2    Bae, I.3    Fornace Jr., A.J.4
  • 63
    • 0041315834 scopus 로고    scopus 로고
    • Delineation of a negative feedback regulatory loop that controls protein translation during endoplasmic reticulum stress
    • Ma Y., and Hendershot L.M. Delineation of a negative feedback regulatory loop that controls protein translation during endoplasmic reticulum stress. J Biol Chem 278 (2003) 34864-34873
    • (2003) J Biol Chem , vol.278 , pp. 34864-34873
    • Ma, Y.1    Hendershot, L.M.2
  • 64
    • 0036175128 scopus 로고    scopus 로고
    • Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes
    • Oyadomari S., Koizumi A., Takeda K., Gotoh T., Akira S., and Mori M. Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes. J Clin Invest 109 (2002) 525-532
    • (2002) J Clin Invest , vol.109 , pp. 525-532
    • Oyadomari, S.1    Koizumi, A.2    Takeda, K.3    Gotoh, T.4    Akira, S.5    Mori, M.6
  • 65
    • 5644231992 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes
    • Ozcan U., Cao Q., Yilmaz E., Lee A.H., Iwakoshi N.N., Tuncman G., et al. Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes. Science 306 (2004) 457-461
    • (2004) Science , vol.306 , pp. 457-461
    • Ozcan, U.1    Cao, Q.2    Yilmaz, E.3    Lee, A.H.4    Iwakoshi, N.N.5    Tuncman, G.6
  • 66
    • 58249131169 scopus 로고    scopus 로고
    • Gregor MG, Hotamisligil GS. Adipocyte stress: the endoplasmic reticulum and metabolic disease. J Lipid Res in press.
    • Gregor MG, Hotamisligil GS. Adipocyte stress: the endoplasmic reticulum and metabolic disease. J Lipid Res in press.
  • 67
    • 34548064947 scopus 로고    scopus 로고
    • Repression of GLUT4 expression by the endoplasmic reticulum stress response in 3T3-L1 adipocytes
    • Miller R.S., Diaczok D., and Cooke D.W. Repression of GLUT4 expression by the endoplasmic reticulum stress response in 3T3-L1 adipocytes. Biochem Biophys Res Commun 362 (2007) 188-192
    • (2007) Biochem Biophys Res Commun , vol.362 , pp. 188-192
    • Miller, R.S.1    Diaczok, D.2    Cooke, D.W.3
  • 68
    • 0030748460 scopus 로고    scopus 로고
    • Insulin resistance due to hyperglycaemia: an adaptation protecting insulin-sensitive tissues
    • Yki-Jarvinen H., and Makimattila S. Insulin resistance due to hyperglycaemia: an adaptation protecting insulin-sensitive tissues. Diabetologia 40 Suppl 2 (1997) S141-144
    • (1997) Diabetologia , vol.40 , Issue.SUPPL. 2
    • Yki-Jarvinen, H.1    Makimattila, S.2
  • 69
    • 0035787070 scopus 로고    scopus 로고
    • Protein glycation, diabetes, and aging
    • Ulrich P., and Cerami A. Protein glycation, diabetes, and aging. Recent Prog Horm Res 56 (2001) 1-21
    • (2001) Recent Prog Horm Res , vol.56 , pp. 1-21
    • Ulrich, P.1    Cerami, A.2
  • 70
    • 0242401999 scopus 로고    scopus 로고
    • Proteomic analysis of the site specificity of glycation and carboxymethylation of ribonuclease
    • Brock J.W., Hinton D.J., Cotham W.E., Metz T.O., Thorpes S.R., Baynes J.W., et al. Proteomic analysis of the site specificity of glycation and carboxymethylation of ribonuclease. J Proteome Res 2 (2003) 506-513
    • (2003) J Proteome Res , vol.2 , pp. 506-513
    • Brock, J.W.1    Hinton, D.J.2    Cotham, W.E.3    Metz, T.O.4    Thorpes, S.R.5    Baynes, J.W.6
  • 72
    • 33646793360 scopus 로고    scopus 로고
    • Accumulation of altered proteins and ageing: causes and effects
    • Hipkiss A.R. Accumulation of altered proteins and ageing: causes and effects. Exp Gerontol 41 (2006) 464-473
    • (2006) Exp Gerontol , vol.41 , pp. 464-473
    • Hipkiss, A.R.1
  • 73
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • Brownlee M. Biochemistry and molecular cell biology of diabetic complications. Nature 414 (2001) 813-820
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 74
    • 39149128004 scopus 로고    scopus 로고
    • On the search for glycated lipoprotein ApoA-I in the plasma of diabetic and nephropathic patients
    • Lapolla A., Brioschi M., Banfi C., Tremoli E., Bonfante L., Cristoni S., et al. On the search for glycated lipoprotein ApoA-I in the plasma of diabetic and nephropathic patients. J Mass Spectrom 43 (2008) 74-81
    • (2008) J Mass Spectrom , vol.43 , pp. 74-81
    • Lapolla, A.1    Brioschi, M.2    Banfi, C.3    Tremoli, E.4    Bonfante, L.5    Cristoni, S.6
  • 75
    • 0023813085 scopus 로고
    • Non enzymatic glycation of apolipoprotein A-I. Effects on its self-association and lipid binding properties
    • Calvo C., Talussot C., Ponsin G., and Berthezene F. Non enzymatic glycation of apolipoprotein A-I. Effects on its self-association and lipid binding properties. Biochem Biophys Res Commun 153 (1988) 1060-1067
    • (1988) Biochem Biophys Res Commun , vol.153 , pp. 1060-1067
    • Calvo, C.1    Talussot, C.2    Ponsin, G.3    Berthezene, F.4
  • 76
    • 84952619562 scopus 로고
    • Association in vivo of glycated apolipoprotein A-I with high density lipoproteins
    • Calvo C., and Verdugo C. Association in vivo of glycated apolipoprotein A-I with high density lipoproteins. Eur J Clin Chem Clin Biochem 30 (1992) 3-5
    • (1992) Eur J Clin Chem Clin Biochem , vol.30 , pp. 3-5
    • Calvo, C.1    Verdugo, C.2
  • 77
    • 0023894054 scopus 로고
    • Characterization of the non enzymatic glycation of high density lipoprotein in diabetic patients
    • Calvo C., Ponsin G., and Berthezene F. Characterization of the non enzymatic glycation of high density lipoprotein in diabetic patients. Diabete Metab 14 (1988) 264-269
    • (1988) Diabete Metab , vol.14 , pp. 264-269
    • Calvo, C.1    Ponsin, G.2    Berthezene, F.3
  • 78
    • 0034962029 scopus 로고    scopus 로고
    • Glycohemoglobin: a primary predictor of the development or reversal of complications of diabetes mellitus
    • Krishnamurti U., and Steffes M.W. Glycohemoglobin: a primary predictor of the development or reversal of complications of diabetes mellitus. Clin Chem 47 (2001) 1157-1165
    • (2001) Clin Chem , vol.47 , pp. 1157-1165
    • Krishnamurti, U.1    Steffes, M.W.2
  • 79
    • 0034893715 scopus 로고    scopus 로고
    • The role of AGEs in aging: causation or correlation
    • Baynes J.W. The role of AGEs in aging: causation or correlation. Exp Gerontol 36 (2001) 1527-1537
    • (2001) Exp Gerontol , vol.36 , pp. 1527-1537
    • Baynes, J.W.1
  • 80
    • 23044442730 scopus 로고    scopus 로고
    • The clinical and biological relationship between Type II diabetes mellitus and Alzheimer's disease
    • Nicolls M.R. The clinical and biological relationship between Type II diabetes mellitus and Alzheimer's disease. Curr Alzheimer Res 1 (2004) 47-54
    • (2004) Curr Alzheimer Res , vol.1 , pp. 47-54
    • Nicolls, M.R.1
  • 81
    • 0031719122 scopus 로고    scopus 로고
    • Advanced glycation end products in neurodegeneration: more than early markers of oxidative stress?
    • Munch G., Gerlach M., Sian J., Wong A., and Riederer P. Advanced glycation end products in neurodegeneration: more than early markers of oxidative stress?. Ann Neurol 44 (1998) S85-88
    • (1998) Ann Neurol , vol.44
    • Munch, G.1    Gerlach, M.2    Sian, J.3    Wong, A.4    Riederer, P.5
  • 82
    • 0032407736 scopus 로고    scopus 로고
    • Immunohistochemical distribution and subcellular localization of three distinct specific molecular structures of advanced glycation end products in human tissues
    • Ling X., Sakashita N., Takeya M., Nagai R., Horiuchi S., and Takahashi K. Immunohistochemical distribution and subcellular localization of three distinct specific molecular structures of advanced glycation end products in human tissues. Lab Invest 78 (1998) 1591-1606
    • (1998) Lab Invest , vol.78 , pp. 1591-1606
    • Ling, X.1    Sakashita, N.2    Takeya, M.3    Nagai, R.4    Horiuchi, S.5    Takahashi, K.6
  • 83
    • 0030477949 scopus 로고    scopus 로고
    • Glycation of collagen: the basis of its central role in the late complications of ageing and diabetes
    • Paul R.G., and Bailey A.J. Glycation of collagen: the basis of its central role in the late complications of ageing and diabetes. Int J Biochem Cell Biol 28 (1996) 1297-1310
    • (1996) Int J Biochem Cell Biol , vol.28 , pp. 1297-1310
    • Paul, R.G.1    Bailey, A.J.2
  • 84
    • 34250176214 scopus 로고    scopus 로고
    • Study of posttranslational non-enzymatic modifications of collagen using capillary electrophoresis/mass spectrometry and high performance liquid chromatography/mass spectrometry
    • Mikulikova K., Eckhardt A., Pataridis S., and Miksik I. Study of posttranslational non-enzymatic modifications of collagen using capillary electrophoresis/mass spectrometry and high performance liquid chromatography/mass spectrometry. J Chromatogr A 1155 (2007) 125-133
    • (2007) J Chromatogr A , vol.1155 , pp. 125-133
    • Mikulikova, K.1    Eckhardt, A.2    Pataridis, S.3    Miksik, I.4
  • 85
    • 0020073553 scopus 로고
    • Glucosylated albumin and its influence on salicylate binding
    • Mereish K.A., Rosenberg H., and Cobby J. Glucosylated albumin and its influence on salicylate binding. J Pharm Sci 71 (1982) 235-238
    • (1982) J Pharm Sci , vol.71 , pp. 235-238
    • Mereish, K.A.1    Rosenberg, H.2    Cobby, J.3
  • 87
    • 0028172694 scopus 로고
    • Drug binding properties of glycosylated bovine serum albumin as measured by circular dichroism
    • Okabe N., and Nakasaka T. Drug binding properties of glycosylated bovine serum albumin as measured by circular dichroism. Biol Pharm Bull 17 (1994) 1505-1507
    • (1994) Biol Pharm Bull , vol.17 , pp. 1505-1507
    • Okabe, N.1    Nakasaka, T.2
  • 88
    • 26444478269 scopus 로고    scopus 로고
    • Advanced glycation end products and RAGE: a common thread in aging, diabetes, neurodegeneration, and inflammation
    • Ramasamy R., Vannucci S.J., Yan S.S., Herold K., Yan S.F., and Schmidt A.M. Advanced glycation end products and RAGE: a common thread in aging, diabetes, neurodegeneration, and inflammation. Glycobiology 15 (2005) 16R-28R
    • (2005) Glycobiology , vol.15
    • Ramasamy, R.1    Vannucci, S.J.2    Yan, S.S.3    Herold, K.4    Yan, S.F.5    Schmidt, A.M.6
  • 89
    • 0029943994 scopus 로고    scopus 로고
    • Advanced glycation end products and their recognition by macrophage and macrophage-derived cells
    • Horiuchi S., Higashi T., Ikeda K., Saishoji T., Jinnouchi Y., Sano H., et al. Advanced glycation end products and their recognition by macrophage and macrophage-derived cells. Diabetes 45 Suppl 3 (1996) S73-76
    • (1996) Diabetes , vol.45 , Issue.SUPPL. 3
    • Horiuchi, S.1    Higashi, T.2    Ikeda, K.3    Saishoji, T.4    Jinnouchi, Y.5    Sano, H.6
  • 90
    • 0016685611 scopus 로고
    • Lysosomal enzymes as agents of turnover of soluble cytoplasmic proteins
    • Dean R.T. Lysosomal enzymes as agents of turnover of soluble cytoplasmic proteins. Eur J Biochem 58 (1975) 9-14
    • (1975) Eur J Biochem , vol.58 , pp. 9-14
    • Dean, R.T.1
  • 91
    • 0027956982 scopus 로고
    • Modification of low density lipoprotein by advanced glycation end products contributes to the dyslipidemia of diabetes and renal insufficiency
    • Bucala R., Makita Z., Vega G., Grundy S., Koschinsky T., Cerami A., et al. Modification of low density lipoprotein by advanced glycation end products contributes to the dyslipidemia of diabetes and renal insufficiency. Proc Natl Acad Sci U S A 91 (1994) 9441-9445
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 9441-9445
    • Bucala, R.1    Makita, Z.2    Vega, G.3    Grundy, S.4    Koschinsky, T.5    Cerami, A.6
  • 92
    • 0032079038 scopus 로고    scopus 로고
    • Circulating advanced glycation peptides in streptozotocin-induced diabetic rats: evidence for preferential modification of IgG light chains
    • Gugliucci A., and Menini T. Circulating advanced glycation peptides in streptozotocin-induced diabetic rats: evidence for preferential modification of IgG light chains. Life Sci 62 (1998) 2141-2150
    • (1998) Life Sci , vol.62 , pp. 2141-2150
    • Gugliucci, A.1    Menini, T.2
  • 93
    • 43549108142 scopus 로고    scopus 로고
    • Glucolipotoxicity: fuel excess and {beta}-cell dysfunction
    • Poitout V., and Robertson R.P. Glucolipotoxicity: fuel excess and {beta}-cell dysfunction. Endocr Rev 29 3 (2008) 351-366
    • (2008) Endocr Rev , vol.29 , Issue.3 , pp. 351-366
    • Poitout, V.1    Robertson, R.P.2
  • 94
    • 43449091944 scopus 로고    scopus 로고
    • PDX-1 and MafA play a crucial role in pancreatic beta-cell differentiation and maintenance of mature beta-cell function
    • Kaneto H., Miyatsuka T., Kawamori D., Yamamoto K., Kato K., Shiraiwa T., et al. PDX-1 and MafA play a crucial role in pancreatic beta-cell differentiation and maintenance of mature beta-cell function. Endocr J 55 2 (2008) 235-252
    • (2008) Endocr J , vol.55 , Issue.2 , pp. 235-252
    • Kaneto, H.1    Miyatsuka, T.2    Kawamori, D.3    Yamamoto, K.4    Kato, K.5    Shiraiwa, T.6
  • 95
    • 0032863183 scopus 로고    scopus 로고
    • Prevention of glucose toxicity in HIT-T15 cells and Zucker diabetic fatty rats by antioxidants
    • Tanaka Y., Gleason C.E., Tran P.O., Harmon J.S., and Robertson R.P. Prevention of glucose toxicity in HIT-T15 cells and Zucker diabetic fatty rats by antioxidants. Proc Natl Acad Sci U S A 96 (1999) 10857-10862
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 10857-10862
    • Tanaka, Y.1    Gleason, C.E.2    Tran, P.O.3    Harmon, J.S.4    Robertson, R.P.5
  • 96
    • 0033667824 scopus 로고    scopus 로고
    • Determinants of glucose toxicity and its reversibility in the pancreatic islet beta-cell line, HIT-T15
    • Gleason C.E., Gonzalez M., Harmon J.S., and Robertson R.P. Determinants of glucose toxicity and its reversibility in the pancreatic islet beta-cell line, HIT-T15. Am J Physiol Endocrinol Metab 279 (2000) E997-1002
    • (2000) Am J Physiol Endocrinol Metab , vol.279
    • Gleason, C.E.1    Gonzalez, M.2    Harmon, J.S.3    Robertson, R.P.4
  • 97
    • 24144490962 scopus 로고    scopus 로고
    • Exposure to chronic high glucose induces beta-cell apoptosis through decreased interaction of glucokinase with mitochondria: downregulation of glucokinase in pancreatic beta-cells
    • Kim W.H., Lee J.W., Suh Y.H., Hong S.H., Choi J.S., Lim J.H., et al. Exposure to chronic high glucose induces beta-cell apoptosis through decreased interaction of glucokinase with mitochondria: downregulation of glucokinase in pancreatic beta-cells. Diabetes 54 (2005) 2602-2611
    • (2005) Diabetes , vol.54 , pp. 2602-2611
    • Kim, W.H.1    Lee, J.W.2    Suh, Y.H.3    Hong, S.H.4    Choi, J.S.5    Lim, J.H.6
  • 98
    • 0033034807 scopus 로고    scopus 로고
    • Hyperglycemia-induced beta-cell apoptosis in pancreatic islets of Psammomys obesus during development of diabetes
    • Donath M.Y., Gross D.J., Cerasi E., and Kaiser N. Hyperglycemia-induced beta-cell apoptosis in pancreatic islets of Psammomys obesus during development of diabetes. Diabetes 48 (1999) 738-744
    • (1999) Diabetes , vol.48 , pp. 738-744
    • Donath, M.Y.1    Gross, D.J.2    Cerasi, E.3    Kaiser, N.4
  • 99
    • 0035432491 scopus 로고    scopus 로고
    • Glucose induces beta-cell apoptosis via upregulation of the Fas receptor in human islets
    • Maedler K., Spinas G.A., Lehmann R., Sergeev P., Weber M., Fontana A., et al. Glucose induces beta-cell apoptosis via upregulation of the Fas receptor in human islets. Diabetes 50 (2001) 1683-1690
    • (2001) Diabetes , vol.50 , pp. 1683-1690
    • Maedler, K.1    Spinas, G.A.2    Lehmann, R.3    Sergeev, P.4    Weber, M.5    Fontana, A.6
  • 101
    • 20444363538 scopus 로고    scopus 로고
    • Beta-cells in type 2 diabetes: a loss of function and mass
    • Maedler K., and Donath M.Y. Beta-cells in type 2 diabetes: a loss of function and mass. Horm Res 62 Suppl 3 (2004) 67-73
    • (2004) Horm Res , vol.62 , Issue.SUPPL. 3 , pp. 67-73
    • Maedler, K.1    Donath, M.Y.2
  • 102
    • 42949085323 scopus 로고    scopus 로고
    • Glucagon as a treatment of severe hypoglycemia: safe and efficacious but underutilized
    • Pearson T. Glucagon as a treatment of severe hypoglycemia: safe and efficacious but underutilized. Diabetes Educ 34 (2008) 128-134
    • (2008) Diabetes Educ , vol.34 , pp. 128-134
    • Pearson, T.1
  • 104
    • 26844556580 scopus 로고    scopus 로고
    • Glucose stimulates glucagon release in single rat alpha-cells by mechanisms that mirror the stimulus-secretion coupling in beta-cells
    • Olsen H.L., Theander S., Bokvist K., Buschard K., Wollheim C.B., and Gromada J. Glucose stimulates glucagon release in single rat alpha-cells by mechanisms that mirror the stimulus-secretion coupling in beta-cells. Endocrinology 146 (2005) 4861-4870
    • (2005) Endocrinology , vol.146 , pp. 4861-4870
    • Olsen, H.L.1    Theander, S.2    Bokvist, K.3    Buschard, K.4    Wollheim, C.B.5    Gromada, J.6
  • 105
    • 33749347851 scopus 로고    scopus 로고
    • Paradoxical stimulation of glucagon secretion by high glucose concentrations
    • Salehi A., Vieira E., and Gylfe E. Paradoxical stimulation of glucagon secretion by high glucose concentrations. Diabetes 55 (2006) 2318-2323
    • (2006) Diabetes , vol.55 , pp. 2318-2323
    • Salehi, A.1    Vieira, E.2    Gylfe, E.3
  • 106
    • 0242432598 scopus 로고    scopus 로고
    • Intra-islet somatostatin regulates glucagon release via type 2 somatostatin receptors in rats
    • Cejvan K., Coy D.H., and Efendic S. Intra-islet somatostatin regulates glucagon release via type 2 somatostatin receptors in rats. Diabetes 52 (2003) 1176-1181
    • (2003) Diabetes , vol.52 , pp. 1176-1181
    • Cejvan, K.1    Coy, D.H.2    Efendic, S.3
  • 107
    • 0347306075 scopus 로고    scopus 로고
    • Intraislet somatostatin inhibits insulin (via a subtype-2 somatostatin receptor) but not islet amyloid polypeptide secretion in the isolated perfused human pancreas
    • discussion 256
    • Atiya A.W., Moldovan S., Adrian T.E., Coy D., Walsh J., and Brunicardi F.C. Intraislet somatostatin inhibits insulin (via a subtype-2 somatostatin receptor) but not islet amyloid polypeptide secretion in the isolated perfused human pancreas. J Gastrointest Surg 1 (1997) 251-256 discussion 256
    • (1997) J Gastrointest Surg , vol.1 , pp. 251-256
    • Atiya, A.W.1    Moldovan, S.2    Adrian, T.E.3    Coy, D.4    Walsh, J.5    Brunicardi, F.C.6
  • 108
    • 0027246174 scopus 로고
    • Both somatostatin and insulin responses to glucose are impaired in the perfused pancreas of the spontaneously noninsulin-dependent diabetic GK (Goto-Kakizaki) rats
    • Abdel-Halim S.M., Guenifi A., Efendic S., and Ostenson C.G. Both somatostatin and insulin responses to glucose are impaired in the perfused pancreas of the spontaneously noninsulin-dependent diabetic GK (Goto-Kakizaki) rats. Acta Physiol Scand 148 (1993) 219-226
    • (1993) Acta Physiol Scand , vol.148 , pp. 219-226
    • Abdel-Halim, S.M.1    Guenifi, A.2    Efendic, S.3    Ostenson, C.G.4
  • 109
    • 0033529410 scopus 로고    scopus 로고
    • Postprandial hypertriglyceridemia and insulin resistance in normoglycemic first-degree relatives of patients with type 2 diabetes
    • Axelsen M., Smith U., Eriksson J.W., Taskinen M.R., and Jansson P.A. Postprandial hypertriglyceridemia and insulin resistance in normoglycemic first-degree relatives of patients with type 2 diabetes. Ann Intern Med 131 (1999) 27-31
    • (1999) Ann Intern Med , vol.131 , pp. 27-31
    • Axelsen, M.1    Smith, U.2    Eriksson, J.W.3    Taskinen, M.R.4    Jansson, P.A.5
  • 110
    • 7044247671 scopus 로고    scopus 로고
    • Phloridzin improves hyperglycemia but not hepatic insulin resistance in a transgenic mouse model of type 2 diabetes
    • Zhao H., Yakar S., Gavrilova O., Sun H., Zhang Y., Kim H., et al. Phloridzin improves hyperglycemia but not hepatic insulin resistance in a transgenic mouse model of type 2 diabetes. Diabetes 53 (2004) 2901-2909
    • (2004) Diabetes , vol.53 , pp. 2901-2909
    • Zhao, H.1    Yakar, S.2    Gavrilova, O.3    Sun, H.4    Zhang, Y.5    Kim, H.6
  • 111
    • 0032797852 scopus 로고    scopus 로고
    • Regulation of glucose production by the liver
    • Nordlie R.C., Foster J.D., and Lange A.J. Regulation of glucose production by the liver. Annu Rev Nutr 19 (1999) 379-406
    • (1999) Annu Rev Nutr , vol.19 , pp. 379-406
    • Nordlie, R.C.1    Foster, J.D.2    Lange, A.J.3
  • 112
    • 33750585132 scopus 로고    scopus 로고
    • Glucose toxicity is responsible for the development of impaired regulation of endogenous glucose production and hepatic glucokinase in Zucker diabetic fatty rats
    • Fujimoto Y., Torres T.P., Donahue E.P., and Shiota M. Glucose toxicity is responsible for the development of impaired regulation of endogenous glucose production and hepatic glucokinase in Zucker diabetic fatty rats. Diabetes 55 (2006) 2479-2490
    • (2006) Diabetes , vol.55 , pp. 2479-2490
    • Fujimoto, Y.1    Torres, T.P.2    Donahue, E.P.3    Shiota, M.4
  • 113
    • 15944429983 scopus 로고    scopus 로고
    • Chronic hyperglycemia enhances PEPCK gene expression and hepatocellular glucose production via elevated liver activating protein/liver inhibitory protein ratio
    • Shao J., Qiao L., Janssen R.C., Pagliassotti M., and Friedman J.E. Chronic hyperglycemia enhances PEPCK gene expression and hepatocellular glucose production via elevated liver activating protein/liver inhibitory protein ratio. Diabetes 54 (2005) 976-984
    • (2005) Diabetes , vol.54 , pp. 976-984
    • Shao, J.1    Qiao, L.2    Janssen, R.C.3    Pagliassotti, M.4    Friedman, J.E.5
  • 114
    • 0036068886 scopus 로고    scopus 로고
    • Normalization of plasma glucose concentration by insulin therapy improves insulin-stimulated glycogen synthesis in type 2 diabetes
    • Pratipanawatr T., Cusi K., Ngo P., Pratipanawatr W., Mandarino L.J., and DeFronzo R.A. Normalization of plasma glucose concentration by insulin therapy improves insulin-stimulated glycogen synthesis in type 2 diabetes. Diabetes 51 (2002) 462-468
    • (2002) Diabetes , vol.51 , pp. 462-468
    • Pratipanawatr, T.1    Cusi, K.2    Ngo, P.3    Pratipanawatr, W.4    Mandarino, L.J.5    DeFronzo, R.A.6
  • 115
    • 0035827501 scopus 로고    scopus 로고
    • Development of glucose-induced insulin resistance in muscle requires protein synthesis
    • Kawanaka K., Han D.H., Gao J., Nolte L.A., and Holloszy J.O. Development of glucose-induced insulin resistance in muscle requires protein synthesis. J Biol Chem 276 (2001) 20101-20107
    • (2001) J Biol Chem , vol.276 , pp. 20101-20107
    • Kawanaka, K.1    Han, D.H.2    Gao, J.3    Nolte, L.A.4    Holloszy, J.O.5
  • 116
    • 0038015693 scopus 로고    scopus 로고
    • Glucose autoregulates its uptake in skeletal muscle: involvement of AMP-activated protein kinase
    • Itani S.I., Saha A.K., Kurowski T.G., Coffin H.R., Tornheim K., and Ruderman N.B. Glucose autoregulates its uptake in skeletal muscle: involvement of AMP-activated protein kinase. Diabetes 52 (2003) 1635-1640
    • (2003) Diabetes , vol.52 , pp. 1635-1640
    • Itani, S.I.1    Saha, A.K.2    Kurowski, T.G.3    Coffin, H.R.4    Tornheim, K.5    Ruderman, N.B.6
  • 117
    • 0034015147 scopus 로고    scopus 로고
    • Hyperglycemia contributes insulin resistance in hepatic and adipose tissue but not skeletal muscle of ZDF rats
    • Nawano M., Oku A., Ueta K., Umebayashi I., Ishirahara T., Arakawa K., et al. Hyperglycemia contributes insulin resistance in hepatic and adipose tissue but not skeletal muscle of ZDF rats. Am J Physiol Endocrinol Metab 278 (2000) E535-543
    • (2000) Am J Physiol Endocrinol Metab , vol.278
    • Nawano, M.1    Oku, A.2    Ueta, K.3    Umebayashi, I.4    Ishirahara, T.5    Arakawa, K.6
  • 118
    • 0036300508 scopus 로고    scopus 로고
    • Sustained exposure of L6 myotubes to high glucose and insulin decreases insulin-stimulated GLUT4 translocation but upregulates GLUT4 activity
    • Huang C., Somwar R., Patel N., Niu W., Török D., and Klip A. Sustained exposure of L6 myotubes to high glucose and insulin decreases insulin-stimulated GLUT4 translocation but upregulates GLUT4 activity. Diabetes 51 (2002) 2090-2098
    • (2002) Diabetes , vol.51 , pp. 2090-2098
    • Huang, C.1    Somwar, R.2    Patel, N.3    Niu, W.4    Török, D.5    Klip, A.6
  • 119
    • 36148955050 scopus 로고    scopus 로고
    • Glucose infusion causes insulin resistance in skeletal muscle of rats without changes in Akt and AS160 phosphorylation
    • Hoy A.J., Bruce C.R., Cederberg A., Turner N., James D.e., Cooney G.J., et al. Glucose infusion causes insulin resistance in skeletal muscle of rats without changes in Akt and AS160 phosphorylation. Am J Physiol Endocrinol Metab 293 (2007) E1358-1364
    • (2007) Am J Physiol Endocrinol Metab , vol.293
    • Hoy, A.J.1    Bruce, C.R.2    Cederberg, A.3    Turner, N.4    James, D.e.5    Cooney, G.J.6
  • 120
    • 33845864967 scopus 로고    scopus 로고
    • Adipocytes as regulators of energy balance and glucose homeostasis
    • Rosen E.D., and Spiegelman B.M. Adipocytes as regulators of energy balance and glucose homeostasis. Nature 444 (2006) 847-853
    • (2006) Nature , vol.444 , pp. 847-853
    • Rosen, E.D.1    Spiegelman, B.M.2
  • 122
    • 33947600110 scopus 로고    scopus 로고
    • Leptin secretion is related to glucose-derived lipogenesis in isolated adipocytes
    • Walker C.G., Bryson J.M., Hancock D.P., and Caterson I.D. Leptin secretion is related to glucose-derived lipogenesis in isolated adipocytes. Int J Obes (Lond) 31 (2007) 723-729
    • (2007) Int J Obes (Lond) , vol.31 , pp. 723-729
    • Walker, C.G.1    Bryson, J.M.2    Hancock, D.P.3    Caterson, I.D.4
  • 123
    • 0034079122 scopus 로고    scopus 로고
    • High glucose and glucosamine induce insulin resistance via different mechanisms in 3T3-L1 adipocytes
    • Nelson B.A., Robinson K.A., and Buse M.G. High glucose and glucosamine induce insulin resistance via different mechanisms in 3T3-L1 adipocytes. Diabetes 49 (2000) 981-991
    • (2000) Diabetes , vol.49 , pp. 981-991
    • Nelson, B.A.1    Robinson, K.A.2    Buse, M.G.3
  • 124
    • 33846087322 scopus 로고    scopus 로고
    • Insulin resistance induced by high glucose and high insulin precedes insulin receptor substrate 1 protein depletion in human adipocytes
    • Renstrom F., Buren J., Svensson M., and Eriksson J.W. Insulin resistance induced by high glucose and high insulin precedes insulin receptor substrate 1 protein depletion in human adipocytes. Metabolism 56 (2007) 190-198
    • (2007) Metabolism , vol.56 , pp. 190-198
    • Renstrom, F.1    Buren, J.2    Svensson, M.3    Eriksson, J.W.4
  • 125
    • 0037341238 scopus 로고    scopus 로고
    • Glucose toxicity in beta-cells: type 2 diabetes, good radicals gone bad, and the glutathione connection
    • Robertson R.P., Harmon J., Tran P.O., Tanaka Y., and Takahashi H. Glucose toxicity in beta-cells: type 2 diabetes, good radicals gone bad, and the glutathione connection. Diabetes 52 (2003) 581-587
    • (2003) Diabetes , vol.52 , pp. 581-587
    • Robertson, R.P.1    Harmon, J.2    Tran, P.O.3    Tanaka, Y.4    Takahashi, H.5
  • 126
    • 42049094276 scopus 로고    scopus 로고
    • Animal models of diabetes mellitus: relevance to vascular complications
    • Thompson C.S. Animal models of diabetes mellitus: relevance to vascular complications. Curr Pharm Des 14 (2008) 309-324
    • (2008) Curr Pharm Des , vol.14 , pp. 309-324
    • Thompson, C.S.1
  • 127
    • 0041885482 scopus 로고    scopus 로고
    • How to ADVANCE prevention of cardiovascular complications in type 2 diabetes
    • Grobbee D.E. How to ADVANCE prevention of cardiovascular complications in type 2 diabetes. Metabolism 52 (2003) 24-28
    • (2003) Metabolism , vol.52 , pp. 24-28
    • Grobbee, D.E.1
  • 128
    • 0030708745 scopus 로고    scopus 로고
    • Cardiomyocyte apoptosis and cardiac angiotensin-converting enzyme in spontaneously hypertensive rats
    • Diez J., Panizo A., Hernandez M., Vega F., Sola I., Fortuno M.A., et al. Cardiomyocyte apoptosis and cardiac angiotensin-converting enzyme in spontaneously hypertensive rats. Hypertension 30 (1997) 1029-1034
    • (1997) Hypertension , vol.30 , pp. 1029-1034
    • Diez, J.1    Panizo, A.2    Hernandez, M.3    Vega, F.4    Sola, I.5    Fortuno, M.A.6
  • 129
    • 36649036593 scopus 로고    scopus 로고
    • Heart failure in diabetes and related conditions
    • Kamalesh M. Heart failure in diabetes and related conditions. J Card Fail 13 (2007) 861-873
    • (2007) J Card Fail , vol.13 , pp. 861-873
    • Kamalesh, M.1
  • 130
    • 37449025486 scopus 로고    scopus 로고
    • Non enzymatic glycated proteins in the blood and cardiovascular disease
    • Misciagna G., De Michele G., and Trevisan M. Non enzymatic glycated proteins in the blood and cardiovascular disease. Curr Pharm Des 13 (2007) 3688-3695
    • (2007) Curr Pharm Des , vol.13 , pp. 3688-3695
    • Misciagna, G.1    De Michele, G.2    Trevisan, M.3
  • 131
    • 27444438346 scopus 로고    scopus 로고
    • Advances in diabetes for the millennium: chronic microvascular complications of diabetes
    • Olansky L. Advances in diabetes for the millennium: chronic microvascular complications of diabetes. MedGenMed 6 (2004) 14
    • (2004) MedGenMed , vol.6 , pp. 14
    • Olansky, L.1
  • 132
    • 21044443182 scopus 로고    scopus 로고
    • Diabetic vascular complications: pathophysiology, biochemical basis and potential therapeutic strategy
    • Yamagishi S., and Imaizumi T. Diabetic vascular complications: pathophysiology, biochemical basis and potential therapeutic strategy. Curr Pharm Des 11 (2005) 2279-2299
    • (2005) Curr Pharm Des , vol.11 , pp. 2279-2299
    • Yamagishi, S.1    Imaizumi, T.2
  • 134
    • 0348048874 scopus 로고    scopus 로고
    • Diabetic retinopathy
    • Frank R.N. Diabetic retinopathy. N Engl J Med 350 (2004) 48-58
    • (2004) N Engl J Med , vol.350 , pp. 48-58
    • Frank, R.N.1
  • 135
    • 33747203244 scopus 로고    scopus 로고
    • Diabetic retinopathy: the latest in current management
    • Bhavsar A.R. Diabetic retinopathy: the latest in current management. Retina 26 (2006) S71-79
    • (2006) Retina , vol.26
    • Bhavsar, A.R.1
  • 136
    • 0029842963 scopus 로고    scopus 로고
    • Initiation and progression of diabetic nephropathy
    • Parving H.H. Initiation and progression of diabetic nephropathy. N Engl J Med 335 (1996) 1682-1683
    • (1996) N Engl J Med , vol.335 , pp. 1682-1683
    • Parving, H.H.1
  • 137
    • 0029960590 scopus 로고    scopus 로고
    • Magnitude of end-stage renal disease in IDDM: a 35 year follow-up study
    • Krolewski M., Eggers P.W., and Warram J.H. Magnitude of end-stage renal disease in IDDM: a 35 year follow-up study. Kidney Int 50 (1996) 2041-2046
    • (1996) Kidney Int , vol.50 , pp. 2041-2046
    • Krolewski, M.1    Eggers, P.W.2    Warram, J.H.3
  • 138
    • 0029076281 scopus 로고
    • Hyperglycemia and diabetic kidney disease
    • Sharma K., and Ziyadeh F.N. Hyperglycemia and diabetic kidney disease. Diabetes 44 (1995) 1139-1146
    • (1995) Diabetes , vol.44 , pp. 1139-1146
    • Sharma, K.1    Ziyadeh, F.N.2
  • 140
    • 37349120735 scopus 로고    scopus 로고
    • The podocyte and diabetes mellitus: is the podocyte the key to the origins of diabetic nephropathy?
    • Reddy G.R., Kotlyarevska K., Ransom R.F., and Menon R.K. The podocyte and diabetes mellitus: is the podocyte the key to the origins of diabetic nephropathy?. Curr Opin Nephrol Hypertens 17 (2008) 32-36
    • (2008) Curr Opin Nephrol Hypertens , vol.17 , pp. 32-36
    • Reddy, G.R.1    Kotlyarevska, K.2    Ransom, R.F.3    Menon, R.K.4
  • 141
    • 33644783770 scopus 로고    scopus 로고
    • Glucose-induced reactive oxygen species cause apoptosis of podocytes and podocyte depletion at the onset of diabetic nephropathy
    • Susztak K., Raff A.C., Schiffer M., and Bottinger E.P. Glucose-induced reactive oxygen species cause apoptosis of podocytes and podocyte depletion at the onset of diabetic nephropathy. Diabetes 55 (2006) 225-233
    • (2006) Diabetes , vol.55 , pp. 225-233
    • Susztak, K.1    Raff, A.C.2    Schiffer, M.3    Bottinger, E.P.4
  • 143
    • 34250321556 scopus 로고    scopus 로고
    • Insight on the pathogenesis of diabetic nephropathy from the study of podocyte and mesangial cell biology
    • Gruden G., Perin P.C., and Camussi G. Insight on the pathogenesis of diabetic nephropathy from the study of podocyte and mesangial cell biology. Curr Diabetes Rev 1 (2005) 27-40
    • (2005) Curr Diabetes Rev , vol.1 , pp. 27-40
    • Gruden, G.1    Perin, P.C.2    Camussi, G.3
  • 144
    • 34548397224 scopus 로고    scopus 로고
    • Molecular mechanisms of diabetic nephropathy and its therapeutic intervention
    • Yamagishi S., Fukami K., Ueda S., and Okuda S. Molecular mechanisms of diabetic nephropathy and its therapeutic intervention. Curr Drug Targets 8 (2007) 952-959
    • (2007) Curr Drug Targets , vol.8 , pp. 952-959
    • Yamagishi, S.1    Fukami, K.2    Ueda, S.3    Okuda, S.4
  • 145
    • 34250026180 scopus 로고    scopus 로고
    • Diabetic nephropathy and proximal tubule ROS: challenging our glomerulocentricity
    • Bagby S.P. Diabetic nephropathy and proximal tubule ROS: challenging our glomerulocentricity. Kidney Int 71 (2007) 1199-1202
    • (2007) Kidney Int , vol.71 , pp. 1199-1202
    • Bagby, S.P.1
  • 147
    • 33645657561 scopus 로고    scopus 로고
    • Diabetic peripheral neuropathic pain: clinical and quality-of-life issues
    • Argoff C.E., Cole B.E., Fishbain D.A., and Irving G.A. Diabetic peripheral neuropathic pain: clinical and quality-of-life issues. Mayo Clin Proc 81 (2006) S3-11
    • (2006) Mayo Clin Proc , vol.81
    • Argoff, C.E.1    Cole, B.E.2    Fishbain, D.A.3    Irving, G.A.4
  • 149
    • 0032805018 scopus 로고    scopus 로고
    • Diabetic neuropathy: mechanisms and future treatment options
    • Thomas P.K. Diabetic neuropathy: mechanisms and future treatment options. J Neurol Neurosurg Psychiatry 67 (1999) 277-279
    • (1999) J Neurol Neurosurg Psychiatry , vol.67 , pp. 277-279
    • Thomas, P.K.1
  • 150
    • 0029954190 scopus 로고    scopus 로고
    • Pathologic alterations in the diabetic neuropathies of humans: a review
    • Dyck P.J., and Giannini C. Pathologic alterations in the diabetic neuropathies of humans: a review. J Neuropathol Exp Neurol 55 (1996) 1181-1193
    • (1996) J Neuropathol Exp Neurol , vol.55 , pp. 1181-1193
    • Dyck, P.J.1    Giannini, C.2
  • 151
    • 0029009982 scopus 로고
    • Glycemic control and complications of diabetes mellitus
    • Hirsch I.B. Glycemic control and complications of diabetes mellitus. West J Med 162 (1995) 430-438
    • (1995) West J Med , vol.162 , pp. 430-438
    • Hirsch, I.B.1
  • 153
    • 0035211205 scopus 로고    scopus 로고
    • Neuropathy in diabetic mice overexpressing human aldose reductase and effects of aldose reductase inhibitor
    • Yagihashi S., Yamagishi S.I., Wada Ri R., Baba M., Hohman T.C., Yabe-Nishimura C., et al. Neuropathy in diabetic mice overexpressing human aldose reductase and effects of aldose reductase inhibitor. Brain 124 (2001) 2448-2458
    • (2001) Brain , vol.124 , pp. 2448-2458
    • Yagihashi, S.1    Yamagishi, S.I.2    Wada Ri, R.3    Baba, M.4    Hohman, T.C.5    Yabe-Nishimura, C.6
  • 154
    • 23744467294 scopus 로고    scopus 로고
    • Role of advanced glycation end products and their receptors in development of diabetic neuropathy
    • Wada R., and Yagihashi S. Role of advanced glycation end products and their receptors in development of diabetic neuropathy. Ann N Y Acad Sci 1043 (2005) 598-604
    • (2005) Ann N Y Acad Sci , vol.1043 , pp. 598-604
    • Wada, R.1    Yagihashi, S.2
  • 155
    • 0037327402 scopus 로고    scopus 로고
    • Oxidative stress and diabetic neuropathy: a new understanding of an old problem
    • Feldman E.L. Oxidative stress and diabetic neuropathy: a new understanding of an old problem. J Clin Invest 111 (2003) 431-433
    • (2003) J Clin Invest , vol.111 , pp. 431-433
    • Feldman, E.L.1
  • 156
    • 0034705104 scopus 로고    scopus 로고
    • Expression profiling of pancreatic beta cells: glucose regulation of secretory and metabolic pathway genes
    • Webb G.C., Akbar M.S., Zhao C., and Steiner D.F. Expression profiling of pancreatic beta cells: glucose regulation of secretory and metabolic pathway genes. Proc Natl Acad Sci U S A 97 (2000) 5773-5778
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 5773-5778
    • Webb, G.C.1    Akbar, M.S.2    Zhao, C.3    Steiner, D.F.4
  • 157
    • 34047161483 scopus 로고    scopus 로고
    • Acute hyperglycemia induces a global downregulation of gene expression in adipose tissue and skeletal muscle of healthy subjects
    • Meugnier E., Faraj M., Rome S., Beauregard G., Michaut A., Pelloux V., et al. Acute hyperglycemia induces a global downregulation of gene expression in adipose tissue and skeletal muscle of healthy subjects. Diabetes 56 (2007) 992-999
    • (2007) Diabetes , vol.56 , pp. 992-999
    • Meugnier, E.1    Faraj, M.2    Rome, S.3    Beauregard, G.4    Michaut, A.5    Pelloux, V.6
  • 158
    • 0036169137 scopus 로고    scopus 로고
    • Gradual loss of pancreatic beta-cell insulin, glucokinase and GLUT2 glucose transporter immunoreactivities during the time course of nutritionally induced type-2 diabetes in Psammomys obesus (sand rat)
    • Jorns A., Tiedge M., Ziv E., Shafrir E., and Lenzen S. Gradual loss of pancreatic beta-cell insulin, glucokinase and GLUT2 glucose transporter immunoreactivities during the time course of nutritionally induced type-2 diabetes in Psammomys obesus (sand rat). Virchows Arch 440 (2002) 63-69
    • (2002) Virchows Arch , vol.440 , pp. 63-69
    • Jorns, A.1    Tiedge, M.2    Ziv, E.3    Shafrir, E.4    Lenzen, S.5
  • 159
    • 23844490919 scopus 로고    scopus 로고
    • High glucose-induced impairment in insulin secretion is associated with reduction in islet glucokinase in a mouse model of susceptibility to islet dysfunction
    • Kooptiwut S., Kebede M., Zraika S., Visinoni S., Aston-Moourney K., Favaloro J., et al. High glucose-induced impairment in insulin secretion is associated with reduction in islet glucokinase in a mouse model of susceptibility to islet dysfunction. J Mol Endocrinol 35 (2005) 39-48
    • (2005) J Mol Endocrinol , vol.35 , pp. 39-48
    • Kooptiwut, S.1    Kebede, M.2    Zraika, S.3    Visinoni, S.4    Aston-Moourney, K.5    Favaloro, J.6
  • 160
    • 0030762209 scopus 로고    scopus 로고
    • Differentiation of glucose toxicity from beta cell exhaustion during the evolution of defective insulin gene expression in the pancreatic islet cell line, HIT-T15
    • Moran A., Zhang H.J., Olson L.K., Harmon J.S., Poitout V., and Robertson R.P. Differentiation of glucose toxicity from beta cell exhaustion during the evolution of defective insulin gene expression in the pancreatic islet cell line, HIT-T15. J Clin Invest 99 (1997) 534-539
    • (1997) J Clin Invest , vol.99 , pp. 534-539
    • Moran, A.1    Zhang, H.J.2    Olson, L.K.3    Harmon, J.S.4    Poitout, V.5    Robertson, R.P.6
  • 161
    • 0032230172 scopus 로고    scopus 로고
    • Glucose rapidly and reversibly decreases INS-1 cell insulin gene transcription via decrements in STF-1 and C1 activator transcription factor activity
    • Olson L.K., Qian J., and Poitout V. Glucose rapidly and reversibly decreases INS-1 cell insulin gene transcription via decrements in STF-1 and C1 activator transcription factor activity. Mol Endocrinol 12 (1998) 207-219
    • (1998) Mol Endocrinol , vol.12 , pp. 207-219
    • Olson, L.K.1    Qian, J.2    Poitout, V.3
  • 162
    • 0029664752 scopus 로고    scopus 로고
    • Chronic exposure of betaTC-6 cells to supraphysiologic concentrations of glucose decreases binding of the RIPE3b1 insulin gene transcription activator
    • Poitout V., Olson L.K., and Robertson R.P. Chronic exposure of betaTC-6 cells to supraphysiologic concentrations of glucose decreases binding of the RIPE3b1 insulin gene transcription activator. J Clin Invest 97 (1996) 1041-1046
    • (1996) J Clin Invest , vol.97 , pp. 1041-1046
    • Poitout, V.1    Olson, L.K.2    Robertson, R.P.3
  • 163
    • 0034982387 scopus 로고    scopus 로고
    • High glucose causes apoptosis in cultured human pancreatic islets of Langerhans: a potential role for regulation of specific Bcl family genes toward an apoptotic cell death program
    • Federici M., Hribal M., Perego L., Ranalli M., Caradonna Z., Perego C., et al. High glucose causes apoptosis in cultured human pancreatic islets of Langerhans: a potential role for regulation of specific Bcl family genes toward an apoptotic cell death program. Diabetes 50 (2001) 1290-1301
    • (2001) Diabetes , vol.50 , pp. 1290-1301
    • Federici, M.1    Hribal, M.2    Perego, L.3    Ranalli, M.4    Caradonna, Z.5    Perego, C.6
  • 164
    • 13844312665 scopus 로고    scopus 로고
    • Differential proteomics: an overview of gel and non-gel based approaches
    • Monteoliva L., and Albar J.P. Differential proteomics: an overview of gel and non-gel based approaches. Brief Funct Genomic Proteomic 3 (2004) 220-239
    • (2004) Brief Funct Genomic Proteomic , vol.3 , pp. 220-239
    • Monteoliva, L.1    Albar, J.P.2
  • 165
    • 26844447225 scopus 로고    scopus 로고
    • Differentially expressed proteins in the pancreas of diet-induced diabetic mice
    • Qiu L., List E.O., and Kopchick J.J. Differentially expressed proteins in the pancreas of diet-induced diabetic mice. Mol Cell Proteomics 4 (2005) 1311-1318
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1311-1318
    • Qiu, L.1    List, E.O.2    Kopchick, J.J.3
  • 167
    • 0035225642 scopus 로고    scopus 로고
    • The mouse SWISS-2D PAGE database: a tool for proteomics study of diabetes and obesity
    • Sanchez J.C., Chiappe D., Converset V., Hoogland C., Binz P.A., Paesano S., et al. The mouse SWISS-2D PAGE database: a tool for proteomics study of diabetes and obesity. Proteomics 1 (2001) 136-163
    • (2001) Proteomics , vol.1 , pp. 136-163
    • Sanchez, J.C.1    Chiappe, D.2    Converset, V.3    Hoogland, C.4    Binz, P.A.5    Paesano, S.6
  • 168
    • 0036652155 scopus 로고    scopus 로고
    • Effect of rosiglitazone on the differential expression of diabetes-associated proteins in pancreatic islets of C57Bl/6 lep/lep mice
    • Sanchez J.C., Converset V., Nolan A., Schmid G., Wang S., Heller M., et al. Effect of rosiglitazone on the differential expression of diabetes-associated proteins in pancreatic islets of C57Bl/6 lep/lep mice. Mol Cell Proteomics 1 (2002) 509-516
    • (2002) Mol Cell Proteomics , vol.1 , pp. 509-516
    • Sanchez, J.C.1    Converset, V.2    Nolan, A.3    Schmid, G.4    Wang, S.5    Heller, M.6
  • 169
    • 20844435281 scopus 로고    scopus 로고
    • Protein profiling of human pancreatic islets by two-dimensional gel electrophoresis and mass spectrometry
    • Ahmed M., Forsberg J., and Bergsten P. Protein profiling of human pancreatic islets by two-dimensional gel electrophoresis and mass spectrometry. J Proteome Res 4 (2005) 931-940
    • (2005) J Proteome Res , vol.4 , pp. 931-940
    • Ahmed, M.1    Forsberg, J.2    Bergsten, P.3
  • 170
  • 171
    • 16844382825 scopus 로고    scopus 로고
    • Glucose-induced changes of multiple mouse islet proteins analysed by two-dimensional gel electrophoresis and mass spectrometry
    • Ahmed M., and Bergsten P. Glucose-induced changes of multiple mouse islet proteins analysed by two-dimensional gel electrophoresis and mass spectrometry. Diabetologia 48 (2005) 477-485
    • (2005) Diabetologia , vol.48 , pp. 477-485
    • Ahmed, M.1    Bergsten, P.2
  • 172
    • 38549143790 scopus 로고    scopus 로고
    • Proteomic analysis of mouse islets after multiple low-dose streptozotocin injection
    • Xie X., Li S., Liu S., Lu Y., Shen P., and Ji J. Proteomic analysis of mouse islets after multiple low-dose streptozotocin injection. Biochim Biophys Acta 1784 (2008) 276-284
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 276-284
    • Xie, X.1    Li, S.2    Liu, S.3    Lu, Y.4    Shen, P.5    Ji, J.6
  • 173
    • 34748899652 scopus 로고    scopus 로고
    • Evaluation of the SELDI-TOF MS technique for protein profiling of pancreatic islets exposed to glucose and oleate
    • Orstäter H., Sundsten T., Lin J.M., and Bergsten P. Evaluation of the SELDI-TOF MS technique for protein profiling of pancreatic islets exposed to glucose and oleate. Proteomics 7 (2007) 3105-3115
    • (2007) Proteomics , vol.7 , pp. 3105-3115
    • Orstäter, H.1    Sundsten, T.2    Lin, J.M.3    Bergsten, P.4
  • 174
    • 33749587601 scopus 로고    scopus 로고
    • Mitochondrial protein patterns correlating with impaired insulin secretion from INS-1E cells exposed to elevated glucose concentrations
    • Nyblom H.K., Thorn K., Ahmed M., and Bergsten P. Mitochondrial protein patterns correlating with impaired insulin secretion from INS-1E cells exposed to elevated glucose concentrations. Proteomics 6 (2006) 5193-5198
    • (2006) Proteomics , vol.6 , pp. 5193-5198
    • Nyblom, H.K.1    Thorn, K.2    Ahmed, M.3    Bergsten, P.4
  • 175
    • 38649130988 scopus 로고    scopus 로고
    • Metabolomic and proteomic analysis of a clonal insulin-producing beta-cell line (INS-1 832/13)
    • Fernandez C., Fransson U., Hallgard E., Spegel P., Holm C., Krogh M., et al. Metabolomic and proteomic analysis of a clonal insulin-producing beta-cell line (INS-1 832/13). J Proteome Res 7 (2008) 400-411
    • (2008) J Proteome Res , vol.7 , pp. 400-411
    • Fernandez, C.1    Fransson, U.2    Hallgard, E.3    Spegel, P.4    Holm, C.5    Krogh, M.6
  • 176
    • 33845997409 scopus 로고    scopus 로고
    • Proteomic screening of glucose-responsive and glucose non-responsive MIN-6 beta cells reveals differential expression of proteins involved in protein folding, secretion and oxidative stress
    • Dowling P., O'Driscoll L., O'Sullivan F., Dowd A., Henry M., Jeppesen P.B., et al. Proteomic screening of glucose-responsive and glucose non-responsive MIN-6 beta cells reveals differential expression of proteins involved in protein folding, secretion and oxidative stress. Proteomics 6 (2006) 6578-6587
    • (2006) Proteomics , vol.6 , pp. 6578-6587
    • Dowling, P.1    O'Driscoll, L.2    O'Sullivan, F.3    Dowd, A.4    Henry, M.5    Jeppesen, P.B.6
  • 177
    • 0035130272 scopus 로고    scopus 로고
    • Beta-cell adaptation and decompensation during the progression of diabetes
    • Weir G.C., Laybutt D.R., Kaneto H., Bonner-Weir S., and Sharma A. Beta-cell adaptation and decompensation during the progression of diabetes. Diabetes 50 Suppl 1 (2001) S154-159
    • (2001) Diabetes , vol.50 , Issue.SUPPL. 1
    • Weir, G.C.1    Laybutt, D.R.2    Kaneto, H.3    Bonner-Weir, S.4    Sharma, A.5
  • 178
    • 0023845174 scopus 로고
    • Treatment of hyperlipidemia reduces glomerular injury in obese Zucker rats
    • Kasiske B.L., O'Donnell M.P., Cleary M.P., and Keane W.F. Treatment of hyperlipidemia reduces glomerular injury in obese Zucker rats. Kidney Int 33 (1988) 667-672
    • (1988) Kidney Int , vol.33 , pp. 667-672
    • Kasiske, B.L.1    O'Donnell, M.P.2    Cleary, M.P.3    Keane, W.F.4
  • 179
    • 0035053220 scopus 로고    scopus 로고
    • Lipotoxicity and glucotoxicity in type 2 diabetes. Effects on development and progression
    • Sivitz W.I. Lipotoxicity and glucotoxicity in type 2 diabetes. Effects on development and progression. Postgrad Med 109 55-59 (2001) 54-63
    • (2001) Postgrad Med , vol.109 , Issue.55-59 , pp. 54-63
    • Sivitz, W.I.1
  • 180
    • 0043268763 scopus 로고    scopus 로고
    • Pancreatic beta-cell lipotoxicity induced by overexpression of hormone-sensitive lipase
    • Winzell M.S., Svensson H., Enerback S., Ravnskjaer K., Mandrup S., Esser V., et al. Pancreatic beta-cell lipotoxicity induced by overexpression of hormone-sensitive lipase. Diabetes 52 (2003) 2057-2065
    • (2003) Diabetes , vol.52 , pp. 2057-2065
    • Winzell, M.S.1    Svensson, H.2    Enerback, S.3    Ravnskjaer, K.4    Mandrup, S.5    Esser, V.6
  • 181
    • 0036254607 scopus 로고    scopus 로고
    • Insulin resistance in type 2 diabetes: role of fatty acids
    • Arner P. Insulin resistance in type 2 diabetes: role of fatty acids. Diabetes Metab Res Rev 18 Suppl 2 (2002) S5-9
    • (2002) Diabetes Metab Res Rev , vol.18 , Issue.SUPPL. 2
    • Arner, P.1
  • 182
    • 43549108142 scopus 로고    scopus 로고
    • Glucolipotoxicity: fuel excess and {beta}-cell dysfunction
    • Poitout V., and Robertson R.P. Glucolipotoxicity: fuel excess and {beta}-cell dysfunction. Endocr Rev 29 3 (2008) 351-366
    • (2008) Endocr Rev , vol.29 , Issue.3 , pp. 351-366
    • Poitout, V.1    Robertson, R.P.2
  • 183
    • 0347916882 scopus 로고    scopus 로고
    • The Rab-binding protein Noc2 is associated with insulin-containing secretory granules and is essential for pancreatic beta-cell exocytosis
    • Cheviet S., Coppola T., Haynes L.P., Burgoyne R.D., and Regazzi R. The Rab-binding protein Noc2 is associated with insulin-containing secretory granules and is essential for pancreatic beta-cell exocytosis. Mol Endocrinol 18 (2004) 117-126
    • (2004) Mol Endocrinol , vol.18 , pp. 117-126
    • Cheviet, S.1    Coppola, T.2    Haynes, L.P.3    Burgoyne, R.D.4    Regazzi, R.5
  • 184
    • 0035985165 scopus 로고    scopus 로고
    • Pancreatic beta-cell protein granuphilin binds Rab3 and Munc-18 and controls exocytosis
    • Coppola T., Frantz C., Perret-Menoud V., Gattesco S., Hirling H., and Regazzi R. Pancreatic beta-cell protein granuphilin binds Rab3 and Munc-18 and controls exocytosis. Mol Biol Cell 13 (2002) 1906-1915
    • (2002) Mol Biol Cell , vol.13 , pp. 1906-1915
    • Coppola, T.1    Frantz, C.2    Perret-Menoud, V.3    Gattesco, S.4    Hirling, H.5    Regazzi, R.6
  • 185
    • 33746853822 scopus 로고    scopus 로고
    • Tomosyn-1 is involved in a post-docking event required for pancreatic beta-cell exocytosis
    • Cheviet S., Bezzi P., Ivarsson R., Renstrom E., Viertl D., Kasas S., et al. Tomosyn-1 is involved in a post-docking event required for pancreatic beta-cell exocytosis. J Cell Sci 119 (2006) 2912-2920
    • (2006) J Cell Sci , vol.119 , pp. 2912-2920
    • Cheviet, S.1    Bezzi, P.2    Ivarsson, R.3    Renstrom, E.4    Viertl, D.5    Kasas, S.6
  • 186
    • 0034066471 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: un amour impossible?
    • Santoni V., Molloy M., and Rabilloud T. Membrane proteins and proteomics: un amour impossible?. Electrophoresis 21 (2000) 1054-1070
    • (2000) Electrophoresis , vol.21 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.2    Rabilloud, T.3
  • 187
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong S.E., Blagoev B., Kratchmarova I., Kristensen D.B., Steen H., Pandey A., et al. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 1 (2002) 376-386
    • (2002) Mol Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6
  • 189
    • 0038364020 scopus 로고    scopus 로고
    • Organelle proteomics: implications for subcellular fractionation in proteomics
    • Huber L.A., Pfaller K., and Vietor I. Organelle proteomics: implications for subcellular fractionation in proteomics. Circ Res 92 (2003) 962-968
    • (2003) Circ Res , vol.92 , pp. 962-968
    • Huber, L.A.1    Pfaller, K.2    Vietor, I.3


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