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Volumn 3, Issue 2, 2001, Pages 189-202

Antioxidant mechanisms of nitric oxide against iron-catalyzed oxidative stress in cells

Author keywords

[No Author keywords available]

Indexed keywords

FREE RADICAL; HEME; IRON; IRON DERIVATIVE; NITRIC OXIDE; NITROSYL RADICAL; OXOFERRYL ASSOCIATED RADICAL; PROTEIN; UNCLASSIFIED DRUG;

EID: 0035018487     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/152308601300185160     Document Type: Article
Times cited : (60)

References (73)
  • 1
    • 0018850440 scopus 로고
    • Iron transport and storage proteins
    • Aisen P, and Listowsky I. Iron transport and storage proteins. Annn Rev Biochem 49: 357-393, 1980.
    • (1980) Annn Rev Biochem , vol.49 , pp. 357-393
    • Aisen, P.1    Listowsky, I.2
  • 3
    • 0023476064 scopus 로고
    • Iron regulates ferritin mRNA translation through a segment of its 5′ untranslated region
    • Aziz N, and Munro HN. Iron regulates ferritin mRNA translation through a segment of its 5′ untranslated region. Proc Natl Acad Sci U S A 84: 8478-8482, 1987.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 8478-8482
    • Aziz, N.1    Munro, H.N.2
  • 4
    • 0034652634 scopus 로고    scopus 로고
    • Peroxidation of linoleate at physiological pH: Hemichrome formation by substrate binding protects against metmyoglobin activation by hydrogen peroxide
    • Baron CP, Skibsted LH, and Andersen HJ. Peroxidation of linoleate at physiological pH: hemichrome formation by substrate binding protects against metmyoglobin activation by hydrogen peroxide. Free Radic Biol Med 28: 549-558, 2000.
    • (2000) Free Radic Biol Med , vol.28 , pp. 549-558
    • Baron, C.P.1    Skibsted, L.H.2    Andersen, H.J.3
  • 5
    • 0033913195 scopus 로고    scopus 로고
    • Nitric oxide regulation of free radical- and enzyme-mediated lipid and lipoprotein oxidation
    • Bloodsworth A, O'Donnell VB, and Freeman BA. Nitric oxide regulation of free radical-and enzyme-mediated lipid and lipoprotein oxidation. Arterioscler Thromb Vasc Biol 20:1707-1715, 2000.
    • (2000) Arterioscler Thromb Vasc Biol , vol.20 , pp. 1707-1715
    • Bloodsworth, A.1    O'Donnell, V.B.2    Freeman, B.A.3
  • 6
    • 0028928738 scopus 로고
    • Induction of ferritin synthesis by oxidative stress. Transcriptional and post-transcriptional regulation by expansion of the "free" iron pool
    • Cairo G, Tacchini L, Pogliaghi G, Anzon E, Tomasi A, and Bernelli-Zazzera A. Induction of ferritin synthesis by oxidative stress. Transcriptional and post-transcriptional regulation by expansion of the "free" iron pool. J Biol Chem 270: 700-703, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 700-703
    • Cairo, G.1    Tacchini, L.2    Pogliaghi, G.3    Anzon, E.4    Tomasi, A.5    Bernelli-Zazzera, A.6
  • 7
    • 0031149875 scopus 로고    scopus 로고
    • The role of desferrioxamine chelatable iron in rat liver mitochondrial dysfunction in chronic dietary iron overload
    • Ceccarelli D, Kozlov AV, Gallesi, D, Tomasi A, Giovannini F, and Masini A. The role of desferrioxamine chelatable iron in rat liver mitochondrial dysfunction in chronic dietary iron overload. Bioelectrochem Bioenerg 42: 169-174, 1997.
    • (1997) Bioelectrochem Bioenerg , vol.42 , pp. 169-174
    • Ceccarelli, D.1    Kozlov, A.V.2    Gallesi, D.3    Tomasi, A.4    Giovannini, F.5    Masini, A.6
  • 9
    • 0032054339 scopus 로고    scopus 로고
    • Absence of hemoprotein-associated free radical events following oxidant challenge of crosslinked hemoglobin-superoxide dismutase catalase
    • D'Agnillo F, and Chang TM. Absence of hemoprotein-associated free radical events following oxidant challenge of crosslinked hemoglobin-superoxide dismutase catalase. Free Radic Biol Med 24: 906-912, 1998.
    • (1998) Free Radic Biol Med , vol.24 , pp. 906-912
    • D'Agnillo, F.1    Chang, T.M.2
  • 10
    • 0023858329 scopus 로고
    • Detection of peroxyl and alkoxyl radicals produced by reaction of hydroperoxides with heme-proteins by electron spin resonance spectroscopy
    • Davies MJ. Detection of peroxyl and alkoxyl radicals produced by reaction of hydroperoxides with heme-proteins by electron spin resonance spectroscopy. Biochim Biophys Acta 964: 28-35, 1988.
    • (1988) Biochim Biophys Acta , vol.964 , pp. 28-35
    • Davies, M.J.1
  • 11
    • 0032557672 scopus 로고    scopus 로고
    • Characterization of cytochrome c free radical reactions with peptides by mass spectrometry
    • Deterding LJ, Barr DP, Mason RP, and Tomer KB. Characterization of cytochrome c free radical reactions with peptides by mass spectrometry. J Biol Chem 273: 12863-12869, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 12863-12869
    • Deterding, L.J.1    Barr, D.P.2    Mason, R.P.3    Tomer, K.B.4
  • 12
    • 0032186410 scopus 로고    scopus 로고
    • [Iron chelation in 1998] La chelation du fer en 1998
    • de Montalembert M. [Iron chelation in 1998] La chelation du fer en 1998. Transfus Clin Biol 5: 353-356, 1998.
    • (1998) Transfus Clin Biol , vol.5 , pp. 353-356
    • De Montalembert, M.1
  • 13
    • 0031068834 scopus 로고    scopus 로고
    • The role of nitric oxide in the regulation of cellular iron metabolism
    • Domachowske JB. The role of nitric oxide in the regulation of cellular iron metabolism. Biochem Mol Med 60: 1-7, 1997.
    • (1997) Biochem Mol Med , vol.60 , pp. 1-7
    • Domachowske, J.B.1
  • 14
    • 0029957216 scopus 로고    scopus 로고
    • Nitric oxide alters the expression of gamma-globin, H-ferritin, and transferrin receptor in human K562 cells at the posttranscriptional level
    • Domachowske JB, Rafferty SP, Singhania N, Mardiney M 3rd, and Malech HL. Nitric oxide alters the expression of gamma-globin, H-ferritin, and transferrin receptor in human K562 cells at the posttranscriptional level. Blood 88: 2980-2988, 1996.
    • (1996) Blood , vol.88 , pp. 2980-2988
    • Domachowske, J.B.1    Rafferty, S.P.2    Singhania, N.3    Mardiney III, M.4    Malech, H.L.5
  • 16
    • 0027301897 scopus 로고
    • Biosynthesis of nitric oxide activates iron regulatory factor in macrophages
    • Drapier JC, Hirling H, Wietzerbin J, Kaldy P, and Kuhn LC. Biosynthesis of nitric oxide activates iron regulatory factor in macrophages. EMBO J 12: 3643-3649, 1993.
    • (1993) EMBO J , vol.12 , pp. 3643-3649
    • Drapier, J.C.1    Hirling, H.2    Wietzerbin, J.3    Kaldy, P.4    Kuhn, L.C.5
  • 17
    • 0031882531 scopus 로고    scopus 로고
    • Chelation therapy in cardiovascular disease: Ethyl-enediaminetetraacetic acid, deferoxamine, and dexrazoxane
    • Elihu N, Anandasbapathy S, and Fishman WH. Chelation therapy in cardiovascular disease: ethyl-enediaminetetraacetic acid, deferoxamine, and dexrazoxane. J Clin Pharmacol 32: 101-105, 1998.
    • (1998) J Clin Pharmacol , vol.32 , pp. 101-105
    • Elihu, N.1    Anandasbapathy, S.2    Fishman, W.H.3
  • 18
    • 0034213869 scopus 로고    scopus 로고
    • Protection of erythrocytes against oxidative damage and autologous immunoglobulin G (IgG) binding by iron chelator fluor-benzoil-pyridoxal hydrazone
    • Ferrali M, Signorini C, Ciccoli L, Bambagioni S, Rossi V, Pompella A, and Comporti M. Protection of erythrocytes against oxidative damage and autologous immunoglobulin G (IgG) binding by iron chelator fluor-benzoil-pyridoxal hydrazone. Biochem Pharmacol 59: 1365-1373, 2000.
    • (2000) Biochem Pharmacol , vol.59 , pp. 1365-1373
    • Ferrali, M.1    Signorini, C.2    Ciccoli, L.3    Bambagioni, S.4    Rossi, V.5    Pompella, A.6    Comporti, M.7
  • 19
    • 0016908351 scopus 로고
    • Ceruloplasmin: The copper transport protein with essential oxidase activity
    • Frieden E, and Hsieh HS. Ceruloplasmin: the copper transport protein with essential oxidase activity. Adv Enzymol Relat Areas Mol Biol 44: 187-236, 1976.
    • (1976) Adv Enzymol Relat Areas Mol Biol , vol.44 , pp. 187-236
    • Frieden, E.1    Hsieh, H.S.2
  • 20
    • 0030039911 scopus 로고    scopus 로고
    • Apoptotic death of human leukemic cells induced by vascular cells expressing nitric oxide synthase in response to gamma-interferon and tumor necrosis factor-alpha
    • Geng YJ, Hellstrand K, Wennmalm A, and Hansson GK. Apoptotic death of human leukemic cells induced by vascular cells expressing nitric oxide synthase in response to gamma-interferon and tumor necrosis factor-alpha. Cancer Res 56: 866-874, 1996.
    • (1996) Cancer Res , vol.56 , pp. 866-874
    • Geng, Y.J.1    Hellstrand, K.2    Wennmalm, A.3    Hansson, G.K.4
  • 21
    • 0027093430 scopus 로고
    • The interaction of trolox C, a water-soluble vitamin E analog, with ferrylmyoglobin: Reduction of the oxoferryl moiety
    • Giulivi C, Romero FJ, and Cadenas E The interaction of trolox C, a water-soluble vitamin E analog, with ferrylmyoglobin: reduction of the oxoferryl moiety. Arch Biochem Biophys 299: 302-312, 1992.
    • (1992) Arch Biochem Biophys , vol.299 , pp. 302-312
    • Giulivi, C.1    Romero, F.J.2    Cadenas, E.3
  • 22
    • 0029069277 scopus 로고
    • Reduction of ferrylmyoglobin and ferrylhemoglobin by nitric oxide: A protective mechanism against ferryl hemoprotein-induced oxidations
    • Gorbunov NV, Osipov AN, Day BW, Zayas-Rivera B, Kagan VE, and Elsayed NM. Reduction of ferrylmyoglobin and ferrylhemoglobin by nitric oxide: a protective mechanism against ferryl hemoprotein-induced oxidations. Biochemistry 34: 6689-6699, 1995.
    • (1995) Biochemistry , vol.34 , pp. 6689-6699
    • Gorbunov, N.V.1    Osipov, A.N.2    Day, B.W.3    Zayas-Rivera, B.4    Kagan, V.E.5    Elsayed, N.M.6
  • 23
    • 0030998378 scopus 로고    scopus 로고
    • Nitric oxide prevents oxidative damage produced by tert-butyl hydroperoxide in erythroleukemia cells via nitrosylation of heme and non-heme iron. Electron paramagnetic resonance evidence
    • Gorbunov NV, Yalowich JC, Gaddam A, Thampatty P, Ritov VB, Kisin ER, Elsayed NM, and Kagan VE. Nitric oxide prevents oxidative damage produced by tert-butyl hydroperoxide in erythroleukemia cells via nitrosylation of heme and non-heme iron. Electron paramagnetic resonance evidence. J Biol Chem 272: 12328-12341, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 12328-12341
    • Gorbunov, N.V.1    Yalowich, J.C.2    Gaddam, A.3    Thampatty, P.4    Ritov, V.B.5    Kisin, E.R.6    Elsayed, N.M.7    Kagan, V.E.8
  • 24
    • 0032571099 scopus 로고    scopus 로고
    • Nitric oxide protects cardiomyocytes against tert-butyl hydroperoxide-induced formation of alkoxyl and peroxyl radicals and peroxidation of phosphatidylserine
    • Gorbunov NV, Tyurina YY, Salama G, Day BW, Claycamp HG, Argyros G, Elsayed NM, and Kagan VE. Nitric oxide protects cardiomyocytes against tert-butyl hydroperoxide-induced formation of alkoxyl and peroxyl radicals and peroxidation of phosphatidylserine. Biochem Biophys Res Commun 244: 647-651, 1998.
    • (1998) Biochem Biophys Res Commun , vol.244 , pp. 647-651
    • Gorbunov, N.V.1    Tyurina, Y.Y.2    Salama, G.3    Day, B.W.4    Claycamp, H.G.5    Argyros, G.6    Elsayed, N.M.7    Kagan, V.E.8
  • 25
    • 0034062553 scopus 로고    scopus 로고
    • A long-lived tyrosyl radical from the reaction between horse metmyoglobin and hydrogen peroxide
    • Gunther MR, Sturgeon BE, and Mason RP. A long-lived tyrosyl radical from the reaction between horse metmyoglobin and hydrogen peroxide. Free Radic Biol Med 28: 709-719, 2000.
    • (2000) Free Radic Biol Med , vol.28 , pp. 709-719
    • Gunther, M.R.1    Sturgeon, B.E.2    Mason, R.P.3
  • 26
    • 0029034338 scopus 로고
    • Characterization and expression of iron regulatory protein 2 (IRP2). Presence of multiple IRP2 transcripts regulated by intracellular iron levels
    • Guo B, Brown FM, Phillips JD, Yu Y, and Leibold EA. Characterization and expression of iron regulatory protein 2 (IRP2). Presence of multiple IRP2 transcripts regulated by intracellular iron levels. J Biol Chem 270: 16529-16535, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 16529-16535
    • Guo, B.1    Brown, F.M.2    Phillips, J.D.3    Yu, Y.4    Leibold, E.A.5
  • 27
    • 0021351203 scopus 로고
    • Oxygen toxicity, oxygen radicals, transition metals and disease
    • Halliwell B, and Gutteridge JM. Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem J 219: 1-14, 1984.
    • (1984) Biochem J , vol.219 , pp. 1-14
    • Halliwell, B.1    Gutteridge, J.M.2
  • 29
    • 0028360648 scopus 로고
    • Most free-radical injury is iron-related: It is promoted by iron, hemin, holoferritin and vitamin C, and inhibited by desferoxamine and apoferritin
    • Herbert V, Shaw S, Jayatilleke E, and Stopler-Kasdan T. Most free-radical injury is iron-related: it is promoted by iron, hemin, holoferritin and vitamin C, and inhibited by desferoxamine and apoferritin. Stem Cells 12: 289-303, 1994.
    • (1994) Stem Cells , vol.12 , pp. 289-303
    • Herbert, V.1    Shaw, S.2    Jayatilleke, E.3    Stopler-Kasdan, T.4
  • 30
    • 0028009430 scopus 로고
    • Mutational analysis of the [4Fe-4S]-cluster converting iron regulatory factor from its RNA-binding form to cytoplasmic aconitase
    • Hirling H, Henderson BR, and Kuhn LC. Mutational analysis of the [4Fe-4S]-cluster converting iron regulatory factor from its RNA-binding form to cytoplasmic aconitase. EMBO J 13: 453-461, 1994.
    • (1994) EMBO J , vol.13 , pp. 453-461
    • Hirling, H.1    Henderson, B.R.2    Kuhn, L.C.3
  • 31
    • 0027527402 scopus 로고
    • Inhibition of low-density lipoprotein oxidation by nitric oxide. Potential role in atherogenesis
    • Hogg N, Kalyanaraman B, Joseph J, Struck A, and Parthasarathy S. Inhibition of low-density lipoprotein oxidation by nitric oxide. Potential role in atherogenesis. FEBS Lett 334: 170-174, 1993.
    • (1993) FEBS Lett , vol.334 , pp. 170-174
    • Hogg, N.1    Kalyanaraman, B.2    Joseph, J.3    Struck, A.4    Parthasarathy, S.5
  • 33
    • 0026948804 scopus 로고
    • Interaction of hypochlorite with oxyhemoglobin leads to liberation of iron in a catalytically active form
    • Russian
    • Iakutova ES, Osipov AN, Kostenko OV, Arnkhol'd I, Arnol'd K, and Vladimirov IuA. Interaction of hypochlorite with oxyhemoglobin leads to liberation of iron in a catalytically active form. [Russian] Biofizika 37: 1021-1028, 1992.
    • (1992) Biofizika , vol.37 , pp. 1021-1028
    • Iakutova, E.S.1    Osipov, A.N.2    Kostenko, O.V.3    Arnkhol'd, I.4    Arnol'd, K.5    Vladimirov, Iu.A.6
  • 34
    • 0342603271 scopus 로고    scopus 로고
    • Generation of N-tert-butyl-alpha-phenylnitrone radical adducts in iron breakdown of tert-butyl-hydroperoxide
    • Iannone A, Tomasi A, and Canfield LM. Generation of N-tert-butyl-alpha-phenylnitrone radical adducts in iron breakdown of tert-butyl-hydroperoxide. Res Chem Intermed 22: 469-479, 1996.
    • (1996) Res Chem Intermed , vol.22 , pp. 469-479
    • Iannone, A.1    Tomasi, A.2    Canfield, L.M.3
  • 35
    • 0033080051 scopus 로고    scopus 로고
    • Myoglobin-induced oxidative damage: Evidence for radical transfer from oxidized myoglobin to other proteins and antioxidants
    • Irwin JA, Ostdal H, and Davies MJ. Myoglobin-induced oxidative damage: evidence for radical transfer from oxidized myoglobin to other proteins and antioxidants. Arch Biochem Biophys 362: 94-104, 1999.
    • (1999) Arch Biochem Biophys , vol.362 , pp. 94-104
    • Irwin, J.A.1    Ostdal, H.2    Davies, M.J.3
  • 36
    • 0017700831 scopus 로고
    • Low molecular weight intracellular iron transport compounds
    • Jacobs A. Low molecular weight intracellular iron transport compounds. Blood 50: 433-439, 1977.
    • (1977) Blood , vol.50 , pp. 433-439
    • Jacobs, A.1
  • 37
    • 0024593361 scopus 로고
    • Redox reactions associated with iron release from mammalian ferritin
    • Jacobs DL, Watt GD, Frankel RB, and Papaefthymiou GC. Redox reactions associated with iron release from mammalian ferritin. Biochemistry 28: 1650-1655, 1989.
    • (1989) Biochemistry , vol.28 , pp. 1650-1655
    • Jacobs, D.L.1    Watt, G.D.2    Frankel, R.B.3    Papaefthymiou, G.C.4
  • 39
    • 0031592750 scopus 로고    scopus 로고
    • Fragmentation of human Cu,Zn-superoxide dismutase by peroxidative reaction
    • Kang JH, and Kim SM. Fragmentation of human Cu,Zn-superoxide dismutase by peroxidative reaction. Mol Cells 7: 553-558, 1997.
    • (1997) Mol Cells , vol.7 , pp. 553-558
    • Kang, J.H.1    Kim, S.M.2
  • 41
    • 0032508548 scopus 로고    scopus 로고
    • Loops and bulge/loops in iron-responsive element isoforms influence iron regulatory protein binding. Fine-tuning of mRNA regulation?
    • Ke Y, Wu J, Leibold EA, Walden WE, and Theil EC. Loops and bulge/loops in iron-responsive element isoforms influence iron regulatory protein binding. Fine-tuning of mRNA regulation? J Biol Chem 273: 23637-23640, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 23637-23640
    • Ke, Y.1    Wu, J.2    Leibold, E.A.3    Walden, W.E.4    Theil, E.C.5
  • 43
    • 0034643867 scopus 로고    scopus 로고
    • Nitric oxide inhibition of free radical-mediated cholesterol peroxidation in liposomal membranes
    • Korytowski W, Zareba M, and Girotti AW. Nitric oxide inhibition of free radical-mediated cholesterol peroxidation in liposomal membranes. Biochemistry 39: 6918-6928, 2000.
    • (2000) Biochemistry , vol.39 , pp. 6918-6928
    • Korytowski, W.1    Zareba, M.2    Girotti, A.W.3
  • 44
    • 0024670323 scopus 로고
    • The measurement of the amount of iron (III) complexes with desferal in the perfused rat liver by an EPR method
    • Russian
    • Kozlov AV, Vladimirov IuA, and Azizova OA. The measurement of the amount of iron (III) complexes with desferal in the perfused rat liver by an EPR method. [Russian] Biull Eksp Biol Med 107: 577-579, 1989.
    • (1989) Biull Eksp Biol Med , vol.107 , pp. 577-579
    • Kozlov, A.V.1    Vladimirov, Iu.A.2    Azizova, O.A.3
  • 45
    • 0026755419 scopus 로고
    • Intracellular free iron in liver tissue and liver homogenate: Studies with electron paramagnetic resonance on the formation of paramagnetic complexes with desferal and nitric oxide
    • Kozlov AV, Yegorov DY, Vladimirov YA, and Azizova OA. Intracellular free iron in liver tissue and liver homogenate: studies with electron paramagnetic resonance on the formation of paramagnetic complexes with desferal and nitric oxide. Free Radic Biol Med 13: 9-16, 1992.
    • (1992) Free Radic Biol Med , vol.13 , pp. 9-16
    • Kozlov, A.V.1    Yegorov, D.Y.2    Vladimirov, Y.A.3    Azizova, O.A.4
  • 46
    • 0000767074 scopus 로고    scopus 로고
    • Role of the heme active site and protein environment, structure, spectra, and function of the cytochrome P450s
    • Loew GH, and Harris DL. Role of the heme active site and protein environment, structure, spectra, and function of the cytochrome P450s. Chem Rev 100:407-419, 2000
    • (2000) Chem Rev , vol.100 , pp. 407-419
    • Loew, G.H.1    Harris, D.L.2
  • 47
    • 0027366718 scopus 로고
    • Detection and reactions of the globin radical in hemoglobin
    • McArthur KM, and Davies MJ. Detection and reactions of the globin radical in hemoglobin. Biochim Biophys Acta 1202: 173-181, 1993.
    • (1993) Biochim Biophys Acta , vol.1202 , pp. 173-181
    • McArthur, K.M.1    Davies, M.J.2
  • 48
    • 0027342560 scopus 로고
    • Hydroxyl and alkoxyl radical production by oxidation products of metmyoglobin
    • Mehlhorn RJ, and Gomez J. Hydroxyl and alkoxyl radical production by oxidation products of metmyoglobin. Free Radic Res Commun 18: 29-41, 1993.
    • (1993) Free Radic Res Commun , vol.18 , pp. 29-41
    • Mehlhorn, R.J.1    Gomez, J.2
  • 49
    • 0031917173 scopus 로고    scopus 로고
    • Translational regulation of mRNAs with distinct IRE sequences by iron regulatory proteins 1 and 2
    • Menotti E, Henderson BR, and Kuhn LC. Translational regulation of mRNAs with distinct IRE sequences by iron regulatory proteins 1 and 2. J Biol Chem 273: 1821-1824, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 1821-1824
    • Menotti, E.1    Henderson, B.R.2    Kuhn, L.C.3
  • 51
    • 0033080372 scopus 로고    scopus 로고
    • Formation of long-lived radicals on proteins by radical transfer from heme enzymes - A common process?
    • Ostdal H, Andersen HJ, and Davies MJ. Formation of long-lived radicals on proteins by radical transfer from heme enzymes - a common process? Arch Biochem Biophys 362: 105-112, 1999.
    • (1999) Arch Biochem Biophys , vol.362 , pp. 105-112
    • Ostdal, H.1    Andersen, H.J.2    Davies, M.J.3
  • 52
    • 0028339363 scopus 로고
    • Release of iron from hemoglobin
    • Panter SS. Release of iron from hemoglobin. Methods Enzymol 231: 502-514, 1994.
    • (1994) Methods Enzymol , vol.231 , pp. 502-514
    • Panter, S.S.1
  • 53
    • 0028929741 scopus 로고
    • Nitric oxide signaling to iron-regulatory protein: Direct control of ferritin mRNA translation and transferrin receptor mRNA stability in transfected fibroblasts
    • Pantopoulos K, and Hentze MW. Nitric oxide signaling to iron-regulatory protein: direct control of ferritin mRNA translation and transferrin receptor mRNA stability in transfected fibroblasts. Proc Natl Acad Sci U S A 92: 1267-1271, 1995.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 1267-1271
    • Pantopoulos, K.1    Hentze, M.W.2
  • 54
    • 0030600134 scopus 로고    scopus 로고
    • Iron-sulphur clusters as genetic regulatory switches: The bifunctional iron regulatory protein-1
    • Paraskeva E, and Hentze MW. Iron-sulphur clusters as genetic regulatory switches: the bifunctional iron regulatory protein-1. FEES Lett 389: 40-43, 1996.
    • (1996) FEES Lett , vol.389 , pp. 40-43
    • Paraskeva, E.1    Hentze, M.W.2
  • 56
    • 0029763714 scopus 로고    scopus 로고
    • Inhibition of hemoglobin expression by heterologous production of nitric oxide synthase in the K562 erythroleukemic cell line
    • Rafferty SP, Domachowske JB, and Malech HL. Inhibition of hemoglobin expression by heterologous production of nitric oxide synthase in the K562 erythroleukemic cell line. Blood 88: 1070-1078,1996.
    • (1996) Blood , vol.88 , pp. 1070-1078
    • Rafferty, S.P.1    Domachowske, J.B.2    Malech, H.L.3
  • 57
    • 0026526023 scopus 로고
    • Ferritin as a source of iron for oxidative damage
    • Reif DW. Ferritin as a source of iron for oxidative damage. Free Radic Biol Med 12: 417-427, 1992.
    • (1992) Free Radic Biol Med , vol.12 , pp. 417-427
    • Reif, D.W.1
  • 58
    • 0031869315 scopus 로고    scopus 로고
    • Development of iron chelators to treat iron overload disease and their use as experimental tools to probe intracellular iron metabolism
    • Richardson DR, and Ponka P. Development of iron chelators to treat iron overload disease and their use as experimental tools to probe intracellular iron metabolism. Am J Hematol 58: 299-305, 1998.
    • (1998) Am J Hematol , vol.58 , pp. 299-305
    • Richardson, D.R.1    Ponka, P.2
  • 59
    • 0028325365 scopus 로고
    • Altered stability of etoposide-induced topoisomerase II-DNA complexes in resistant human leukemia K562 cells
    • Ritke MK, Roberts D, Allan WP, Raymond J, Bergottz W, and Yalowich JC. Altered stability of etoposide-induced topoisomerase II-DNA complexes in resistant human leukemia K562 cells. Br J Cancer 69: 687-697, 1994.
    • (1994) Br J Cancer , vol.69 , pp. 687-697
    • Ritke, M.K.1    Roberts, D.2    Allan, W.P.3    Raymond, J.4    Bergottz, W.5    Yalowich, J.C.6
  • 60
    • 0028151406 scopus 로고
    • Nitric oxide regulation of superoxide and peroxynitrite-dependent lipid peroxidation. Formation of novel nitrogen-containing oxidized lipid derivatives
    • Rubbo H, Radi R, Trujillo M, Telleri R, Kalyanaraman B, Barnes S, Kirk M, and Freeman BA. Nitric oxide regulation of superoxide and peroxynitrite-dependent lipid peroxidation. Formation of novel nitrogen-containing oxidized lipid derivatives. J Biol Chem 269: 26066-26075, 1994
    • (1994) J Biol Chem , vol.269 , pp. 26066-26075
    • Rubbo, H.1    Radi, R.2    Trujillo, M.3    Telleri, R.4    Kalyanaraman, B.5    Barnes, S.6    Kirk, M.7    Freeman, B.A.8
  • 61
    • 0028143071 scopus 로고
    • Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2. Structure, function, and post-translational regulation
    • Samaniego F, Chin J, Iwai K, Rouault TA, and Klausner RD. Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2. Structure, function, and post-translational regulation. J Biol Chem 269: 30904-30910, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 30904-30910
    • Samaniego, F.1    Chin, J.2    Iwai, K.3    Rouault, T.A.4    Klausner, R.D.5
  • 64
    • 0027104253 scopus 로고
    • Biochemistry of nitric oxide and its redox-activated forms
    • Stamler JS, Singel DJ, and Loscalzo J. Biochemistry of nitric oxide and its redox-activated forms. Science 258: 1898-1902, 1992.
    • (1992) Science , vol.258 , pp. 1898-1902
    • Stamler, J.S.1    Singel, D.J.2    Loscalzo, J.3
  • 65
    • 0028990048 scopus 로고
    • Reactions of reducing xenobiotics with oxymyoglobin. Formation of metmyoglobin, ferryl myoglobin and free radicals: An electron spin resonance and chemiluminescence study
    • Stolze K, and Nohl H. Reactions of reducing xenobiotics with oxymyoglobin. Formation of metmyoglobin, ferryl myoglobin and free radicals: an electron spin resonance and chemiluminescence study. Biochem Pharmacol 49: 1261-1267, 1995.
    • (1995) Biochem Pharmacol , vol.49 , pp. 1261-1267
    • Stolze, K.1    Nohl, H.2
  • 66
    • 0029864259 scopus 로고    scopus 로고
    • An EPR investigation of human methaemoglobin oxidation by hydrogen peroxide: Methods to quantify all paramagnetic species observed in the reaction
    • Svistunenko DA, Patel RP, and Wilson MT. An EPR investigation of human methaemoglobin oxidation by hydrogen peroxide: methods to quantify all paramagnetic species observed in the reaction. Free Radic Res 24: 269-280, 1996.
    • (1996) Free Radic Res , vol.24 , pp. 269-280
    • Svistunenko, D.A.1    Patel, R.P.2    Wilson, M.T.3
  • 67
    • 0000910313 scopus 로고
    • A possible model of a hemoprotein-hydrogen peroxide complex
    • Tajima K. A possible model of a hemoprotein-hydrogen peroxide complex. Inorg Chim Acta 163: 115-122, 1989.
    • (1989) Inorg Chim Acta , vol.163 , pp. 115-122
    • Tajima, K.1
  • 68
    • 0028114730 scopus 로고
    • Iron regulatory elements (IREs): A family of mRNA non-coding sequences
    • Theil EC. Iron regulatory elements (IREs): a family of mRNA non-coding sequences. Biochem J 304: 1-11, 1994.
    • (1994) Biochem J , vol.304 , pp. 1-11
    • Theil, E.C.1
  • 69
    • 0032878232 scopus 로고    scopus 로고
    • Iron-regulatory proteins, iron-responsive elements and ferritin mRNA translation
    • Thomson AM, Rogers JT, and Leedman PJ. Iron-regulatory proteins, iron-responsive elements and ferritin mRNA translation. Int J Biochem Cell Biol 31: 1139-1152, 1999.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 1139-1152
    • Thomson, A.M.1    Rogers, J.T.2    Leedman, P.J.3
  • 70
    • 0014312679 scopus 로고
    • Paramagnetic nitrosyl complexes of heme and nonheme iron
    • Russian
    • Vanin AF, and Chetverikov AG. Paramagnetic nitrosyl complexes of heme and nonheme iron. [Russian] Biofizika 13: 608-615, 1968.
    • (1968) Biofizika , vol.13 , pp. 608-615
    • Vanin, A.F.1    Chetverikov, A.G.2
  • 71
    • 0014132132 scopus 로고
    • EPR study of non-heme iron complexes in cells and tissues
    • Russian
    • Vanin AF, Bliumenfel'd LA, and Chetverikov AG. EPR study of non-heme iron complexes in cells and tissues. [Russian] Biofizika 12: 829-838, 1967.
    • (1967) Biofizika , vol.12 , pp. 829-838
    • Vanin, A.F.1    Bliumenfel'd, L.A.2    Chetverikov, A.G.3
  • 72
    • 0033578353 scopus 로고    scopus 로고
    • Mechanisms of nitric oxide protection against tert-butyl hydroperoxide-induced cytotoxicity in iNOS-transduced human erythroleukemia cells
    • Yalowich JC, Gorbunov NV, Kozlov AV, Allan W, and Kagan VE. Mechanisms of nitric oxide protection against tert-butyl hydroperoxide-induced cytotoxicity in iNOS-transduced human erythroleukemia cells. Biochemistry 38: 10691-10698, 1999.
    • (1999) Biochemistry , vol.38 , pp. 10691-10698
    • Yalowich, J.C.1    Gorbunov, N.V.2    Kozlov, A.V.3    Allan, W.4    Kagan, V.E.5


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