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Volumn 47, Issue 10, 1998, Pages 1578-1585

Complementary action of antioxidant enzymes in the protection of bioengineered insulin-producing RINm5F cells against the toxicity of reactive oxygen species

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT; CATALASE; COPPER ZINC SUPEROXIDE DISMUTASE; GLUTATHIONE PEROXIDASE; HYDROGEN PEROXIDE; INSULIN; MENADIONE; REACTIVE OXYGEN METABOLITE; XANTHINE OXIDASE;

EID: 0031669435     PISSN: 00121797     EISSN: None     Source Type: Journal    
DOI: 10.2337/diabetes.47.10.1578     Document Type: Article
Times cited : (179)

References (75)
  • 1
    • 0028068186 scopus 로고
    • Free radicals, antioxidants, and human disease: Curiosity, cause, or consequence?
    • Halliwell B: Free radicals, antioxidants, and human disease: curiosity, cause, or consequence? Lancet 344:721-724, 1994
    • (1994) Lancet , vol.344 , pp. 721-724
    • Halliwell, B.1
  • 2
    • 0023770113 scopus 로고
    • Free radicals and diabetes
    • Oberley LW: Free radicals and diabetes. Free Radic Biol Med 5:113-124, 1988
    • (1988) Free Radic Biol Med , vol.5 , pp. 113-124
    • Oberley, L.W.1
  • 4
    • 0026683354 scopus 로고
    • Does nitric oxide mediate autoimmune destruction of beta-cells? Possible therapeutic interventions in IDDM
    • Corbett JA, McDaniel ML: Does nitric oxide mediate autoimmune destruction of beta-cells? Possible therapeutic interventions in IDDM. Diabetes 41:897-903, 1992
    • (1992) Diabetes , vol.41 , pp. 897-903
    • Corbett, J.A.1    McDaniel, M.L.2
  • 5
    • 0027054055 scopus 로고
    • Interleukin 1 beta induces the formation of nitric oxide by beta-cells purified from rodent islets of Langerhans: Evidence for the beta-cell as a source and site of action of nitric oxide
    • Corbett JA, Wang JL, Sweetland MA, Lancaster JR Jr, McDaniel ML: Interleukin 1 beta induces the formation of nitric oxide by beta-cells purified from rodent islets of Langerhans: evidence for the beta-cell as a source and site of action of nitric oxide. J Clin Invest 90:2384-2391, 1992
    • (1992) J Clin Invest , vol.90 , pp. 2384-2391
    • Corbett, J.A.1    Wang, J.L.2    Sweetland, M.A.3    Lancaster Jr., J.R.4    McDaniel, M.L.5
  • 6
    • 0028026652 scopus 로고
    • Insulin-dependent diabetes mellitus as an autoimmune disease
    • Bach JF: Insulin-dependent diabetes mellitus as an autoimmune disease. Endocr Rev 15:516-542, 1994
    • (1994) Endocr Rev , vol.15 , pp. 516-542
    • Bach, J.F.1
  • 7
    • 23444462519 scopus 로고
    • Reactive oxygen intermediates in autoimmune islet cell destruction of fhe NOD mouse induced by peritoneal exudate cells (rich in macrophages) but not T cells
    • Horio F, Fukuda M, Katoh H, Petruzzelli M, Yano N, Rittershaus C, Bonner-Weir S, Hattori M: Reactive oxygen intermediates in autoimmune islet cell destruction of fhe NOD mouse induced by peritoneal exudate cells (rich in macrophages) but not T cells. Diabetologia 37:22-31, 1994
    • (1994) Diabetologia , vol.37 , pp. 22-31
    • Horio, F.1    Fukuda, M.2    Katoh, H.3    Petruzzelli, M.4    Yano, N.5    Rittershaus, C.6    Bonner-Weir, S.7    Hattori, M.8
  • 9
    • 0030005411 scopus 로고    scopus 로고
    • The harmony of the spheres: Inducible nitric oxide synthase and related genes in pancreatic beta cells
    • Eizirik DL, Flodström M, Karlsen AE, Welsh N: The harmony of the spheres: inducible nitric oxide synthase and related genes in pancreatic beta cells. Diabetologia 39:875-890, 1996
    • (1996) Diabetologia , vol.39 , pp. 875-890
    • Eizirik, D.L.1    Flodström, M.2    Karlsen, A.E.3    Welsh, N.4
  • 10
    • 0029817047 scopus 로고    scopus 로고
    • The role of interleukin-1 in the pathogenesis of IDDM
    • Mandrup-Poulsen T: The role of interleukin-1 in the pathogenesis of IDDM. Diabetologia 39:1005-1029, 1996
    • (1996) Diabetologia , vol.39 , pp. 1005-1029
    • Mandrup-Poulsen, T.1
  • 11
    • 0026510118 scopus 로고
    • Cytotoxic effects of cytokines on rat islets: Evidence for involvement of free radicals and lipid peroxidation
    • Rabinovitch A, Suarez WL, Thomas PD, Strynadka K, Simpson I: Cytotoxic effects of cytokines on rat islets: evidence for involvement of free radicals and lipid peroxidation. Diabetologia 35:409-413, 1992
    • (1992) Diabetologia , vol.35 , pp. 409-413
    • Rabinovitch, A.1    Suarez, W.L.2    Thomas, P.D.3    Strynadka, K.4    Simpson, I.5
  • 12
    • 0029795599 scopus 로고    scopus 로고
    • Human pancreatic islet beta-cell destruction by cytokines involves oxygen free radicals and aldehyde production
    • Rabinovitch A, Suarez-Pinzon WL, Strynadka K, Lakey JR, Rajotte RV: Human pancreatic islet beta-cell destruction by cytokines involves oxygen free radicals and aldehyde production. J Clin Endocrinol Metab 81:3197-3202, 1996
    • (1996) J Clin Endocrinol Metab , vol.81 , pp. 3197-3202
    • Rabinovitch, A.1    Suarez-Pinzon, W.L.2    Strynadka, K.3    Lakey, J.R.4    Rajotte, R.V.5
  • 13
    • 0026563728 scopus 로고
    • Nitric oxide: A pathogenetic factor in autoimmunity
    • Kolb H, Kolb-Bachofen V: Nitric oxide: a pathogenetic factor in autoimmunity. Immunol Today 13:157-160, 1992
    • (1992) Immunol Today , vol.13 , pp. 157-160
    • Kolb, H.1    Kolb-Bachofen, V.2
  • 16
    • 0023748601 scopus 로고
    • Alloxan: History and mechanism of action
    • Lenzen S, Panten U: Alloxan: history and mechanism of action. Diabetologia 31:337-342, 1988
    • (1988) Diabetologia , vol.31 , pp. 337-342
    • Lenzen, S.1    Panten, U.2
  • 17
    • 0019852821 scopus 로고
    • CuZn-superoxide dismutase, Mn-superoxide dismutase, catalase and glutathione peroxidase in pancreatic islets and other tissues in the mouse
    • Grankvist K, Marklund SL, Täljedal IB: CuZn-superoxide dismutase, Mn- superoxide dismutase, catalase and glutathione peroxidase in pancreatic islets and other tissues in the mouse. Biochem J 199:393-398, 1981
    • (1981) Biochem J , vol.199 , pp. 393-398
    • Grankvist, K.1    Marklund, S.L.2    Täljedal, I.B.3
  • 18
    • 0029984682 scopus 로고    scopus 로고
    • Low antioxidant enzyme gene expression in pancreatic islets compared with various other mouse tissues
    • Lenzen S, Drinkgern J, Tiedge M: Low antioxidant enzyme gene expression in pancreatic islets compared with various other mouse tissues. Free Radic Biol Med 20:463-466, 1996
    • (1996) Free Radic Biol Med , vol.20 , pp. 463-466
    • Lenzen, S.1    Drinkgern, J.2    Tiedge, M.3
  • 19
    • 0030689041 scopus 로고    scopus 로고
    • Relation between antioxidant enzyme gene expression and antioxidative defense status of insulin-producing cells
    • Tiedge M, Lortz S, Drinkgern J, Lenzen S: Relation between antioxidant enzyme gene expression and antioxidative defense status of insulin-producing cells. Diabetes 46:1733-1742, 1997
    • (1997) Diabetes , vol.46 , pp. 1733-1742
    • Tiedge, M.1    Lortz, S.2    Drinkgern, J.3    Lenzen, S.4
  • 20
    • 1842373814 scopus 로고    scopus 로고
    • Comparative toxicity of alloxan, N- alkylalloxans and ninhydrin to isolated pancreatic islets in vitro
    • Jörns A, Munday R, Tiedge M, Lenzen S: Comparative toxicity of alloxan, N- alkylalloxans and ninhydrin to isolated pancreatic islets in vitro. J Endocrinol 155:283-293, 1997
    • (1997) J Endocrinol , vol.155 , pp. 283-293
    • Jörns, A.1    Munday, R.2    Tiedge, M.3    Lenzen, S.4
  • 21
    • 0027430323 scopus 로고
    • The relationship between the physicochemical properties and the biological effects of alloxan and several N-alkyl substituted alloxan derivatives
    • Munday R, Ludwig K, Lenzen S: The relationship between the physicochemical properties and the biological effects of alloxan and several N-alkyl substituted alloxan derivatives. J Endocrinol 139:153-163, 1993
    • (1993) J Endocrinol , vol.139 , pp. 153-163
    • Munday, R.1    Ludwig, K.2    Lenzen, S.3
  • 22
    • 0028206471 scopus 로고
    • MTT-assay and neutral red release (NRR)-assay: Relative role in the prediction of the irritancy potential of surfactants
    • Korting HC, Schindler S, Hartinger A, Kerscher M, Angerpointner T, Maibach HI: MTT-assay and neutral red release (NRR)-assay: relative role in the prediction of the irritancy potential of surfactants. Life Sci 55:533-540, 1994
    • (1994) Life Sci , vol.55 , pp. 533-540
    • Korting, H.C.1    Schindler, S.2    Hartinger, A.3    Kerscher, M.4    Angerpointner, T.5    Maibach, H.I.6
  • 23
    • 0002486606 scopus 로고
    • Nucleotide sequence of a rat glutathione peroxidase cDNA
    • Ho YS, Howard AJ, Crapo JD: Nucleotide sequence of a rat glutathione peroxidase cDNA. Nucleic Acids Res 16:5207, 1988
    • (1988) Nucleic Acids Res , vol.16 , pp. 5207
    • Ho, Y.S.1    Howard, A.J.2    Crapo, J.D.3
  • 24
    • 0021746044 scopus 로고
    • Isolation of human fibroblast catalase cDNA clones: Sequence of clones derived from spliced and unspliced mRNA
    • Korneluk RG, Quan F, Lewis WH, Guise KS, Willard HF, Holmes MT, Gravel RA: Isolation of human fibroblast catalase cDNA clones: sequence of clones derived from spliced and unspliced mRNA. J Biol Chem 259:13819-13823, 1984
    • (1984) J Biol Chem , vol.259 , pp. 13819-13823
    • Korneluk, R.G.1    Quan, F.2    Lewis, W.H.3    Guise, K.S.4    Willard, H.F.5    Holmes, M.T.6    Gravel, R.A.7
  • 25
    • 0023664899 scopus 로고
    • CDNA and deduced amino acid sequence of rat copper-zinc- containing superoxide dismutase
    • Ho YS, Crapo JD: cDNA and deduced amino acid sequence of rat copper-zinc- containing superoxide dismutase. Nucleic Acids Res 15:6746, 1987
    • (1987) Nucleic Acids Res , vol.15 , pp. 6746
    • Ho, Y.S.1    Crapo, J.D.2
  • 27
    • 0000416248 scopus 로고
    • PCR protocols: Current methods and applications
    • Walker JM, Ed. Totowa, NJ, Humana Press
    • White BA: PCR protocols: current methods and applications. In Methods in Molecular Biology. Vol. 15. Walker JM, Ed. Totowa, NJ, Humana Press, 1993
    • (1993) In Methods in Molecular Biology , vol.15
    • White, B.A.1
  • 29
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P, Sacchi N: Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 162:156-159, 1987
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 30
    • 0028169847 scopus 로고
    • Purification and immunoelectron microscopic localization of cellular glutathione peroxidase in rat hepatocytes: Quantitative analysis by postembedding method
    • Asayama K, Yokota S, Dobashi K, Hayashibe H, Kawaoi A, Nakazawa S: Purification and immunoelectron microscopic localization of cellular glutathione peroxidase in rat hepatocytes: quantitative analysis by postembedding method. Histochemistry 102:213-219, 1994
    • (1994) Histochemistry , vol.102 , pp. 213-219
    • Asayama, K.1    Yokota, S.2    Dobashi, K.3    Hayashibe, H.4    Kawaoi, A.5    Nakazawa, S.6
  • 31
    • 85008419562 scopus 로고
    • Immunohistochemical localization of copper-zinc and manganese superoxide dismutases in rat tissues
    • Dobashi K, Asayama K, Kato K, Kobayashi M, Kawaoi A: Immunohistochemical localization of copper-zinc and manganese superoxide dismutases in rat tissues. Acta Histochem Cytochem 22:351-365, 1989
    • (1989) Acta Histochem Cytochem , vol.22 , pp. 351-365
    • Dobashi, K.1    Asayama, K.2    Kato, K.3    Kobayashi, M.4    Kawaoi, A.5
  • 32
    • 0021288861 scopus 로고
    • Assay of superoxide dismutase activity in tumor tissue
    • Oberley LW, Spitz DR: Assay of superoxide dismutase activity in tumor tissue. Methods Enzymol 105:457-464, 1984
    • (1984) Methods Enzymol , vol.105 , pp. 457-464
    • Oberley, L.W.1    Spitz, D.R.2
  • 35
    • 0027468539 scopus 로고
    • Antioxidant enzyme activities in IDD- prone and IDD-resistant mice: A comparative study
    • Cornelius JG, Luttge BG, Peck AB: Antioxidant enzyme activities in IDD- prone and IDD-resistant mice: a comparative study. Free Radic Biol Med 14:409-420, 1993
    • (1993) Free Radic Biol Med , vol.14 , pp. 409-420
    • Cornelius, J.G.1    Luttge, B.G.2    Peck, A.B.3
  • 37
    • 0027487870 scopus 로고
    • Expression of human catalase in acatalasemic murine SV-B2 cells confers protection from oxidative damage
    • Lindau-Shepard BA, Shaffer JB: Expression of human catalase in acatalasemic murine SV-B2 cells confers protection from oxidative damage. Free Radic Biol Med 15:581-588, 1993
    • (1993) Free Radic Biol Med , vol.15 , pp. 581-588
    • Lindau-Shepard, B.A.1    Shaffer, J.B.2
  • 38
    • 0030728071 scopus 로고    scopus 로고
    • Overexpression of superoxide dismutase and catalase in immortalized neural cells: Toxic effects of hydrogen peroxide
    • Mann H, McCoy MT, Subramaniam J, Van Remmen H, Cadet JL: Overexpression of superoxide dismutase and catalase in immortalized neural cells: toxic effects of hydrogen peroxide. Brain Res 770:163-168, 1997
    • (1997) Brain Res , vol.770 , pp. 163-168
    • Mann, H.1    McCoy, M.T.2    Subramaniam, J.3    Van Remmen, H.4    Cadet, J.L.5
  • 39
    • 0014644243 scopus 로고
    • Kinetics of glutathione peroxidase
    • Flohé L, Brand I: Kinetics of glutathione peroxidase. Biochim Biophys Acta 191:541-549, 1969
    • (1969) Biochim Biophys Acta , vol.191 , pp. 541-549
    • Flohé, L.1    Brand, I.2
  • 40
    • 0025820066 scopus 로고
    • Catalases and peroxidases and glutathione and hydrogen peroxide: Mysteries of the bestiary
    • Eaton JW: Catalases and peroxidases and glutathione and hydrogen peroxide: mysteries of the bestiary. J Lab Clin Med 118:3-4, 1991
    • (1991) J Lab Clin Med , vol.118 , pp. 3-4
    • Eaton, J.W.1
  • 41
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human disease: An overview
    • Halliwell B, Gutteridge JM: Role of free radicals and catalytic metal ions in human disease: an overview. Methods Enzymol 186:1-85, 1990
    • (1990) Methods Enzymol , vol.186 , pp. 1-85
    • Halliwell, B.1    Gutteridge, J.M.2
  • 42
    • 0022381068 scopus 로고
    • Ferric iron and superoxide ions are required for the killing of cultured hepatocytes by hydrogen peroxide: Evidence for the participation of hydroxyl radicals formed by an iron-catalyzed Haber-Weiss reaction
    • Starke PE, Farber JL: Ferric iron and superoxide ions are required for the killing of cultured hepatocytes by hydrogen peroxide: evidence for the participation of hydroxyl radicals formed by an iron-catalyzed Haber-Weiss reaction. J Biol Chem 260:10099-10104, 1985
    • (1985) J Biol Chem , vol.260 , pp. 10099-10104
    • Starke, P.E.1    Farber, J.L.2
  • 43
    • 0020490598 scopus 로고
    • Superoxide radical inhibits catalase
    • Kono Y, Fridovich I: Superoxide radical inhibits catalase. J Biol Chem 257:5751-5754, 1982
    • (1982) J Biol Chem , vol.257 , pp. 5751-5754
    • Kono, Y.1    Fridovich, I.2
  • 44
    • 0021261887 scopus 로고
    • The reaction of superoxide radical with catalase: Mechanism of the inhibition of catalase by superoxide radical
    • Shimizu N, Kobayashi K, Hayashi K: The reaction of superoxide radical with catalase: mechanism of the inhibition of catalase by superoxide radical. J Biol Chem 259:4414-4418, 1984
    • (1984) J Biol Chem , vol.259 , pp. 4414-4418
    • Shimizu, N.1    Kobayashi, K.2    Hayashi, K.3
  • 45
    • 0014962562 scopus 로고
    • Quantitative aspects of the production of superoxide anion radical by milk xanthine oxidase
    • Fridovich I: Quantitative aspects of the production of superoxide anion radical by milk xanthine oxidase. J Biol Chem 245:4053-4057, 1970
    • (1970) J Biol Chem , vol.245 , pp. 4053-4057
    • Fridovich, I.1
  • 46
    • 0019452692 scopus 로고
    • Hydrogen peroxide causes the fatal injury to human fibroblasts exposed to oxygen radicals
    • Simon RH, Scoggin CH, Patterson D: Hydrogen peroxide causes the fatal injury to human fibroblasts exposed to oxygen radicals. J Biol Chem 256:7181-7186, 1981
    • (1981) J Biol Chem , vol.256 , pp. 7181-7186
    • Simon, R.H.1    Scoggin, C.H.2    Patterson, D.3
  • 47
    • 0025719233 scopus 로고
    • Differential protective effects of o-phenanthroline and catalase on H2O2-induced DMA damage and inhibition of protein synthesis in endothelial cells
    • Jornot L, Petersen H, Junod AF: Differential protective effects of o-phenanthroline and catalase on H2O2-induced DMA damage and inhibition of protein synthesis in endothelial cells. J Cell Physiol 149:408-413, 1991
    • (1991) J Cell Physiol , vol.149 , pp. 408-413
    • Jornot, L.1    Petersen, H.2    Junod, A.F.3
  • 48
    • 0021105282 scopus 로고
    • Superoxide anion permeability of phospholipid membranes and chloroplast thylakoids
    • Takahashi MA, Asada K: Superoxide anion permeability of phospholipid membranes and chloroplast thylakoids. Arch Biochem Biophys 226:558-566, 1983
    • (1983) Arch Biochem Biophys , vol.226 , pp. 558-566
    • Takahashi, M.A.1    Asada, K.2
  • 49
    • 0016414528 scopus 로고
    • Superoxide dismutases
    • Fridovich I: Superoxide dismutases. Annu Rev Biochem 44:147-159, 1975
    • (1975) Annu Rev Biochem , vol.44 , pp. 147-159
    • Fridovich, I.1
  • 50
    • 0011235078 scopus 로고
    • The formation and catalytic role of catalase peroxide compound II
    • Nicholls P: The formation and catalytic role of catalase peroxide compound II. Biochim Biophys Acta 81:479-495, 1964
    • (1964) Biochim Biophys Acta , vol.81 , pp. 479-495
    • Nicholls, P.1
  • 52
    • 0020377461 scopus 로고
    • The role of superoxide in xanthine oxidase- induced autooxidation of linoleic acid
    • Thomas MJ, Mehl KS, Pryor WA: The role of superoxide in xanthine oxidase- induced autooxidation of linoleic acid. J Biol Chem 257:8343-8347, 1982
    • (1982) J Biol Chem , vol.257 , pp. 8343-8347
    • Thomas, M.J.1    Mehl, K.S.2    Pryor, W.A.3
  • 53
    • 0024592332 scopus 로고
    • Free radical formation by antitumor quinones
    • Powis G: Free radical formation by antitumor quinones. Free Radic Biol Med 6:63-101, 1989
    • (1989) Free Radic Biol Med , vol.6 , pp. 63-101
    • Powis, G.1
  • 54
    • 0024394691 scopus 로고
    • Detection of free radicals as a consequence of dog tracheal epithelial cellular xenobiotic metabolism
    • Rosen GM, Hassett DJ, Yankaskas JR, Cohen MS: Detection of free radicals as a consequence of dog tracheal epithelial cellular xenobiotic metabolism. Xenobiotica 19:635-643, 1989
    • (1989) Xenobiotica , vol.19 , pp. 635-643
    • Rosen, G.M.1    Hassett, D.J.2    Yankaskas, J.R.3    Cohen, M.S.4
  • 56
    • 0022481327 scopus 로고
    • Mechanisms of toxicity of naphthoquinones to isolated hepatocytes
    • Miller MG, Rodgers A, Cohen GM: Mechanisms of toxicity of naphthoquinones to isolated hepatocytes. Biochem Pharmacol 35:1177-1184, 1986
    • (1986) Biochem Pharmacol , vol.35 , pp. 1177-1184
    • Miller, M.G.1    Rodgers, A.2    Cohen, G.M.3
  • 57
    • 0028260509 scopus 로고
    • One- and two-electron reduction of quinones by rat liver subcellular fractions
    • Nakamura M, Hayashi T: One- and two-electron reduction of quinones by rat liver subcellular fractions. J Biochem (Tokyo) 115:1141-1147, 1994
    • (1994) J Biochem (Tokyo) , vol.115 , pp. 1141-1147
    • Nakamura, M.1    Hayashi, T.2
  • 58
    • 0025070274 scopus 로고
    • Dual effects of superoxide dismutase on the autooxidation of 1,4-naphthohydroquinone
    • Ishii T, Fridovich I: Dual effects of superoxide dismutase on the autooxidation of 1,4-naphthohydroquinone. Free Radic Biol Med 8:21-24, 1990
    • (1990) Free Radic Biol Med , vol.8 , pp. 21-24
    • Ishii, T.1    Fridovich, I.2
  • 59
    • 0001340876 scopus 로고
    • One-electron transfer equilibria and redox potentials of radicals studied by pulse radiolysis
    • Meisel D, Czapski G: One-electron transfer equilibria and redox potentials of radicals studied by pulse radiolysis. J Phys Chem 79:1503-1509, 1975
    • (1975) J Phys Chem , vol.79 , pp. 1503-1509
    • Meisel, D.1    Czapski, G.2
  • 60
    • 0018129988 scopus 로고
    • Superoxide dismutase as an inhibitor of reactions of semiquinone radicals
    • Winterbourn CC, French JK, Claridge RFC: Superoxide dismutase as an inhibitor of reactions of semiquinone radicals. FEBS Lett 94:269-272, 1978
    • (1978) FEBS Lett , vol.94 , pp. 269-272
    • Winterbourn, C.C.1    French, J.K.2    Claridge, R.F.C.3
  • 61
    • 0025786654 scopus 로고
    • Overexpression of selenoglutathione peroxidase by gene transfer enhances the resistance of T47D human breast cells to clastogenic oxidants
    • Mirault ME, Tremblay A, Beaudoin N, Tremblay M: Overexpression of selenoglutathione peroxidase by gene transfer enhances the resistance of T47D human breast cells to clastogenic oxidants. J Biol Chem 266:20752-20760, 1991
    • (1991) J Biol Chem , vol.266 , pp. 20752-20760
    • Mirault, M.E.1    Tremblay, A.2    Beaudoin, N.3    Tremblay, M.4
  • 62
    • 0023831181 scopus 로고
    • Dialuric acid autooxidation: Effects of transition metals on the reaction rate and on the generation of "active oxygen" species
    • Munday R: Dialuric acid autooxidation: effects of transition metals on the reaction rate and on the generation of "active oxygen" species. Biochem Pharmacol 37:409-413, 1988
    • (1988) Biochem Pharmacol , vol.37 , pp. 409-413
    • Munday, R.1
  • 63
    • 0024520376 scopus 로고
    • Glutathione-mediated redox cycling of alloxan: Mechanisms of superoxide dismutase inhibition and of metal-catalyzed OH. formation
    • Winterbourn CC, Munday R: Glutathione-mediated redox cycling of alloxan: mechanisms of superoxide dismutase inhibition and of metal-catalyzed OH. formation. Biochem Pharmacol 38:271-277, 1989
    • (1989) Biochem Pharmacol , vol.38 , pp. 271-277
    • Winterbourn, C.C.1    Munday, R.2
  • 64
    • 0025823868 scopus 로고
    • Thiol-group reactivity, hydrophilicity and stability of alloxan, its reduction products and its N-methyl derivatives and a comparison with ninhydrin
    • Lenzen S, Munday R: Thiol-group reactivity, hydrophilicity and stability of alloxan, its reduction products and its N-methyl derivatives and a comparison with ninhydrin. Biochem Pharmacol 42:1385-1391, 1991
    • (1991) Biochem Pharmacol , vol.42 , pp. 1385-1391
    • Lenzen, S.1    Munday, R.2
  • 65
    • 0029072441 scopus 로고
    • Insulinoma cells in culture show pronounced sensitivity to alloxan-induced oxidative stress
    • Zhang H, Öllinger K, Brunk U: Insulinoma cells in culture show pronounced sensitivity to alloxan-induced oxidative stress. Diabetologia 38:635-641, 1995
    • (1995) Diabetologia , vol.38 , pp. 635-641
    • Zhang, H.1    Öllinger, K.2    Brunk, U.3
  • 66
    • 0030582831 scopus 로고    scopus 로고
    • Ebselen and cytokine-induced nitric oxide synthase expression in insulin-producing cells
    • de Mello MA, Flodström M, Eizirik DL: Ebselen and cytokine-induced nitric oxide synthase expression in insulin-producing cells. Biochem Pharmacol 52:1703-1709, 1996
    • (1996) Biochem Pharmacol , vol.52 , pp. 1703-1709
    • De Mello, M.A.1    Flodström, M.2    Eizirik, D.L.3
  • 67
    • 0029765063 scopus 로고    scopus 로고
    • Effects of sodium butyrate on glucose transporter and glucose-phosphorylating enzyme gene expression in RINm5F insulinoma cells
    • Hedge M, Lenzen S: Effects of sodium butyrate on glucose transporter and glucose-phosphorylating enzyme gene expression in RINm5F insulinoma cells. J Mol Endocrinol 11:19-26, 1996
    • (1996) J Mol Endocrinol , vol.11 , pp. 19-26
    • Hedge, M.1    Lenzen, S.2
  • 68
    • 0028049833 scopus 로고
    • Major species differences between humans and rodents in the susceptibility to pancreatic beta-cell injury
    • Eizirik DL, Pipeleers DG, Ling Z, Welsh N, Hellerström C, Andersson A: Major species differences between humans and rodents in the susceptibility to pancreatic beta-cell injury. Proc Natl Acad Sci USA 91:925:3-9256, 1994
    • (1994) Proc Natl Acad Sci USA , vol.91 , Issue.925 , pp. 3-9256
    • Eizirik, D.L.1    Pipeleers, D.G.2    Ling, Z.3    Welsh, N.4    Hellerström, C.5    Andersson, A.6
  • 71
    • 0030798658 scopus 로고    scopus 로고
    • Targeted overexpression of Cu/Zn superoxide dismutase protects pancreatic beta-cells against oxidative stress
    • Kubisch HM, Wang J, Bray TM, Phillips JP: Targeted overexpression of Cu/Zn superoxide dismutase protects pancreatic beta-cells against oxidative stress. Diabetes 46:1563-1566, 1997
    • (1997) Diabetes , vol.46 , pp. 1563-1566
    • Kubisch, H.M.1    Wang, J.2    Bray, T.M.3    Phillips, J.P.4
  • 72
    • 0029401861 scopus 로고
    • Differences in the expression of heat-shock proteins and antioxidant enzymes between human and rodent pancreatic islets: Implications for the pathogenesis of insulin- dependent diabetes mellitus
    • Welsh N, Margulis B, Borg LA, Wiklund HJ, Saldeen J, Flodström M, Mello MA, Andersson A, Pipeleers DG, Hellerström C, Eizirik DL: Differences in the expression of heat-shock proteins and antioxidant enzymes between human and rodent pancreatic islets: implications for the pathogenesis of insulin- dependent diabetes mellitus. Mol Med 1:806-820, 1995
    • (1995) Mol Med , vol.1 , pp. 806-820
    • Welsh, N.1    Margulis, B.2    Borg, L.A.3    Wiklund, H.J.4    Saldeen, J.5    Flodström, M.6    Mello, M.A.7    Andersson, A.8    Pipeleers, D.G.9    Hellerström, C.10    Eizirik, D.L.11
  • 73
    • 0028177211 scopus 로고
    • The role of O2• in the production of HO: In vitro and in vivo
    • Liochev SI, Fridovich I: The role of O2• in the production of HO: in vitro and in vivo. Free Radic Biol Med 16:29-33, 1994
    • (1994) Free Radic Biol Med , vol.16 , pp. 29-33
    • Liochev, S.I.1    Fridovich, I.2
  • 74
    • 0024463482 scopus 로고
    • Oxygen free radical scavengers protect rat islet cells from damage by cytokines
    • Sumoski W, Baquerizo H, Rabinovitch A: Oxygen free radical scavengers protect rat islet cells from damage by cytokines. Diabetologia 32:792-796, 1989
    • (1989) Diabetologia , vol.32 , pp. 792-796
    • Sumoski, W.1    Baquerizo, H.2    Rabinovitch, A.3
  • 75
    • 0030987135 scopus 로고    scopus 로고
    • Development of autoimmune diabetes in NOD mice is associated with the formation of peroxynitrite in pancreatic islet beta-cells
    • Suarez-Pinzon WL, Szabo C, Rabinovitch A: Development of autoimmune diabetes in NOD mice is associated with the formation of peroxynitrite in pancreatic islet beta-cells. Diabetes 46:907-911, 1997
    • (1997) Diabetes , vol.46 , pp. 907-911
    • Suarez-Pinzon, W.L.1    Szabo, C.2    Rabinovitch, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.