Iron homeostasis and eye disease

Biochimica et Biophysica Acta - General Subjects

Volumn 1790, Issue 7, 2009, Pages 637-649

  Loh, Allison ^a   Hadziahmetovic, Majda ^a   Dunaief, Joshua L ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Chelator; Cornea; Iron; Lens; Oxidative stress; Retina

Indexed keywords

ALPHA TOCOPHEROL; ANTIOXIDANT; ASCORBIC ACID; BETA CAROTENE; DEFERASIROX; DEFEROXAMINE MESYLATE; FERROUS ION; HFE PROTEIN; IRON; IRON CHELATING AGENT; LACTOFERRIN; REACTIVE OXYGEN METABOLITE; SALICYLALDEHYDE ISONICOTINOYL HYDRAZONE; TRANSFERRIN RECEPTOR; UNCLASSIFIED DRUG; XANTHOPHYLL; ZEAXANTHIN; ZINC;

ALZHEIMER DISEASE; CATARACT; CATARACTOGENESIS; CLINICAL TRIAL; CONTINUOUS INFUSION; CORNEA DISEASE; DRUG MEGADOSE; EYE DISEASE; EYE PROTECTION; EYE TOXICITY; GLAUCOMA; HUMAN; IRON METABOLISM DISORDER; IRON OVERLOAD; IRON STORAGE; ISCHEMIC OPTIC NEUROPATHY; KERATOCONUS; LENS DISEASE; NONHUMAN; OPTIC NERVE DISEASE; OPTIC NEURITIS; OXIDATIVE STRESS; PARKINSON DISEASE; PRIORITY JOURNAL; PTERYGIUM; RETINA DISEASE; RETINA MACULA AGE RELATED DEGENERATION; REVIEW;

ANTIOXIDANTS; CATARACT; CORNEAL DISEASES; EYE DISEASES; HOMEOSTASIS; HUMANS; IRON; IRON CHELATING AGENTS; IRON OVERLOAD; KERATOCONUS; MACULAR DEGENERATION; OPTIC NERVE DISEASES; OPTIC NERVE INJURIES; PTERYGIUM; REACTIVE OXYGEN SPECIES;

EID: 67349135968     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2008.11.001     Document Type: Review

References (151)

1. Anderson G. Mechanisms of iron loading and toxicity. Am. J. Hepatol. 82 S12 (2007) 1128-1131
2. Wong R., et al. Iron toxicity as a potential factor in AMD. Retina 27 (2007) 997-1003
3. He X., et al. Iron homeostasis and toxicity in retinal degeneration. Prog. Retin. Eye Res. 26 (2007) 649-673
4. Fleming M.D., et al. Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene. Nat. Genet. 16 4 (1997) 383-386
5. Abboud S., and Haile D.J. A novel mammalian iron-regulated protein involved in intracellular iron metabolism. J. Biol. Chem. 275 26 (2000) 19906-19912
6. Burdo J.R., and Connor J.R. Brain iron uptake and homeostatic mechanisms: an overview. Biometals 16 1 (2003) 63-75
7. Dentchev T., Hahn P., and Dunaief J.L. Strong labeling for iron and the iron-handling proteins ferritin and ferroportin in the photoreceptor layer in age-related macular degeneration. Arch. Ophthalmol. 123 12 (2005) 1745-1746
8. Donovan A., et al. Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter. Nature 403 6771 (2000) 776-781
9. Yang F., et al. Iron increases expression of iron-export protein MTP1 in lung cells. Am. J. Physiol. Lung Cell. Mol. Physiol. 283 5 (2002) L932-939
10. Atanasiu V., Manolescu B., and Stoian I. Hepcidin - central regulator of iron metabolism. Eur. J. Haematol. 78 1 (2007) 1-10
11. Lesbordes-Brion J.C., et al. Targeted disruption of the hepcidin 1 gene results in severe hemochromatosis. Blood 108 (2006) 1402-1405
12. Nicolas G., et al. Severe iron deficiency anemia in transgenic mice expressing liver hepcidin. Proc. Natl. Acad. Sci. U. S. A. 99 7 (2002) 4596-4601
13. Aisen P., Enns C., and Wessling-Resnick M. Chemistry and biology of eukaryotic iron metabolism. Int. J. Biochem. Cell Biol. 33 (2001) 940-959
14. Goralska M., Holley B.L., and McGahan M.C. Overexpression of H- and L-ferritin subunits in lens epithelial cells: Fe metabolism and cellular response to UVB irradiation. Invest. Ophthalmol. Vis. Sci. 42 8 (2001) 1721-1727
15. Purves, D., et al., eds. Neuroscience. 1997.
16. Spector A. Oxidative stress-induced cataract: mechanism of action. FASEB J. 9 (1995) 1173-1182
17. Taylor V., et al. Morphology of the normal human lens. Invest. Ophthalmol. Vis. Sci. 37 (1996) 1396-1410
18. Goralska M., Holley B.L., and McGahan M.C. Identification of a mechanism by which lens epithelial cells limit accumulation of overexpressed ferritin H-chain. J. Biol. Chem. 278 Oct (2003) 42920-42926
19. Goralska M., et al. Differential degradation of ferritin H- and L-chains: accumulation of L-chain-rich ferritin in lens epithelial cells. Invest. Ophthalmol. Vis. Sci. 46 Oct (2005) 3521-3529
20. Lee W., et al. Mature cataract and lens-induced glaucoma associated with an asymptomatic intralenticular foreign body. J. Cataract Refract. Surg. 33 (2007) 550-552
21. Rozanowski B., et al. Human RPE melanosomes protect from photosensitized and iron-mediated oxidation but become pro-oxidant in the presence of iron upon photodegradation. Invest. Ophthalmol. Vis. Sci. 49 7 (2008) 2838-2847
22. Zarbin M.A. Current concepts in the pathogenesis of age-related macular degeneration. Arch. Ophthalmol. 122 4 (2004) 598-614
23. Dunaief J.L. Iron induced oxidative damage as a potential factor in age-related macular degeneration: the Cogan Lecture. Invest. Ophthalmol. Vis. Sci. 47 11 (2006) 4660-4664
24. Picard E., et al. The protective role of transferrin in Muller glial cells after iron-induced toxicity. Mol. Vis. 14 (2008) 928-941
25. Qi X., et al. Suppression of mitochondrial oxidative stress provides long-term neuroprotection in experimental optic neuritis. Invest. Ophthalmol. Vis. Sci. 48 2 (2007) 681-691
26. Abu-Amero K.K., and Bosley T.M. Increased relative mitochondrial DNA content in leucocytes of patients with NAION. Br. J. Ophthalmol. 90 (2006) 823-825
27. Levin L.A., and Geszvain K.M. Expression of ceruloplasmin in the retina: induction after optic nerve crush. Invest. Ophthalmol. Vis. Sci. 39 1 (1998) 157-163
28. Swanson K.I., et al. Neuroprotective effect of sulfhydryl reduction in a rat optic nerve crush model. Invest. Ophthalmol. Vis. Sci. 46 10 (2005) 3737-3741
29. Farkas R.H., et al. Increased expression of iron-regulating genes in monkey and human glaucoma. Invest. Ophthalmol. Vis. Sci. 45 5 (2004) 1410-1417
30. Ward P., Paz E., and Conneely O. Multifunctional roles of lactoferrin: a critical overview. Cell Mol. Life Sci. 62 (2005) 2540-2548
31. Levay P., and Viljoen M. Lactoferrin: a general review. Haematologica 80 (1995) 252-267
32. Kuizenga A., vanHaeringen N., and Kijlstra A. Inhibition of hydroxyl radical formation by human tears. Invest. Ophthalmol. Vis. Sci. 28 (1987) 305-313
33. Reitz C., et al. Analysis of tear proteins by one- and two-dimensional thin-layer iosoelectric focusing, sodium dodecyl sulfate electrophoresis and lectin blotting. Detection of a new component: cystatin C. Graefes Arch. Clin. Exp. Ophthalmol. 236 12 (1998) 894-899
34. Shimmura S., et al. Subthreshold UV radiation-induced peroxide formation in cultured corneal epithelial cells: the protective effects of lactoferrin. Exp. Eye Res. 63 (1996) 519-526
35. Ellison R. The effects of lactoferrin on Gram-negative bacteria. Adv. Exp. Med. Biol. 357 (1994) 71-90
36. Singh B., et al. A component of innate immunity prevents bacterial biofilm development. Nature 417 (2002) 552-555
37. Cai C., Birk D., and Linsenmayer T. Ferritin is a developmentally regulated nuclear protein of avian corneal epithelial cells. J. Biol. Chem. 272 19 (1997) 12831-12839
38. Millholland J., et al. Ferritoid, a tissue-specific nuclear transport protein for ferritin in corneal epithelial cells. J. Biol. Chem. 278 26 (2003) 23963-23970
39. McGuinnes R., and Knight-Jones D. Iron-containing corneal rust rings treated with desferrioxamine. Br. J. Ophthalmol. 52 10 (1968) 777-780
40. Galin M., Harris L., and Papariello G. Nonsurgical removal of corneal rust stains. Arch. Ophthalmol. 74 (1965) 674
41. Kymionis G., et al. Corneal iron ring after conductive keratoplasty. Am. J. Ophthalmol. 136 (2003) 378-379
42. Iwamoto T., and DeVoe G. Electron microscopical study of the Fleischer ring. Arch. Ophthalmol. 94 (1976) 1579-1583
43. Hiratsuka Y., Nakayasu K., and Kanai A. Secondary keratoconus with corneal epithelial iron ring similar to Fleischer's ring. Jpn. J. Ophthalmol. 44 4 (2000) 381-386
44. Riordan-Eva P., and Whitcher J. Vaughan & Asbury's General Ophthalmology. 17th ed. (2007)
45. Steinberg E., et al. Stellate iron lines in the corneal epithelium after radial keratotomy. Am. J. Ophthalmol. 98 (1984) 416-421
46. Koenig S.B., et al. Corneal iron lines after refractive keratoplasty. Arch. Ophthalmol. 101 12 (1983) 1862-1865
47. Assil K., et al. Corneal iron lines associated with the intrastromal corneal ring. Am. J. Ophthalmol. 116 3 (1993) 350-356
48. In: Tasman W., and EA J. (Eds). Duane's Clinical Ophthalmology Vol. 4 (1992), Lippincott-Raven, Philadelphia 1-53
49. Gass J. The iron lines of the superficial cornea. Arch. Ophthalmol. 71 (1964) 348-351
50. Prydal J., and Campbell F. Study of precorneal tear film thickness and structure by interferometry and confocal microscopy. Invest. Ophthalmol. Vis. Sci. 33 (1992) 1996
51. Norn M. Acta II. Aetiological studies. Ophthalmology 46 (1968) 119-128
52. Rose G., and Lavin M. The Hudson-Stähli Line III: observations on morphology, a critical review of aetiology and a unified theory for the formation of iron lines of the corneal epithelium. Eye 1 (1987) 475-479
53. Sureda A., et al. Extracellular H2O2 and not superoxide determines the compartment-specific activation of transferrin receptor by iron regulatory protein 1. Free Radic. Res. 39 8 (2005) 817-824
54. Every S., et al. Ultraviolet photography of the in vivo human cornea unmasks the Hudson-Stähli Line and physiologic vortex patterns. Invest. Ophthalmol. Vis. Sci. 46 10 (2005)
55. Rose G., and Lavin M. The Hudson-Stähli line I: an epidemiological study. Eye 1 (1987) 466-470
56. Holly F., and Lemp M. Tear physiology and dry eyes. Surv. Ophthalmol. 22 (1977) 69-87
57. Tseng S., and Tsubota K. Important concepts for treating ocular surface and tear disorders. Am. J. Ophthalmol. 124 825-835 (1997)
58. Yanoff, M., Ophthalmology. 2nd ed, ed. Yanoff, M., and J.S. Duker, 2004: Mosby Inc.
59. Nakamura S., et al. Involvement of oxidative stress on corneal epithelial alteration in blink-suppressed dry eye. Invest. Ophthalmol. Vis. Sci. 48 4 (2007) 1552-1558
60. Vitali C., Moutsopoulos H., and Bombardieri S. The European Community Study Group on diagnostic criteria for Sjögren's syndrome. Sensitivity and specificity of tests for ocular and oral involvement in Sjögren's syndrome. Ann. Rheum. Dis. 53 10 (1994) 637-647
61. Fujihara T., et al. Lactoferrin suppresses loss of corneal epithelial integrity in a rabbit short-term dry eye model. J. Ocul. Pharmacol. Ther. 14 (1998) 99-107
62. Dogru M., et al. Lactoferrin in Sjögren's Syndrome. Ophthalmology 114 12 (2007) 2366-2367
63. Lawless M., et al. Keratoconus: diagnosis and management. Aust. N. Z. J. Ophthalmol. 17 1 (1989) 33-60
64. Gay S., and Miller E. Collagen in the physiology and pathology of connective tissue (1978), Gustav Fisher Inc, New York 106
65. Cannon A., and Foster C. Collagen crosslinking in keratoconus. Invest. Ophthalmol. Vis. Sci. 17 (1978) 63-65
66. Foster C., Asar D., and Dohlman C. The Cornea: Scientific Foundation and Clinical Practice. 4th ed (2004)
67. Memarzadeh, F., et al., Comparison of de-epithelialized amniotic membrane transplantation and conjunctival autograft after primary pterygium excision. Eye, 2006. Jun: p. Epub ahead of print.
68. Khoo J., et al. Outdoor work and the risk of pterygia: a case-control study. Int. Ophthalmol. 22 5 (1998) 293-298
69. Moran D., and Hollows F. Pterygium and ultraviolet radiation: a positive correlation. Br. J. Ophthalmol. 68 5 (1984) 343-346
70. Taylor H., et al. Corneal changes associated with chronic UV irradiation. Arch. Ophthalmol. 107 10 (1989) 1481-1484
71. Mackenzie F., et al. Risk analysis in the development of pterygia. Ophthalmol 99 7 (1992) 1056-1061
72. Threlfall T., and English D. Sun exposure and pterygium of the eye: a dose-response curve. Am. J. Ophthalmol. 128 3 (1999) 280-287
73. Ferry A. A "new" iron line of the superficial cornea. Arch. Ophthalmol. 79 (1968) 142-145
74. Weinreb R., and Khaw P. Primary open-angle glaucoma. Lancet 363 9422 (2004) 1711-1720
75. Coats G. Two cases showing a small superficial opaque white ring in the cornea. Trans. Ophthal. Soc. U.K. 32 (1912) 53-56
76. Nevins R., and Elliott J. White ring of the cornea. Arch. Ophthalmol. 82 (1969) 457
77. Halmay O. Data concerning the origin of the white rings in the cornea. Br. J. Ophthalmol. 49 (1965) 87-92
78. Uyana Y. White ring of the cornea. Arch. Ophthalmol. 15 (1936) 309-311
79. Reinach N., and Baum J. A corneal pigmented line associated with Salzmann's nodular degeneration. Am. J. Ophthalmol. 91 (1981) 677
80. Germundsson J., and Fagerholm P. Phototherapeutic keratectomy in Salzmann's nodular degeneration. Acta Ophthalmol. Scand. 82 (2004) 148-153
81. Sujata D., Link B., and Seitz B. Salzmann's nodular degeneration of the cornea: a review and case series. Cornea 24 7 (2005) 772-777
82. Partridge E. Origins: Short Etymological Dictionary of Modern English (1977) 992
83. Stark W., Sommer A., and Smith R. Changing trends in intraocular lens implantation. Arch. Ophthalmol. 107 (1989) 1441-1444
84. West S. Does smoke get in your eyes?. JAMA 268 (1992) 1025
85. West S.K., et al. Exposure to sunlight and other risk factors for age-related macular degeneration. Arch. Ophthalmol. 107 6 (1989) 875-879
86. Bhuyan K., and Bhuyan D. Lipid peroxidation in cataract of the human. Life Sci. 38 1463-1471 (1986)
87. Zigler J., Huang Q., and Du X. Oxidative modification of lens crystallins by H2O2 and chelated iron. Free Radic. Biol. Med. 7 (1989) 499
88. Hope-Ross M., Mahon G., and Johnston P. Ocular siderosis. Eye 7 (1993) 419-425
89. Sneed S.R., and Weingeist T.A. Management of siderosis bulbi due to a retained iron-containing intraocular foreign body. Ophthalmology 97 3 (1990) 375-379
90. Girelli D., et al. Molecular basis for the recently described Hereditary Hyperferritinemia-Cataract Syndrome: a mutation in the Iron-responsive element of ferritin L-subunit gene (the "Verona" mutation). Blood 86 11 (1995) 4050-4053
91. Edwards C., and Kushner J. Screening for hemochromotosis. N. Engl. J. Med. 328 (1993) 1616
92. Mumford A., et al. The lens in hereditary hyperferritinaemia cataract syndrome contains crystallin deposits of L-ferritin. Br. J. Ophthalmol. 84 (2000) 697-700
93. Brooks D.G., et al. Ferritin crystal cataracts in hereditary hyperferritinemia cataract syndrome. Invest. Ophthalmol. Vis. Sci. 43 4 (2002) 1121-1126
94. Schichi, H., Microsomal electron. 1969.
95. Moiseyev G., et al. RPE65 is an iron(II)-dependent isomerohydrolase in the retinoid visual cycle. J. Biol. Chem. (2005)
96. Klein R., et al. The relationship of age-related maculopathy, cataract, and glaucoma to visual acuity. Invest. Ophthalmol. Vis. Sci. 36 1 (1995) 182-191
97. Beatty S., et al. The role of oxidative stress in the pathogenesis of age-related macular degeneration. Surv. Ophthalmol. 45 2 (2000) 115-134
98. AREDS. A randomized, placebo-controlled clinical trial of high-dose supplementation with vitamins C and E, beta carotene, and zinc for age-related macular degeneration and vision loss. Arch. Ophthalmol. 119 (2001) 1417-1436
99. Shen J., et al. Oxidative damage in age-related macular degeneration. Histol. Histopathol. 22 12 (2007) 1301-1308
100. Hageman G.S., et al. A common haplotype in the complement regulatory gene factor H (HF1/CFH) predisposes individuals to age-related macular degeneration. Proc. Natl. Acad. Sci. U. S. A. 102 20 (2005) 7227-7232
101. Klein R.J., et al. Complement factor H polymorphism in age-related macular degeneration. Science 308 5720 (2005) 385-389
102. Edwards A.O., et al. Complement factor H polymorphism and age-related macular degeneration. Science 308 5720 (2005) 421-424
103. Ganz T. Hepcidin and its role in regulating systemic iron metabolism. Hematology Am. Soc. Hematol. Educ. Program. (2006) 29-35
104. Hahn P., Milam A., and Dunaief J. Maculas affected by age-related macular degeneration contain increased chelatable iron in the retinal pigment epithelium and Bruch's membrane. Arch. Ophthalmol. 121 8 (2003) 1099-1105
105. Dunaief J.L., et al. Macular degeneration in a patient with aceruloplasminemia, a disease associated with retinal iron overload. Ophthalmology 112 6 (2005) 1062-1065
106. Hahn P., et al. Disruption of ceruloplasmin and hephaestin in mice causes retinal iron overload and retinal degeneration with features of age-related macular degeneration. Proc. Natl. Acad. Sci. U. S. A. 101 38 (2004) 13850-13855
107. Masciulli L., Anderson D.R., and Charles S. Experimental ocular siderosis in the squirrel monkey. Am. J. Ophthalmol. 74 4 (1972) 638-661
108. Declercq S.S., Meredith P.C., and Rosenthal A.R. Experimental siderosis in the rabbit: correlation between electroretinography and histopathology. Arch. Ophthalmol. 95 6 (1977) 1051-1058
109. Harris Z., Klomp L., and Gitlin J. Aceruloplasminemia: an inherited neurodegenerative disease with impairment of iron homeostasis. Am. J. Clin. Nutr. 65 5 Suppl (1998) 972S-977S
110. Beutler E. Hemochromatosis: genetics and pathophysiology. Annu. Rev. Med. 57 (2006) 331-347
111. Beutler E. Iron storage disease: facts, fiction and progress. Blood Cells Mol. Dis. 39 2 (2007) 140-147
112. Rouault T.A. Iron on the brain. Nat. Genet. 28 4 (2001) 299-300
113. Levin L.A., Clark J., and Johns L. Effect of lipid peroxidation inhibition on retinal ganglion cell death. Invest. Ophthalmol. Vis. Sci. 37 (1996) 2744-2749
114. Garcia-Valenzuela E., et al. Apoptosis in adult retinal ganglion cells after axotomy. J. Neurobiol. 25 (1994) 431-438
115. Nguyen S., Alexejun C., and Levin L. Amplification of a reactive oxygen species signal in axotomized retinal ganglion cells. Antioxid. Redox Signal. 5 (2003) 629-634
116. Lieven C., Vrabec J., and Levin L. The effects of oxidative stress on mitochondrial transmembrane potential in retinal ganglion cells. Antioxid. Redox Signal. 5 (2003) 641-646
117. Balcer L. Optic neuritis. N. Engl. J. Med. 354 (2006) 1273-1280
118. Guy J., Ellis E., and Mames R. Role of hydrogen peroxide in experimental optic neuritis: a serial quantitative ultrastructural study. Ophthalmic. Res. 25 (1993) 253-264
119. Guy J., McGorray S., and Fitzsimmons J. Disruption of the blood-brain barrier in experimental optic neuritis: immunocytochemical co-localization of H2O2 and extravasated serum albumin. Invest. Ophthalmol. Vis. Sci. 35 (1994) 1114-1123
120. Kalman B., and Leist T. A mitochondrial component of neurodegeneration in multiple sclerosis. Neuromol. Med. 3 (2003) 147-158
121. Wang Y., et al. Ischemia-reperfusion injury causes oxidative stress and apoptosis of Schwann cell in acute and chronic experimental diabetic neuropathy. Antioxid. Redox Signal. 7 11-12 (2005) 1513-1520
122. Szabo M., et al. Antioxidant properties of calcium dobesilate in ischemic/reperfused diabetic rat retina. Eur. J. Pharmacol. 428 2 (2001) 277-286
123. Qi X., et al. Use of mitochondrial antioxidant defenses for rescue of cells with a Leber hereditary optic neuropathy-causing mutation. Arch. Ophthalmol. 125 Feb (2007) 268-272
124. Danielson S., Wong A., and Carelli V. Cells bearing mutation causing Leber's hereditary optic neuropathy are sensitized to Fas-induced apoptosis. J. Biol. Chem. 277 (2002) 5810-5815
125. Klocker N., Cellerino A., and B.M. Free radical scavenging and inhibition of nitric oxide synthase potentiates the neurotrophic effects of brain-derived neurotrophic factor on axotomized retinal ganglion cells in vivo. J. Neurosci. 18 (1998) 1038-1046
126. Ko M., et al. The combined effect of brain-derived neurotrophic factor and a free radical scavenger in experimental glaucoma. Invest. Ophthalmol. Vis. Sci. 41 (2000) 2967-2971
127. Lee I., et al. p-Terphenyl curtisians protect cultured neuronal cells against glutamate neurotoxicity via iron chelation. Planta Med. 69 6 (2003) 513-517
128. Cheah J., et al. NMDA receptor-nitric oxide transmission mediates neuronal iron homeostasis via the GTPase Dexras1. Neuron 51 4 (2006) 431-440
129. Moreno M., et al. Retinal oxidative stress induced by high intraocular pressure. Free Radic. Biol. Med. 37 6 (2004) 803-812
130. Liu Q., et al. Oxidative stress is an early event in hydrostatic pressure-induced retinal ganglion cell damage. Invest. Ophthalmol. Vis. Sci. 48 10 (2007) 4580-4589
131. Tripathi R., et al. Quantitative and qualitative analyses of transferrin in aqueous humor from patients with primary and secondary glaucomas. Invest. Ophthalmol. Vis. Sci. 33 (1992) 2866-2873
132. AREDS. The relationship of dietary carotenoid and vitamin A, E, and C intake with age-related macular degeneration in a case-control study. Arch. Ophthalmol. 125 9 (2007) 1225-1232
133. Krinsky N., Landrum J., and Bone R. Biologic mechanisms of the protective role of lutein and zeaxanthin in the eye. Annu. Rev. Nutr. 23 (2003) 171-201
134. Reiter R. Functional pleiotropy of the neurohormone melatonin: antioxidant protection and neuroendocrine regulation. Front. Neuroendocrinol. 16 (1995) 383-415
135. Celebi S., et al. Effects of melatonin, vitamin E and octreotide on lipid peroxidation during ischemia-reperfusion in the guinea pig retina. Eur. J. Ophthalmol. 12 (2002) 77-83
136. Jacques P., et al. Long-term nutrient intake and 5-year change in nuclear lens opacities. Arch. Ophthalmol. 123 4 (2005) 517-526
137. Zheng H., et al. Design, synthesis, and evaluation of novel bifunctional iron-chelators as potential agents for neuroprotection in Alzheimer's, Parkinson's, and other neurodegenerative diseases. Bioorg. Med. Chem. 13 3 (2005) 773-783
138. Liu Z.D., et al. Design, synthesis, and evaluation of novel 2-substituted 3-hydroxypyridin-4-ones: structure-activity investigation of metalloenzyme inhibition by iron chelators. J. Med. Chem. 45 3 (2002) 631-639
139. Kalinowski D.S., and Richardson D.R. The evolution of iron chelators for the treatment of iron overload disease and cancer. Pharmacol. Rev. 57 4 (2005) 547-583
140. Neufeld E. Oral chelators deferasirox and deferiprone for transfusional iron overload in thalassemia major: new data, new questions. Blood 107 9 (2006) 3436-3441
141. Allain P., et al. Pharmacokinetics and renal elimination of desferrioxamine and ferrioxamine in healthy subjects and patients with haemochromatosis. Br. J. Clin. Pharmacol. 24 (1987) 207-212
142. Harmatz P., et al. Phase Ib clinical trial of starch-conjugated deferoxamine (40SD02): a novel long-acting iron chelator. Br. J. Haematol. 138 3 (2007) 374-381
143. Lu M., et al. Effects of desferoxamine on retinal and visual function. Arch. Ophthalmol. 125 11 (2007) 1581-1582
144. Charkoudian L., Pham D., and Franz K. A pro-chelator triggered by hydrogen peroxide inhibits iron-promoted hydroxyl radical formation. J. Am. Chem. Soc. 128 38 (2006) 12424-12425
145. Glickstein H., et al. Intracellular labile iron pools as direct targets of iron chelators: a fluorescence study of chelator action in living cells. Blood 106 9 (2005) 3242-3250
146. Horackova M., Ponka P., and Byczko Z. The antioxidant effects of a novel iron chelator salicylaldehyde isonicotinoyl hydrazone in the prevention of H(2)O(2) injury in adult cardiomyocytes. Cardiovasc. Res. 47 3 (2000) 529-536
147. Simunek T., et al. SIH-a novel lipophilic iron chelator-protects H9c2 cardiomyoblasts from oxidative stress-induced mitochondrial injury and cell death. J. Mol. Cell. Cardiol. 39 2 (2005) 345-354
148. Klimtova I., et al. A study of potential toxic effects after repeated 10-week administration of a new iron chelator-salicylaldehyde isonicotinoyl hydrazone (SIH) to rabbits. Acta Med. (Hradec Kralove) 46 4 (2003) 163-170
149. Amado D., et al. The iron chelator SIH is effective in protecting retinal pigment epithelial cells against oxidative damage. Invest. Ophthalmol. Vis. Sci 47 (2006) E-Abstract 2081
150. Tuomainen T.P., et al. Association between body iron stores and the risk of acute myocardial infarction in men. Circulation 97 15 (1999) 1461-1466
151. Tuomainen T.P., et al. Cohort study of relation between donating blood and risk of myocardial infarction in 2682 men in eastern Finland. BMJ 314 7083 (1997) 793-794