Reorganizing Metals: The Use of Chelating Compounds as Potential Therapies for Metal-Related Neurodegenerative Disease

Current Topics in Medicinal Chemistry

Volumn 11, Issue 5, 2011, Pages 543-552

  Badrick, Alison C ^a   Jones, Christopher E ^a,b  

^a Center for Metals in Biology   (Australia)

^b UNIVERSITY OF QUEENSLAND   (Australia)

Author keywords

Alzheimer's; Chelator; Copper; Iron; Neurodegeneration; Parkinson's; Prion; Redox

Indexed keywords

2,2' BIQUINOLINE; ACETYLCYSTEINE AMIDE; ALUMINUM; CHELATING AGENT; CIMETIDINE; CLIOQUINOL; COPPER; DEFEROXAMINE MESYLATE; DP 109; EPIGALLOCATECHIN GALLATE; ETOXAZENE; EUK 189; EUK 207; IRON; JKL 1291; JKL 169; MEPACRINE; METAL COMPLEX; METAL ION; PENICILLAMINE; PRION PROTEIN; REACTIVE OXYGEN METABOLITE; THIOSEMICARBAZONE; UNCLASSIFIED DRUG; ZINC;

ALZHEIMER DISEASE; AMYLOID NEUROPATHY; ARTICLE; COPPER DEFICIENCY; CREUTZFELDT JAKOB DISEASE; DEGENERATIVE DISEASE; DRUG BINDING; DRUG BIOAVAILABILITY; DRUG WITHDRAWAL; FATAL FAMILIAL INSOMNIA; HUMAN; INTESTINE INFECTION; OXIDATIVE STRESS; PARKINSON DISEASE; PEPTIC ULCER; PROTEIN FOLDING; PROTEIN FUNCTION; REDOX STRESS; RHEUMATOID ARTHRITIS; SIDE EFFECT; STRUCTURE ACTIVITY RELATION; WILSON DISEASE;

ANIMALS; CHELATING AGENTS; CHELATION THERAPY; HUMANS; METALS; NEURODEGENERATIVE DISEASES; ORGANOMETALLIC COMPOUNDS;

EID: 79952763943     PISSN: 15680266     EISSN: None     Source Type: Journal    
DOI: 10.2174/156802611794785181     Document Type: Article

References (152)

1. Rambaran, R.N.; Serpell, L.C. Amyloid fibrils: abnormal protein assembly. Prion, 2008, 2, 112-117.
2. Pedersen, J.S.; Otzen, D.E. Amyloid - a state in many guises: Survival of the fittest fibril fold. Protein Sci., 2008, 17, 2-10.
3. Walsh, D.M.; Klyubin, I.; Fadeeva, J.V.; Cullen, W.K.; Anwyl, R.; Wolfe, M.S.; Rowan, M.J.; Selkoe, D.J. Naturally secreted oligomers of amyloid b protein potently inhibit hippocampal long term potentiation in vivo. Nature, 2002, 416, 535-539.
4. Lesne, S.; Koh, M.T.; Kotilinek, L.; Kayed, R.; Glabe, C.G.; Yang, A.; Gallagher, M.; Ashe, K.H. A specific amyloid-β protein assembly in the brain impairs memory. Nature, 2006, 440, 352-357.
5. Treusch, S.; Cyr, D.M.; Lindquist, S. Amyloid deposits: Protection against toxic protein species? Cell Cycle, 2009, 8, 1668-1674.
6. Nicolas, O.; Gavin, R.; del Rio, J.A. New insights into cellular prion protein (PrPc) functions: The ying and yang of a relevant protein. Brain Res. Rev., 2009, 61, 170-184.
7. Thinakaran, G.; Koo, E.H. Amyloid precursor protein trafficking, processing, and function. J. Biol. Chem., 2008, 283, 29615-29619.
8. Bisaglia, M.; Mammi, S.; Bubacco, L. Structural insights on physiological functions and pathological effects of α-synuclein. FASEB J., 2009, 23, 329-340.
9. Suazo, M.; Hodar, C.; Morgan, C.; Cerpa, W.; Cambiazo, V.; Ine-strosa, N.C.; Gonzalez, M. Overexpression of amyloid precursor protein increases copper content in HEK293 cells. Biochem. Biophys. Res. Commun., 2009, 382, 740-744.
10. Smith, D.G.; Cappai, R.; Barnham, K. J. The redox chemistry of the Alzheimer's disease amyloid-β peptide. BBA-Biomembranes, 2007, 1768, 1976-1990.
11. Lu, K.; Jacob, J.; Thiyagarajan, P.; Conticello, V.P.; Lynn, D.G. Exploiting amyloid fibril lamination for nanotube self-assembly. J. Am. Chem. Soc., 2003, 125, 6391-6393.
12. Bush, A. I. The metallobiology of Alzheimer's disease. Trends Neurosci., 2003, 26, 207-214.
13. Cherny, R. A.; Barnham, K. J.; Lynch, T.; Volitakis, I.; Li, Q. X.; McLean, C.A.; Multhaup, G.; Beyreuher, K.; Tanzi, R. E.; Masters, C. L.; Bush, A. I. Chelation and intercalation: complementary properties in a compound for the treatment of Alzheimer's disease. J. Struct. Biol., 2000, 130, 209-216.
14. Atwood, C. S.; Perry, G.; Zeng, H.; Kato, Y.; Jones, W. D.; Ling, K.Q.; Huang, X. D.; Moir, R. D.; Wang, D. D.; Sayre, L. M.; Smith, M. A.; Chen, S.G.; Bush, A.I. Copper mediates dityrosine cross-linking of Alzheimer's amyloid-β. Biochemistry, 2004, 43, 560-568.
15. Barnham, K. J.; Bush, A. I. Metals in Alzheimer's and Parkinson's diseases. Curr. Opin. Chem. Biol., 2008, 12, 222-228.
16. Curtain, C. C.; Ali, F.; Volitakis, I.; Cherny, R. A.; Norton, R. S.; Beyreuther, K.; Barrow, C. J.; Masters, C. L.; Bush, A. I.; Barnham, K. J. Alzheimer's disease amyloid-β binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits. J. Biol. Chem., 2001, 276, 20466-20473.
17. Guilloreau, L.; Combalbert, S.; Sournia-Saquet, A.; Mazarguil, H.; Faller, P. Redox chemistry of copper-amyloid-β: the generation of hydroxyl radical in the presence of ascorbate is linked to redox-potentials and aggregation state. ChemBioChem, 2007, 8, 1317-1325.
18. Huang, X.; Atwood, C. S.; Hartshorn, M. A.; Multhaup, G.; Gold-stein, L. E.; Scarpa, R.C.; Cuajungco, M. P.; Gray, D. N.; Lim, J.; Moir, R. D.; Tanzi, R. E.; Bush, A. I. The A peptide of Alzheimer's disease directly produces hydrogen peroxide through metal ion reduction. Biochemistry, 1999, 38, 7609-7616.
19. Atwood, C. S.; Scarpa, R. C.; Huang, X. D.; Moir, R. D.; Jones, W. D.; Fairlie, D. P.; Tanzi, R. E.; Bush, A. I. Characterization of copper interactions with Alzheimer amyloid-β peptides: Identification of an attomolar-affinity copper binding site on amyloid b1-42. J. Neurochem., 2000, 75, 1219-1233.
20. Szegedi, V.; Juhasz, G.; Rozsa, E.; Juhasz-Vedres, G.; Datki, Z.; Fulop, L.; Bozso, Z.; Lakatos, A.; Laczko, I.; Farkas, T.; Kis, Z.; Toth, G.; Soos, K.; Zarandi, M.; Denes, B.; Toldi, J.; Penke, B. Endomorphin-2, an endogenous tetrapeptide, protects against Ab1-42 in vitro and in vivo. FASEB J., 2006, 20, 1191-1193.
21. Binder, L. I.; Guillozet-Bongaarts, A. L.; Garcia-Sierra, F.; Berry, R.W. Tau, tangles, and Alzheimer's disease. BBA-Mol. Basis Dis., 2005, 1739, 216-223.
22. Mazanetz, M. P.; Fischer, P. M. Untangling tau hyperphosphorylation in drug design for neurodegenerative diseases. Nat. Rev. Drug Discov., 2007, 6, 464-479.
23. Linden, R.; Martins, V. R.; Prado, M. A. M.; Cammarota, M.; Izquierdo, I.; Brentani, R.R. Physiology of the prion protein. Physiol. Rev., 2008, 88, 673-728.
24. Bueler, H.; Fischer, M.; Lang, Y.; Bluethmann, H.; Lipp, H. P.; Dearmond, S.J.; Prusiner, S.B.; Aguet, M.; Weissmann, C. Normal development and behavior of mice lacking the neuronal cellsurface PrP protein. Nature, 1992, 356, 577-582.
25. Aguzzi, A.; Baumann, F.; Bremer, J. The prion's elusive reason for being. Annu. Rev. Neurosci., 2008, 31, 439-477.
26. Haraguchi, T.; Fisher, S.; Olofsson, S.; Endo, T.; Groth, D.; Tarentino, A.; Borchelt, D.R.; Teplow, D.; Hood, L.; Burlingame, A.; Lycke, E.; Kobata, A.; Prusiner, S.B. Asparagine-linked glycosylation of the scrapie and cellular prion proteins. Arch. Biochem. Biophys., 1989, 274, 1-13.
27. Watt, N. T.; Hooper, N. M. Reactive oxygen species (ROS)mediated β-cleavage of the prion protein in the mechanism of the cellular response to oxidative stress. Biochem. Soc. Trans., 2005, 33, 1123-1125.
28. Hooper, N. M. Roles of proteolysis and lipid rafts in the processing of the amyloid precursor protein and prion protein. Biochem. Soc. Trans., 2005, 33, 335-338.
29. Lauren, J.; Gimbel, D.A.; Nygaard, H. B.; Gilbert, J. W.; Strittmatter, S. M. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers. Nature, 2009, 457, 1128-U1184.
30. Balducci, C.; Beeg, M.; Stravalaci, M.; Bastone, A.; Sclip, A.; Biasini, E.; Tapella, L.; Colombo, L.; Manzoni, C.; Borsello, T.; Chiesa, R.; Gobbi, M.; Salmona, M.; Forloni, G. Synthetic amyloid-{beta} oligomers impair long-term memory independently of cellular prion protein. Proc. Natl. Acad. Sci. USA, 2010, 107, 2295-2300.
31. Spillantini, M.G.; Schmidt, M. L.; Lee, V. M. Y.; Trojanowski, J. Q.; Jakes, R.; Goedert, M.α-synuclein in Lewy bodies. Nature, 1997, 388, 839-840.
32. Snyder, A.M.; Connor, J. R. Iron, the substantia nigra and related neurological disorders. BBA-Gen. Subjects, 2009, 1790, 606-614.
33. Bartzokis, G.; Sultzer, D.; Cummings, J.; Holt, L.E.; Hance, D. B.; Henderson, V.W.; Mintz, J. In vivo evaluation of brain iron in Alzheimer disease using magnetic resonance imaging. Arch. Gen. Psychiat., 2000, 57, 47-53.
34. Rhodes, S.L.; Ritz, B. Genetics of iron regulation and the possible role of iron in Parkinson's disease. Neurobiol. Dis., 2008, 32, 183-195.
35. Cooper, A.A.; Gitler, A.D.; Cashikar, A.; Haynes, C. M.; Hill, K. J.; Bhullar, B.; Liu, K. N.; Xu, K. X.; Strathearn, K. E.; Liu, F.; Cao, S. S.; Caldwell, K. A.; Caldwell, G. A.; Marsischky, G.; Kolodner, R.D.; LaBaer, J.; Rochet, J.C.; Bonini, N.M.; Lindquist, S.α-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models. Science, 2006, 313, 324-328.
36. Larsen, K.E.; Schmitz, Y.; Troyer, M.D.; Mosharov, E.; Dietrich, P.; Quazi, A.Z.; Savalle, M.; Nemani, V.; Chaudhry, F.A.; Edwards, R.H.; Stefanis, L.; Sulzer, D. α-synuclein overexpression in PC12 and chromaffin cells impairs catecholamine release by interfering with a late step in exocytosis. J. Neurosci., 2006, 26, 11915-11922.
37. Brown, D.R. Interactions between metals and α-synuclein - function or artefact? FEBS J., 2007, 274, 3766-3774.
38. Frederickson, C.J.; Koh, J.Y.; Bush, A.I. The neurobiology of zinc in health and disease. Nat. Rev. Neurosci., 2005, 6, 449-462.
39. Linkous, D.H.; Flinn, J.M.; Koh, J.Y.; Lanzirotti, A.; Bertsch, P.M.; Jones, B.F.; Giblin, L.J.; Frederickson, C.J. Evidence that the ZNT3 protein controls the total amount of elemental zinc in synaptic vesicles. J. Hisstochem. Cytochem., 2008, 56, 3-6.
40. Palmiter, R.D.; Cole, T.B.; Quaife, C.J.; Findley, S.D. ZnT-3, a putative transporter of zinc into synaptic vesicles. Proc. Natl. Acad. Sci. USA, 1996, 93, 14934-14939.
41. Frederickson, C.J. Neurobiology of zinc and zinc-containing neurons. Int. Rev. Neurobiol., 1989, 31, 145-238.
42. Birinyi, A.; Parker, D.; Antal, M.; Shupliakov, O. Zinc co-localizes with GABA and glycine in synapses in the lamprey spinal cord. J. Comp. Neurol., 2001, 433, 208-221.
43. Prohaska, J.R. Functions of trace elements in brain metabolism. Physiol. Rev., 1987, 67, 858-901.
44. Waggoner, D.J.; Drisaldi, B.; Bartnikas, T.B.; Casareno, R.L.B.; Prohaska, J.R.; Gitlin, J.D.; Harris, D.A. Brain copper content and cuproenzyme activity do not vary with prion protein expression level. J. Biol. Chem., 2000, 275, 7455-7458.
45. Kardos, J.; Kovács, I.; Hajós, F.; Kálmán, M.; Simonyi, M. Nerve endings from rat brain tissue release copper upon depolarization. A possible role in regulating neuronal excitability. Neurosci. Lett., 1989, 103, 139-144.
46. Hopt, A.; Korte, S.; Fink, H.; Panne, U.; Niessner, R.; Jahn, R.; Kretzchmar, H.; Herms, J. Methods for studying synaptosomal copper release. J. Neurosci. Methods, 2003, 128, 159-172.
47. Takeda, A.; Minami, A.; Seki, Y.; Oku, N. Differential effects of zinc on glutamatergic and GABAergic neurotransmitter systems in the hippocampus. J. Neurosci. Res., 2004, 75, 225-229.
48. Huidobro-Toro, J.P.; Lorca, R.A.; Coddou, C. Trace metals in the brain: allosteric modulators of ligand-gated receptor channels, the case of ATP-gated P2X receptors. Eur. Biophys. J., 2008, 37, 301-314.
49. Badrick, A. C.; Jones, C. E. In: Horizons in Neuroscience Research, Costa, A.; Villalba, E. Eds.; Nova Publishers: New York, In Press; Vol. 2.
50. Millhauser, G. L. Copper and the prion protein: Methods, structures, function, and disease. Annu. Rev. Phys. Chem., 2007, 58, 299-320.
51. 111 induces -βsheet formation in the unstructured amyloidogenic region of the prion protein. J. Biol. Chem., 2004, 279, 32018-32027.
52. Rebec, G. V.; Witowski, S. R.; Sandstrom, M. I.; Rostand, R. D.; Kennedy, R.T. Extracellular ascorbate modulates cortically evoked glutamate dynamics in rat striatum. Neurosci. Lett., 2005, 378, 166-170.
53. Minich, T.; Riemer, J.; Schulz, J.B.; Wielinga, P.; Wijnholds, J.; Dringen, R. The multidrug resistance protein 1 (Mrp1), but not Mrp5, mediates export of glutathione and glutathione disulfide from brain astrocytes. J. Neurochem., 2006, 97, 373-384.
54. Erecinska, M.; Silver, I. A. Tissue oxygen tension and brain sensitivity to hypoxia. Resp. Physiol., 2001, 128, 263-276.
55. Schlief, M. L.; Gitlin, J. D. Copper homeostasis in the CNS: a novel link between the NMDA receptor and copper homeostasis in the hippocampus. Mol. Neurobiol., 2006, 33, 81-90.
56. Takeda, A. Analysis of brain function and prevention of brain diseases: the action of trace metals. J. Health Sci., 2004, 50, 429-442.
57. Ke, Y.; Qian, Z. M. Brain iron metabolism: Neurobiology and neurochemistry. Prog. Neurobiol., 2007, 83, 149-173.
58. Moos, T.; Morgan, E. H. Transferrin and transferrin receptor function in brain barrier systems. Cell Mol. Neurobiol., 2000, 20, 77-95.
59. ] Zhao, Z. S.; Khan, S.; O'Brien, P. J. Catecholic iron complexes ascytoprotective superoxide scavengers against hypoxia: reoxygenation injury in isolated hepatocytes. Biochem. Pharmacol., 1998, 56, 825-830.
60. Smythies, J. Redox mechanisms at the glutamate synapse and their significance: a review. Eur. J. Pharmacol., 1999, 370, 1-7.
61. Thompson, K. J.; Shoham, S.; Connor, J. R. Iron and neurodegen erative disorders. Brain Res. Bull., 2001, 55, 155-164.
62. Kaur, D.; Lee, D.; Ragapolan, S.; Andersen, J. K. Glutathione depletion in immortalized midbrain-derived dopaminergic neurons results in increases in the labile iron pool: Implications for Parkinson's disease. Free Radic. Biol. Med., 2009, 46, 593-598.
63. Syme, C.D.; Nadal, R.C.; Rigby, S.E.J.; Viles, J.H. Copper binding to the amyloid-β(Ab) peptide associated with Alzheimer's disease - Folding, coordination geometry, pH dependence, stoichiometry, and affinity of A -(1-28): Insights from a range of complementary spectroscopic techniques. J. Biol. Chem., 2004, 279, 18169-18177.
64. Davies, P.; Marken, F.; Salter, S.; Brown, D.R. Thermodynamic and voltammetric characterization of the metal binding to the prion protein: Insights into pH dependence and redox chemistry. Biochemistry, 2009, 48, 2610-2619.
65. 2 Cu(I) binding site. J. Inorg. Biochem., 2009, 103, 1169-1175.
66. Shearer, J.; Soh, P. The copper(II) adduct of the unstructured region of the amyloidogenic fragment derived from the human prion protein is redox-active at physiological pH. Inorg. Chem., 2007, 46, 710-719.
67. Kong, G. K.W.; Adams, J. J.; Harris, H. H.; Boas, J. F.; Curtain, C. C.; Galatis, D.; Masters, C. L.; Barnham, K. J.; McKinstry, W. J.; Cappai, R.; Parker, M. W. Structural studies of the Alzheimer's amyloid precursor protein copper-binding domain reveal how it binds copper ions. J. Mol. Biol., 2007, 367, 148-161.
68. Maynard, C. J.; Cappai, R.; Volitakis, I.; Laughton, K. M.; Masters, C. L.; Bush, A.I.; Li, Q.X. Chronic exposure to high levels of zinc or copper has little effect on brain metal homeostasis or A accumulation in transgenic APP-C100 Mice. Cell. Mol. Neurobiol., 2009, 29, 757-767.
69. Lee, J. Y.; Cole, T. B.; Palmiter, R. D.; Suh, S. W.; Koh, J. Y. Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice. Proc. Natl. Acad. Sci. USA, 2002, 99, 7705-7710.
70. Lovell, M.A.; Robertson, J. D.; Teesdale, W.J.; Campbell, J.L.; Markesbery, W.R. Copper, iron and zinc in Alzheimer's disease senile plaques. J. Neurol. Sci., 1998, 158, 47-52.
71. Bush, A. I.; Pettingell, W. H.; Multhaup, G.; Paradis, M. D.; Vonsattel, J. P.; Gusella, J. F.; Beyreuther, K.; Masters, C.L.; Tanzi, R. E. Rapid induction of Alzheimer Aβ amyloid formation by zinc. Science, 1994, 265, 1464-1467.
72. Dong, J. J.; Shokes, J. E.; Scott, R. A.; Lynn, D.G. Modulating amyloid self-assembly and fibril morphology with Zn(II). J. Am. Chem. Soc., 2006, 128, 3540-3542.
73. Sarell, C. J.; Syme, C. D.; Rigby, S. E.; Viles, J.H. Copper(II) binding to amyloid-β fibrils of Alzheimer's disease reveals a picomolar affinity: stoichiometry and coordination geometry are independent of Ab oligomeric form. Biochemistry, 2009, 48, 4388-4402.
74. Dong, J.; Canfield, J. M.; Mehta, A. K.; Shokes, J. E.; Tian, B.; Childers, W. S.; Simmons, J. A.; Mao, Z.; Scott, R. A.; Warncke, K.; Lynn, D. G. Engineering metal ion coordination to regulate amyloid fibril assembly and toxicity. Proc. Natl. Acad. Sci. USA, 2007, 104, 13313-13318.
75. Karr, J.W.; Szalai, V. A. Cu(II) binding to monomeric, oligomeric, and fibrillar forms of the Alzheimer's disease amyloid-β peptide. Biochemistry, 2008, 47, 5006-5016.
76. Baskakov, I.V.; Bocharova, O.V. In vitro conversion of mammalian prion protein into amyloid fibrils displays unusual features. Biochemistry, 2005, 44, 2339-2348.
77. Wright, J.A.; Wang, X.Y.; Brown, D.R. Unique copper-induced oligomers mediate alpha-synuclein toxicity. FASEB J., 2009, 23, 2384-2393.
78. Grundke-Iqbal, I.; Fleming, J.; Tung, Y.C.; Lassmann, H.; Iqbal, K.; Joshi, J.G. Ferritin is a component of the neuritic (senile) plaque in Alzheimer dementia. Acta Neuropathol., 1990, 81, 105-110.
79. Basu, S.; Mohan, M.L.; Luo, X.; Kundu, B.; Kong, Q.Z.; Singh, N. Modulation of proteinase K-resistant prion protein in cells and infectious brain homogenate by redox iron: Implications for prion replication and disease pathogenesis. Mol. Biol. Cell, 2007, 18, 3302-3312.
80. Singh, A.; Isaac, A.O.; Luo, X.; Mohan, M.L.; Cohen, M.L.; Chen, F.S.; Kong, Q.Z.; Bartz, J.; Singh, N. Abnormal brain iron homeostasis in human and animal prion disorders. PLoS Pathog., 2009, 5,e1000336.
81. Singh, A.; Kong, Q.; Luo, X.; Petersen, R.B.; Meyerson, H.; Singh, N. Prion protein (PrP) knock-out mice show altered iron metabolism: a functional role for PrP in iron uptake and transport. PLoS One, 2009, 4, e6115.
82. Yamamoto, A.; Shin, R.W.; Hasegawa, K.; Naiki, H.; Sato, H.; Yoshimasu, F.; Kitamoto, T. Iron (III) induces aggregation of hyperphosphorylated tau and its reduction to iron (II) reverses the aggregation: implications in the formation of neurofibrillary tangles of Alzheimer's disease. J. Neurochem., 2002, 82, 1137-1147.
83. Soragni, A.; Zambelli, B.; Mukrasch, M.D.; Biemat, J.; Jeganathan, S.; Griesinger, C.; Ciurli, S.; Mandelkow, E.; Zweckstetter, M. Structural characterization of binding of Cu(II) to Tau protein. Biochemistry, 2008, 47, 10841-10851.
84. Brazier, M.W.; Davies, P.; Player, E.; Marken, F.; Viles, J.H.; Brown, D.R. Manganese binding to the prion protein. J. Biol. Chem., 2008, 283, 12831-12839.
85. Zatta, P.; Drago, D.; Bolognin, S.; Sensi, S.L. Alzheimer's disease, metal ions and metal homeostatic therapy. Trends Pharmacol. Sci., 2009, 30, 346-355.
86. Gitler, A.D.; Chesi, A.; Geddie, M.L.; Strathearn, K.E.; Hamamichi, S.; Hill, K.J.; Caldwell, K.A.; Caldwell, G.A.; Cooper, A.A.; Rochet, J.C.; Lindquist, S. a-Synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity. Nat. Genet., 2009, 41, 308-315.
87. th ed. Oxford University Press: Oxford; New York, 2007.
88. Filiz, G.; Price, K.A.; Caragounis, A.; Du, T.; Crouch, P.J.; White, A.R. The role of metals in modulating metalloprotease activity in the AD brain. Eur. Biophys. J., 2008, 37, 315-321.
89. Charkoudian, L.K.; Dentchev, T.; Lukinova, N.; Wolkow, N.; Dunaief, J.L.; Franz, K.J. Iron prochelator BSIH protects retinal pigment epithelial cells against cell death induced by hydrogen peroxide. J. Inorg. Biochem., 2008, 102, 2130-2135.
90. Kozlowski, H.; Janicka-Klos, A.; Brasun, J.; Gaggelli, E.; Valensin, D.; Valensin, G. Copper, iron, and zinc ions homeostasis and their role in neurodegenerative disorders (metal uptake, transport, distribution and regulation). Coord. Chem. Rev., 2009, 253, 2665-2685.
91. Singh, N.; Singh, A.; Das, D.; Mohan, M. Redox control of prion and disease pathogenesis. Antioxid. Redox Signal., 2010, 12, 1271-1294.
92. 7metallothionein-3 and amyloid-β-Cu protects against amyloid-ββ-toxicity. Nat. Chem. Biol., 2008, 4, 366-372.
93. 2+ ions. J. Biol. Chem., 2007, 282, 16068-16078.
94. Turnbull, S.; Tabner, B. J.; El-Agnaf, O. M. A.; Moore, S.; Davies, Y.; Allsop, D. a-synuclein implicated in Parkinson's disease catalyses the formation of hydrogen peroxide in vitro. Free Radic. Biol.Med., 2001, 30, 1163-1170.
95. Hoogenraad, T.U. Paradigm shift in treatment of Wilson's disease: zinc therapy now treatment of choice. Brain Dev., 2006, 28, 141-146.
96. Adlard, P.A.; Cherny, R.A.; Finkelstein, D.I.; Gautier, E.; Robb, E.; Cortes, M.; Volitakis, I.; Liu, X.; Smith, J.P.; Perez, K.; Laughton, K.; Li, Q.X.; Charman, S.A.; Nicolazzo, J.A.; Wilkins, S.; Deleva, K.; Lynch, T.; Kok, G.; Ritchie, C.W.; Tanzi, R. E.; Cappai, R.; Masters, C. L.; Barnham, K. J.; Bush, A. I. Rapid restoration of cognition in Alzheimer's transgenic mice with 8-hydroxy quinoline analogs is associated with decreased interstitial Ab. Neuron, 2008, 59, 43-55.
97. Yassin, M. S.; Ekblom, J.; Xilinas, M.; Gottfries, C. G.; Oreland, L. Changes in uptake of vitamin B12 and trace metals in brains of mice treated with clioquinol. J. Neurol. Sci., 2000, 173, 40-44.
98. Cherny, R. A.; Atwood, C. S.; Xilinas, M. E.; Gray, D. N.; Jones, W.D.; McLean, C. A.; Barnham, K. J.; Volitakis, I.; Fraser, F. W.; Kim, Y.S.; Huang, X. D.; Goldstein, L.E.; Moir, R.D.; Lim, J.T.; Beyreuther, K.; Zheng, H.; Tanzi, R.E.; Masters, C. L.; Bush, A. I. Treatment with a copper-zinc chelator markedly and rapidly inhibits β-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron, 2001, 30, 665-676.
99. Bolognin, S.; Zatta, P.; Drago, D.; Parnigotto, P.P.; Ricchelli, F.; Tognon, G. Mutual stimulation of-amyloid fibrillogenesis by clioquinol and divalent metals. NeuroMol. Med., 2008, 10, 322-332.
100. Crouch, P.J.; Hung, L.W.; Adlard, P.A.; Cortes, M.; Lal, V.; Filiz, G.; Perez, K.A.; Nurjono, M.; Caragounis, A.; Du, T.; Laughton, K.; Volitakis, I.; Bush, A.I.; Li, Q. X.; Masters, C.L.; Cappal, R.; Cherny, R. A.; Donnelly, P. S.; White, A.R.; Barnham, K.J. Increasing Cu bioavailability inhibits Aβ oligomers and tau phosphorylation. Proc. Natl. Acad. Sci. USA, 2009, 106, 381-386.
101. Bush, A. I.; Tanzi, R. E. Therapeutics for Alzheimer's disease based on the metal hypothesis. Neurotherapeutics, 2008, 5, 421-432.
102. Crapper McLachlan, D.R. C.; Dalton, A. J.; Kruck, T. P. A.; Bell, M.Y.; Smith, W. L.; Kalow, W.; Andrews, D. F. Intramuscular desferrioxamine in patients with Alzheimer's Disease. Lancet, 1991, 337, 1304-1308.
103. Petri, S.; Calingasan, N. Y.; Alsaied, S. A.; Wille, E.; Kiaei, M.; Friedman, J. E.; Baranova, O.; Chavez, J. C.; Beal, M. F. The lipophilic metal chelators DP-109 and DP-460 are neuroprotective in a transgenic mouse model of amyotrophic lateral sclerosis. J. Neurochem., 2007, 102, 991-1000.
104. Lee, J.Y.; Friedman, J. E.; Angel, I.; Kozak, A.; Koh, J. Y. The lipophilic metal chelator DP-109 reduces amyloid pathology in brains of human β-amyloid precursor protein transgenic mice. Neurobiol. Aging, 2004, 25, 1315-1321.
105. Moret, V.; Laras, Y.; Pietrancosta, N.; Garino, C.; Quelever, G.; Rolland, A.; Mallet, B.; Norreel, J.C.; Kraus, J. L. 1,1 '-Xylyl bis- 1,4,8,11-tetraaza cyclotetradecane: A new potential copper chelator agent for neuroprotection in Alzheimer's disease. Its comparative effects with clioquinol on rat brain copper distribution. Bioorg.Med. Chem. Lett., 2006, 16, 3298-3301.
106. Kimura, E.; Koike, T.; Shimizu, Y.; Kodama, M. Complexes of the histamine H2-antagonist cimetidine with divalent and mono-valent copper ions. Inorg. Chem., 1986, 25, 2242-2246.
107. Sigurdsson, E.M.; Brown, D.R.; Alim, M.A.; Scholtzova, H.; Carp, R.; Meeker, H.C.; Prelli, F.; Frangione, B.; Wisniewski, T. Copper chelation delays the onset of prion disease. J. Biol. Chem., 2003, 278, 46199-46202.
108. Doh-Ura, K.; Tamura, K.; Karube, Y.; Naito, M.; Tsuruo, T.; Kataoka, Y. Chelating compound, chrysoidine, is more effective in both antiprion activity and brain endothelial permeability than quinacrine. Cell Mol. Neurobiol., 2007, 27, 303-316.
109. Murakami-Kubo, I.; Doh-ura, K.; Ishikawa, K.; Kawatake, S.; Sasaki, K.; Kira, J.; Ohta, S.; Iwaki, T. Quinoline derivatives are therapeutic candidates for transmissible spongiform encephalopathies. J. Virol., 2004, 78, 1281-1288.
110. Wong, B. S.; Chen, S. G.; Colucci, M.; Xie, Z. L.; Pan, T.; Liu, T.; Li, R. L.; Gambetti, P.; Sy, M. S.; Brown, D. R. Aberrant metal binding by prion protein in human prion disease. J. Neurochem., 2001, 78, 1400-1408.
111. Hesketh, S.; Sassoon, J.; Knight, R.; Brown, D. R. Elevated manganese levels in blood and CNS in human prion disease. Mol. Cell. Neurosci., 2008, 37, 590-598.
112. Schafer, S.; Pajonk, F. G.; Multhaup, G.; Bayer, T. A. Copper and clioquinol treatment in young APP transgenic and wild-type mice: effects on life expectancy, body weight, and metal-ion levels. J. Mol. Med., 2007, 85, 405-413.
113. Bayer, T. A.; Schafer, S.; Simons, A.; Kemmling, A.; Kamer, T.; Tepest, R.; Eckert, A.; Schussel, K.; Eikenberg, O.; SturchlerPierrat, C.; Abramowski, D.; Staufenbiel, M.; Multhaup, G. Dietary Cu stabilizes brain superoxide dismutase 1 activity and reduces amyloid Aβ production in APP23 transgenic mice. Proc. Natl. Acad. Sci. USA, 2003, 100, 14187-14192.
114. Phinney, A.L.; Drisaldi, B.; Schmidt, S.D.; Lugowski, S.; Coronado, V.; Liang, Y.; Horne, P.; Yang, J.; Sekoulidis, J.; Coomaraswamy, J.; Chishti, M.A.; Cox, D.W.; Mathews, P. M.; Nixon, R. A.; Carlson, G. A.; St George-Hyslop, P.; Westaway, D. In vivo reduction of amyloid-β by a mutant copper transporter. Proc. Natl. Acad. Sci. USA, 2003, 100, 14193-14198.
115. Borchardt, T.; Camakaris, J.; Cappai, R.; Masters, C. L.; Beyreuther, K.; Multhaup, G. Copper inhibits β-amyloid production and stimulates the non-amyloidogenic pathway of amyloid-β precursor-protein secretion. Biochem. J., 1999, 344(Pt 2), 461-467.
116. Donnelly, P. S.; Caragounis, A.; Du, T.; Laughton, K. M.; Volitakis, I.; Cherny, R.A.; Sharples, R. A.; Hill, A.F.; Li, Q. X.; Masters, C.L.; Barnham, K. J.; White, A. R. Selective intracellular release of copper and zinc ions from bis(thiosemicarbazonato) complexes reduces levels of Alzheimer disease amyloid-ββ peptide. J. Biol. Chem., 2008, 283, 4568-4577.
117. Kitazawa, M.; Cheng, D.; LaFerla, F. M. Chronic copper exposure exacerbates both amyloid and tau pathology and selectively dysregulates cdk5 in a mouse model of AD. J. Neurochem., 2009, 108, 1550-1560.
118. Bush, A. I. Metal complexing agents as therapies for Alzheimer's disease. Neurobiol. Aging, 2002, 23, 1031-1038.
119. Wisniewski, T.; Sigurdsson, E.M. Therapeutic approaches for prion and Alzheimer's diseases. FEBS J., 2007, 274, 3784-3798.
120. Orem, N. R.; Geoghegan, J. C.; Deleault, N. R.; Kascsak, R.; Supattapone, S. Copper(II) ions potently inhibit purified PrPres amplification. J. Neurochem., 2006, 96, 1409-1415.
121. Pauly, P. C.; Harris, D.A. Copper stimulates endocytosis of the prion protein. J. Biol. Chem., 1998, 273, 33107-33110.
122. Taylor, D. R.; Watt, N.T.; Perera, W. S. S.; Hooper, N. M. Assigning functions to distinct regions of the N-terminus of the prion protein that are involved in its copper-stimulated, clathrin-dependent endocytosis. J. Cell Sci., 2005, 118, 5141-5153.
123. Haigh, C. L.; Edwards, K.; Brown, D.R. Copper binding is the governing determinant of prion protein turnover. Mol. Cell. Neurosci., 2005, 30, 186-196.
124. C may inhibit prion disease propagation. Brain Res., 2003, 993, 192-200.
125. Barnham, K. J.; Masters, C. L.; Bush, A. I. Neurodegenerative diseases and oxidative stress. Nat. Rev. Drug Discov., 2004, 3, 205-214.
126. Halliwell, B. The wanderings of a free radical. Free Radic. Biol. Med., 2008, 45, S2-S2.
127. Gaggelli, E.; Kozlowski, H.; Valensin, D.; Valensin, G. Copper homeostasis and neurodegenerative disorders (Alzheimer's, prion, and Parkinson's diseases and amyotrophic lateral sclerosis). Chem. Rev., 2006, 106, 1995-2044.
128. Galaris, D.; Pantopoulos, K. Oxidative stress and iron homeostasis: mechanistic and health aspects. Crit. Rev. Clin. Lab. Sci., 2008, 45,1-23.
129. Kakhlon, O.; Cabantchik, Z. I. The labile iron pool: characterization, measurement, and participation in cellular processes. Free Radic. Biol. Med., 2002, 33, 1037-1046.
130. Ullrich, V.; Kissner, R. Redox signaling: bioinorganic chemistry at its best. J. Inorg. Biochem., 2006, 100, 2079-2086.
131. Dong, J.; Atwood, C. S.; Anderson, V. E.; Siedlak, S.L.; Smith, M. A.; Perry, G.; Carey, P.R. Metal binding and oxidation of amyloid-β within isolated senile plaque cores: Raman microscopic evidence. Biochemistry, 2003, 42, 2768-2773.
132. Requena, J. R.; Dimitrova, M. N.; Legname, G.; Teijeira, S.; Prusiner, S. B.; Levine, R.L. Oxidation of methionine residues in the prion protein by hydrogen peroxide. Arch. Biochem. Biophys., 2004, 432, 188-195.
133. Requena, J. R.; Groth, D.; Legname, G.; Stadtman, E. R.; Prusiner, S.B.; Levine, R.L. Copper-catalyzed oxidation of the recombinant SHa(29-231) prion protein. Proc. Natl. Acad. Sci. USA, 2001, 98, 7170-7175.
134. Hou, L.M.; Shao, H.Y.; Zhang, Y. B.; Li, H.; Menon, N. K.; Neuhaus, E. B.; Brewer, J. M.; Byeon, I. J.L.; Ray, D. G.; Vitek, M. P.; Iwashita, T.; Makula, R. A.; Przybyla, A B.; Zagorski, M.G. Solution NMR studies of the Aβ (1-40) and Aβ (1-42) peptides establish that the Met35 oxidation state affects the mechanism of amyloid formation. J. Am. Chem. Soc., 2004, 126, 1992-2005.
135. Heegaard, P. M. H.; Pedersen, H. G.; Flink, J.; Boas, U. Amyloid aggregates of the prion peptide PrP106-126 are destabilised by oxidation and by the action of dendrimers. FEBS Lett., 2004, 577, 127-133.
136. Opazo, C.; Huang, X. D.; Cherny, R. A.; Moir, R. D.; Roher, A. E.; White, A. R.; Cappai, R.; Masters, C. L.; Tanzi, R. E.; Inestrosa, N. C.; Bush, A. I. Metalloenzyme-like activity of Alzheimer's disease β-amyloid - Cu-dependent catalytic conversion of dopamine, cholesterol, and biological reducing agents to neurotoxic H2O2. J. Biol.Chem., 2002, 277, 40302-40308.
137. 2+, but is a sacrificial quencher of hydroxyl radicals. Free Radic. Biol. Med., 2007, 42, 79-89.
138. Hague, T.; Andrews, P. L. R.; Barker, J.; Naughton, D. P. Dietary chelators as antioxidant enzyme mimetics: implications for dietary intervention in neurodegenerative diseases. Behav. Pharmacol., 2006, 17, 425-430.
139. Bartov, O.; Sultana, R.; Butterfield, D. A.; Atlas, D. Low molecular weight thiol amides attenuate MAPK activity and protect primary neurons from Ab(1-42) toxicity. Brain Res., 2006, 1069, 198-206.
140. Moreira, P. I.; Harris, P. L.; Zhu, X.; Santos, M.S.; Oliveira, C. R.; Smith, M. A.; Perry, G. Lipoic acid and N-acetyl cysteine decrease mitochondrial-related oxidative stress in Alzheimer disease patient fibroblasts. J. Alzheimer's Dis., 2007, 12, 195-206.
141. Singh, N.; Pillay, V.; Choonara, Y. E. Advances in the treatment of Parkinson's disease. Prog. Neurobiol., 2007, 81, 29-44.
142. Pan, T. H.; Jankovic, J.; Le, W. D. Potential therapeutic properties of green tea polyphenols in Parkinson's disease. Drugs Aging, 2003, 20, 711-721.
143. Perron, N. R.; Brumaghim, J. L. A review of the antioxidant mechanisms of polyphenol compounds related to iron binding. Cell Biochem. Biophys., 2009, 53, 75-100.
144. Ehrnhoefer, D. E.; Bieschke, J.; Boeddrich, A.; Herbst, M.; Masino, L.; Lurz, R.; Engemann, S.; Pastore, A.; Wanker, E.E. EGCG redirects amyloidogenic polypeptides into unstructured, off- pathway oligomers. Nat. Struct. Mol. Biol., 2008, 15, 558-566.
145. Melov, S.; Wolf, N.; Strozyk, D.; Doctrow, S. R.; Bush, A. I. Mice transgenic for Alzheimer disease β-amyloid develop lens cataracts that are rescued by antioxidant treatment. Free Radic. Biol. Med., 2005, 38, 258-261.
146. Rosenthal, R. A.; Huffman, K. D.; Fisette, L. W.; Damphousse, C. A.; Callaway, W. B.; Malfroy, B.; Doctrow, S. R. Orally available Mn porphyrins with superoxide dismutase and catalase activities. J. Biol. Inorg. Chem., 2009, 14, 979-991.
147. Haigh, C. L.; Brown, D. R. Prion protein reduces both oxidative and non-oxidative copper toxicity. J. Neurochem., 2006, 98, 677-689.
148. Reddy, P. V.; Rama Rao, K. V.; Norenberg, M. D. The mitochondrial permeability transition, and oxidative and nitrosative stress in the mechanism of copper toxicity in cultured neurons and astrocytes. Lab. Invest., 2008, 88, 816-830.
149. Shiraishi, N.; Ohta, Y.; Nishikimi, M. The octapeptide repeat region of prion protein binds Cu(II) in the redox-inactive state. Bio.chem. Biophys. Res. Commun., 2000, 267, 398-402.
150. Chacon, M. A.; Barria, M. I.; Lorca, R.; Huidobro-Toro, J. P.; Inestrosa, N. C. A human prion protein peptide (PrP59-91) protects against copper neurotoxicity. Mol. Psychiatry, 2003, 8, 853-862, 835.
151. Brown, D. R.; Wong, B. S.; Hafiz, F.; Clive, C.; Haswell, S. J.; Jones, I. M. Normal prion protein has an activity like that of superoxide dismutase. Biochem. J., 1999, 344(Pt 1), 1-5.
152. Fukuuchi, T.; Doh-Ura, K.; Yoshihara, S.; Ohta, S. Metal complexes with superoxide dismutase-like activity as candidates for anti-prion drug. Bioorg. Med. Chem. Lett., 2006, 16, 5982-5987.