Reactive oxygen species and Alzheimer's disease

Biochemical Pharmacology

Volumn 54, Issue 5, 1997, Pages 533-539

  Multhaup, Gerd ^a   Ruppert, Thomas ^a   Schlicksupp, Andrea ^a   Hesse, Lars ^a   Beher, Dirk ^a   Masters, Colin L ^a,b,c   Beyreuther, Konrad ^a  

^a UNIVERSITY OF HEIDELBERG   (Germany)

^b UNIVERSITY OF MELBOURNE   (Australia)

^c FLOREY INSTITUTE OF NEUROSCIENCE AND MENTAL HEALTH   (Australia)

Author keywords

Alzheimer's disease; Copper mediated toxicity; Familial amyotrophic lateral sclerosis (FALS); Free radicals; Hydrogen peroxide; A4 toxicity

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; COPPER; FREE RADICAL; REACTIVE OXYGEN METABOLITE;

AGED; ALZHEIMER DISEASE; AMYOTROPHIC LATERAL SCLEROSIS; HUMAN; NERVE DEGENERATION; PRIORITY JOURNAL; REVIEW;

EID: 0030827975     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(97)00062-2     Document Type: Note

References (85)

1. Scheuner D, Eckman C, Jensen M, Song X, Citron M, Suzuki N, Bird TD, Hardy J, Hutton M, Kukull W, Larson E, Levy-Lahad E, Viitanen M, Peskind E, Poorkaj P, Schellen-Berg G, Tanzi R, Wasco W, Lannfelt L, Selkoe D and Younkin S, Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nature Med 2: 864-870, 1996.
2. Selkoe DJ, Amyloid β-protein and the genetics of Alzheimer's disease. J Biol Chem 271: 18295-18298, 1996.
3. Goate A, Chartier-Harlin M-C, Mullan M, Brown J, Crawford F, Fidani L, Giuffra L, Haynes A, Irving M, James L, Mant R, Newton P, Rooke K, Roques P, Talbot C, Pericak-Vance M, Roses A, Williamson R, Rossor M, Owen M and Hardy J, Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease. Nature 349: 704-706, 1991.
4. Chartier-Harlin M-C, Crawford F, Houlden H, Warren A, Hughes D, Fidani L, Goate A, Rossor M, Roques P, Hardy J and Mullan M, Early-onset Alzheimer's disease caused by mutation at codon 717 of the β-amyloid precursor protein gene. Nature 353: 844-846, 1991.
5. Naruse S, Igarashi S, Kobayashi H, Aoki K, Inuzuka T, Kaneko K, Shimizu T, lihara K, Kojima T, Miyatake T and Tsuji S, Mis-sense mutation Val → Ile in exon 17 of amyloid precursor protein gene in Japanese familial Alzheimer's disease. Lancet 337: 978-979, 1991.
6. Mullan M, Crawford F, Axelman K, Houlden H, Lilius L, Winblad B and Lannfelt L, A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of β-amyloid. Nat Genet 1: 345-347, 1992.
7. Hendriks L, van Duijn CM, Cras P, Cruts M, Van Hul W, van Harskamp F, Warren A, McInnis MG, Antonarakis SE, Martin J-J, Hofman A and Van Broeckhoven C, Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the β-amyloid precursor protein gene. Nat Genet 1: 218-221, 1992.
8. Sherrington R, Rogaev EI, Liang Y, Rogaeva EA, Levesque G, Ikeda M, Chi H, Lin C, Li G, Holman K, Tsuda T, Mar L, Foncin J-F, Bruni AC, Montesi MP, Sorbi S, Rainero I, Pinessi L, Nee L, Chumakov I, Pollen D, Brookes A, Sanseau P, Polinsky RJ, Wasco W, Da Silva HAR, Haines JL, Pericak-Vance MA, Tanzi RE, Roses AD, Fraser PE, Rommens JM and St. George-Hyslop PH, Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature 375: 754-760, 1995.
9. Slunt HH, Thinakaran G, Lee MK and Sisodia SS, Nucleotide sequence of the chromosome 14-encoded S182 cDNA and revised secondary structure prediction. Amyloid Im J Exp Clin Invest 2: 188-190, 1995.
10. 717) mutants. Science 264: 1336-1340, 1994.
11. Citron M, Oltersdorf T, Haass C, McConlogue L, Hung AY, Seubert P, Vigo-Pelfrey C, Lieberburg I and Selkoe DJ, Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production. Nature 360: 672-674, 1992.
12. Cai X-D, Golde TE and Younkin SG, Release of excess amyloid β protein from a mutant amyloid β protein precursor. Science 259: 514-516, 1993.
13. Iwatsubo T, Mann DMA, Odaka A, Suzuki N and Ihara Y, Amyloid β protein (Aβ) deposition: Aβ42(43) precedes Aβ40 in Down syndrome. Ann Neurol 37: 294-299, 1995.
14. Burdick D, Soreghan B, Kwon M, Kosmoski J, Knauer M, Henschen A, Yates J, Cotman C and Glabe C, Assembly and aggregation properties of synthetic Alzheimer's A4/β amyloid peptide analogs. J Biol Chem 267: 546-554, 1992.
15. Jarrett JT and Lansbury PT Jr, Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73: 1055-1058, 1993.
16. Jarrett JT, Berger EP and Lansbury PT Jr, The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease. Biochemistry 32: 4693-4697, 1993.
17. Rumble B, Retallack R, Hilbich C, Simms G, Multhaup G, Martins R, Hockey A, Montgomery P, Beyreuther K and Masters CL, Amyloid A4 protein and its precursor in Down's syndrome and Alzheimer's disease. N Engl J Med 320: 1446-1452, 1989.
18. Iwatsubo T, Odaka A, Suzuki N, Mizusawa H, Nukina N and Ihara Y, Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ42(43). Neuron 13: 45-53, 1994.
19. Seubert P, Vigo-Pelfrey C, Esch F, Lee M, Dovey H, Davis D, Sinha S, Schlossmacher M, Whaley J, Swindlehurst C, McCormack R, Wolfert R, Selkoe D, Lieberburg I and Schenk D, Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids. Nature 359: 325-327, 1992.
20. Shoji M, Golde TE, Ghiso J, Cheung TT, Estus S, Shaffer LM, Cai X-D, McKay DM, Tintner R, Frangione B and Younkin SG, Production of the Alzheimer amyloid β protein by normal proteolytic processing. Science 258: 126-129, 1992.
21. Haass C, Schlossmacher MG, Hung AY, Vigo-Pelfrey C, Mellon A, Ostaszewski BL, Lieberburg I, Koo EH, Schenk D, Teplow DB and Selkoe DJ, Amyloid β-peptide is produced by cultured cells during normal metabolism. Nature 359: 322-325, 1992.
22. Busciglio J, Gabuzda DH, Matsudaira P and Yankner BA, Generation of β-amyloid in the secretary pathway in neuronal and nonneuronal cells. Proc Natl Acad Sci USA 90: 2092-2096, 1993.
23. Kuo Y-M, Emmerling MR, Vigo-Pelfrey C, Kasunic TC, Kirkpatrick JB, Murdoch GH, Ball MJ and Roher AE, Water-soluble Aβ (N-40, N-42) oligomers in normal and Alzheimer disease brains. J Biol Chem 271: 4077-4081, 1996.
24. Smith MA, Sayre LM, Monnier VM and Perry G, Radical AGEing in Alzheimer's disease. Trends Neurosci 18: 172-176, 1995.
25. 2+ homeostasis and cell death. J Neurosci 15: 6239-6249, 1995.
26. Mattson MP, Calcium and neuronal injury in Alzheimer's disease. Contributions of β-amyloid precursor protein mismetabolism, free radicals, and metabolic compromise. Ann NY Acad Sci 747: 50-76, 1994.
27. Busciglio J, Yeh J and Yankner BA, β-Amyloid neurotoxicity in human cortical culture is not mediated by excitotoxins. J Neurochem 61: 1565-1568, 1993.
28. Araujo DM and Cotman CW, β-Amyloid stimulates glial cells in vitro to produce growth factors that accumulate in senile plaques in Alzheimer's disease. Brain Res 569: 141-145, 1992.
29. Yan SD, Chen X, Fu J, Chen M, Zhu H, Roher A, Slattery T, Zhao L, Nagashima M, Morser J, Migheli A, Nawroth P, Stern D and Schmidt AM, RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease. Nature 382: 685-691, 1996.
30. Yankner BA, Mechanisms of neuronal degeneration in Alzheimer's disease. Neuron 16: 921-932, 1996.
31. Martins RN, Harper CG, Stokes GB and Masters CL, Increased cerebral glucose-6-phosphate dehydrogenase activity in Alzheimer's disease may reflect oxidative stress. J Neurochem 46: 1042-1045, 1986.
32. Yankner BA, Duffy LK and Kirschner DA, Neurotrophic and neurotoxic effects of amyloid β protein: Reversal by tachykinin neuropeptides. Science 250: 279-282, 1990.
33. Mattson MP, Cheng B, Davis D, Bryant K, Lieberburg I and Rydel RE, β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J Neurosci 12: 376-389, 1992.
34. Loo DT, Copani A, Pike CJ, Whittemore ER, Walencewicz AJ and Cotman CW, Apoptosis is induced by β-amyloid in cultured central nervous system neurons. Proc Natl Acad Sci USA 90: 7951-7955, 1993.
35. Hockenbery DM, Oltvai ZN, Yin X-M, Milliman CL and Korsmeyer SJ, Bcl-2 functions in an antioxidant pathway to prevent apoptosis. Cell 75: 241-251, 1993.
36. Shearman MS, Ragan CI and Iversen LL, Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of β-amyloid-mediated cell death. Proc Natl Acad Sci USA 91: 1470-1474, 1994.
37. Behl C, Davis JB, Lesley R and Schubert D, Hydrogen peroxide mediates amyloid β protein toxicity. Cell 77: 817-827, 1994.
38. Behl C, Davis JB, Klier FG and Schubert D, Amyloid β peptide induces necrosis rather than apoptosis. Brain Res 645: 253-264, 1994.
39. Thomas T, Thomas G, McLendon C, Sutton T and Mullan M, β-Amyloid-mediated vasoactivity and vascular endothelial damage. Nature 380: 168-171, 1996.
40. Hensley K, Carney JM, Mattson MP, Aksenova M, Harris M, Wu JF, Floyd RA and Butterfield DA, A model for β-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: Relevance to Alzheimer disease. Proc Natl Acad Sci USA 91: 3270-3274, 1994.
41. Roher AE, Chaney MO, Kuo Y-M, Webster SD, Stine WB, Haverkamp LJ, Woods AS, Cotter RJ, Tuohy JM, Krafft GA, Bonnell BS and Emmerling MR, Morphology and toxicity of Aβ-(1-42) dimer derived from neuritic and vascular amyloid deposits of Alzheimer's disease. J Biol Chem 271: 20631-20635, 1996.
42. Banati RB, Gehrmann J, Czech C, Mönning U, Jones LL, König G, Beyreuther K and Kreutzberg GW, Early and rapid de novo synthesis of Alzheimer βA-4-amyloid precursor protein (APP) in activated microglia. GLIA 9: 199-210, 1993.
43. Bush AI, Multhaup G, Moir RD, Williamson TG, Small DH, Rumble B, Pollwein P, Beyreuther K and Masters CL, A novel zinc(II) binding site modulates the function of the βA4 amyloid protein precursor of Alzheimer's disease. J Biol Chem 268: 16109-16112, 1993.
44. Dyrks T, Dyrks E, Hartmann T, Masters C and Beyreuther K, Amyloidogenicity of βA4 and βA4-bearing amyloid protein precursor fragments by metal-catalyzed oxidation. J Biol Chem 267: 18210-18217, 1992.
45. Bush AI, Pettingell WH, Multhaup G, d Paradis M, Vonsattel J-P, Gusella JF, Beyreuther K, Masters CL and Tanzi RE, Rapid induction of Alzheimer Aβ amyloid formation by zinc. Science 265: 1464-1467, 1994.
46. Mantyh PW, Ghilardi JR, Rogers S, DeMaster E, Allen CJ, Stimson ER and Maggio JE, Aluminum, iron, and zinc ions promote aggregation of physiological concentrations of β-amyloid peptide. J Neurochem 61: 1171-1174, 1993.
47. Multhaup G, Identification and regulation of the high affinity binding site of the Alzheimer's disease amyloid protein precursor (APP) to glycosaminoglycans. Biochimie 76: 304-311, 1994.
48. Multhaup G, Bush AI, Pollwein P and Masters CL, Interaction between the zinc(II) and the heparin binding site of the Alzheimer's disease βA4 amyloid precursor protein (APP). FEBS Lett 355: 151-154, 1994.
49. Komiyama Y, Murakami T, Egawa H, Okubo S, Yasunaga K and Murata K, Purification of factor XIa inhibitor from human platelets. Thromb Res 66: 397-408, 1992.
50. Van Nostrand WE, Zinc (II) selectively enhances the inhibition of coagulation factor XIa by protease nexin-2/amyloid β-protein precursor. Thromb Res 78: 43-53, 1995.
51. Simons M, Ikonen E, Tienari PJ, Cidarregui A, Monning U, Beyreuther K and Dotti CG, Intracellular routing of human amyloid protein precursor: Axonal delivery followed by transport to the dendrites. J Neurosci Res 41: 121-128, 1995.
52. Hesse L, Beher D, Masters CL and Multhaup G, The βA4 amyloid precursor protein binding to copper. FEBS Lett 349: 109-116, 1994.
53. Multhaup G, Schlicksupp A, Hesse L, Beher D, Ruppert T, Masters CL and Beyreuther K, The amyloid precursor protein of Alzheimer's disease in the reduction of copper (II) to copper(I). Science 271: 1406-1409, 1996.
54. Sies H, Strategies of antioxidant defense. Eur J Biochem 215: 213-219, 1993.
55. Beckman JS, Beckman TW, Chen J, Marshall PA and Freeman BA, Apparent hydroxyl radical production by peroxynitrite: Implications for endothelial injury from nitric oxide and superoxide. Proc Natl Acad Sci USA 87: 1620-1624, 1990.
56. Chance B, Sies H and Boveris A, Hydroperoxide metabolism in mammalian organs. Physiol Rev 59: 527-605, 1979.
57. Fridovich I, Superoxide dismutases. Annu Rev Biochem 44: 147-159, 1975.
58. Halliwell B and Gutteridge JM, Role of free radicals and catalytic metal ions in human disease: An overview. Methods Enzymol 186: 1-85, 1990.
59. Takahashi M-A and Asada K, Superoxide anion permeability of phospholipid membranes and chloroplast thylakoids. Arch Biochem Biophys 226: 558-566, 1983.
60. Lynch RE and Fridovich I, Permeation of the erythrocyte stroma by superoxide radical. J Biol Chem 253: 4697-4699, 1978.
61. Halliwell B and Gutteridge JM, Biologically relevant metal ion-dependent hydroxyl radical generation. An update. FEBS Lett 307: 108-112, 1992.
62. Smith CD, Carney JM, Starke Reed PE, Oliver CN, Stadtman ER, Floyd RA and Markesbery WR, Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease. Proc Natl Acad Sci USA 88: 10540-10543, 1991.
63. Busciglio J and Yankner BA, Apoptosis and increased generation of reactive oxygen species in Down's syndrome neurons in vitro. Nature 378: 776-779, 1995.
64. Stadtman ER, Protein oxidation and aging. Science 257: 1220-1224, 1992.
65. Smith MA, Perry G, Richey PL, Sayre LM, Anderson VE, Beal MF and Kowall N, Oxidative damage in Alzheimer's. Nature 382: 120-121, 1996.
66. Pacifici RE, Sato DC and Davies KJ, Macroxyproteinase (M.O.P.): A 670 kDa proteinase complex that degrades oxidatively denatured proteins in red blood cells. Free Radic Biiol Med 7: 521-536, 1989.
67. Marcillat O, Zhang Y, Lin SW and Davies KJ, Mitochondria contain a proteolytic system which can recognize and degrade oxidatively-denatured proteins. Biochem J 254: 677-683, 1988.
68. Davies KJ and Delsignore ME, Protein damage and degradation by oxygen radicals. III. Modification of secondary and tertiary structure. J Biol Chem 262: 9908-9913, 1987.
69. Davies KJ, Lin SW and Pacifici RE, Protein damage and degradation by oxygen radicals. IV. Degradation of denatured protein. J Biol Chem 262: 9914-9920, 1987.
70. Brown RH Jr, Amyotrophic lateral sclerosis: Recent insights from genetics and transgenic mice. Cell 80: 687-692, 1995.
71. Horton WA, Eldridge R and Brody JA, Familial motor neuron disease. Evidence for at least three different types. Neurology 26: 460-465, 1976.
72. Deng H-X, Hentati A, Tainer JA, Iqbal Z, Cayabyab A, Hung W-Y, Getzoff ED, Hu P, Herzfeldt B, Roos RP, Warner C, Deng G, Soriano E, Smyth C, Parge HE, Ahmed A, Roses AD, Hallewell RA, Pericak-Vance MA and Siddique T, Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase. Science 261: 1047-1051, 1993.
73. Wong PC, Pardo CA, Borchelt DR, Lee MK, Copeland NG, Jenkins NA, Sisodia SS, Cleveland DW and Price DL, An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron 14: 1105-1116, 1995.
74. Gurney ME, Pu H, Chiu AY, Dal Canto MC, Polchow CY, Alexander DD, Caliendo J, Hentati A, Kwon YW, Deng H-X, Chen W, Zhai P, Sufit RL and Siddique T, Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation. Science 264: 1772-1775, 1994.
75. Hodgson EK and Fridovich I, The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: Inactivation of the enzyme. Biochemistry 14: 5294-5299, 1975.
76. 2 plus Cu,Zn-superoxide dismutase reflects the activity of free copper released from the oxidatively damaged enzyme. J Biol Chem 267: 25371-25377, 1992.
77. m for hydrogen peroxide. Proc Natl Acad Sci USA 93: 5709-5714, 1996.
78. Wiedau-Pazos M, Goto JJ, Rabizadeh S, Gralla EB, Roe JA, Lee MK, Valentine JS and Bredesen DE, Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis. Science 271: 515-518, 1996.
79. Rosen DR, Siddique T, Patterson D, Figlewicz DA, Sapp P, Hentati A, Donaldson D, Goto J, O'Regan JP, Deng HX, Rahmani Z, Krizus A, McKenna-Yasek D, Cayabyab A, Gaston SM, Berger R, Tanzi RE, Halperin JJ, Herzfeldt B, Van den Bergh R, Hung WY, Bird T, Deng G, Mulder DW, Smyth C, Laing NG, Soriano E, Pericak-Vance MA, Haines J, Rouleau GA, Gusella JS, Horvitz HR and Brown RH Jr, Mutations in Cu/Zu superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362: 59-62, 1993.
80. Epstein CJ, Avraham KB, Lovett M, Smith S, Elroy Stein O, Rotman G, Bry C and Groner Y, Transgenic mice with increased Cu/Zn-superoxide dismutase activity: Animal model of dosage effects in Down syndrome. Proc Natl Acad Sci USA 84: 8044-8048, 1987.
81. Fitzgerald DJ, Zinc and Alzheimer's disease Science 268: 1920 (discussion 1921-1923), 1995.
82. Hershey CO, Hershey LA, Varnes A, Vibhakar SD, Lavin P and Strain WH, Cerebrospinal fluid trace element content in dementia: Clinical, radiologic, and pathologic correlations. Neurology 33: 1350-1353, 1983.
83. Basun H, Forssell LG, Wetterberg L and Winblad B, Metals and trace elements in plasma and cerebrospinal fluid in normal aging and Alzheimer's disease. J Neural Transm Park Dis Dement Sect 3: 231-258, 1991.
84. Pike CJ and Cotman CW, Cultured GABA-immunoreactive neurons are resistant to toxicity induced by β-amyloid. Neuroscience 56: 269-274, 1993.
85. Dyrks T, Dyrks E, Mönning U, Urmoneit B, Turner J and Beyreuther K, Generation of βA4 from the amyloid protein precursor and fragments thereof. FEBS Lett 335: 89-93, 1993.