Potential Use of Iron Chelators against Oxidative Damage

Advances in Pharmacology

Volumn 38, Issue C, 1996, Pages 167-203

  Galey, Jean Baptiste ^a  

^a Department of Chemistry C'OREAL Research Center ^*  (France)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0006348848     PISSN: 10543589     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1054-3589(08)60984-9     Document Type: Article

References (141)

1. Adarnson G.M., and Harman A.W. Oxidative stress in cultured hepatocytes exposed to acetaminophen. Biochem. Pharmacol. 45 (1993) 2289-2294
2. Atamna H., and Ginsburg H. Heme degradation in the presence of glutathione. J. Biol. Chem. 270 (1995) 24876-24883
3. Aubailly M., Santus R., and Salmon S. Ferrous iron release from ferritin by ultraviolet-A radiations. Photochem. Photobiol. 54 (1991) 769-773
4. Basilion J.P., Rouault T.A., Massinople C.M., Klausner R.D., and Burgess W.H. The iron-responsive element-binding protein: Localization of the RNA-binding site to the aconitase active-site cleft. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 574-578
5. Behl C., Davis J.B., Lesley R., and Schubert D. Hydrogen peroxide mediates amyloid b protein toxicity. Cell 77 (1994) 817-827
6. Bergeron R.J., Wiegand J., Dionis J.B., Egli-Karmakka M., Frei J., Huxley-Tencer A., and Peter H.H. Evaluation of desferrithiocin and its synthetic analogues as orally effective iron chelators. J. Med. Chem. 34 (1991) 2072-2078
7. Biemond P., Swaak A.J.G., Beindorf C.M., and Koster J.F. Superoxide-dependent and independent mechanisms of iron mobilization from ferritin by xanthine oxidase. Biochem. J. 239 (1986) 169-173
8. Birnboim H.C. Effect of lipophilic chelators on oxyradical-induced DNA strand breaks in human granulocytes: paradoxical effect of 1,lO-phenantroline. Arch. Biochem. Biophys. 294 (1992) 17-21
9. Bissett D.L., Chatterjee R., and Hannon D.P. Chronic ultraviolet radiation-induced increase in skin iron and the photoprotective effect of topically applied iron chelators. Photochem. Photobiol. 54 (1991) 215-223
10. Blake R.R., Hall N.D., Bacon P.A., Dieppe P.A., Halliwell B., and Gutteridge J.M.G. Effect of a specific iron chelating agent on animal models of inflammation. Ann. Rheum. Dis. 42 (1983) 89-93
11. Bomford A., Isaac J., Roberts S., Edwards A., Young S., and Williams R. The effect of desferrioxamine on transferrin receptors, the cell cycle and growth rates of human leukaemic cells. Biochem. J. 236 (1986) 243-249
12. Borg D.C., and Schaich K. Prooxidant action of desferrioxamine: Fenton-like production of hydroxyl radicals by reduced ferrioxamine. J. Free Rad. Biol. Med. 2 (1986) 237-243
13. Bors W., and Saran M. Radical scavenging by flavonoi'd antioxidants. Free Rad. Res. Commun. 2 (1987) 289-294
14. Bosque M.A., Domingo J.L., and Corbella J. Assessment of the developmental toxicity of deferoxamine. Arch. Toxicol. 469 (1995) 467-471
15. Braughler J.M., Hall E.D., Jacobsen E.J., Mccall J.M., and Means E.D. The 21-aminosteroids: Potent inhibitors of lipid peroxidation for the treatment of central nervous system trauma and ischemia. Drugs Future 14 (1989) 143-152
16. Braughler J.M., Pregenzer J.F., Chase R.L., Duncan L.A., Jacobsen E.J., and Mccall J.M. Novel 21-amino steroids as potent inhibitors of iron dependent lipid peroxidation. J. Biol. Chem. 262 (1987) 10438-10440
17. Breuer W., Epsztejn S., and Cabantchik Z.I. Iron acquired from transferrin by K562 cells is delivered into a cytoplasmic pool of chelatable iron(II). J. Biol. Chem. 270 (1995) 24209-24215
18. Burkia M.J. ESR spin trapping studies into the nature of the oxidizing species formed in the Fenton reaction: Pitfalls associated with the use of 5,5-dimethyl-1-pyrroline-N-oxide in the detection of the hydroxyl radical. Free Rad. Res. Commun. 18 (1993) 43-57
19. Burkitt M.J., and Gilbert B.C. Model studies of the iron-catalysed Haber-Weiss cycle and the ascorbate-driven Fenton reaction. Free Rad. Res. Commun. 10 (1990) 265-280
20. Burkitt M.J., and Gilbert B.C. The autoxidation of iron(II) in aqueous systems: The effects of iron chelation by physiological, nonphysiological and therapeutic chelators on the generation of reactive oxygen species and the inducement of biomolecular damage. Free Rad. Res. Commun. 14 (1991) 107-123
21. Burkitt M.J., Milne L., Tsang S.Y., and Tam S.C. Calcium indicator dye Quin2 inhibits hydrogen peroxide-induced DNA strand break formation via chelation of iron. Arch. Biochem. Biophys. 311 (1994) 321-328
22. 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 (1995) 700-703
23. Cantoni O., Sestili P., Cattabeni F., Bellomo G., Pou S., Cohen M., and Cerutti P. Calcium chelator Quin 2 prevents hydrogen peroxide-induced DNA breakage and cytotoxicity. EUT. J. Biochem. 182 (1989) 209-212
24. Chevion M. A site-specific mechanism for free radical induced biological damage: The essential role of redox-active transition metals. Free Rad. Biol. Med. 5 (1988) 27-37
25. Crichton R.R. "Inorganic Biochemistry of Iron Metabolism" (1991), Elis Horwood, New York, London
26. Davies K.J.A., Sevanian A., Muakkassah-Kelly S.F., and Hochstein P. Uric acid-iron ion complexes: A new aspect of the antioxidant functions of uric acid. Biochem. J. 235 (1986) 747-754
27. Davies M.J., Donkor R., Duster C.A., Gee C.A., Jonas S., and Willson R.L. Desferrioxamine (desferal) and superoxide free radicals: Formation of an enzyme-damaging nitroxide. Biochem. J. 246 (1987) 725-729
28. Dawson R.M.C., Elliott D.C., Elliott W.H., and Jones K.M. "Data for Biochemical Research". 3rd Ed (1986), Clarendon Press, Oxford
29. Dean R.T., and Nicholson P. The action of nine chelators on iron-dependent radical damage. Free Rad. Res. 20 (1994) 83-101
30. Egan T.J., Barthakur S.R., and Aisen P. Catalysis of the Haber-Weiss reaction by iron-diethylenetriaminepentaacetate. J. Inorg. Biochem. 48 (1992) 241-249
31. Eisinger J., Shulman R.G., and Szymanski B.M. Transition metal binding in DNA solutions. J. Chem. Phys. 36 (1962) 1721-1729
32. Farber J.M., and Levine R.L. Sequence of a peptide susceptible to mixed-function oxidation: Probable cation binding site in glutamine synthetase. J. Biol. Chem. 261 (1986) 4574-4578
33. Ferrali M., Ciccoli L., and Comporti M. Allyl alcohol-induced hemolysis and its relation to iron release and lipid peroxidation. Biochem. Pharmacol. 38 (1989) 1819-1825
34. Ferrali M., Signorini C., Ciccoli L., and Comporti M. Iron release and membrane damage in erythrocytes exposed to oxidizing agents, phenylhydrazine, divicine and isoura-mil. Biochem. J. 285 (1992) 295-301
35. Fontecave M., and Pierre J.L. Iron: Metabolism, toxicity and therapy. Biochimie 75 (1993) 767-773
36. Fontecave M., and Pierre J.L. Fer et peroxyde d'hydrogkne: Aspects chimiques d'un probleme biologique fondamental. Bull. Soc. Chim. Fr. 130 (1993) 77-85
37. Fridovich I. Biological effects of the superoxide radical. Arch. Biochem. Biophys. 274 (1986) 1-11
38. Funk F., Lenders J.P., Crichton R.R., and Schneider W. Reductive mobilization of ferritin iron. Eur. J. Biochem. 152 (1985) 167-172
39. Galey J.-B., Dumats J., Beck I., Fernandez B., and Hocquaux M. N,N-Bis-dibenzyl ethylenediaminediacetic acid (DBED): A site specific hydroxyl radical scavenger acting as an "oxidative stress activatable iron chelator" in vitro. Free Rad. Res. 22 (1995) 67-86
40. Galey J.-B., Dumats J., Genard S., Destrke O., Pichaud P., Catroux P., Marrot L., Beck I., Fernandez B., Barre G., Seite M., Hussler G., and Hocquaw M. N,N'-Bis- (3,4,5-trimethoxybenzyl) ethylenediamine N,N'-diacetic acid as a new iron chelator with potential medicinal applications against oxidative stress. Biochem. Pharmacol. 91 (1996) 103-115
41. Ganeshaguru K., Lally J.M., Piga A., Hoffbrand A.V., and Kontoghiorghes G.J. Cytotoxic mechanisms of iron chelators. Drugs Today 28 Suppl. A (1992) 29-34
42. Gardner P.R., Raineri I., Epstein L.B., and White C.W. Superoxide radical and iron modulate aconitase activity in mammalian cells. J. Biol. Chem. 270 (1995) 13399-13405
43. Gerlach M., Ben-Schachar D., Riederer P., and Youdim M.B.H. Altered brain metabolism of iron as a cause of newodegenerative diseases. J. Neurochern. 63 (1994) 793-807
44. Gille J.J.P., Van Berkel C.G.M., and Joenje H. Effect of iron chelators on the cytotoxic and genotoxic action of hyperoxia in Chinese hamster ovary cells. Mutat. Res. 275 (1992) 31-39
45. Gordeuk V.R., Thuma P.E., and Brittenham G.M. Iron chelation therapy for malaria. In: Hershko C., et al. (Ed). "Progress in Iron Research" (1994), Plenum Press, New York 371-383
46. Grady R.W., and Hershko C. HBED: A potential oral iron chelator. Ann. N.Y. Acad. Sci. 612 (1990) 361-368
47. Grady R.W., Salbe A.D., Hilgartner M.W., and Giardina P.J. Results from a phase I clinical trial of HBED. In: Hershko C., et al. (Ed). "Progress in Iron Research" (1994), Plenum Press, New York 351-359
48. Graf E., Empson K.L., and Eaton J.W. Phytic acid: A natural antioxydant. J. Biol. Chem. 262 (1987) 11647-11650
49. Graf E., Mahoney J.R., Bryant R., and Eaton J.W. Iron-catalysed hydroxyl radical formation: Stringent requirement for free iron coordination site. J. Biol. Chem. 259 (1984) 3620-3624
50. Gutteridge J.M.C. Superoxide-dependent formation of hydroxyl radicals from ferric-complexes and hydrogen peroxide: An evaluation of fourteen iron chelators. Free Rad. Res. Commun. 9 (1990) 119-125
51. Gutteridge J.M.C., Richmond R., and Halliwell B. Inhibition of the iron-catalysed formation of hydroxyl radicals from superoxide and of lipid petoxidation by desferrioxa-mine. Biochem. J. 184 (1979) 469-472
52. Gutteridge J.M.C., Rowley D.A., and Halliwell B. Superoxide-dependent formation of hydroxyl radicals in the presence of iron salts: Detection of "free" iron in biological systems by using bleomycin-dependent degradation of DNA. Biochem. J. 199 (1981) 263-265
53. Hallaway P.E., Eaton J.W., Panter S.S., and Hedlund B.E. Modulation of deferoxamine toxicity and clearance by covalent attachment to biocompatible polymers. Proc. Natl. Auzd. Sci. U.S.A. 86 (1989) 10108-10112
54. Halliwell B. Use of desferrioxamine as a "probe" for iron-dependent formation of hydroxyl radicals. Biochem. Pharmacol. 34 (1985) 229-233
55. Halliwell B. Protection against tissue damage in vivo by desferrioxamine: What is its mechanism of action. J. Free Rad. Biol. Med. 7 (1989) 645-651
56. Halliwell B. How to characterize a biological antioxidant. Free Rad. Res. Commun. 9 (1990) 1-32
57. Halliwell B. Reactive oxygen species and the central nervous system. J. Neurochem. 59 (1992) 1609-1623
58. Halliwell B., and Gutteridge J.M.C. "Free Radicals in Biology and Medicine". 2nd Ed. (1989), Clarendon Press, Oxford
59. Halliwell B., Gutteridge J.M.C., and Cross C.E. Free radicals, antioxidants, and human disease: Where are we now. J. Lab. Clin. Med. 119 (1992) 598-620
60. Harris W.R., Carrano C.J., and Raymond K.N. Coordination chemistry of microbial iron transport compounds. 16. Isolation, characterisation, and formation constants of ferric aerobactin. J. Am. Chem. Soc. 101 (1979) 2722-2727
61. Hasinoff B.B. Pharmacodynamics of the hydrolysis-activation of the cardioprotective agent (+)-1,2-bis(3,5-dioxopiperazin-1-yl) propane. J. Pharm. Sci. 83 (1994) 64-67
62. Herschko C. Iron chelators in medicine. Mol. Aspects Med. 13 (1992) 113-165
63. Hider R.C., and Singh S. Iron chelating agents with clinical potential. Procs. Roy. Soc. Ed. 99B (1992) 137-168
64. Iuliano L., Pedersen J.Z., Ghiselli A., Pratico D., Rotilio G., and Violi F. Mechanism of reaction of a suggested superoxide-disrnutase mimic, Fe(H)-N,N,N',N'-tetrakis(2-pyridylmethyl)ethylenediamine. Arch. Biochem. Biophys. 293 (1992) 153-157
65. Jacobs D.J., Watt G.D., Frankel R.B., and Papaefthymiou G.C. Redox reactions associated with iron release from mammalian ferritin. Biochemistry 28 (1989) 1650-1655
66. Jovanovic S.V., Steenken S., Tosic M., Marjanovic M., and Sirnic M.G. Flavono'ids as antioxidants. J. Am. Chem. Soc. 116 (1994) 4846-4851
67. Keyse S.M., and Tyrrell R.M. Induction of the heme oxygenase gene in human skin fibroblasts by hydrogen peroxide and UV-A 365 nm radiation. Carcinogenesis 11 (1990) 787-791
68. Kiss Z. The zinc chelator, 1,lO-phenanthroline enhances the stimulatory effects of protein kinase C activators and staurosporine, but not sphingosine and H202, on phopholi-pase D activity in NIH 3T3 fibroblasts. Biochem. J. 298 (1994) 93-98
69. Klausner R.D., Rouault T.A., and Harford J.B. Regulating the fate of mRNA: The control of cellular iron metabolism. Cell 72 (1993) 19-28
70. Kohen R., and Chevion M. Paraquat toxicity is enhanced by iron and reduced by desferrioxamine in laboratory mice. Biochem. Pharmacol. 34 (1985) 1841-1843
71. Komara J.S., Nayini N.R., Bialik H.A., Indrien R.J., Evans A.T., Garritano A.M., Hoehner T.J., Jacobs W.A., Huang R.R., Krause G.S., White B.C., and Aust S.D. Brain iron delocalization and lipid peroxidation following cardiac arrest. Ann. Emerg. Med. 15 (1986) 384-389
72. Kontoghiorghes G.J. Comparative efficacy and toxicity of desferrioxamine, deferiprone and other iron and aluminium chelating drugs. Toxicol. Lett. 80 (1995) 1-18
73. Kontoghiorghes G.J., Jackson M.J., and Lunec J. In vitro screening of iron chelators using models of free radical damage. Free Rad. Res. Commun. 91 (1986) 115-124
74. Kozlov A.V., Yegorov D.Y., Vladimirov Y.A., and Azizova O.A. Intracellular free iron in liver tissue and liver homogenate: Studies with electron paramagnetic resonance on the formation of paramagnetic complexes with desferal with nitric oxide. Free Rad. Biol. Med. 13 (1992) 9-16
75. Kretchmar Nguyen S.A., Craig A., and Raymond K.N. Transferrin: The role of conformational changes in iron removal by chelators. J. Am. Chem. Soc. 115 (1993) 6758-6764
76. Laughton M.J., Moroney M.A., Hoult J.R.S., and Halliwell B. Effects of desferrioxamine on eicosanoid production in two intact cell systems. Biochem. Pharmacol. 38 (1989) 189-193
77. LaulhÈRe J.-P., and Fontecave M. Nitric oxide does not promote iron release from ferritin. BioMetals 9 (1996) 10-14
78. L'Eplattenier F., Murase I., and Martell A.E. New multidentate ligands. VI. Chelating tendencies of N,N'-Di(2-hydroxybenzyl)ethylenediamine-N,N'-diacetic acid. J. Am. Chem. Soc. 89 (1967) 837-843
79. Li J.L., Okada S., Hamazaki S., Ebina Y., and Midorikawa O. Subacute nephrotoxicity and induction of renal cell carcinoma in mice with ferric nitrilotriacetate. Cancer Res. 47 (1987) 1867-1869
80. Lind M.D., Hamor M.J., Hamor T.A., and Hoard J.L. Stereochemistry of ethylenediamine-tetraacetato complexes. Inorg. Chem. 3 (1964) 34-43
81. Liu M., and Okada S. Induction of free radicals and tumors in the kidney of Wistar rats by ferric ethylenediamine-N,N'-diacetic acid. Carcinogenesis 15 (1994) 2817-2821
82. Lloyd J.B., Cable H., and Rice-Evans C. Evidence that desferrioxarnine cannot enter cells by passive diffusion. Biochem. Pharmacol. 41 (1991) 1361-1363
83. Lytton S.D., Mester B., Libman J., Shanzer A., and Cabantchik Z.I. Monitoring of iron(III) removal from biological sources using a fluorescent siderophore. Anal. Biochem. 205 (1992) 326-333
84. Malisza K.L., and Hasinoff B.B. Doxorubicin reduces the iron(III) complexes of the hydrolysis products of the antioxidant cardioprotective agent dexrazoxane (ICRF-187) and produces hydroxyl radicals. Arch. Biochem. Biophys. 316 (1995) 680-688
85. In: Martell A.E., Anderson W.F., and Badman D.G. (Eds). "Development of Iron Chelators for Clinical Use" (1981), Elsevier North Holland, New York
86. Martell A.E., Motekaitis R.J., Murase I., Sala L.F., Stoldt R., and Ng C.Y. Development of iron chelators for Cooley's anemia. Inorgan. Chim. Acta. 138 (1987) 215-230
87. Mclachlan D.R.C., Dalton A.J., Kruck T.P.A., Bell M.Y., Smith W.L., Kallow W., and Andrews D.F. Intramuscular desferrioxamine in patients with Alzheimer's disease. Lancet 337 (1991) 1304-1308
88. Mazur A., Baez S., and Schorr E. The mechanism of iron release from ferritin as related to its biological properties. J. Biol. Chem. 213 (1955) 147-160
89. Mello Filho A.C., and Meneghini R. Protection of mammalian cells by o-phenanthroline from lethal and DNA-damaging effects produced by active oxygen species. Biochim. Biophys. Acta 847 (1985) 82-89
90. Mello Filho A.C., Hoffmann M.E., and Meneghini R. Cell killing and DNA damage by hydrogen peroxide are mediated by intracellular iron. Biochem. J. 218 (1984) 273-275
91. Miller D.M., Buettner G.R., and Aust S.D. Transition metals as catalysts of "autoxidation" reactions. Free Rad. Biol. Med. 8 (1990) 95-108
92. Miller M.J. Synthesis and therapeutic potential of hydroxamic base siderophores and analogues. Chem. Rev. 89 (1989) 1563-1579
93. Molenda J.J., Jones M.J., Cecil K.M., and Basinger M.A. Structure/activity relationships afffecting the ability of monoanionic 3-hydroxypyrid-4-ones to mobilize iron. Chem. Res. Toxicol. 7 (1994) 815-822
94. Morel I., Lescoat G., Cogrel P., Sergent O., Pasdeloup N., Brissot P., Cillard P., and Cillard J. Antioxidant and iron-chelating activities of the flavonoids catechin, quercetin, and diosmetin on iron-loaded rat hepatocyte culture. Biochem. Pharmacol. 45 (1993) 13-19
95. Murphy T.B., Rose N.J., Schomaker V., and Aruffo A. Synthesis of iron(III) aroyl hydrazones containing pyridoxal and salicyladehyde: The crystal and molecular structure of two iron(III)-pyridoxal isonicotinoyl hydrazone complexes. Inorgan. Chim. Acta 108 (1985) 183-194
96. Nagano T., Hirano T., and Hirobe M. Superoxide dismutase mimics based on iron in vivo. J. Biol. Chem. 264 (1989) 9243-9249
97. Nathan D.G. An orally active iron chelator. N. Engl. J. Med. 332 (1995) 953-954
98. Olanow C.W., and Arendash G.W. Metals and free radicals in neurodegeneration. Curr. Opin. Neurof. 7 (1994) 548-558
99. Olivieri N.F., Brittenham G.M., Matsui D., Berkovitch M., Blendis L.M., Cameron R.G., Mcclelland R.A., Liu P.P., Templeton D.M., and Koren G. Iron-chelation therapy with oral deferiprone in patients with thalassemia major. N. Engi. J. Med. 332 (1995) 918-922
100. Olszewer E., Sabbag F.C., and Carter J.P. A pilot double-blind study of sodium-magnesium EDTA in peripheral vascular disease. J. Natl. Med. Assoc. 82 (1990) 173-177
101. Osheroff K.M., Schaich K.M., Drew R.T., and Borg D.C. Failure of desferrioxamine to modify the toxicity of paraquat in rats. J. Free Rad. Biol. Med. 1 (1985) 71-82
102. Paller M.S., and Hedlund B.E. Extracellular iron chelators protect kidney cells from hypoxiaheoxygenation. Free Rad. Biol. Med. 17 (1994) 597-603
103. Pantopoulos K., and Hentze M.W. 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 (1995) 1267-1271
104. Pitt C.G., Bao Y., Thompson J., Wani M.C., Rosenkrantz H., and Metterville J. Esters and lactones of phenolic amino carboxylic acids: Prodrugs for iron chelation. J. Med. Chem. 29 (1986) 1231-1237
105. Polson R.J., Jawed A., Bomford A., Berry H., and Williams R. Treatment of rheumatoid arthritis with desferrioxamine: Relation between stores of iron before treatment and side effects. Br. Med. J. (Clin. Res. Ed.) 291 (1985) 448
106. Ponka P., Borova J., Neuwirt J., and Fuchs O. Mobilization of iron from reticulocytes; identification of pyridoxal isonicotinoyl hydrazones as a new iron chelating agent. FEBS Lett. 97 (1979) 317-321
107. Porter J.B., and Huens E.R. The toxic effects of desferrioxamine. Bailliere's Clin.Haematol. 2 (1989) 459-474
108. Porter J.B., Huens E.R., and Hider R.C. The development of iron chelating drugs. Bailliere's Clin. Haematol. 2 (1989) 257-292
109. Porter J.B., Singh S., Hoyes K.P., Epemolu O., Abeysinghe R.D., and Hider R.C. Lessons from preclinical and clinical studies with 1,2-diethyI-3-hydroxypyrid-4-one, CP94 and related compounds. In: Hershko C., et al. (Ed). "Progress in Iron Research" (1994), Plenum Press, New York 361-370
110. Reddy B.R., Kloner R.A., and Przyklenk K. Early treatment with deferoxamine limits myocardial ischemidreperfusion injury. Free Rad. Biol. Med. 7 (1989) 45-52
111. Reif D.W. Ferritin as a source of iron for oxidative damage. Free Rad. Biol. Med. 12 (1992) 417-427
112. Reif D.W., and Simmons R.D. Nitric oxide mediates iron release from ferritin. Arch. Biochem. Biophys. 283 (1990) 537-541
113. Rush J.D., and Koppenol W.H. Oxidizing intermediates in the reaction of ferrous EDTA with hydrogen peroxide. J. Biol. Chem. 261 (1986) 6730-6733
114. Ryan T.P., and Aust S.D. The role of iron in oxygen-mediated toxicities. Crit. Rev.Toxicol. 22 (1992) 119-141
115. Ryan T.P., and Petry T.W. The effects of 21-aminosteroids on the redox status of iron in solution. Arch. Biochem. Biophys. 300 (1993) 699-704
116. Sakaida S., Kyle M.E., and Farber J.L. Autophagic degradation of protein generates a pool of ferric iron required for the killing of cultured hepatocytes by an oxidative stress. Mol. Pharmacol. 37 (1990) 435-442
117. Samuni A., Aranovich J., Godinger D., Chevion M., and Czapski G. On the cytotoxicity of vitC and metal ions: A site specific mechanism. Eur. J. Biochem. 137 (1983) 119-124
118. SandstrÖM B.E., GranstrÖM M., and Marklund S.L. New roles for quinl: Powerful transition metal ion chelator that inhibits copper but potentiates iron-driven, Fenton-type reactions. Free Rad. Biol, Med. 16 (1994) 177-185
119. Singh S., and Hider R.C. Colorimetric detection of the hydroxyl radical: Comparison of the hydroxyl-radical-generating ability of various iron complexes. Anal. Biochem. 171 (1988) 47-54
120. Smith C., Mitchinson M.J., Aruoma O.I., and Halliwell B. Stimulation of lipid peroxidation and hydroxyl radical generation by the contents of human artherosclerotic lesions. Biochem. I. 286 (1992) 901-905
121. Smith J.B., Cusumano J.C., and Babbs C.F. Quantitative effects of iron chelators on hydroxyl radical production by the superoxide-driven Fenton reaction. Free Rad. Res. Commun. 8 (1990) 101-106
122. Stadtman E.R. Metal ion-catalysed oxidation of proteins: Biochemical mechanism and biological consequences. Free Rad. Biol. Med. 9 (1990) 315-325
123. Stadtman E.R. Protein oxidation and aging. Science 257 (1992) 1220-1224
124. Starke P.E., and Farber J.L. Ferric iron and superoxide ions are required for the killing of cultured hepatocytes by hydrogen peroxide. J. Biol. Chem. 260 (1985) 10099-10104
125. Stubbe J., and Kozarich J.W. Mechanisms of bleomycin-induced DNA degradation. Chem. Rev. 87 (1987) 1107-1136
126. Tachon P. Ferric and cupric ions requirement for DNA single-strand breakage by H202. Free Rad. Res. Commun. 7 (1989) 1-10
127. Taliaferro C.H., Motekaitis R.J., and Martell A.E. New multidentates ligands. 22. N,N'-Dipyridoxylethylenediamine-N,N'-diacetic acid: A new chelating ligand for trivalent metal ions. Inorg. Chem. 23 (1984) 1188-1192
128. Thomas C., Vile G.F., and Winterbourn C.C. The hydrolysis product of ICRF-187 promotes iron-catalysed hydroxyl radical production via the Fenton reaction. Biochem. Pharmacol. 45 (1993) 1967-1972
129. Thomas C.G., and Aust S.D. Reductive release of iron from ferritin by cation free radicals of paraquat and other bipyridyls. J. Biol. Chem. 261 (1986) 13064-13070
130. Toyokuni S., and Sagripanti J.L. Iron-mediated DNA damage: Sensitive detection of DNA strand breakage catalysed by iron. J. Inorg. Biochem. 47 (1992) 241-248
131. Trenam C.W., Blake D.R., and Morris C.J. Skin inflammation: Reactive oxygen species and the role of iron. J. Invest. Dermatol. 99 (1992) 675-682
132. Tsien R., Pozzan T., and Rink T.J. Calcium homeostasis in intact lymphocytes: Cytoplasmic free calcium monitored with a new, intracellularly trapped fluorescent indicator. J. Cell Biol. 94 (1982) 325-334
133. Van Der Kraaij A.M.M., Vaneijk H.G., and Koster J.F. Prevention of post ischemic cardiac injury by the orally active iron chelator 1,2-dimethyl-3-hydroxy-4-pyridone (Ll) and the antioxidant (+)-cyanidanol-3. Circulation 80 (1989) 158-164
134. Van Der Wal N.A.A., Van Oirschot J.F.L.M., Van Dijk A., Verhoef J., and Van Asbeck B.S. Mechanism of protection of alveolar type Il cells against paraquat-induced cytotoxicity by deferoxamine. Biochem. Pharmacol. 39 (1990) 1665-1671
135. Vile G.F., and Tyrrell R.M. Oxidative stress resulting from ultraviolet A irradiation of human skin fibroblasts leads to a heme oxygenase-dependent increase in ferritin. J. Biol. Chem. 268 (1993) 14678-14681
136. Voest E.E., Vreugdenhil G., and Marx J.J.M. Iron chelating agents in non-iron overload conditions. Ann. Intern. Med. 120 (1994) 490-499
137. Voogt A., Sluiter W., Van Eijk H.G., and Koster J.F. Low molecular weight iron and the oxygen paradox in isolated rat hearts. J. Clin. Invest. 90 (1992) 2050-2055
138. Ward R.J., Dexter D., Florence A., Aouad F., Hider R., Jenner P., and Crichton R.R. Brain iron in the ferrocene-loaded rat: Its chelation and influence on dopamine metabolism. Biochem. Pharmacol. 49 (1995) 1821-1826
139. Watt G.D., Frankel R.B., and Papaefthymiou G.C. Reduction of mammalian ferritin. Proc. Natl. Acad. Sci. U.S.A. 82 (1985) 3640-3643
140. Williams A., Hoy T., Pugh A., and Jacobs A. Pyridoxal complexes as potential chelating agents for oral therapy in transfusion iron overload. J. Pharm. Pharmacol. 34 (1982) 730-732
141. Yamazaki I., and Piette L.H. EPR spin-trapping study on the oxidizing species formed in the reaction of the ferrous ion with hydrogen peroxide. J. Am. Chem. Soc. 113 (1991) 7588-7593