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Volumn 8, Issue , 2007, Pages

Mitochondrial respiratory chain is involved in insulin-stimulated hydrogen peroxide production and plays an integral role in insulin receptor autophosphorylation in neurons

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCYSTEINE; CARBONYL CYANIDE 4 (TRIFLUOROMETHOXY)PHENYLHYDRAZONE; HYDROGEN PEROXIDE; INSULIN; INSULIN RECEPTOR; MALONIC ACID; SUCCINIC ACID DERIVATIVE;

EID: 36348947406     PISSN: None     EISSN: 14712202     Source Type: Journal    
DOI: 10.1186/1471-2202-8-84     Document Type: Article
Times cited : (60)

References (46)
  • 1
    • 0018071115 scopus 로고
    • Endogenous hydrogen peroxide and peroxidative metabolism in adipocytes in response to insulin and sulfhydryl reagents
    • 10.1016/0006-2952(78)90332-5 728211
    • Mukherjee SP Lane RH Lynn WS Endogenous hydrogen peroxide and peroxidative metabolism in adipocytes in response to insulin and sulfhydryl reagents Biochem Pharmacol 1978, 27(22):2589-94. 10.1016/ 0006-2952(78)90332-5 728211
    • (1978) Biochem Pharmacol , vol.27 , Issue.22 , pp. 2589-2594
    • Mukherjee, S.P.1    Lane, R.H.2    Lynn, W.S.3
  • 2
    • 0018382583 scopus 로고
    • Insulin-stimulated intracellular hydrogen peroxide production in rat epididymal fat cells
    • 429281
    • May JM de Haen C Insulin-stimulated intracellular hydrogen peroxide production in rat epididymal fat cells J Biol Chem 1979, 254(7):2214-20. 429281
    • (1979) J Biol Chem , vol.254 , Issue.7 , pp. 2214-2220
    • May, J.M.1    de Haen, C.2
  • 3
    • 17644399404 scopus 로고    scopus 로고
    • Role of insulin-induced reactive oxygen species in the insulin signaling pathway
    • 1434604 15998257 10.1089/ars.2005.7.1021
    • Goldstein BJ Mahadev K Wu X Zhu L Motoshima H Role of insulin-induced reactive oxygen species in the insulin signaling pathway Antioxid Redox Signal 2005, 7(7-8):1021-31. 1434604 15998257 10.1089/ars.2005.7.1021
    • (2005) Antioxid Redox Signal , vol.7 , Issue.7-8 , pp. 1021-1031
    • Goldstein, B.J.1    Mahadev, K.2    Wu, X.3    Zhu, L.4    Motoshima, H.5
  • 4
    • 12744279326 scopus 로고    scopus 로고
    • Redox paradox: Insulin action is facilitated by insulin-stimulated reactive oxygen species with multiple potential signaling targets
    • 1464057 15677487 10.2337/diabetes.54.2.311
    • Goldstein BJ Mahadev K Wu X Redox paradox: Insulin action is facilitated by insulin-stimulated reactive oxygen species with multiple potential signaling targets Diabetes 2005, 54(2):311-21. 1464057 15677487 10.2337/ diabetes.54.2.311
    • (2005) Diabetes , vol.54 , Issue.2 , pp. 311-321
    • Goldstein, B.J.1    Mahadev, K.2    Wu, X.3
  • 5
    • 0031750534 scopus 로고    scopus 로고
    • Redox priming of the insulin receptor β-chain associated with altered tyrosine kinase activity and insulin responsiveness in the absence of tyrosine autophosphorylation
    • 9657526
    • Schmid E El Benna J Galter D Klein G Droge W Redox priming of the insulin receptor β-chain associated with altered tyrosine kinase activity and insulin responsiveness in the absence of tyrosine autophosphorylation FASEB J 1998, 12:863-870. 9657526
    • (1998) FASEB J , vol.12 , pp. 863-870
    • Schmid, E.1    El Benna, J.2    Galter, D.3    Klein, G.4    Droge, W.5
  • 6
    • 0032867462 scopus 로고    scopus 로고
    • Phosphorylation of the insulin receptor kinase by phosphocreatine in combination with hydrogen peroxide: The structural basis of redox priming
    • 10463939
    • Schmid E Hotz-Wagenblatt A Hack V Droge W Phosphorylation of the insulin receptor kinase by phosphocreatine in combination with hydrogen peroxide: The structural basis of redox priming FASEB J 1999, 13:1491-1500. 10463939
    • (1999) FASEB J , vol.13 , pp. 1491-1500
    • Schmid, E.1    Hotz-Wagenblatt, A.2    Hack, V.3    Droge, W.4
  • 7
    • 13544268735 scopus 로고    scopus 로고
    • Interdependent regulation of insulin receptor kinase activity by ADP and hydrogen peroxide
    • 10.1074/jbc.M410352200 15563471
    • Schmitt TL Hotz-Wagenblatt A Klein H Droge W Interdependent regulation of insulin receptor kinase activity by ADP and hydrogen peroxide J Biol Chem 2005, 280(5):3795-3801. 10.1074/jbc.M410352200 15563471
    • (2005) J Biol Chem , vol.280 , Issue.5 , pp. 3795-3801
    • Schmitt, T.L.1    Hotz-Wagenblatt, A.2    Klein, H.3    Droge, W.4
  • 8
    • 0035877633 scopus 로고    scopus 로고
    • Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade
    • 10.1074/jbc.C100109200 11297536
    • Mahadev K Zilbering A Zhu L Goldstein BJ Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade J Biol Chem 2001, 276(24):21938-42. 10.1074/jbc.C100109200 11297536
    • (2001) J Biol Chem , vol.276 , Issue.24 , pp. 21938-21942
    • Mahadev, K.1    Zilbering, A.2    Zhu, L.3    Goldstein, B.J.4
  • 9
    • 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
    • 10.1074/jbc.M105061200 11598110
    • Mahadev K Wu X Zilbering A Zhu L Lawrence JT 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 2001, 276(52):48662-9. 10.1074/jbc.M105061200 11598110
    • (2001) J Biol Chem , vol.276 , Issue.52 , pp. 48662-48669
    • Mahadev, K.1    Wu, X.2    Zilbering, A.3    Zhu, L.4    Lawrence, J.T.5    Goldstein, B.J.6
  • 10
    • 4444233558 scopus 로고    scopus 로고
    • Regulation of insulin signaling through reversible oxidation of the protein-tyrosine phosphatases TC45 and PTP1B
    • 10.1074/jbc.M404606200 15192089
    • Meng T-C Buckley DA Galic S Tiganis T Tonks NK Regulation of insulin signaling through reversible oxidation of the protein-tyrosine phosphatases TC45 and PTP1B J Biol Chem 2004, 279(36):37716-37725. 10.1074/jbc.M404606200 15192089
    • (2004) J Biol Chem , vol.279 , Issue.36 , pp. 37716-37725
    • Meng, T.-C.1    Buckley, D.A.2    Galic, S.3    Tiganis, T.4    Tonks, N.K.5
  • 11
    • 17644384828 scopus 로고    scopus 로고
    • Hyperglycemia potentiates H(2)O(2) production in adipocytes and enhances insulin signal transduction: Potential role for oxidative inhibition of thiol-sensitive protein-tyrosine phosphatases
    • 1435729 15889998 10.1089/ars.2005.7.526
    • Wu X Zhu L Zilbering A Mahadev K Motoshima H Yao J Goldstein BJ Hyperglycemia potentiates H(2)O(2) production in adipocytes and enhances insulin signal transduction: Potential role for oxidative inhibition of thiol-sensitive protein-tyrosine phosphatases Antioxid Redox Signal 2005, 7(5-6):526-37. 1435729 15889998 10.1089/ars.2005.7.526
    • (2005) Antioxid Redox Signal , vol.7 , Issue.5-6 , pp. 526-557
    • Wu, X.1    Zhu, L.2    Zilbering, A.3    Mahadev, K.4    Motoshima, H.5    Yao, J.6    Goldstein, B.J.7
  • 12
    • 11144279346 scopus 로고    scopus 로고
    • The major target of the endogenously generated reactive oxygen species in response to insulin stimulation is phosphatase and tensin homolog and not phosphoinositide-3 kinase (PI-3 kinase) in the PI-3 kinase/Akt pathway
    • 539178 15537704 10.1091/mbc.E04-05-0369
    • Seo JH Ahn Y Lee SR Yeol Yeo C Chung Hur K The major target of the endogenously generated reactive oxygen species in response to insulin stimulation is phosphatase and tensin homolog and not phosphoinositide-3 kinase (PI-3 kinase) in the PI-3 kinase/Akt pathway Mol Biol Cell 2005, 16(1):348-57. 539178 15537704 10.1091/mbc.E04-05-0369
    • (2005) Mol Biol Cell , vol.16 , Issue.1 , pp. 348-357
    • Seo, J.H.1    Ahn, Y.2    Lee, S.R.3    Yeol Yeo, C.4    Chung Hur, K.5
  • 13
    • 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
    • 10.1016/0003-9861(77)90327-7 21633
    • Mukherjee SP 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 1977, 184(1):69-76. 10.1016/0003-9861(77)90327-7 21633
    • (1977) Arch Biochem Biophys , vol.184 , Issue.1 , pp. 69-76
    • Mukherjee, S.P.1    Lynn, W.S.2
  • 14
    • 0026572097 scopus 로고
    • Human fat cells possess a plasma membrane-bound H2O2-generating system that is activated by insulin via a mechanism bypassing the receptor kinase
    • 442950 1311714
    • Krieger-Brauer HI Kather H Human fat cells possess a plasma membrane-bound H2O2-generating system that is activated by insulin via a mechanism bypassing the receptor kinase J Clin Invest 1992, 89(3):1006-13. 442950 1311714
    • (1992) J Clin Invest , vol.89 , Issue.3 , pp. 1006-1013
    • Krieger-Brauer, H.I.1    Kather, H.2
  • 15
    • 0030894971 scopus 로고    scopus 로고
    • Insulin-induced activation of NADPH-dependent H2O2 generation in human adipocyte plasma membranes is mediated by Galphai2
    • 10.1074/jbc.272.15.10135 9092559
    • Krieger-Brauer HI Medda PK Kather H Insulin-induced activation of NADPH-dependent H2O2 generation in human adipocyte plasma membranes is mediated by Galphai2 J Biol Chem 1997, 272(15):10135-43. 10.1074/ jbc.272.15.10135 9092559
    • (1997) J Biol Chem , vol.272 , Issue.15 , pp. 10135-10143
    • Krieger-Brauer, H.I.1    Medda, P.K.2    Kather, H.3
  • 16
    • 3042701041 scopus 로고    scopus 로고
    • Ligand-dependent autophosphorylation of the insulin receptor is positively regulated by Gi-proteins
    • 1224225 15025562 10.1042/BJ20031659
    • Kreuzer J Nurnberg B Krieger-Brauer HI Ligand-dependent autophosphorylation of the insulin receptor is positively regulated by Gi-proteins Biochem J 2004, 380(Pt 3):831-6. 1224225 15025562 10.1042/ BJ20031659
    • (2004) Biochem J , vol.380 , Issue.PART 3 , pp. 831-836
    • Kreuzer, J.1    Nurnberg, B.2    Krieger-Brauer, H.I.3
  • 17
    • 1342304048 scopus 로고    scopus 로고
    • The NAD(P)H oxidase homolog Nox4 modulates insulin-stimulated generation of H2O2 and plays an integral role in insulin signal transduction
    • 350558 14966267 10.1128/MCB.24.5.1844-1854.2004
    • Mahadev K Motoshima H Wu X Ruddy JM Arnold RS Cheng G Lambeth JD Goldstein BJ The NAD(P)H oxidase homolog Nox4 modulates insulin-stimulated generation of H2O2 and plays an integral role in insulin signal transduction Mol Cell Biol 2004, 24(5):1844-54. 350558 14966267 10.1128/MCB.24.5.1844-1854.2004
    • (2004) Mol Cell Biol , vol.24 , Issue.5 , pp. 1844-1854
    • Mahadev, K.1    Motoshima, H.2    Wu, X.3    Ruddy, J.M.4    Arnold, R.S.5    Cheng, G.6    Lambeth, J.D.7    Goldstein, B.J.8
  • 18
    • 0141962639 scopus 로고    scopus 로고
    • Insulin-stimulated hydrogen peroxide increases guanylate cyclase activity in vascular smooth muscle
    • 10.1161/01.HYP.0000092441.27668.BD 12963680
    • Yang M Yang Y Zhang S Kahn AM Insulin-stimulated hydrogen peroxide increases guanylate cyclase activity in vascular smooth muscle Hypertension 2003, 42(4):569-73. 10.1161/01.HYP.0000092441.27668.BD 12963680
    • (2003) Hypertension , vol.42 , Issue.4 , pp. 569-573
    • Yang, M.1    Yang, Y.2    Zhang, S.3    Kahn, A.M.4
  • 19
    • 25844520154 scopus 로고    scopus 로고
    • Insulin-stimulated NAD(P)H oxidase activity increases migration of cultured vascular smooth muscle cells
    • 10.1016/j.amjhyper.2005.04.012 16202857
    • Yang M Foster E Kahn AM Insulin-stimulated NAD(P)H oxidase activity increases migration of cultured vascular smooth muscle cells Am J Hypertens 2005, 18(10):1329-34. 10.1016/j.amjhyper.2005.04.012 16202857
    • (2005) Am J Hypertens , vol.18 , Issue.10 , pp. 1329-1334
    • Yang, M.1    Foster, E.2    Kahn, A.M.3
  • 20
    • 0036625030 scopus 로고    scopus 로고
    • Key role of succinate dehydrogenase in insulin-induced inactivation of protein tyrosine phosphatases
    • 10.1023/A:1020229724717 12447467
    • Pomytkin IA Kolesova OE Key role of succinate dehydrogenase in insulin-induced inactivation of protein tyrosine phosphatases Bull Exp Biol Med 2002, 133(6):568-70. 10.1023/A:1020229724717 12447467
    • (2002) Bull Exp Biol Med , vol.133 , Issue.6 , pp. 568-570
    • Pomytkin, I.A.1    Kolesova, O.E.2
  • 21
    • 0242468627 scopus 로고    scopus 로고
    • Effect of insulin on the rate of hydrogen peroxide generation in mitochondria
    • 10.1023/A:1025412915297 12937667
    • Pomytkin IA Kolesova OE Effect of insulin on the rate of hydrogen peroxide generation in mitochondria Bull Exp Biol Med 2003, 135(6):541-2. 10.1023/A:1025412915297 12937667
    • (2003) Bull Exp Biol Med , vol.135 , Issue.6 , pp. 541-542
    • Pomytkin, I.A.1    Kolesova, O.E.2
  • 22
    • 33645224486 scopus 로고    scopus 로고
    • Insulin cannot activate extracellular-signal-related kinase due to inability to generate reactive oxygen species in SK-N-BE(2) human neuroblastoma cells
    • 16267404
    • Hwang J-J Hur KC Insulin cannot activate extracellular-signal-related kinase due to inability to generate reactive oxygen species in SK-N-BE(2) human neuroblastoma cells Mol Cells 2005, 20(2):280-287. 16267404
    • (2005) Mol Cells , vol.20 , Issue.2 , pp. 280-287
    • Hwang, J.-J.1    Hur, K.C.2
  • 23
    • 0345476725 scopus 로고
    • Phosphorylation activates the insulin receptor tyrosine protein kinase
    • 394015 6574482 10.1073/pnas.80.11.3237
    • Rosen OM Herrera R Olowe Y Petruzzelli LM Cobb MH Phosphorylation activates the insulin receptor tyrosine protein kinase Proc Natl Acad Sci USA 1983, 80(11):3237-40. 394015 6574482 10.1073/pnas.80.11.3237
    • (1983) Proc Natl Acad Sci USA , vol.80 , Issue.11 , pp. 3237-3240
    • Rosen, O.M.1    Herrera, R.2    Olowe, Y.3    Petruzzelli, L.M.4    Cobb, M.H.5
  • 24
    • 0023244139 scopus 로고
    • Identification of insulin receptor tyrosine residues autophosphorylated in vitro
    • 3038872
    • Tornqvist HE Pierce MW Frackelton AR Nemenoff RA Avruch J Identification of insulin receptor tyrosine residues autophosphorylated in vitro J Biol Chem 1987, 262(21):10212-9. 3038872
    • (1987) J Biol Chem , vol.262 , Issue.21 , pp. 10212-10219
    • Tornqvist, H.E.1    Pierce, M.W.2    Frackelton, A.R.3    Nemenoff, R.A.4    Avruch, J.5
  • 25
    • 0023834406 scopus 로고
    • A cascade of tyrosine autophosphorylation in the β-subunit activates the phosphotransferase of the insulin receptor
    • 2449432
    • White MF Shoelson SE Keutmann H Kahn CR A cascade of tyrosine autophosphorylation in the β-subunit activates the phosphotransferase of the insulin receptor J Biol Chem 1988, 263:2969-2980. 2449432
    • (1988) J Biol Chem , vol.263 , pp. 2969-2980
    • White, M.F.1    Shoelson, S.E.2    Keutmann, H.3    Kahn, C.R.4
  • 26
    • 0025964033 scopus 로고
    • The regulatory role of known tyrosine autophosphorylation sites of the insulin receptor kinase domain. An assessment by replacement with neutral and negatively charged amino acids
    • 1846000
    • Zhang B Tavare JM Ellis L Roth RA The regulatory role of known tyrosine autophosphorylation sites of the insulin receptor kinase domain. An assessment by replacement with neutral and negatively charged amino acids J Biol Chem 1991, 266(2):990-996. 1846000
    • (1991) J Biol Chem , vol.266 , Issue.2 , pp. 990-996
    • Zhang, B.1    Tavare, J.M.2    Ellis, L.3    Roth, R.A.4
  • 27
    • 0023882103 scopus 로고
    • Identification of the insulin receptor tyrosine residues undergoing insulin-stimulated phosphorylation in intact rat hepatoma cells
    • 3275643
    • Tornqvist HE Gunsalus JR Nemenoff RA Frackelton AR Pierce MW Avruch J Identification of the insulin receptor tyrosine residues undergoing insulin-stimulated phosphorylation in intact rat hepatoma cells J Biol Chem 1988, 263(1):350-359. 3275643
    • (1988) J Biol Chem , vol.263 , Issue.1 , pp. 350-359
    • Tornqvist, H.E.1    Gunsalus, J.R.2    Nemenoff, R.A.3    Frackelton, A.R.4    Pierce, M.W.5    Avruch, J.6
  • 28
    • 0025843532 scopus 로고
    • Analysis of insulin receptor phosphorylation sites in intact rat liver cells by two-dimensional phosphopeptide mapping. Predominance of the trisphosphorylated form of the kinase domain after stimulation by insulin
    • 1150006 1708233
    • Issad T Tavare JM Denton RM Analysis of insulin receptor phosphorylation sites in intact rat liver cells by two-dimensional phosphopeptide mapping. Predominance of the trisphosphorylated form of the kinase domain after stimulation by insulin Biochem J 1991, 275(Pt 1):15-21. 1150006 1708233
    • (1991) Biochem J , vol.275 , Issue.PART 1 , pp. 15-21
    • Issad, T.1    Tavare, J.M.2    Denton, R.M.3
  • 29
    • 0028582185 scopus 로고
    • Crystal structure of the tyrosine kinase domain of the human insulin receptor
    • 10.1038/372746a0 7997262
    • Hubbard SR Wei L Ellis L Hendrickson WA Crystal structure of the tyrosine kinase domain of the human insulin receptor Nature 1994, 372(6508):746-54. 10.1038/372746a0 7997262
    • (1994) Nature , vol.372 , Issue.6508 , pp. 746-754
    • Hubbard, S.R.1    Wei, L.2    Ellis, L.3    Hendrickson, W.A.4
  • 30
    • 0030766163 scopus 로고    scopus 로고
    • Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog
    • 1170189 9312016 10.1093/emboj/16.18.5572
    • Hubbard SR Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog EMBO J 1997, 16(18):5572-81. 1170189 9312016 10.1093/emboj/16.18.5572
    • (1997) EMBO J , vol.16 , Issue.18 , pp. 5572-5581
    • Hubbard, S.R.1
  • 31
    • 0028957904 scopus 로고
    • Expression, Characterization, and Crystallization of the Catalytic Core of the Human Insulin Receptor Protein-tyrosine Kinase Domain
    • 10.1074/jbc.270.14.8122 7713916
    • Wie L Hubbard SR Hendrickson WA Ellis L Expression, Characterization, and Crystallization of the Catalytic Core of the Human Insulin Receptor Protein-tyrosine Kinase Domain J Biol Chem 1995, 270(14):8122-8130. 10.1074/jbc.270.14.8122 7713916
    • (1995) J Biol Chem , vol.270 , Issue.14 , pp. 8122-8130
    • Wie, L.1    Hubbard, S.R.2    Hendrickson, W.A.3    Ellis, L.4
  • 32
    • 0015363173 scopus 로고
    • The cellular production of hydrogen peroxide
    • 1173814 4404507
    • Boveris A Oshino N Chance B The cellular production of hydrogen peroxide Biochem J 1972, 128(3):617-30. 1173814 4404507
    • (1972) Biochem J , vol.128 , Issue.3 , pp. 617-630
    • Boveris, A.1    Oshino, N.2    Chance, B.3
  • 33
    • 0034740585 scopus 로고    scopus 로고
    • DeltaPsi(m)-Dependent and - Independent production of reactive oxygen species by rat brain mitochondria
    • 10.1046/j.1471-4159.2001.00548.x 11677254
    • Votyakova TV Reynolds IJ DeltaPsi(m)-Dependent and - independent production of reactive oxygen species by rat brain mitochondria J Neurochem 2001, 79(2):266-77. 10.1046/j.1471-4159.2001.00548.x 11677254
    • (2001) J Neurochem , vol.79 , Issue.2 , pp. 266-277
    • Votyakova, T.V.1    Reynolds, I.J.2
  • 34
    • 0016148483 scopus 로고
    • Superoxide radicals as precursors of mitochondrial hydrogen peroxide
    • 10.1016/0014-5793(74)80281-4 4859511
    • Loschen G Azzi A Richter C Flohe L Superoxide radicals as precursors of mitochondrial hydrogen peroxide FEBS Lett 1974, 42(1):68-72. 10.1016/ 0014-5793(74)80281-4 4859511
    • (1974) FEBS Lett , vol.42 , Issue.1 , pp. 68-72
    • Loschen, G.1    Azzi, A.2    Richter, C.3    Flohe, L.4
  • 35
    • 0030729851 scopus 로고    scopus 로고
    • High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
    • 10.1016/S0014-5793(97)01159-9 9369223
    • Korshunov SS Skulachev VP Starkov AA High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria FEBS Lett 1997, 416(1):15-8. 10.1016/S0014-5793(97)01159-9 9369223
    • (1997) FEBS Lett , vol.416 , Issue.1 , pp. 15-18
    • Korshunov, S.S.1    Skulachev, V.P.2    Starkov, A.A.3
  • 36
    • 0032544720 scopus 로고    scopus 로고
    • Fatty acids as natural uncouplers preventing generation of O2.- and H2O2 by mitochondria in the resting state
    • 10.1016/S0014-5793(98)01073-4 9762912
    • Korshunov SS Korkina OV Ruuge EK Skulachev VP Starkov AA Fatty acids as natural uncouplers preventing generation of O2.- and H2O2 by mitochondria in the resting state FEBS Lett 1998, 435(2-3):215-8. 10.1016/S0014-5793(98)01073-4 9762912
    • (1998) FEBS Lett , vol.435 , Issue.2-3 , pp. 215-218
    • Korshunov, S.S.1    Korkina, O.V.2    Ruuge, E.K.3    Skulachev, V.P.4    Starkov, A.A.5
  • 37
    • 17144422877 scopus 로고    scopus 로고
    • Mitochondrial metabolism of reactive oxygen species
    • 10.1007/s10541-005-0102-7 15807660
    • Andreyev AY Kushnareva YE Starkov AA Mitochondrial metabolism of reactive oxygen species Biochemistry (Mosc) 2005, 70(2):200-14. 10.1007/ s10541-005-0102-7 15807660
    • (2005) Biochemistry (Mosc) , vol.70 , Issue.2 , pp. 200-214
    • Andreyev, A.Y.1    Kushnareva, Y.E.2    Starkov, A.A.3
  • 38
    • 0022491149 scopus 로고
    • Intracellular site of insulin action: Mitochondrial Krebs cycle
    • 323891 3523482 10.1073/pnas.83.14.5067
    • Bessman SP Mohan C Zaidise I Intracellular site of insulin action: mitochondrial Krebs cycle Proc Natl Acad Sci USA 1986, 83(14):5067-70. 323891 3523482 10.1073/pnas.83.14.5067
    • (1986) Proc Natl Acad Sci USA , vol.83 , Issue.14 , pp. 5067-5070
    • Bessman, S.P.1    Mohan, C.2    Zaidise, I.3
  • 39
    • 0030826585 scopus 로고    scopus 로고
    • Insulin as a probe of mitochondrial metabolism in situ
    • 10.1023/A:1006834408181 9309671
    • Bessman SP Mohan C Insulin as a probe of mitochondrial metabolism in situ Mol Cell Biochem 1997, 174(1-2):91-6. 10.1023/A:1006834408181 9309671
    • (1997) Mol Cell Biochem , vol.174 , Issue.1-2 , pp. 91-96
    • Bessman, S.P.1    Mohan, C.2
  • 40
    • 28444459842 scopus 로고    scopus 로고
    • Insulin resistance syndrome and Alzheimer's disease: Age- and obesity-related effects on memory, amyloid, and inflammation
    • 10.1016/j.neurobiolaging.2005.08.021 16266773
    • Craft S Insulin resistance syndrome and Alzheimer's disease: Age- and obesity-related effects on memory, amyloid, and inflammation Neurobiol Aging 2005, 26(Suppl 1):65-9. 10.1016/j.neurobiolaging.2005.08.021 16266773
    • (2005) Neurobiol Aging , vol.26 , Issue.SUPPL. 1 , pp. 65-69
    • Craft, S.1
  • 41
    • 1842785179 scopus 로고    scopus 로고
    • Glucose metabolism and insulin receptor signal transduction in Alzheimer disease
    • 10.1016/j.ejphar.2004.02.049 15094078
    • Hoyer S Glucose metabolism and insulin receptor signal transduction in Alzheimer disease Eur J Pharmacol 2004, 490(1-3):115-25. 10.1016/ j.ejphar.2004.02.049 15094078
    • (2004) Eur J Pharmacol , vol.490 , Issue.1-3 , pp. 115-125
    • Hoyer, S.1
  • 42
    • 15244350991 scopus 로고    scopus 로고
    • Review of insulin and insulin-like growth factor expression, signaling, and malfunction in the central nervous system: Relevance to Alzheimer's disease
    • 15750214
    • de la Monte SM Wands JR Review of insulin and insulin-like growth factor expression, signaling, and malfunction in the central nervous system: Relevance to Alzheimer's disease J Alzheimers Dis 2005, 7:45-61. 15750214
    • (2005) J Alzheimers Dis , vol.7 , pp. 45-61
    • de la Monte, S.M.1    Wands, J.R.2
  • 44
    • 0025922865 scopus 로고
    • Inhibition of Na+/Ca2+ exchange enhances delayed neuronal death elicited by glutamate in cerebellar granule cell cultures
    • 10.1016/0006-8993(91)91141-M 1678303
    • Andreeva N Khodorov B Stelmashook E Cragoe E Jr Victorov I Inhibition of Na+/Ca2+ exchange enhances delayed neuronal death elicited by glutamate in cerebellar granule cell cultures Brain Res 1991, 548(1-2):322-5. 10.1016/0006-8993(91)91141-M 1678303
    • (1991) Brain Res , vol.548 , Issue.1-2 , pp. 322-325
    • Andreeva, N.1    Khodorov, B.2    Stelmashook, E.3    Cragoe Jr., E.4    Victorov, I.5
  • 45
    • 0028256101 scopus 로고
    • Glutamate impairs neuronal calcium extrusion while reducing sodium gradient
    • 10.1016/0896-6273(94)90272-0 7906528
    • Kiedrowski L Brooker G Costa E Wroblewski JT Glutamate impairs neuronal calcium extrusion while reducing sodium gradient Neuron 1994, 12(2):295-300. 10.1016/0896-6273(94)90272-0 7906528
    • (1994) Neuron , vol.12 , Issue.2 , pp. 295-300
    • Kiedrowski, L.1    Brooker, G.2    Costa, E.3    Wroblewski, J.T.4
  • 46
    • 4544359913 scopus 로고    scopus 로고
    • Mitochondrial alpha-ketoglutarate dehydrogenase complex generates reactive oxygen species
    • 10.1523/JNEUROSCI.1899-04.2004 15356189
    • Starkov AA Fiskum G Chinopoulos C Lorenzo BJ Browne SE Patel MS Beal MF Mitochondrial alpha-ketoglutarate dehydrogenase complex generates reactive oxygen species J Neurosci 2004, 24(36):7779-88. 10.1523/ JNEUROSCI.1899-04.2004 15356189
    • (2004) J Neurosci , vol.24 , Issue.36 , pp. 7779-7788
    • Starkov, A.A.1    Fiskum, G.2    Chinopoulos, C.3    Lorenzo, B.J.4    Browne, S.E.5    Patel, M.S.6    Beal, M.F.7


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