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Volumn 14, Issue 9, 2000, Pages 1215-1223

The pro-oxidative activity of SOD and nitroxide SOD mimics

Author keywords

Hydrogen peroxide; Oxidative damage; Papain; Superoxide; Thiol

Indexed keywords

FERROCYANIDE; SUPEROXIDE DISMUTASE; THIOL DERIVATIVE;

EID: 0034042319     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.14.9.1215     Document Type: Article
Times cited : (116)

References (50)
  • 1
    • 0031126569 scopus 로고    scopus 로고
    • Free radicals in rabbit retina under ocular hyperpressure and functional consequences
    • Muller, A., Pietri, S., Villain, M., Frejaville, C., Bonne, C., and Culcas, M. (1997) Free radicals in rabbit retina under ocular hyperpressure and functional consequences. Exp. Eye. Res. 64, 637-643
    • (1997) Exp. Eye. Res. , vol.64 , pp. 637-643
    • Muller, A.1    Pietri, S.2    Villain, M.3    Frejaville, C.4    Bonne, C.5    Culcas, M.6
  • 2
    • 0029788363 scopus 로고    scopus 로고
    • Protective effect of the nitroxide tempol against the cardiotoxicity of Adriamycin
    • Monti, E., Cova, D., Guido, E., Morelli, R., and Oliva, C. (1996) Protective effect of the nitroxide tempol against the cardiotoxicity of Adriamycin. Free Rad. Biol. Med. 21, 463-470
    • (1996) Free Rad. Biol. Med. , vol.21 , pp. 463-470
    • Monti, E.1    Cova, D.2    Guido, E.3    Morelli, R.4    Oliva, C.5
  • 3
    • 0029267363 scopus 로고
    • In vivo ESR studies of antioxidant activity on free radical reaction in living mice under oxidative stress
    • Miura, Y., Hamada, A., and Utsumi, H. (1995) In vivo ESR studies of antioxidant activity on free radical reaction in living mice under oxidative stress. Free Rad. Res. 22, 209-214
    • (1995) Free Rad. Res. , vol.22 , pp. 209-214
    • Miura, Y.1    Hamada, A.2    Utsumi, H.3
  • 5
    • 0028967848 scopus 로고
    • Nitrone spin traps and a nitroxide antioxidant inhibit a common pathway of thymocyte apoptosis
    • Slater, A. F., Nobel, C. S., Maellaro, E., Bustamante, J., Kimland, M., and Orrenius, S. (1995) Nitrone spin traps and a nitroxide antioxidant inhibit a common pathway of thymocyte apoptosis. Biochem. J. 306, 771-778
    • (1995) Biochem. J. , vol.306 , pp. 771-778
    • Slater, A.F.1    Nobel, C.S.2    Maellaro, E.3    Bustamante, J.4    Kimland, M.5    Orrenius, S.6
  • 6
    • 0026032484 scopus 로고
    • Nitroxides block DNA scission and protect cells from oxidative damage
    • Samuni, A., Godinger, D., Aronovitch, J., Russo, A., and Mitchell, J. B. (1991) Nitroxides block DNA scission and protect cells from oxidative damage. Biochemistry 30, 555-561
    • (1991) Biochemistry , vol.30 , pp. 555-561
    • Samuni, A.1    Godinger, D.2    Aronovitch, J.3    Russo, A.4    Mitchell, J.B.5
  • 7
  • 8
    • 0024224555 scopus 로고
    • A novel metal-free low molecular weight superoxide dismutase mimic
    • Samuni, A., Krishna, C. M., Riesz, P., Finkelstein, E., and Russo, A. (1988) A novel metal-free low molecular weight superoxide dismutase mimic. J. Biol. Chem. 263, 17921-17924
    • (1988) J. Biol. Chem. , vol.263 , pp. 17921-17924
    • Samuni, A.1    Krishna, C.M.2    Riesz, P.3    Finkelstein, E.4    Russo, A.5
  • 10
    • 0029957646 scopus 로고    scopus 로고
    • Stimulation by nitroxides of catalase-like activity of hemeproteins. Kinetics and mechanism
    • Krishna, M. C., Samuni, A., Taira, J., Goldstein, S., Mitchell, J. B., and Russo, A. (1996) Stimulation by nitroxides of catalase-like activity of hemeproteins. Kinetics and mechanism. J. Biol. Chem. 271, 26018-26025
    • (1996) J. Biol. Chem. , vol.271 , pp. 26018-26025
    • Krishna, M.C.1    Samuni, A.2    Taira, J.3    Goldstein, S.4    Mitchell, J.B.5    Russo, A.6
  • 11
    • 0023837018 scopus 로고
    • 2 and charge on radical scavenging by nitroxides
    • 2 and charge on radical scavenging by nitroxides. Environ. Sci. Technol. 22, 77-82
    • (1988) Environ. Sci. Technol. , vol.22 , pp. 77-82
    • Blough, N.V.1
  • 12
    • 0024402710 scopus 로고
    • Inhibition of lipid peroxidation by spin labels. Relationships between structure and function
    • Nilsson, U. A., Olsson, L. I., Carlin, G., and Bylund, F. A. (1989) Inhibition of lipid peroxidation by spin labels. Relationships between structure and function. J. Biol. Chem. 264, 11131-11135
    • (1989) J. Biol. Chem. , vol.264 , pp. 11131-11135
    • Nilsson, U.A.1    Olsson, L.I.2    Carlin, G.3    Bylund, F.A.4
  • 13
    • 0026745007 scopus 로고
    • Mutagenicity of nitroxyl compounds: Structure-activity relationships
    • Gallez, B. C. D., Debuyst, R., Dejehet, F., and Dumont, P. (1992) Mutagenicity of nitroxyl compounds: structure-activity relationships. Toxicol. Lett. 63, 35-45
    • (1992) Toxicol. Lett. , vol.63 , pp. 35-45
    • Gallez, B.C.D.1    Debuyst, R.2    Dejehet, F.3    Dumont, P.4
  • 14
    • 0023022582 scopus 로고
    • Mutagenicity of nitroxide-free radicals
    • Seis, H., and Mehlhorn, R. (1986) Mutagenicity of nitroxide-free radicals. Arch. Biochem. Biophys. 251, 393-396
    • (1986) Arch. Biochem. Biophys. , vol.251 , pp. 393-396
    • Seis, H.1    Mehlhorn, R.2
  • 15
    • 0026731503 scopus 로고
    • Increased hydrogen peroxide concentration in human tumor cells due to a nitroxide free radical
    • Voest, E. E., van Fassen, E., van Asbeck, B. S., Neijt, J. P., and Marx, J. J. M. (1992) Increased hydrogen peroxide concentration in human tumor cells due to a nitroxide free radical. Biochim. Biophys. Acta 1136, 113-118
    • (1992) Biochim. Biophys. Acta , vol.1136 , pp. 113-118
    • Voest, E.E.1    Van Fassen, E.2    Van Asbeck, B.S.3    Neijt, J.P.4    Marx, J.J.M.5
  • 16
    • 0032053876 scopus 로고    scopus 로고
    • Antiproliferative effect of the piperidine nitroxide tempol on neoplastic and nonneoplastic mammalian cell lines
    • Gariboldi, M. B., Lucchi, S., Caserini, C., Supino, R., Oliva, C., and Monti, E. (1998) Antiproliferative effect of the piperidine nitroxide tempol on neoplastic and nonneoplastic mammalian cell lines. Free Rad. Biol. Med. 24, 913-923
    • (1998) Free Rad. Biol. Med. , vol.24 , pp. 913-923
    • Gariboldi, M.B.1    Lucchi, S.2    Caserini, C.3    Supino, R.4    Oliva, C.5    Monti, E.6
  • 17
    • 0024359606 scopus 로고
    • Reperfusion arrhythmias: Dose-related protection by anti-free radical interventions
    • Bernier, M., Manning, A. S., and Hearse, D. J. (1989) Reperfusion arrhythmias: dose-related protection by anti-free radical interventions. Am. J. Physiol. 256, 1344-1352
    • (1989) Am. J. Physiol. , vol.256 , pp. 1344-1352
    • Bernier, M.1    Manning, A.S.2    Hearse, D.J.3
  • 18
    • 0025678229 scopus 로고
    • The cardioprotective effect of Mn-superoxide dismutase is lost at high doses in the postischemic isolated rabbit heart
    • Omar, B. A., and McCord, J. M. (1990) The cardioprotective effect of Mn-superoxide dismutase is lost at high doses in the postischemic isolated rabbit heart. Free Rad. Biol. Med. 9, 473-478
    • (1990) Free Rad. Biol. Med. , vol.9 , pp. 473-478
    • Omar, B.A.1    McCord, J.M.2
  • 21
    • 0001936360 scopus 로고    scopus 로고
    • The importance of oxidant-antioxidant balance
    • (Montagnier, L., Olivier, R., and Pasquier, C., eds) Marcel Dekker, New York
    • McCord, J. M. (1998) The importance of oxidant-antioxidant balance. In Oxidative Stress in Cancer, AIDS, and Neurodegenerative Diseases (Montagnier, L., Olivier, R., and Pasquier, C., eds) pp. 1-7, Marcel Dekker, New York
    • (1998) Oxidative Stress in Cancer, AIDS, and Neurodegenerative Diseases , pp. 1-7
    • McCord, J.M.1
  • 22
    • 0025316007 scopus 로고
    • Cytotoxic effects of expression of human superoxide dismutase in bovine adrenocortical cells
    • Norris, K. H., and Hornsby, P. (1990) Cytotoxic effects of expression of human superoxide dismutase in bovine adrenocortical cells. Mutat. Res. 237, 95-106
    • (1990) Mutat. Res. , vol.237 , pp. 95-106
    • Norris, K.H.1    Hornsby, P.2
  • 23
    • 0022684839 scopus 로고
    • Overproduction of human Cu/Zn-superoxide dismutase in transfected cells: Extension of paraquat-mediated cytotoxicity and enhancement of lipid peroxidation
    • Elroy-Stein, O., Bernstein, Y., and Groner, Y. (1986) Overproduction of human Cu/Zn-superoxide dismutase in transfected cells: extension of paraquat-mediated cytotoxicity and enhancement of lipid peroxidation. EMBO J. 5, 615-622
    • (1986) EMBO J. , vol.5 , pp. 615-622
    • Elroy-Stein, O.1    Bernstein, Y.2    Groner, Y.3
  • 24
    • 0024504551 scopus 로고
    • Superoxide dismutase amplifies organismal sensitivity to ionizing radiation
    • Scott, M. D., Meshnick, S. R., and Eaton, J. W. (1989) Superoxide dismutase amplifies organismal sensitivity to ionizing radiation. J. Biol. Chem. 264, 2498-2501
    • (1989) J. Biol. Chem. , vol.264 , pp. 2498-2501
    • Scott, M.D.1    Meshnick, S.R.2    Eaton, J.W.3
  • 25
    • 0025285382 scopus 로고
    • Copper, zinc superoxide dismutase catalyzes hydroxyl radical production from hydrogen peroxide
    • Yim, M. B., Chock, P. B., and Stadtman, E. R. (1990) Copper, zinc superoxide dismutase catalyzes hydroxyl radical production from hydrogen peroxide. Proc. Natl. Acad. Sci. USA 87, 5006-5010
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5006-5010
    • Yim, M.B.1    Chock, P.B.2    Stadtman, E.R.3
  • 26
    • 0025801343 scopus 로고
    • Superoxide dismutase enhances the toxicity of 3-hydroxyanthranilic acid to bacteria
    • Ishii, T., Iwahashi, H., Sugata, R., and Kido, R. (1991) Superoxide dismutase enhances the toxicity of 3-hydroxyanthranilic acid to bacteria. Free Rad. Res. Commun. 14, 187-194
    • (1991) Free Rad. Res. Commun. , vol.14 , pp. 187-194
    • Ishii, T.1    Iwahashi, H.2    Sugata, R.3    Kido, R.4
  • 27
    • 0023654270 scopus 로고
    • Superoxide dismutase-rich bacteria. Paradoxical increase in oxidant toxicity
    • Scott, M. D., Meshnick, S. R., and Eaton, J. W. (1987) Superoxide dismutase-rich bacteria. Paradoxical increase in oxidant toxicity. J. Biol. Chem. 262, 3640-3645
    • (1987) J. Biol. Chem. , vol.262 , pp. 3640-3645
    • Scott, M.D.1    Meshnick, S.R.2    Eaton, J.W.3
  • 28
    • 0023880939 scopus 로고
    • Down's syndrome: A pathology involving the lack of balance of reactive oxygen species
    • Kedziora, J., and Bartosz, G. (1988) Down's syndrome: a pathology involving the lack of balance of reactive oxygen species. Free Rad. Biol. Med. 4, 317-330
    • (1988) Free Rad. Biol. Med. , vol.4 , pp. 317-330
    • Kedziora, J.1    Bartosz, G.2
  • 29
  • 30
    • 0022472686 scopus 로고
    • Biological effects of the superoxide radical
    • Fridovich, I. (1986) Biological effects of the superoxide radical. Arch. Biochem. Biophys. 247, 1-11
    • (1986) Arch. Biochem. Biophys. , vol.247 , pp. 1-11
    • Fridovich, I.1
  • 33
    • 0032212613 scopus 로고    scopus 로고
    • An SOD-mimicry mechanism underlies the role of nitroxides in protecting papain from oxidative inactivation
    • Offer, T., Mohsen, M., and Samuni, A. (1998) An SOD-mimicry mechanism underlies the role of nitroxides in protecting papain from oxidative inactivation. Free Rad. Biol. Med. 25, 832-838
    • (1998) Free Rad. Biol. Med. , vol.25 , pp. 832-838
    • Offer, T.1    Mohsen, M.2    Samuni, A.3
  • 35
    • 0033520921 scopus 로고    scopus 로고
    • Evidence against the generation of free hydroxyl radicals from the interaction of copper,zinc-superoxide dismutase and hydrogen peroxide
    • Sankarapandi, S., and Zweier, J. L. (1999) Evidence against the generation of free hydroxyl radicals from the interaction of copper,zinc-superoxide dismutase and hydrogen peroxide. J. Biol. Chem. 274, 34576-34583
    • (1999) J. Biol. Chem. , vol.274 , pp. 34576-34583
    • Sankarapandi, S.1    Zweier, J.L.2
  • 36
    • 0033214459 scopus 로고    scopus 로고
    • Bicarbonate enhances the peroxidase activity of Cu,Zn-superoxide dismutase. Role of carbonate anion radical
    • Goss, S. P., Singh, R. J., and Kalyanaraman, B. (1999) Bicarbonate enhances the peroxidase activity of Cu,Zn-superoxide dismutase. Role of carbonate anion radical. J. Biol. Chem. 274, 28233-28239
    • (1999) J. Biol. Chem. , vol.274 , pp. 28233-28239
    • Goss, S.P.1    Singh, R.J.2    Kalyanaraman, B.3
  • 37
    • 0026101656 scopus 로고
    • Phosphate, not superoxide dismutase, facilitates electron transfer from ferrous salts to cytochrome c
    • Beyer, F. W., and Fridovich, I. (1991) Phosphate, not superoxide dismutase, facilitates electron transfer from ferrous salts to cytochrome c. Arch. Biochem. Biophys. 285, 60-63
    • (1991) Arch. Biochem. Biophys. , vol.285 , pp. 60-63
    • Beyer, F.W.1    Fridovich, I.2
  • 38
    • 0028111408 scopus 로고
    • A novel antiulcerogenic stable radical prevents gastric mucosal lesions in rats
    • Rachmilewitz, D., Karmeli, F., Okon, E., and Samuni, A. (1994) A novel antiulcerogenic stable radical prevents gastric mucosal lesions in rats. Gut. 35, 1181-1188
    • (1994) Gut. , vol.35 , pp. 1181-1188
    • Rachmilewitz, D.1    Karmeli, F.2    Okon, E.3    Samuni, A.4
  • 39
    • 0015921527 scopus 로고
    • On the mechanism of superoxide dismutase. Reaction of the bovine enzyme with hydrogen peroxide and ferrocyanide
    • Rotilio, G., Morpurgo, L., Calabrese, L., and Mondovi, B. (1973) On the mechanism of superoxide dismutase. Reaction of the bovine enzyme with hydrogen peroxide and ferrocyanide. Biochim. Biophys. Acta 302, 229-235
    • (1973) Biochim. Biophys. Acta , vol.302 , pp. 229-235
    • Rotilio, G.1    Morpurgo, L.2    Calabrese, L.3    Mondovi, B.4
  • 40
    • 0026594013 scopus 로고
    • Effects of overproduction of superoxide dismutases in Escherichia coli on inhibition of growth and on induction of glucose-6-phosphate dehydrogenase by paraquat
    • Liochev, S. I., and Fridovich, I. (1992) Effects of overproduction of superoxide dismutases in Escherichia coli on inhibition of growth and on induction of glucose-6-phosphate dehydrogenase by paraquat. Arch. Biochem. Biophys. 294, 138-143
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 138-143
    • Liochev, S.I.1    Fridovich, I.2
  • 41
    • 0016816805 scopus 로고
    • The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: Chemiluminescence and peroxidation
    • Hodgson, E. K., and Fridovich, I. (1975) The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: chemiluminescence and peroxidation. Biochemistry 14, 5299-5303
    • (1975) Biochemistry , vol.14 , pp. 5299-5303
    • Hodgson, E.K.1    Fridovich, I.2
  • 42
    • 0031572869 scopus 로고    scopus 로고
    • Superoxide-dependent peroxidase activity of H48Q: A superoxide dismutase variant associated with familial amyotrophic lateral sclerosis
    • Liochev, S. I., Chen, L. L., Hallewell, R. A., and Fridovich, I. (1997) Superoxide-dependent peroxidase activity of H48Q: a superoxide dismutase variant associated with familial amyotrophic lateral sclerosis. Arch. Biochem. Biophys. 346, 263-268
    • (1997) Arch. Biochem. Biophys. , vol.346 , pp. 263-268
    • Liochev, S.I.1    Chen, L.L.2    Hallewell, R.A.3    Fridovich, I.4
  • 43
    • 0029051192 scopus 로고
    • Superoxide radical: Controversies, contradictions, and paradoxes
    • McCord, J. M. (1995) Superoxide radical: controversies, contradictions, and paradoxes [see comments]. Proc. Soc. Exp. Biol. Med. 209, 112-117
    • (1995) Proc. Soc. Exp. Biol. Med. , vol.209 , pp. 112-117
    • McCord, J.M.1
  • 44
    • 0028280787 scopus 로고
    • The toxicity of high-dose superoxide dismutase suggests that superoxide can both initiate and terminate lipid peroxidation in the reperfused heart
    • Nelson, S. K., Swapan, K. B., and McCord, J. M. (1994) The toxicity of high-dose superoxide dismutase suggests that superoxide can both initiate and terminate lipid peroxidation in the reperfused heart. Free Rad. Biol. Med. 16, 195-200
    • (1994) Free Rad. Biol. Med. , vol.16 , pp. 195-200
    • Nelson, S.K.1    Swapan, K.B.2    McCord, J.M.3
  • 45
    • 0026505347 scopus 로고
    • Antimutagenicity of a low molecular weight superoxide dismutase mimic against oxidative mutagens
    • DeGraff, W. G., Krishna, M. C., Russo, A., and Mitchell, J. B. (1992) Antimutagenicity of a low molecular weight superoxide dismutase mimic against oxidative mutagens. Environ. Mol. Mutagen. 19, 21-26
    • (1992) Environ. Mol. Mutagen. , vol.19 , pp. 21-26
    • DeGraff, W.G.1    Krishna, M.C.2    Russo, A.3    Mitchell, J.B.4
  • 46
    • 0029933628 scopus 로고    scopus 로고
    • Cerebroprotective effect of stable nitroxide radicals in closed head injury in the rat
    • Beit-Yannai, E., Zhang, R., Trembovler, V., Samuni, A., and Shohami, E. (1996) Cerebroprotective effect of stable nitroxide radicals in closed head injury in the rat. Brain. Res. 717, 22-28
    • (1996) Brain. Res. , vol.717 , pp. 22-28
    • Beit-Yannai, E.1    Zhang, R.2    Trembovler, V.3    Samuni, A.4    Shohami, E.5
  • 47
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich, I. (1995) Superoxide radical and superoxide dismutases. Annu. Rev. Biochem. 64, 97-112
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 49
    • 0029744988 scopus 로고    scopus 로고
    • Mechanistic studies on the inactivation of papain by epoxysuccinyl inhibitors
    • Meara, J. P., and Rich, D. H. (1996) Mechanistic studies on the inactivation of papain by epoxysuccinyl inhibitors. J. Med. Chem. 39, 3357-3366
    • (1996) J. Med. Chem. , vol.39 , pp. 3357-3366
    • Meara, J.P.1    Rich, D.H.2
  • 50
    • 0029784865 scopus 로고    scopus 로고
    • Effects of oxidative stress on the model thiol-protease papain: An investigation of changes in activity and structure
    • Subramainan, R., Cole, P., Hensely, K., Azhar, S., Bummer, P., Carney, J. M., and Butterfield, D. A. (1996) Effects of oxidative stress on the model thiol-protease papain: an investigation of changes in activity and structure. Biochem. Arch. 12, 105-116
    • (1996) Biochem. Arch. , vol.12 , pp. 105-116
    • Subramainan, R.1    Cole, P.2    Hensely, K.3    Azhar, S.4    Bummer, P.5    Carney, J.M.6    Butterfield, D.A.7


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