메뉴 건너뛰기




Volumn 7, Issue 7-8, 2005, Pages 1040-1052

The molecular basis for oxidative stress-induced insulin resistance

Author keywords

[No Author keywords available]

Indexed keywords

2,4 DINITROPHENYLHYDRAZINE; ACETYLCYSTEINE; ALPHA TOCOPHEROL; ANISOMYCIN; ANTIOXIDANT; ARGININE; ASCORBIC ACID; CATALASE; GLUTATHIONE; GLUTATHIONE PEROXIDASE; HYDROGEN PEROXIDE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INSULIN; INSULIN RECEPTOR; INSULIN RECEPTOR SUBSTRATE 1; METALLOTHIONEIN; PROTEIN SERINE THREONINE KINASE; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; STRESS ACTIVATED PROTEIN KINASE; SUPEROXIDE DISMUTASE; TAURINE; THIOCTIC ACID; THIOREDOXIN; TUMOR NECROSIS FACTOR ALPHA;

EID: 22044443268     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2005.7.1040     Document Type: Review
Times cited : (497)

References (157)
  • 1
    • 0033230607 scopus 로고    scopus 로고
    • Role of redox potential and reactive oxygen species in stress signaling
    • Adler V, Yin Z, Tew KD, and Ronai Z. Role of redox potential and reactive oxygen species in stress signaling. Oncogene 18: 6104-6111, 1999.
    • (1999) Oncogene , vol.18 , pp. 6104-6111
    • Adler, V.1    Yin, Z.2    Tew, K.D.3    Ronai, Z.4
  • 4
    • 0033231351 scopus 로고    scopus 로고
    • Gene expression and the thiol redox state
    • Arrigo AP. Gene expression and the thiol redox state. Free Radic Biol Med 27: 936-944, 1999.
    • (1999) Free Radic Biol Med , vol.27 , pp. 936-944
    • Arrigo, A.P.1
  • 5
    • 0020420363 scopus 로고
    • Insulin-stimulated tyrosine phosphorylation of the insulin receptor in detergent extracts of human placental membranes. Comparison to epidermal growth factor-stimulated phosphorylation
    • Avruch J, Nemenoff RA, Blackshear PJ, Pierce MW, and Osathanondh R. Insulin-stimulated tyrosine phosphorylation of the insulin receptor in detergent extracts of human placental membranes. Comparison to epidermal growth factor-stimulated phosphorylation. J Biol Chem 257: 15162-15166, 1982.
    • (1982) J Biol Chem , vol.257 , pp. 15162-15166
    • Avruch, J.1    Nemenoff, R.A.2    Blackshear, P.J.3    Pierce, M.W.4    Osathanondh, R.5
  • 7
    • 0031916984 scopus 로고    scopus 로고
    • The free radical theory of aging matures
    • Beckman KB and Ames BN. The free radical theory of aging matures. Physiol Rev 78: 547-581, 1998.
    • (1998) Physiol Rev , vol.78 , pp. 547-581
    • Beckman, K.B.1    Ames, B.N.2
  • 8
    • 0034794965 scopus 로고    scopus 로고
    • Turning down insulin signaling
    • Birnbaum MJ. Turning down insulin signaling. J Clin Invest 108: 655-659, 2001.
    • (2001) J Clin Invest , vol.108 , pp. 655-659
    • Birnbaum, M.J.1
  • 9
    • 0033579515 scopus 로고    scopus 로고
    • Regulation of glucose transport and glycogen synthesis in L6 muscle cells during oxidative stress. Evidence for cross-talk between the insulin and SAPK2/p38 mitogen-activated protein kinase signaling pathways
    • Blair AS, Hajduch E, Litherland GJ, and Hundal HS. Regulation of glucose transport and glycogen synthesis in L6 muscle cells during oxidative stress. Evidence for cross-talk between the insulin and SAPK2/p38 mitogen-activated protein kinase signaling pathways. J Biol Chem 274: 36293-36299, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 36293-36299
    • Blair, A.S.1    Hajduch, E.2    Litherland, G.J.3    Hundal, H.S.4
  • 10
    • 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: 813-820, 2001.
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 11
    • 0042822096 scopus 로고    scopus 로고
    • Intramuscular heat shock protein 72 and heme oxygenase-1 mRNA are reduced in patients with type 2 diabetes: Evidence that insulin resistance is associated with a disturbed antioxidant defense mechanism
    • Bruce CR, Carey AL, Hawley JA, and Febbraio MA. Intramuscular heat shock protein 72 and heme oxygenase-1 mRNA are reduced in patients with type 2 diabetes: evidence that insulin resistance is associated with a disturbed antioxidant defense mechanism. Diabetes 52: 2338-2345, 2003.
    • (2003) Diabetes , vol.52 , pp. 2338-2345
    • Bruce, C.R.1    Carey, A.L.2    Hawley, J.A.3    Febbraio, M.A.4
  • 12
    • 0031771146 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatases: Structure, mechanism, and inhibitor discovery
    • Burke TR Jr and Zhang ZY. Protein-tyrosine phosphatases: structure, mechanism, and inhibitor discovery. Biopolymers 47: 225-241, 1998.
    • (1998) Biopolymers , vol.47 , pp. 225-241
    • Burke Jr., T.R.1    Zhang, Z.Y.2
  • 13
    • 0027716328 scopus 로고
    • Vitamin E improves the action of insulin
    • Caballero B. Vitamin E improves the action of insulin. Nutr Rev 51:339-340, 1993.
    • (1993) Nutr Rev , vol.51 , pp. 339-340
    • Caballero, B.1
  • 14
    • 0033980885 scopus 로고    scopus 로고
    • Oxidative stress and glycemic regulation
    • Ceriello A. Oxidative stress and glycemic regulation. Metabolism 49: 27-29, 2000.
    • (2000) Metabolism , vol.49 , pp. 27-29
    • Ceriello, A.1
  • 15
    • 0042093769 scopus 로고    scopus 로고
    • New insights on oxidative stress and diabetic complications may lead to a "causal" antioxidant therapy
    • Ceriello A. New insights on oxidative stress and diabetic complications may lead to a "causal" antioxidant therapy. Diabetes Care 26: 1589-1596, 2003.
    • (2003) Diabetes Care , vol.26 , pp. 1589-1596
    • Ceriello, A.1
  • 16
    • 0028904053 scopus 로고
    • Insulin action and the insulin signaling network
    • Cheatham B and Kahn CR. Insulin action and the insulin signaling network. Endocr Rev 16: 117-142, 1995.
    • (1995) Endocr Rev , vol.16 , pp. 117-142
    • Cheatham, B.1    Kahn, C.R.2
  • 17
    • 0030358424 scopus 로고    scopus 로고
    • Dissection of protein kinase cascades that mediate cellular response to cytokines and cellular stress
    • Cohen P. Dissection of protein kinase cascades that mediate cellular response to cytokines and cellular stress. Adv Pharmacol 36: 15-27, 1996.
    • (1996) Adv Pharmacol , vol.36 , pp. 15-27
    • Cohen, P.1
  • 18
    • 0015501791 scopus 로고
    • ++-dependent thiol stimulation of glucose metabolism in white fat cells
    • ++-dependent thiol stimulation of glucose metabolism in white fat cells. J Biol Chem 247: 6218-6223, 1972.
    • (1972) J Biol Chem , vol.247 , pp. 6218-6223
    • Czech, M.P.1    Fain, J.N.2
  • 19
    • 0015959226 scopus 로고
    • 2+-dependent thiol activation of fat cell glucose utilization
    • 2+-dependent thiol activation of fat cell glucose utilization. J Biol Chem 249: 1001-1006, 1974.
    • (1974) J Biol Chem , vol.249 , pp. 1001-1006
    • Czech, M.P.1    Lawrence Jr., J.C.2    Lynn, W.S.3
  • 20
    • 0016284089 scopus 로고
    • Evidence for the involvement of sulfhydryl oxidation in the regulation of fat cell hexose transport by insulin
    • Czech MP, Lawrence JC Jr, and Lynn WS. Evidence for the involvement of sulfhydryl oxidation in the regulation of fat cell hexose transport by insulin. Proc Natl Acad Sci U S A 71: 4173-4177, 1974.
    • (1974) Proc Natl Acad Sci U S A , vol.71 , pp. 4173-4177
    • Czech, M.P.1    Lawrence Jr., J.C.2    Lynn, W.S.3
  • 21
    • 0030724591 scopus 로고    scopus 로고
    • Pathogenesis of type 2 diabetes: Metabolic and molecular implications for identifying diabetes genes
    • DeFronzo RA. Pathogenesis of type 2 diabetes: metabolic and molecular implications for identifying diabetes genes. Diabet Rev 5: 177-269, 1997.
    • (1997) Diabet Rev , vol.5 , pp. 177-269
    • DeFronzo, R.A.1
  • 22
    • 0032176512 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: Mechanisms of catalysis and regulation
    • Denu JM and Dixon JE. Protein tyrosine phosphatases: mechanisms of catalysis and regulation. Curr Opin Chem Biol 2: 633-541, 1998.
    • (1998) Curr Opin Chem Biol , vol.2 , pp. 633-1541
    • Denu, J.M.1    Dixon, J.E.2
  • 23
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Dröge W. Free radicals in the physiological control of cell function. Physiol Rev 82: 47-95, 2002.
    • (2002) Physiol Rev , vol.82 , pp. 47-95
    • Dröge, W.1
  • 24
    • 0032897899 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: Their role in insulin action and potential as drug targets
    • Evans JL and Jallal B. Protein tyrosine phosphatases: their role in insulin action and potential as drug targets. Exp Opin Invest Drugs 8: 139-160, 1999.
    • (1999) Exp Opin Invest Drugs , vol.8 , pp. 139-160
    • Evans, J.L.1    Jallal, B.2
  • 25
    • 0036796875 scopus 로고    scopus 로고
    • Oxidative stress and stress-activated signaling pathways: A unifying hypothesis of type 2 diabetes
    • Evans JL, Goldfine ID, Maddux BA, and Grodsky GM. Oxidative stress and stress-activated signaling pathways: a unifying hypothesis of type 2 diabetes. Endocr Rev 23: 599-622, 2002.
    • (2002) Endocr Rev , vol.23 , pp. 599-622
    • Evans, J.L.1    Goldfine, I.D.2    Maddux, B.A.3    Grodsky, G.M.4
  • 26
    • 0036161589 scopus 로고    scopus 로고
    • Pharmacokinetics, tolerability, and fructosamine-lowering effect of a novel, controlled release formulation of α-lipoic acid
    • Evans JL, Heymann CJ, Goldfine ID, and Gavin LA. Pharmacokinetics, tolerability, and fructosamine-lowering effect of a novel, controlled release formulation of α-lipoic acid. Endocr Pract 8: 29-35, 2002.
    • (2002) Endocr Pract , vol.8 , pp. 29-35
    • Evans, J.L.1    Heymann, C.J.2    Goldfine, I.D.3    Gavin, L.A.4
  • 27
    • 0037219409 scopus 로고    scopus 로고
    • Are oxidative stress-activated signaling pathways mediators of insulin resistance and β-cell dysfunction?
    • Evans JL, Goldfine ID, Maddux BA, and Grodsky GM. Are oxidative stress-activated signaling pathways mediators of insulin resistance and β-cell dysfunction? Diabetes 52: 1-8, 2003.
    • (2003) Diabetes , vol.52 , pp. 1-8
    • Evans, J.L.1    Goldfine, I.D.2    Maddux, B.A.3    Grodsky, G.M.4
  • 28
    • 7444232013 scopus 로고    scopus 로고
    • Antioxidants in diabetic complications and insulin resistance
    • edited by Raz I, Skyler JS, and Shafrir E. London: Martin Dunitz
    • Evans JL, Maddux BA, and Goldfine ID. Antioxidants in diabetic complications and insulin resistance. In: Diabetes: From Research to Diagnosis and Treatment, edited by Raz I, Skyler JS, and Shafrir E. London: Martin Dunitz, 2003, pp. 479-496.
    • (2003) Diabetes: From Research to Diagnosis and Treatment , pp. 479-496
    • Evans, J.L.1    Maddux, B.A.2    Goldfine, I.D.3
  • 29
    • 0034672599 scopus 로고    scopus 로고
    • Hyperinsulinemia: The missing link among oxidative stress and age-related diseases?
    • Facchini FS, Hau NW, Reaven GM, and Stoohs RA. Hyperinsulinemia: the missing link among oxidative stress and age-related diseases? Free Radic Biol Med 29: 1302-1306, 2000.
    • (2000) Free Radic Biol Med , vol.29 , pp. 1302-1306
    • Facchini, F.S.1    Hau, N.W.2    Reaven, G.M.3    Stoohs, R.A.4
  • 30
    • 0030296632 scopus 로고    scopus 로고
    • Structure and function of the protein tyrosine phosphatases
    • Fauman EB and Saper MA. Structure and function of the protein tyrosine phosphatases. Trends Biochem Sci 21: 413-417, 1996.
    • (1996) Trends Biochem Sci , vol.21 , pp. 413-417
    • Fauman, E.B.1    Saper, M.A.2
  • 31
    • 0037707406 scopus 로고    scopus 로고
    • Decreased total antioxidant status and increased oxidative stress in women with polycystic ovary syndrome may contribute to the risk of cardiovascular disease
    • Fenkci V, Fenkci S, Yilmazer M, and Serteser M. Decreased total antioxidant status and increased oxidative stress in women with polycystic ovary syndrome may contribute to the risk of cardiovascular disease. Fertil Steril 80: 123-127, 2003.
    • (2003) Fertil Steril , vol.80 , pp. 123-127
    • Fenkci, V.1    Fenkci, S.2    Yilmazer, M.3    Serteser, M.4
  • 32
    • 0042822019 scopus 로고    scopus 로고
    • The metabolic syndrome and antioxidant concentrations: Findings from the Third National Health and Nutrition Examination Survey
    • Ford ES, Mokdad AH, Giles WH, and Brown DW. The metabolic syndrome and antioxidant concentrations: findings from the Third National Health and Nutrition Examination Survey. Diabetes 52: 2346-2352, 2003.
    • (2003) Diabetes , vol.52 , pp. 2346-2352
    • Ford, E.S.1    Mokdad, A.H.2    Giles, W.H.3    Brown, D.W.4
  • 34
    • 0032411042 scopus 로고    scopus 로고
    • Roles of reactive oxygen species: Signaling and regulation of cellular functions
    • Gamaley IA and Klyubin IV. Roles of reactive oxygen species: signaling and regulation of cellular functions. Int Rev Cytol 188: 203-255, 1999.
    • (1999) Int Rev Cytol , vol.188 , pp. 203-255
    • Gamaley, I.A.1    Klyubin, I.V.2
  • 35
    • 0037073679 scopus 로고    scopus 로고
    • Serine phosphorylation of insulin receptor substrate 1 by inhibitor kappa B kinase complex
    • Gao Z, Hwang D, Bataille F, Lefevre M, York D, Quon MJ, and Ye J. Serine phosphorylation of insulin receptor substrate 1 by inhibitor kappa B kinase complex. J Biol Chem 277: 48115-48121, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 48115-48121
    • Gao, Z.1    Hwang, D.2    Bataille, F.3    Lefevre, M.4    York, D.5    Quon, M.J.6    Ye, J.7
  • 36
    • 0042591261 scopus 로고    scopus 로고
    • Aspirin inhibits serine phosphorylation of insulin receptor substrate 1 in tumor necrosis factor-treated cells through targeting multiple serine kinases
    • Gao Z, Zuberi A, Quon MJ, Dong Z, and Ye J. Aspirin inhibits serine phosphorylation of insulin receptor substrate 1 in tumor necrosis factor-treated cells through targeting multiple serine kinases. J Biol Chem 278: 24944-24950, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 24944-24950
    • Gao, Z.1    Zuberi, A.2    Quon, M.J.3    Dong, Z.4    Ye, J.5
  • 38
    • 0023392635 scopus 로고
    • The insulin receptor: Molecular biology and transmembrane signaling
    • Goldfine ID. The insulin receptor: molecular biology and transmembrane signaling. Endocr Rev 8: 235-255, 1987.
    • (1987) Endocr Rev , vol.8 , pp. 235-255
    • Goldfine, I.D.1
  • 39
    • 0035502381 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase 1B (PTP1B): A novel therapeutic target for type 2 diabetes mellitus, obesity, and related states of insulin resistance
    • Goldstein BJ. Protein-tyrosine phosphatase 1B (PTP1B): a novel therapeutic target for type 2 diabetes mellitus, obesity, and related states of insulin resistance. Curr Drug Targets Immune Endocr Metabol Disord 1: 265-275, 2001.
    • (2001) Curr Drug Targets Immune Endocr Metabol Disord , vol.1 , pp. 265-275
    • Goldstein, B.J.1
  • 40
    • 0022225151 scopus 로고
    • Intracellular mediators of insulin action
    • Gottschalk WK and Jarett L. Intracellular mediators of insulin action. Diabetes Metab Rev 1: 229-259, 1985.
    • (1985) Diabetes Metab Rev , vol.1 , pp. 229-259
    • Gottschalk, W.K.1    Jarett, L.2
  • 41
    • 1542284652 scopus 로고    scopus 로고
    • Modulation of human insulin receptor substrate-1 tyrosine phosphorylation by protein kinase Cδ
    • Greene MW, Morrice N, Garofalo RS, and Roth RA. Modulation of human insulin receptor substrate-1 tyrosine phosphorylation by protein kinase Cδ. Biochem J 378 (Pt 1): 105-116, 2004.
    • (2004) Biochem J , vol.378 , Issue.PART 1 , pp. 105-116
    • Greene, M.W.1    Morrice, N.2    Garofalo, R.S.3    Roth, R.A.4
  • 42
    • 0037424466 scopus 로고    scopus 로고
    • Modulation of insulin-stimulated degradation of human insulin receptor substrate-1 by serine 312 phosphorylation
    • Greene MW, Sakaue H, Wang L, Alessi DR, and Roth RA. Modulation of insulin-stimulated degradation of human insulin receptor substrate-1 by serine 312 phosphorylation. J Biol Chem 278: 8199-8211, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 8199-8211
    • Greene, M.W.1    Sakaue, H.2    Wang, L.3    Alessi, D.R.4    Roth, R.A.5
  • 43
  • 44
    • 0038712570 scopus 로고    scopus 로고
    • Hyperosmotic stress inhibits insulin receptor substrate-1 function by distinct mechanisms in 3T3-L1 adipocytes
    • Gual P, Gonzalez T, Gremeaux T, Barres R, Marchand-Brustel Y, and Tanti JF. Hyperosmotic stress inhibits insulin receptor substrate-1 function by distinct mechanisms in 3T3-L1 adipocytes. J Biol Chem 278: 26550-26557, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 26550-26557
    • Gual, P.1    Gonzalez, T.2    Gremeaux, T.3    Barres, R.4    Marchand-Brustel, Y.5    Tanti, J.F.6
  • 46
    • 0025847218 scopus 로고
    • Insulin resistance in normal rats infused with glucose for 72 h
    • Hager SR, Jochen AL, and Kalkhoff RK. Insulin resistance in normal rats infused with glucose for 72 h. Am J Physiol 260: E353-E362, 1991.
    • (1991) Am J Physiol , vol.260
    • Hager, S.R.1    Jochen, A.L.2    Kalkhoff, R.K.3
  • 48
    • 77049308856 scopus 로고
    • Aging: A theory based on free radical and radiation chemistry
    • Harman D. Aging: a theory based on free radical and radiation chemistry. J Gerontol 11: 298-300, 1956.
    • (1956) J Gerontol , vol.11 , pp. 298-300
    • Harman, D.1
  • 49
    • 0142213542 scopus 로고    scopus 로고
    • The free radical theory of aging
    • Harman D. The free radical theory of aging. Antioxid Redox Signal 5: 557-561, 2003.
    • (2003) Antioxid Redox Signal , vol.5 , pp. 557-561
    • Harman, D.1
  • 50
    • 0034463918 scopus 로고    scopus 로고
    • A rapamycin-sensitive pathway down-regulates insulin signaling via phosphorylation and proteasomal degradation of insulin receptor substrate-1
    • Haruta T, Uno T, Kawahara J, Takano A, Egawa K, Sharma PM, Olefsky JM, and Kobayashi M. A rapamycin-sensitive pathway down-regulates insulin signaling via phosphorylation and proteasomal degradation of insulin receptor substrate-1. Mol Endocrinol 14: 783-794, 2000.
    • (2000) Mol Endocrinol , vol.14 , pp. 783-794
    • Haruta, T.1    Uno, T.2    Kawahara, J.3    Takano, A.4    Egawa, K.5    Sharma, P.M.6    Olefsky, J.M.7    Kobayashi, M.8
  • 51
    • 0023442337 scopus 로고
    • Role of insulin receptor phosphorylation in the insulinomimetic effects of hydrogen peroxide
    • Hayes GR and Lockwood DH. Role of insulin receptor phosphorylation in the insulinomimetic effects of hydrogen peroxide. Proc Natl Acad Sci U S A 84: 8115-8119, 1987.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 8115-8119
    • Hayes, G.R.1    Lockwood, D.H.2
  • 52
    • 0037088604 scopus 로고    scopus 로고
    • Transactivation of ErbB2 and ErbB3 by tumor necrosis factor-alpha and anisomycin leads to impaired insulin signaling through serine/threonine phosphorylation of IRS proteins
    • Hemi R, Paz K, Wertheim N, Karasik A, Zick Y, and Kanety H. Transactivation of ErbB2 and ErbB3 by tumor necrosis factor-alpha and anisomycin leads to impaired insulin signaling through serine/threonine phosphorylation of IRS proteins. J Biol Chem 277: 8961-8969, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 8961-8969
    • Hemi, R.1    Paz, K.2    Wertheim, N.3    Karasik, A.4    Zick, Y.5    Kanety, H.6
  • 53
    • 0000429415 scopus 로고    scopus 로고
    • Oxidative stress and antioxidant treatment: Effects on muscle glucose transport in animal models of type 1 and type 2 diabetes
    • edited by Packer L, Rosen P, Tritschler HJ, and King GL. New York: Marcel Dekker
    • Henriksen EJ. Oxidative stress and antioxidant treatment: effects on muscle glucose transport in animal models of type 1 and type 2 diabetes. In: Antioxidants in Diabetes Management, edited by Packer L, Rosen P, Tritschler HJ, and King GL. New York: Marcel Dekker, 2000, pp. 303-317.
    • (2000) Antioxidants in Diabetes Management , pp. 303-317
    • Henriksen, E.J.1
  • 54
    • 0037391426 scopus 로고    scopus 로고
    • Exercise training and antioxidants: Relief from oxidative stress and insulin resistance
    • Henriksen EJ and Saengsirisuwan V. Exercise training and antioxidants: relief from oxidative stress and insulin resistance. Exerc Sport Sci Rev 31: 79-84, 2003.
    • (2003) Exerc Sport Sci Rev , vol.31 , pp. 79-84
    • Henriksen, E.J.1    Saengsirisuwan, V.2
  • 56
    • 0034129013 scopus 로고    scopus 로고
    • Improvement of endothelial function and insulin sensitivity with vitamin C in patients with coronary spastic angina: Possible role of reactive oxygen species
    • Hirashima O, Kawano H, Motoyama T, Hirai N, Ohgushi M, Kugiyama K, Ogawa H, and Yasue H. Improvement of endothelial function and insulin sensitivity with vitamin C in patients with coronary spastic angina: possible role of reactive oxygen species. J Am Coll Cardiol 35: 1860-1866, 2000.
    • (2000) J Am Coll Cardiol , vol.35 , pp. 1860-1866
    • Hirashima, O.1    Kawano, H.2    Motoyama, T.3    Hirai, N.4    Ohgushi, M.5    Kugiyama, K.6    Ogawa, H.7    Yasue, H.8
  • 61
    • 0033765672 scopus 로고    scopus 로고
    • High glucose level and free fatty acid stimulate reactive oxygen species production through protein kinase C-dependent activation of NAD(P)H oxidase in cultured vascular cells
    • Inoguchi T, Li P, Umeda F, Yu HY, Kakimoto M, Imamura M, Aoki T, Etoh T, Hashimoto T, Naruse M, Sano H, Utsumi H, and Nawata H. High glucose level and free fatty acid stimulate reactive oxygen species production through protein kinase C-dependent activation of NAD(P)H oxidase in cultured vascular cells. Diabetes 49: 1939-1945, 2000.
    • (2000) Diabetes , vol.49 , pp. 1939-1945
    • Inoguchi, T.1    Li, P.2    Umeda, F.3    Yu, H.Y.4    Kakimoto, M.5    Imamura, M.6    Aoki, T.7    Etoh, T.8    Hashimoto, T.9    Naruse, M.10    Sano, H.11    Utsumi, H.12    Nawata, H.13
  • 64
    • 0029978685 scopus 로고    scopus 로고
    • Improvement of insulin-stimulated glucose-disposal in type 2 diabetes after repeated patenteral administration of thioctic acid
    • Jacob S, Henriksen EJ, Tritschler HJ, Augustin HJ, and Dietze GJ. Improvement of insulin-stimulated glucose-disposal in type 2 diabetes after repeated patenteral administration of thioctic acid. Exp Clin Endocrinol Diabetes 104: 284-288, 1996.
    • (1996) Exp Clin Endocrinol Diabetes , vol.104 , pp. 284-288
    • Jacob, S.1    Henriksen, E.J.2    Tritschler, H.J.3    Augustin, H.J.4    Dietze, G.J.5
  • 65
    • 0032840875 scopus 로고    scopus 로고
    • Oral administration of RAC-alpha-lipoic acid modulates insulin sensitivity in patients with type 2 diabetes mellitus: A placebo-controlled pilot trial
    • Jacob S, Ruus P, Hermann R, Tritschler HJ, Maerker E, Renn W, Augustin HJ, Dietze GJ, and Rett K. Oral administration of RAC-alpha-lipoic acid modulates insulin sensitivity in patients with type 2 diabetes mellitus: a placebo-controlled pilot trial. Free Radic Biol Med 27: 309-314, 1999.
    • (1999) Free Radic Biol Med , vol.27 , pp. 309-314
    • Jacob, S.1    Ruus, P.2    Hermann, R.3    Tritschler, H.J.4    Maerker, E.5    Renn, W.6    Augustin, H.J.7    Dietze, G.J.8    Rett, K.9
  • 66
    • 0037414811 scopus 로고    scopus 로고
    • Salicylic acid reverses phorbol 12-myristate-13-acetate (PMA)- and tumor necrosis factor alpha (TNFalpha)-induced insulin receptor substrate 1 (IRS1) serine 307 phosphorylation and insulin resistance in human embryonic kidney 293 (HEK293) cells
    • Jiang G, Dallas-Yang Q, Liu F, Moller DE, and Zhang BB. Salicylic acid reverses phorbol 12-myristate-13-acetate (PMA)- and tumor necrosis factor alpha (TNFalpha)-induced insulin receptor substrate 1 (IRS1) serine 307 phosphorylation and insulin resistance in human embryonic kidney 293 (HEK293) cells. J Biol Chem 278: 180-186, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 180-186
    • Jiang, G.1    Dallas-Yang, Q.2    Liu, F.3    Moller, D.E.4    Zhang, B.B.5
  • 67
    • 0020360817 scopus 로고
    • Insulin stimulation of phosphorylation of the beta subunit of the insulin receptor. Formation of both phosphoserine and phosphotyrosine
    • Kasuga M, Zick Y, Blith DL, Karlsson FA, Haring HU, and Kahn CR. Insulin stimulation of phosphorylation of the beta subunit of the insulin receptor. Formation of both phosphoserine and phosphotyrosine. J Biol Chem 257: 9891-9894, 1982.
    • (1982) J Biol Chem , vol.257 , pp. 9891-9894
    • Kasuga, M.1    Zick, Y.2    Blith, D.L.3    Karlsson, F.A.4    Haring, H.U.5    Kahn, C.R.6
  • 68
    • 0020046655 scopus 로고
    • Insulin stimulates tyrosine phosphorylation of the insulin receptor in a cell-free system
    • Kasuga M, Zick Y, Blithe DL, Crettaz M, and Kahn CR. Insulin stimulates tyrosine phosphorylation of the insulin receptor in a cell-free system. Nature 298: 667-669, 1982.
    • (1982) Nature , vol.298 , pp. 667-669
    • Kasuga, M.1    Zick, Y.2    Blithe, D.L.3    Crettaz, M.4    Kahn, C.R.5
  • 69
    • 0015172327 scopus 로고
    • Effects of phenazine methosulfate on glucose metabolism in rat adipose tissue
    • Katz J and Wals PA. Effects of phenazine methosulfate on glucose metabolism in rat adipose tissue. Arch Biochem Biophys 147: 405-418, 1971.
    • (1971) Arch Biochem Biophys , vol.147 , pp. 405-418
    • Katz, J.1    Wals, P.A.2
  • 70
    • 0031809427 scopus 로고    scopus 로고
    • Protein kinase C isoforms alpha, delta and theta require insulin receptor substrate-1 to inhibit the tyrosine kinase activity of the insulin receptor in human kidney embryonic cells (HEK 293 cells)
    • Kellerer M, Mushack J, Seffer E, Mischak H, Ullrich A, and Haring HU. Protein kinase C isoforms alpha, delta and theta require insulin receptor substrate-1 to inhibit the tyrosine kinase activity of the insulin receptor in human kidney embryonic cells (HEK 293 cells). Diabetologia 41: 833-838, 1998.
    • (1998) Diabetologia , vol.41 , pp. 833-838
    • Kellerer, M.1    Mushack, J.2    Seffer, E.3    Mischak, H.4    Ullrich, A.5    Haring, H.U.6
  • 71
    • 0029810614 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase 1B is a negative regulator of insulin- and insulin-like growth factor-I-stimulated signaling
    • Kenner KA, Anyanwu E, Olefsky JM, and Kusari J. Protein-tyrosine phosphatase 1B is a negative regulator of insulin- and insulin-like growth factor-I-stimulated signaling. J Biol Chem 271: 19810-19816, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 19810-19816
    • Kenner, K.A.1    Anyanwu, E.2    Olefsky, J.M.3    Kusari, J.4
  • 73
    • 0023028522 scopus 로고
    • Insulin-dependent phosphorylation of the insulin receptor-protein kinase and activation of glucose transport in 3T3-L1 adipocytes
    • Kohanski RA, Frost SC, and Lane MD. Insulin-dependent phosphorylation of the insulin receptor-protein kinase and activation of glucose transport in 3T3-L1 adipocytes. J Biol Chem 261: 12272-12281, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 12272-12281
    • Kohanski, R.A.1    Frost, S.C.2    Lane, M.D.3
  • 74
    • 0034987312 scopus 로고    scopus 로고
    • The antihyperglycemic drug alpha-lipoic acid stimulates glucose uptake via both GLUT4 translocation and GLUT4 activation: Potential role of p38 mitogen-activated protein kinase in GLUT4 activation
    • Konrad D, Somwar R, Sweeney G, Yaworsky K, Hayashi M, Ramlal T, and Klip A. The antihyperglycemic drug alpha-lipoic acid stimulates glucose uptake via both GLUT4 translocation and GLUT4 activation: potential role of p38 mitogen-activated protein kinase in GLUT4 activation. Diabetes 50: 1464-1471, 2001.
    • (2001) Diabetes , vol.50 , pp. 1464-1471
    • Konrad, D.1    Somwar, R.2    Sweeney, G.3    Yaworsky, K.4    Hayashi, M.5    Ramlal, T.6    Klip, A.7
  • 75
    • 0032904416 scopus 로고    scopus 로고
    • Alpha-lipoic acid treatment decreases serum lactate and pyruvate concentrations and improves glucose effectiveness in lean and obese patients with type 2 diabetes
    • Konrad T, Vicini P, Kusterer K, Hoflich A, Assadkhani A, Bohles HJ, Sewell A, Tritschler HJ, Cobelli C, and Usadel KH. Alpha-lipoic acid treatment decreases serum lactate and pyruvate concentrations and improves glucose effectiveness in lean and obese patients with type 2 diabetes. Diabetes Care 22: 280-287, 1999.
    • (1999) Diabetes Care , vol.22 , pp. 280-287
    • Konrad, T.1    Vicini, P.2    Kusterer, K.3    Hoflich, A.4    Assadkhani, A.5    Bohles, H.J.6    Sewell, A.7    Tritschler, H.J.8    Cobelli, C.9    Usadel, K.H.10
  • 76
    • 0026572097 scopus 로고
    • 2-generating system that is activated by insulin via a mechanism bypassing the receptor kinase
    • 2-generating system that is activated by insulin via a mechanism bypassing the receptor kinase. J Clin Invest 89: 1006-1013, 1992.
    • (1992) J Clin Invest , vol.89 , pp. 1006-1013
    • Krieger-Brauer, H.I.1    Kather, H.2
  • 77
    • 0030894971 scopus 로고    scopus 로고
    • 2 generation in human adipocyte plasma membranes is mediated by Galphai2
    • 2 generation in human adipocyte plasma membranes is mediated by Galphai2. J Biol Chem 272: 10135-10143, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 10135-10143
    • Krieger-Brauer, H.I.1    Medda, P.K.2    Kather, H.3
  • 78
    • 0029744885 scopus 로고    scopus 로고
    • Sounding the alarm: Protein kinase cascades activated by stress and inflammation
    • Kyriakis JM and Avruch J. Sounding the alarm: protein kinase cascades activated by stress and inflammation. J Biol Chem 271: 24313-24316, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 24313-24316
    • Kyriakis, J.M.1    Avruch, J.2
  • 79
    • 0035066383 scopus 로고    scopus 로고
    • Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation
    • Kyriakis JM and Avruch J. Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation. Physiol Rev 81: 807-869, 2001.
    • (2001) Physiol Rev , vol.81 , pp. 807-869
    • Kyriakis, J.M.1    Avruch, J.2
  • 80
    • 0031036917 scopus 로고    scopus 로고
    • An essential role for free radicals and derived species in signal transduction
    • Lander HM. An essential role for free radicals and derived species in signal transduction. FASEB J 11: 118-124, 1997.
    • (1997) FASEB J , vol.11 , pp. 118-124
    • Lander, H.M.1
  • 82
    • 0017853459 scopus 로고
    • Activation of glycogen synthase in rat adipocytes by insulin and glucose involves increased glucose transport and phosphorylation
    • Lawrence JC Jr and Larner J. Activation of glycogen synthase in rat adipocytes by insulin and glucose involves increased glucose transport and phosphorylation. J Biol Chem 253: 2104-2113, 1978.
    • (1978) J Biol Chem , vol.253 , pp. 2104-2113
    • Lawrence Jr., J.C.1    Larner, J.2
  • 83
    • 33745359912 scopus 로고    scopus 로고
    • Specific adaptations in muscle and adipose tissue in response to chronic systemic glucose oversupply in rats
    • Laybutt DR, Chisholm DJ, and Kraegen EW. Specific adaptations in muscle and adipose tissue in response to chronic systemic glucose oversupply in rats. Am J Physiol Endocrinol Metab 36: E1-E9, 1997.
    • (1997) Am J Physiol Endocrinol Metab , vol.36
    • Laybutt, D.R.1    Chisholm, D.J.2    Kraegen, E.W.3
  • 84
    • 0033399406 scopus 로고    scopus 로고
    • Muscle lipid accumulation and protein kinase C activation in the insulin-resistant chronically glucose-infused rat
    • Laybutt DR, Schmitz-Peiffer C, Saha AK, Ruderman NB, Biden TJ, and Kraegen EW. Muscle lipid accumulation and protein kinase C activation in the insulin-resistant chronically glucose-infused rat. Am J Physiol 277: E1070-E1076, 1999.
    • (1999) Am J Physiol , vol.277
    • Laybutt, D.R.1    Schmitz-Peiffer, C.2    Saha, A.K.3    Ruderman, N.B.4    Biden, T.J.5    Kraegen, E.W.6
  • 85
    • 0035177601 scopus 로고    scopus 로고
    • Oxidative stress markers in Korean subjects with insulin resistance syndrome
    • Lee KU. Oxidative stress markers in Korean subjects with insulin resistance syndrome. Diabetes Res Clin Pract 54 Suppl 2: S29-S33, 2001.
    • (2001) Diabetes Res Clin Pract , vol.54 , Issue.SUPPL. 2
    • Lee, K.U.1
  • 86
    • 0037474274 scopus 로고    scopus 로고
    • c-Jun N-terminal kinase (JNK) mediates feedback inhibition of the insulin signaling cascade
    • Lee YH, Giraud J, Davis RJ, and White MF. c-Jun N-terminal kinase (JNK) mediates feedback inhibition of the insulin signaling cascade. J Biol Chem 278: 2896-2902, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 2896-2902
    • Lee, Y.H.1    Giraud, J.2    Davis, R.J.3    White, M.F.4
  • 87
    • 0033515459 scopus 로고    scopus 로고
    • Modulation of insulin receptor substrate-1 tyrosine phosphorylation by an Akt/phosphatidylinositol 3-kinase pathway
    • Li J, DeFea K, and Roth RA. Modulation of insulin receptor substrate-1 tyrosine phosphorylation by an Akt/phosphatidylinositol 3-kinase pathway. J Biol Chem 274: 9351-9356, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 9351-9356
    • Li, J.1    DeFea, K.2    Roth, R.A.3
  • 89
    • 0018243636 scopus 로고
    • Studies of glucose transport system of fat cells: Effects of insulin and insulin mimickers
    • Livingston JN, Amatruda JM, and Lockwood DH. Studies of glucose transport system of fat cells: effects of insulin and insulin mimickers. Am J Physiol 234: E484-E488, 1978.
    • (1978) Am J Physiol , vol.234
    • Livingston, J.N.1    Amatruda, J.M.2    Lockwood, D.H.3
  • 90
    • 0035140346 scopus 로고    scopus 로고
    • Protection against oxidative stress-induced insulin resistance in rat L6 muscle cells by micromolar concentrations of α-lipoic acid
    • Maddux BA, See W, Lawrence JC Jr, Goldine AL, Goldfine ID, and Evans JL. Protection against oxidative stress-induced insulin resistance in rat L6 muscle cells by micromolar concentrations of α-lipoic acid. Diabetes 50: 404-410, 2001.
    • (2001) Diabetes , vol.50 , pp. 404-410
    • Maddux, B.A.1    See, W.2    Lawrence Jr., J.C.3    Goldine, A.L.4    Goldfine, I.D.5    Evans, J.L.6
  • 91
    • 0035966052 scopus 로고    scopus 로고
    • Hydrogen peroxide generated during cellular insulin stimulation is integral to activation of the distal insulin signaling cascade in 3T3-L1 adipocytes
    • Mahadev K, Wu X, Zilbering A, Zhu L, Lawrence JT, and Goldstein BJ. Hydrogen peroxide generated during cellular insulin stimulation is integral to activation of the distal insulin signaling cascade in 3T3-L1 adipocytes. J Biol Chem 276: 48662-48669, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 48662-48669
    • Mahadev, K.1    Wu, X.2    Zilbering, A.3    Zhu, L.4    Lawrence, J.T.5    Goldstein, B.J.6
  • 92
    • 0035877633 scopus 로고    scopus 로고
    • Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade
    • Mahadev K, Zilbering A, Zhu L, and Goldstein BJ. Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade. J Biol Chem 276: 21938-21942, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 21938-21942
    • Mahadev, K.1    Zilbering, A.2    Zhu, L.3    Goldstein, B.J.4
  • 95
    • 0018382583 scopus 로고
    • Insulin-stimulated intracellular hydrogen peroxide production in rat epididymal fat cells
    • May JM and de Haen C. Insulin-stimulated intracellular hydrogen peroxide production in rat epididymal fat cells. J Biol Chem 254: 2214-2220, 1979.
    • (1979) J Biol Chem , vol.254 , pp. 2214-2220
    • May, J.M.1    De Haen, C.2
  • 96
    • 0018716904 scopus 로고
    • The insulin-like effect of hydrogen peroxide on pathways of lipid synthesis in rat adipocytes
    • May JM and de Haen C. The insulin-like effect of hydrogen peroxide on pathways of lipid synthesis in rat adipocytes. J Biol Chem 254: 9017-9021, 1979.
    • (1979) J Biol Chem , vol.254 , pp. 9017-9021
    • May, J.M.1    De Haen, C.2
  • 98
    • 0036092239 scopus 로고    scopus 로고
    • Banting lecture 2001: Dysregulation of fatty acid metabolism in the etiology of type 2 diabetes
    • McGarry JD. Banting lecture 2001: dysregulation of fatty acid metabolism in the etiology of type 2 diabetes. Diabetes 51: 7-18, 2002.
    • (2002) Diabetes , vol.51 , pp. 7-18
    • McGarry, J.D.1
  • 99
    • 0028007581 scopus 로고
    • Hormone- and growth factor-stimulated NADH oxidase
    • Morre DJ. Hormone- and growth factor-stimulated NADH oxidase. J Bioenerg Biomembr 26: 421-433, 1994.
    • (1994) J Bioenerg Biomembr , vol.26 , pp. 421-433
    • Morre, D.J.1
  • 100
    • 0030025047 scopus 로고    scopus 로고
    • Insulin action impaired by deficiency of the G-protein subunit G ialpha2
    • Moxham CM and Malbon CC. Insulin action impaired by deficiency of the G-protein subunit G ialpha2. Nature 379: 840-844, 1996.
    • (1996) Nature , vol.379 , pp. 840-844
    • Moxham, C.M.1    Malbon, C.C.2
  • 101
    • 0017671212 scopus 로고
    • Reduced nicotinamide adenine dinucleotide phosphate oxidase in adipocyte plasma membrane and its activation by insulin. Possible role in the hormone's effects on adenylate cyclase and the hexose monophosphate shunt
    • Mukherjee SP and Lynn WS. Reduced nicotinamide adenine dinucleotide phosphate oxidase in adipocyte plasma membrane and its activation by insulin. Possible role in the hormone's effects on adenylate cyclase and the hexose monophosphate shunt. Arch Biochem Biophys 184: 69-76, 1977.
    • (1977) Arch Biochem Biophys , vol.184 , pp. 69-76
    • Mukherjee, S.P.1    Lynn, W.S.2
  • 102
    • 0020051165 scopus 로고
    • Stimulation of pyruvate dehydrogenase activity in adipocytes by oxytocin: Evidence for mediation of the insulin-like effect by endogenous hydrogen peroxide independent of glucose transport
    • Mukherjee SP and Mukherjee C. Stimulation of pyruvate dehydrogenase activity in adipocytes by oxytocin: evidence for mediation of the insulin-like effect by endogenous hydrogen peroxide independent of glucose transport. Arch Biochem Biophys 214: 211-222, 1982.
    • (1982) Arch Biochem Biophys , vol.214 , pp. 211-222
    • Mukherjee, S.P.1    Mukherjee, C.2
  • 103
    • 0033826520 scopus 로고    scopus 로고
    • Role for mitochondrial oxidants as regulators of cellular metabolism
    • Nemoto S, Takeda K, Yu ZX, Ferrans VJ, and Finkel T. Role for mitochondrial oxidants as regulators of cellular metabolism. Mol Cell Biol 20: 7311-7318, 2000.
    • (2000) Mol Cell Biol , vol.20 , pp. 7311-7318
    • Nemoto, S.1    Takeda, K.2    Yu, Z.X.3    Ferrans, V.J.4    Finkel, T.5
  • 104
    • 0034097798 scopus 로고    scopus 로고
    • MAP kinase pathways activated by stress: The p38 MAPK pathway
    • Obata T, Brown GE, and Yaffe MB. MAP kinase pathways activated by stress: the p38 MAPK pathway. Crit Care Med 28: N67-N77, 2000.
    • (2000) Crit Care Med , vol.28
    • Obata, T.1    Brown, G.E.2    Yaffe, M.B.3
  • 105
    • 0030042738 scopus 로고    scopus 로고
    • Oxidative stress and insulin action: Is there a relationship?
    • Paolisso G and Giugliano D. Oxidative stress and insulin action: is there a relationship? Diabetologia 39: 357-363, 1996.
    • (1996) Diabetologia , vol.39 , pp. 357-363
    • Paolisso, G.1    Giugliano, D.2
  • 108
    • 0032729731 scopus 로고    scopus 로고
    • Primary and secondary prevention of atheroslcerosis: Is there a role for antioxidants?
    • Paolisso G, Esposito R, D'Alessio MA, and Barbieri M. Primary and secondary prevention of atheroslcerosis: is there a role for antioxidants? Diabetes Metab 25: 298-306, 1999.
    • (1999) Diabetes Metab , vol.25 , pp. 298-306
    • Paolisso, G.1    Esposito, R.2    D'Alessio, M.A.3    Barbieri, M.4
  • 109
    • 0347926092 scopus 로고    scopus 로고
    • Insulin regulation of hepatic insulin-like growth factor-binding protein-1 (IGFBP-1) gene expression and mammalian target of rapamycin (mTOR) signalling is impaired by the presence of hydrogen peroxide
    • Patel S, Van Der Kaay J, and Sutherland C. Insulin regulation of hepatic insulin-like growth factor-binding protein-1 (IGFBP-1) gene expression and mammalian target of rapamycin (mTOR) signalling is impaired by the presence of hydrogen peroxide. Biochem J 365: 537-545, 2002.
    • (2002) Biochem J , vol.365 , pp. 537-545
    • Patel, S.1    Van Der Kaay, J.2    Sutherland, C.3
  • 110
    • 0029924172 scopus 로고    scopus 로고
    • Interaction between the insulin receptor and its downstream effectors - Use of individually expressed receptor domains for structure function analysis
    • Paz K, Voliovitch H, Hadari YR, Roberts CT, LeRoith D, and Zick Y. Interaction between the insulin receptor and its downstream effectors - use of individually expressed receptor domains for structure function analysis. J Biol Chem 271: 6998-7003, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 6998-7003
    • Paz, K.1    Voliovitch, H.2    Hadari, Y.R.3    Roberts, C.T.4    LeRoith, D.5    Zick, Y.6
  • 111
    • 0030669392 scopus 로고    scopus 로고
    • A molecular basis for insulin resistance. Elevated serine/threonine phosphorylation of IRS-1 and IRS-2 inhibits their binding to the juxtamembrane region of the insulin receptor and impairs their ability to undergo insulin-induced tyrosine phosphorylation
    • Paz K, Hemi R, LeRoith D, Karasik A, Elhanany E, Kanety H, and Zick Y. A molecular basis for insulin resistance. Elevated serine/threonine phosphorylation of IRS-1 and IRS-2 inhibits their binding to the juxtamembrane region of the insulin receptor and impairs their ability to undergo insulin-induced tyrosine phosphorylation. J Biol Chem 272: 29911-29918, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 29911-29918
    • Paz, K.1    Hemi, R.2    LeRoith, D.3    Karasik, A.4    Elhanany, E.5    Kanety, H.6    Zick, Y.7
  • 112
    • 0035155272 scopus 로고    scopus 로고
    • Serine/ threonine phosphorylation of IRS-1 triggers its degradation: Possible regulation by tyrosine phosphorylation
    • Pederson TM, Kramer DL, and Rondinone CM. Serine/ threonine phosphorylation of IRS-1 triggers its degradation: possible regulation by tyrosine phosphorylation. Diabetes 50: 24-31, 2001.
    • (2001) Diabetes , vol.50 , pp. 24-31
    • Pederson, T.M.1    Kramer, D.L.2    Rondinone, C.M.3
  • 113
    • 0037026745 scopus 로고    scopus 로고
    • Pathogenesis of skeletal muscle insulin resistance in type 2 diabetes mellitus
    • Petersen KF and Shulman GI. Pathogenesis of skeletal muscle insulin resistance in type 2 diabetes mellitus. Am J Cardiol 90: 11G-18G, 2002.
    • (2002) Am J Cardiol , vol.90
    • Petersen, K.F.1    Shulman, G.I.2
  • 114
    • 0038691609 scopus 로고    scopus 로고
    • IRSl degradation and increased serine phosphorylation cannot predict the degree of metabolic insulin resistance induced by oxidative stress
    • Potashnik R, Bloch-Damti A, Bashan N, and Rudich A. IRSl degradation and increased serine phosphorylation cannot predict the degree of metabolic insulin resistance induced by oxidative stress. Diabetologia 46: 639-648, 2003.
    • (2003) Diabetologia , vol.46 , pp. 639-648
    • Potashnik, R.1    Bloch-Damti, A.2    Bashan, N.3    Rudich, A.4
  • 115
    • 0033537931 scopus 로고    scopus 로고
    • Identification of enhanced serine kinase activity in insulin resistance
    • Qiao LY, Goldberg JL, Russell JC, and Sun XJ. Identification of enhanced serine kinase activity in insulin resistance. J Biol Chem 274: 10625-10632, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 10625-10632
    • Qiao, L.Y.1    Goldberg, J.L.2    Russell, J.C.3    Sun, X.J.4
  • 116
    • 0037135547 scopus 로고    scopus 로고
    • In vivo phosphorylation of insulin receptor substrate 1 at serine 789 by a novel serine kinase in insulin-resistant rodents
    • Qiao LY, Zhande R, Jetton TL, Zhou G, and Sun XJ. In vivo phosphorylation of insulin receptor substrate 1 at serine 789 by a novel serine kinase in insulin-resistant rodents. J Biol Chem 277: 26530-26539, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 26530-26539
    • Qiao, L.Y.1    Zhande, R.2    Jetton, T.L.3    Zhou, G.4    Sun, X.J.5
  • 117
    • 0001952829 scopus 로고    scopus 로고
    • Redox signaling: Hydrogen peroxide as intracellular messenger
    • Rhee SG. Redox signaling: hydrogen peroxide as intracellular messenger. Exp Mol Med 31: 53-59, 1999.
    • (1999) Exp Mol Med , vol.31 , pp. 53-59
    • Rhee, S.G.1
  • 118
    • 0024294407 scopus 로고
    • Phosphatidylinositol-glycan anchors of membrane proteins: Potential precursors of insulin mediators
    • Romero G, Luttrell L, Rogol A, Zeller K, Hewlett E, and Larner J. Phosphatidylinositol-glycan anchors of membrane proteins: potential precursors of insulin mediators. Science 240: 509-511, 1988.
    • (1988) Science , vol.240 , pp. 509-511
    • Romero, G.1    Luttrell, L.2    Rogol, A.3    Zeller, K.4    Hewlett, E.5    Larner, J.6
  • 119
    • 0023188325 scopus 로고
    • After insulin binds
    • Rosen OM. After insulin binds. Science 237: 1452-1458, 1988.
    • (1988) Science , vol.237 , pp. 1452-1458
    • Rosen, O.M.1
  • 121
    • 0034939115 scopus 로고    scopus 로고
    • The role of oxidative stress in the onset and progression of diabetes and its complications: A summary of a Congress Series sponsored by UNESCO-MCBN, the American Diabetes Association, and the German Diabetes Society
    • Rosen R, Nawroth PP, King G, Moller W, Tritschler HJ, and Packer L. The role of oxidative stress in the onset and progression of diabetes and its complications: a summary of a Congress Series sponsored by UNESCO-MCBN, the American Diabetes Association, and the German Diabetes Society. Diabetes Metab Res Rev 17: 189-212, 2001.
    • (2001) Diabetes Metab Res Rev , vol.17 , pp. 189-212
    • Rosen, R.1    Nawroth, P.P.2    King, G.3    Moller, W.4    Tritschler, H.J.5    Packer, L.6
  • 122
    • 0029582922 scopus 로고
    • Glucose toxicity - The implications of hyperglycemia in the pathophysiology of diabetes mellitus
    • Rossetti L. Glucose toxicity - the implications of hyperglycemia in the pathophysiology of diabetes mellitus. Clin Invest Med 18: 255-260, 1995.
    • (1995) Clin Invest Med , vol.18 , pp. 255-260
    • Rossetti, L.1
  • 123
    • 2442520561 scopus 로고    scopus 로고
    • Glucose toxicity: Effect of chronic hyperglycemia on insulin action
    • edited by LeRoith D, Taylor ST, and Olefsky JM. Philadelphia: Lippincott Williams & Wilkins
    • Rossetti L. Glucose toxicity: effect of chronic hyperglycemia on insulin action. In: Diabetes Mellitus: A Fundamental and Clinical Text, edited by LeRoith D, Taylor ST, and Olefsky JM. Philadelphia: Lippincott Williams & Wilkins, 2000, pp. 641-651.
    • (2000) Diabetes Mellitus: A Fundamental and Clinical Text , pp. 641-651
    • Rossetti, L.1
  • 124
    • 0034610759 scopus 로고    scopus 로고
    • Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IkappaB kinase
    • Rossi A, Kapahi P, Natoli G, Takahashi T, Chen Y, Karin M, and Santoro MG. Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IkappaB kinase. Nature 403: 103-108, 2000.
    • (2000) Nature , vol.403 , pp. 103-108
    • Rossi, A.1    Kapahi, P.2    Natoli, G.3    Takahashi, T.4    Chen, Y.5    Karin, M.6    Santoro, M.G.7
  • 125
    • 0020702372 scopus 로고
    • Insulin receptor: Evidence that it is aprotein kinase
    • Roth RA and Cassell DJ. Insulin receptor: evidence that it is aprotein kinase. Science 219: 299-301, 1983.
    • (1983) Science , vol.219 , pp. 299-301
    • Roth, R.A.1    Cassell, D.J.2
  • 126
    • 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, and Bashan N. Prolonged oxidative stress impairs insulin-induced GLUT4 translocation in 3T3-L1 adipocytes. Diabetes 41: 1562-1569, 1998.
    • (1998) Diabetes , vol.41 , pp. 1562-1569
    • Rudich, A.1    Tirosh, A.2    Potashnik, R.3    Hemi, R.4    Kanety, H.5    Bashan, N.6
  • 127
    • 0032799487 scopus 로고    scopus 로고
    • Lipoic acid protects against oxidative stress induced impairment in insulin stimulation of protein kinase B and glucose transport in 3T3-L1 adipocytes
    • Rudich A, Tirosh A, Potashnik R, Khamaisi M, and Bashan N. Lipoic acid protects against oxidative stress induced impairment in insulin stimulation of protein kinase B and glucose transport in 3T3-L1 adipocytes. Diabetologia 42: 949-957, 1999.
    • (1999) Diabetologia , vol.42 , pp. 949-957
    • Rudich, A.1    Tirosh, A.2    Potashnik, R.3    Khamaisi, M.4    Bashan, N.5
  • 128
  • 129
    • 0022548269 scopus 로고
    • Insulin-stimulated hydrolysis of a novel glycolipid generates modulators of cAMP phosphodiesterase
    • Saltiel AR, Fox JA, Sherline P, and Cuatrecasas P. Insulin-stimulated hydrolysis of a novel glycolipid generates modulators of cAMP phosphodiesterase. Science 233: 967-972, 1986.
    • (1986) Science , vol.233 , pp. 967-972
    • Saltiel, A.R.1    Fox, J.A.2    Sherline, P.3    Cuatrecasas, P.4
  • 131
    • 0036065047 scopus 로고    scopus 로고
    • G(q/11) is involved in insulin-stimulated inositol phosphoglycan putative mediator generation in rat liver membranes: Co-localization of G(q/11) with the insulin receptor in membrane vesicles
    • Sleight S, Wilson BA, Heimark DB, and Larner J. G(q/11) is involved in insulin-stimulated inositol phosphoglycan putative mediator generation in rat liver membranes: co-localization of G(q/11) with the insulin receptor in membrane vesicles. Biochem Biophys Res Commun 295: 561-569, 2002.
    • (2002) Biochem Biophys Res Commun , vol.295 , pp. 561-569
    • Sleight, S.1    Wilson, B.A.2    Heimark, D.B.3    Larner, J.4
  • 132
    • 0038692862 scopus 로고    scopus 로고
    • A promoter genotype and oxidative stress potentially link resistin to human insulin resistance
    • Smith SR, Bai F, Charbonneau C, Janderova L, and Argyropoulos G. A promoter genotype and oxidative stress potentially link resistin to human insulin resistance. Diabetes 52: 1611-1618, 2003.
    • (2003) Diabetes , vol.52 , pp. 1611-1618
    • Smith, S.R.1    Bai, F.2    Charbonneau, C.3    Janderova, L.4    Argyropoulos, G.5
  • 133
    • 0017592986 scopus 로고
    • Involvement of membrane sulfhydryls in the activation and maintenance of nutrient transport in chick embryo fibroblasts
    • Smith-Johannsen H, Perdue JF, Ramjeesingh M, and Kahlenberg A. Involvement of membrane sulfhydryls in the activation and maintenance of nutrient transport in chick embryo fibroblasts. J Supramol Struct 7: 37-48, 1977.
    • (1977) J Supramol Struct , vol.7 , pp. 37-48
    • Smith-Johannsen, H.1    Perdue, J.F.2    Ramjeesingh, M.3    Kahlenberg, A.4
  • 135
    • 0033537853 scopus 로고    scopus 로고
    • An inhibitor of p38 mitogen-activated protein kinase prevents insulin-stimulated glucose transport but not glucose transporter translocation in 3T3-L1 adipocytes and L6 myotubes
    • Sweeney G, Somwar R, Ramlal T, Volchuk A, Ueyama A, and Klip A. An inhibitor of p38 mitogen-activated protein kinase prevents insulin-stimulated glucose transport but not glucose transporter translocation in 3T3-L1 adipocytes and L6 myotubes. J Biol Chem 274: 10071-10078, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 10071-10078
    • Sweeney, G.1    Somwar, R.2    Ramlal, T.3    Volchuk, A.4    Ueyama, A.5    Klip, A.6
  • 136
    • 0034751858 scopus 로고    scopus 로고
    • Serine phosphorylation of insulin receptor substrate-1: A novel target for the reversal of insulin resistance
    • Sykiotis GP and Papavassiliou AG. Serine phosphorylation of insulin receptor substrate-1: a novel target for the reversal of insulin resistance. Mol Endocrinol 15: 1864-1869, 2001.
    • (2001) Mol Endocrinol , vol.15 , pp. 1864-1869
    • Sykiotis, G.P.1    Papavassiliou, A.G.2
  • 137
    • 0033567291 scopus 로고    scopus 로고
    • The stress-activated protein kinase pathways
    • Tibbies LA and Woodgett JR. The stress-activated protein kinase pathways. Cell Mol Life Sci 55: 1230-1254, 1999.
    • (1999) Cell Mol Life Sci , vol.55 , pp. 1230-1254
    • Tibbies, L.A.1    Woodgett, J.R.2
  • 138
    • 0033537830 scopus 로고    scopus 로고
    • Oxidative stress disrupts insulin-induced cellular redistribution of insulin receptor substrate-1 and phosphatidylinositol 3-kinase in 3T3-L1 adipocytes-a putative cellular mechanism for impaired protein kinase B activation and GLUT4 translocation
    • Tirosh A, Potashnik R, Bashan N, and Rudich A. Oxidative stress disrupts insulin-induced cellular redistribution of insulin receptor substrate-1 and phosphatidylinositol 3-kinase in 3T3-L1 adipocytes-a putative cellular mechanism for impaired protein kinase B activation and GLUT4 translocation. J Biol Chem 274: 10595-10602, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 10595-10602
    • Tirosh, A.1    Potashnik, R.2    Bashan, N.3    Rudich, A.4
  • 139
    • 0035340017 scopus 로고    scopus 로고
    • Oxidative stress impairs insulin but not platelet-derived growth factor signalling in 3T3-L1 adipocytes
    • Tirosh A, Rudich A, Potashnik R, and Bashan N. Oxidative stress impairs insulin but not platelet-derived growth factor signalling in 3T3-L1 adipocytes. Biochem J 355: 757-763, 2001.
    • (2001) Biochem J , vol.355 , pp. 757-763
    • Tirosh, A.1    Rudich, A.2    Potashnik, R.3    Bashan, N.4
  • 140
    • 0345275811 scopus 로고    scopus 로고
    • Elevation of free fatty acids induces inflammation and impairs vascular reactivity in healthy subjects
    • Tripathy D, Mohanty P, Dhindsa S, Syed T, Ghamm H, Aljada A, and Dandona P. Elevation of free fatty acids induces inflammation and impairs vascular reactivity in healthy subjects. Diabetes 52: 2882-2887, 2003.
    • (2003) Diabetes , vol.52 , pp. 2882-2887
    • Tripathy, D.1    Mohanty, P.2    Dhindsa, S.3    Syed, T.4    Ghamm, H.5    Aljada, A.6    Dandona, P.7
  • 141
    • 0021961644 scopus 로고
    • Hyperglycaemia as an inducer as well as a consequence of impaired islet cell function and insulin resistance: Implications for the management of diabetes
    • Unger RH and Grundy S. Hyperglycaemia as an inducer as well as a consequence of impaired islet cell function and insulin resistance: implications for the management of diabetes. Diabetologia 28: 119-121, 1985.
    • (1985) Diabetologia , vol.28 , pp. 119-121
    • Unger, R.H.1    Grundy, S.2
  • 143
    • 0038749600 scopus 로고    scopus 로고
    • Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B
    • van Montfort RL, Congreve M, Tisi D, Carr R, and Jhoti H. Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature 423: 773-777, 2003.
    • (2003) Nature , vol.423 , pp. 773-777
    • Van Montfort, R.L.1    Congreve, M.2    Tisi, D.3    Carr, R.4    Jhoti, H.5
  • 144
    • 0033994409 scopus 로고    scopus 로고
    • Radicals and oxidative stress in diabetes
    • West IC. Radicals and oxidative stress in diabetes. Diabet Med 17: 171-180, 2000.
    • (2000) Diabet Med , vol.17 , pp. 171-180
    • West, I.C.1
  • 145
    • 0036710280 scopus 로고    scopus 로고
    • 1RS proteins and the common path to diabetes
    • White MF. 1RS proteins and the common path to diabetes. Am J Physiol Endocrinol Metab 283: E413-E422, 2002.
    • (2002) Am J Physiol Endocrinol Metab , vol.283
    • White, M.F.1
  • 146
    • 0029903001 scopus 로고    scopus 로고
    • Are insulin resistance and atheroslerosis the consequences of oxidative stress?
    • Wittmann I and Nagy J. Are insulin resistance and atheroslerosis the consequences of oxidative stress? Diabetologia 39: 1002-1003, 1996.
    • (1996) Diabetologia , vol.39 , pp. 1002-1003
    • Wittmann, I.1    Nagy, J.2
  • 147
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • Wood ZA, Poole LB, and Karplus PA. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300: 650-653, 2003.
    • (2003) Science , vol.300 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 148
    • 0032568401 scopus 로고    scopus 로고
    • Novel 5-(3-aryl-2-propynyl)-5-(arylsulfonyl) thiazolidine-2,4-diones as antihyperglycemic agents
    • Wrobel J, Li ZN, Dietrich A, McCaleb M, Mihan B, Sredy J, and Sullivan D. Novel 5-(3-aryl-2-propynyl)-5-(arylsulfonyl) thiazolidine-2,4-diones as antihyperglycemic agents. J Med Chem 41: 1084-1091, 1998.
    • (1998) J Med Chem , vol.41 , pp. 1084-1091
    • Wrobel, J.1    Li, Z.N.2    Dietrich, A.3    McCaleb, M.4    Mihan, B.5    Sredy, J.6    Sullivan, D.7
  • 149
    • 0038818983 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase activity in human adipocytes is strongly correlated with insulin-stimulated glucose uptake and is a target of insulin-induced oxidative inhibition
    • Wu X, Hardy VE, Joseph JI, Jabbour S, Mahadev K, Zhu L, and Goldstein BJ. Protein-tyrosine phosphatase activity in human adipocytes is strongly correlated with insulin-stimulated glucose uptake and is a target of insulin-induced oxidative inhibition. Metabolism 52: 705-712, 2003.
    • (2003) Metabolism , vol.52 , pp. 705-712
    • Wu, X.1    Hardy, V.E.2    Joseph, J.I.3    Jabbour, S.4    Mahadev, K.5    Zhu, L.6    Goldstein, B.J.7
  • 150
    • 0038508928 scopus 로고    scopus 로고
    • Skeletal muscle sarcoplasmic reticulum contains a NADH-dependent oxidase that generates superoxide
    • Xia R, Webb JA, Gnall LL, Cutler K, and Abramson JJ. Skeletal muscle sarcoplasmic reticulum contains a NADH-dependent oxidase that generates superoxide. Am J Physiol Cell Physiol 285: C215-C221, 2003.
    • (2003) Am J Physiol Cell Physiol , vol.285
    • Xia, R.1    Webb, J.A.2    Gnall, L.L.3    Cutler, K.4    Abramson, J.J.5
  • 151
    • 0021321439 scopus 로고
    • Tyrosine phosphorylation of the insulin receptor β subunit activates the receptor-associated tyrosine kinase activity
    • Yu K-T and Czech MP. Tyrosine phosphorylation of the insulin receptor β subunit activates the receptor-associated tyrosine kinase activity. J Biol Chem 259: 5277-5286, 1984.
    • (1984) J Biol Chem , vol.259 , pp. 5277-5286
    • Yu, K.-T.1    Czech, M.P.2
  • 152
    • 0023003503 scopus 로고
    • Tyrosine phosphorylation of insulin receptor beta subunit activates the receptor tyrosine kinase in intact H-35 hepatoma cells
    • Yu KT and Czech MP. Tyrosine phosphorylation of insulin receptor beta subunit activates the receptor tyrosine kinase in intact H-35 hepatoma cells. J Biol Chem 261: 4715-4722, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 4715-4722
    • Yu, K.T.1    Czech, M.P.2
  • 153
    • 4243379141 scopus 로고    scopus 로고
    • Salicylate inhibition of IKKβ (IκB kinase) reverses insulin resistance in Zucker (fa/fa) rats
    • Yuan M, Lee J, Konstantopoulos N, Hansen L, and Shoelson SE. Salicylate inhibition of IKKβ (IκB kinase) reverses insulin resistance in Zucker (fa/fa) rats. Diabetes 49 (Suppl 1): A292, 2000.
    • (2000) Diabetes , vol.49 , Issue.SUPPL. 1
    • Yuan, M.1    Lee, J.2    Konstantopoulos, N.3    Hansen, L.4    Shoelson, S.E.5
  • 154
    • 0035979775 scopus 로고    scopus 로고
    • Reversal of obesity- and diet-induced insulin resistance with salicylates or targeted disruption of IKKβ
    • Yuan M, Konstantopoulos N, Lee J, Hansen L, Li ZW, Karin M, and Shoelson SE. Reversal of obesity- and diet-induced insulin resistance with salicylates or targeted disruption of IKKβ. Science 293: 1673-1677, 2001.
    • (2001) Science , vol.293 , pp. 1673-1677
    • Yuan, M.1    Konstantopoulos, N.2    Lee, J.3    Hansen, L.4    Li, Z.W.5    Karin, M.6    Shoelson, S.E.7
  • 156
    • 0036149984 scopus 로고    scopus 로고
    • Molecular mechanism of insulin-induced degradation of insulin receptor substrate 1
    • Zhande R, Mitchell JJ, Wu J, and Sun XJ. Molecular mechanism of insulin-induced degradation of insulin receptor substrate 1. Mol Cell Biol 22: 1016-1026, 2002.
    • (2002) Mol Cell Biol , vol.22 , pp. 1016-1026
    • Zhande, R.1    Mitchell, J.J.2    Wu, J.3    Sun, X.J.4
  • 157
    • 0035500813 scopus 로고    scopus 로고
    • Insulin resistance: A phosphorylation-based uncoupling of insulin signaling
    • Zick Y. Insulin resistance: a phosphorylation-based uncoupling of insulin signaling. Trends Cell Biol 11: 437-441, 2001.
    • (2001) Trends Cell Biol , vol.11 , pp. 437-441
    • Zick, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.