The metallobiology of Alzheimer's disease

Trends in Neurosciences

Volumn 26, Issue 4, 2003, Pages 207-214

  Bush, Ashley I ^a,b  

^a MASSACHUSETTS GENERAL HOSPITAL   (United States)

^b UNIVERSITY OF MELBOURNE   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; CLIOQUINOL; COPPER; DEFEROXAMINE; IRON; PENICILLAMINE; TRIENTINE; ZINC;

ALZHEIMER DISEASE; AUTOOXIDATION; CATABOLISM; CLINICAL TRIAL; HUMAN; MOLECULAR MODEL; NEOCORTEX; NEUROTOXICITY; NONHUMAN; PRECIPITATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN INTERACTION; REVIEW;

EID: 0037386086     PISSN: 01662236     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-2236(03)00067-5     Document Type: Review

References (78)

1. Atwood C.S., et al. Role of free radicals and metal ions in the pathogenesis of Alzheimer's disease. Met. Ions Biol. Syst. 36:1999;309-364.
2. Cuajungco M.P., et al. Metal chelation as a potential therapy for Alzheimer's disease. Ann. New York Acad. Sci. 920:2000;292-304.
3. Schenk D., et al. Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature. 400:1999;173-177.
4. Callahan M.J., et al. Augmented senile plaque load in aged female β-amyloid precursor protein-transgenic mice. Am. J. Pathol. 158:2001;1173-1177.
5. Vaughan D.W., Peters A. The structure of neuritic plaques in the cerebral cortex of aged rats. J. Neuropathol. Exp. Neurol. 40:1981;472-487.
6. McLean C., et al. Soluble pool of Aβ amyloid as a determinant of severity of neurodegeneration in Alzheimer's Disease. Ann. Neurol. 46:1999;860-866.
7. Cherny R.A., et al. Aqueous dissolution of Alzheimer's disease Aβ amyloid deposits by biometal depletion. J. Biol. Chem. 274:1999;23223-23228.
8. Bush A.I., et al. Modulation of Aβ adhesiveness and secretase site cleavage by zinc. J. Biol. Chem. 269:1994;12152-12158.
9. Bush A.I., et al. Rapid induction of Alzheimer Aβ amyloid formation by zinc. Science. 265:1994;1464-1467.
10. Miura T., et al. Metal binding modes of Alzheimer's amyloid β-peptide in insoluble aggregates and soluble complexes. Biochemistry. 39:2000;7024-7031.
11. Atwood C.S., et al. Dramatic aggregation of Alzheimer Aβ by Cu(II) is induced by conditions representing physiological acidosis. J. Biol. Chem. 273:1998;12817-12826.
12. 67copper by two ligand-dependent saturable processes. J. Biol. Chem. 263:1988;799-805.
13. 67copper. Synapse. 2:1988;412-415.
14. 2+ from brain tissue during activity. Nature. 308:1984;734-736.
15. Howell G.A., et al. Stimulation-induced uptake and release of zinc in hippocampal slices. Nature. 308:1984;736-738.
16. Lovell M.A., et al. Copper, iron and zinc in Alzheimer's disease senile plaques. J. Neurol. Sci. 158:1998;47-52.
17. Suh S.W., et al. Histological evidence implicating zinc in Alzheimer's disease. Brain Res. 852:2000;274-278.
18. 2. J. Biol. Chem. 277:2002;40302-40308.
19. Liu S.T., et al. Histidine-13 is a crucial residue in the zinc ion-induced aggregation of the Aβ peptide of Alzheimer's disease. Biochemistry. 38:1999;9373-9378.
20. Curtain C., et al. Alzheimer's disease amyloid binds Cu and Zn to generate an allosterically-ordered membrane-penetrating structure containing SOD-like subunits. J. Biol. Chem. 276:2001;20466-20473.
21. Morgan D.M., et al. Metal switch for amyloid formation: insight into the structure of the nucleus. J. Am. Chem. Soc. 124:2002;12644-12645.
22. Duff K., et al. Increased amyloid-β42(43) in brains of mice expressing mutant presenilin 1. Nature. 383:1996;710-713.
23. Cole T.B., et al. Elimination of zinc from synaptic vesicles in the intact mouse brain by disruption of the ZnT3 gene. Proc. Natl. Acad. Sci. U. S. A. 96:1999;1716-1721.
24. Lee J.-Y., et al. Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice. Proc. Natl. Acad. Sci. U. S. A. 99:2002;7705-7710.
25. Palmiter R.D., et al. ZnT-3, a putative transporter of zinc into synaptic vesicles. Proc. Natl. Acad. Sci. U. S. A. 93:1996;14934-14939.
26. Frederickson C.J., Bush A.I. Synaptically released zinc: physiological functions and pathological effects. Biometals. 14:2001;353-366.
27. Bush A.I. Metals and neuroscience. Curr. Opin. Chem. Biol. 4:2000;184-191.
28. Atwood C.S., et al. Characterization of copper interactions with Alzheimer Aβ peptides - identification of an attomolar affinity copper binding site on Aβ1-42. J. Neurochem. 75:2000;1219-1233.
29. Grundke-Iqbal I., et al. Ferritin is a component of the neuritic (senile) plaque in Alzheimer dementia. Acta Neuropathol. 81:1990;105-110.
30. Huang X., et al. The Aβ peptide of Alzheimer's disease directly produces hydrogen peroxide through metal ion reduction. Biochemistry. 38:1999;7609-7616.
31. Huang X., et al. Cu(II) potentiation of Alzheimer Aβ neurotoxicity: correlation with cell-free hydrogen peroxide production and metal reduction. J. Biol. Chem. 274:1999;37111-37116.
32. Rottkamp C., et al. Redox-active iron mediates amyloid-β toxicity. Free Radic. Biol. Med. 30:2001;447-450.
33. Smith M.A., et al. Oxidative damage in Alzheimer's. Nature. 382:1996;120-121.
34. Sayre L.M., et al. 4-Hydroxynonenal-derived advanced lipid peroxidation end products are increased in Alzheimer's disease. J. Neurochem. 68:1997;2092-2097.
35. Nunomura A., et al. RNA oxidation is a prominent Feature of vulnerable neurons in Alzheimer's disease. J. Neurosci. 19:1999;1959-1964.
36. Nunomura A., et al. Neuronal oxidative stress precedes amyloid-β deposition in Down syndrome. J. Neuropathol. Exp. Neurol. 59:2000;1011-1017.
37. Nunomura A., et al. Oxidative damage is the earliest event in Alzheimer disease. J. Neuropathol. Exp. Neurol. 60:2001;759-767.
38. Lovell M.A., et al. Protection against amyloid β peptide toxicity by zinc. Brain Res. 823:1999;88-95.
39. Cuajungco M.P., et al. Evidence that the β-amyloid plaques of Alzheimer's disease represent the redox-silencing and entombment of Aβ by zinc. J. Biol. Chem. 275:2000;19439-19442.
40. Sayre L.M., et al. In situ oxidative catalysis by neurofibrillary tangles and senile plaques in Alzheimer's disease: a central role for bound transition metals. J. Neurochem. 74:2000;270-279.
41. Lue L.F., et al. Soluble amyloid β peptide concentration as a predictor of synaptic change in Alzheimer's disease. Am. J. Pathol. 155:1999;853-862.
42. Wang J., et al. The levels of soluble versus insoluble brain Aβ distinguish Alzheimer's disease from normal and pathologic aging. Exp. Neurol. 158:1999;328-337.
43. Atwood C.S., et al. Copper catalyzed oxidation of Alzheimer Aβ Cell. Mol. Biol. 46:2000;777-783.
44. Kuo Y.M., et al. Water-soluble Aβ (N-40, N-42) oligomers in normal and Alzheimer disease brains. J. Biol. Chem. 271:1996;4077-4081.
45. Walsh D.M., et al. Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo. Nature. 416:2002;535-539.
46. Stadtman E.R., Oliver C.N. Metal-catalyzed oxidation of proteins. Physiological consequences. J. Biol. Chem. 266:1991;2005-2008.
47. Curtain C.C., et al. Metal ions, pH and cholesterol regulate the interactions of Alzheimer's disease amyloid-β peptide with membrane lipid. J. Biol. Chem. 278:2003;2977-2982.
48. Maynard C., et al. Overexpression of Alzheimer's disease β-amyloid opposes the age-dependent elevations of brain copper and iron levels. J. Biol. Chem. 277:2002;44670-44676.
49. Frederikse P.H., et al. Oxidative stress increases production of β-amyloid precursor protein and β-amyloid (A-β) in mammalian lenses, and A-β has toxic effects on lens epithelial cells. J. Biol. Chem. 271:1996;10169-10174.
50. 65zinc uptake from blood into brain and other tissues in the rat. Neurochem. Res. 15:1990;1003-1008.
51. 65Zn uptake from blood into brain in the rat. J. Neurochem. 56:1991;485-489.
52. Kalaria R.N., Harik S.I. Reduced glucose transporter at the blood-brain barrier. J. Neurochem. 53:1989;1083-1088.
53. Kalaria R.N., Hedera P. Differential degeneration of the cerebral microvasculature in Alzheimer's disease. NeuroReport. 6:1995;477-480.
54. Bush A.I., et al. A novel zinc(II) binding site modulates the function of the βA4 amyloid protein precursor of Alzheimer's disease. J. Biol. Chem. 268:1993;16109-16112.
55. Van Nostrand W.E. Zinc(II) selectively enhances the inhibition of coagulation factor XIa by protease nexin-2/amyloid -β-protein precursor. Thromb. Res. 78:1995;43-53.
56. Simons A., et al. Evidence for a copper-binding superfamily of the amyloid precursor protein. Biochemistry. 41:2002;9310-9320.
57. White A.R., et al. Copper levels are increased in the cerebral cortex and liver of APP and APLP2 knockout mice. Brain Res. 842:1999;439-444.
58. Rogers J., et al. An iron-responsive element type II in the 5′ untranslated region of the Alzheimer's amyloid precursor protein transcript. J. Biol. Chem. 277:2002;45518-45528.
59. Kontush A., et al. Amyloid-β is an antioxidant for lipoproteins in cerebrospinal fluid and plasma. Free Radic. Biol. Med. 30:2001;119-128.
60. Kontush A., et al. Resistance of human cerebrospinal fluid to in vitro oxidation is directly related to its amyloid-β content. Free Radic. Res. 35:2001;507-517.
61. Zou K., et al. A novel function of monomeric amyloid β-protein serving as an antioxidant molecule against metal-induced oxidative damage. J. Neurosci. 22:2002;4833-4841.
62. Squitti R., et al. Elevation of serum copper levels in Alzheimer's disease. Neurology. 59:2002;1153-1161.
63. Rao G.H., et al. Effects of 2,2′-dipyridyl and related compounds on platelet prostaglandin synthesis and platelet function. Biochim. Biophys. Acta. 628:1980;468-479.
64. Rao G.H., et al. Ibuprofen protects platelet cyclooxygenase from irreversible inhibition by aspirin. Arteriosclerosis. 3:1983;383-388.
65. Cherny R.A., et al. Treatment with a copper-zinc chelator markedly and rapidly inhibits β-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron. 30:2001;665-676.
66. Regland B., et al. Treatment of Alzheimer's disease with clioquinol. Dement. Geriatr. Cogn. Disord. 12:2001;408-414.
67. Huang X., et al. Zinc-induced Alzheimer's Aβ1-40 aggregation is mediated by conformational factors. J. Biol. Chem. 272:1997;26464-26470.
68. Wu S.M., et al. The binding of receptor-recognized α2-macroglobulin to the low density lipoprotein receptor-related protein and the α2M signaling receptor is decoupled by oxidation. J. Biol. Chem. 272:1997;20627-20635.
69. DeMattos R.B., et al. Peripheral anti-Aβ antibody alters CNS and plasma Aβ clearance and decreases brain Aβ burden in a mouse model of Alzheimer's disease. Proc. Natl. Acad. Sci. U. S. A. 98:2001;8850-8855.
70. 12 and trace metals in brains of mice treated with clioquinol. J. Neurol. Sci. 173:2000;40-44.
71. Crapper-McLachlan D.R., et al. Intramuscular desferrioxamine in patients with Alzheimer's disease. Lancet. 337:1991;1304-1308.
72. May P.M., Bulman R. The present status of chelating agents in medicine. Prog. Med. Chem. 20:1983;225-336.
73. McKenzie D., et al. Reversibility of scrapie inactivation is enhanced by copper. J. Biol. Chem. 273:1998;25545-25547.
74. Estevez A.G., et al. Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase. Science. 286:1999;2498-2500.
75. Goldstein L.E., et al. 3-Hydroxykynurenine and 3-hydroxyanthranilic acid generate hydrogen peroxide and promote α-crystallin cross-linking by metal ion reduction. Biochemistry. 39:2000;7266-7275.
76. Paik S.R., et al. Copper(II)-induced self-oligomerization of α-synuclein. Biochem. J. 340:1999;821-828.
77. Head E., et al. Oxidation of Aβ and plaque biogenesis in Alzheimer's disease and Down syndrome. Neurobiol. Dis. 8:2001;792-806.
78. Giulian D., et al. The HHQK domain of β-amyloid provides a structural basis for the immunopathology of Alzheimer's disease. J. Biol. Chem. 273:1998;29719-29726.