Chapter 5 Mitochondrial Abnormalities in Neurodegenerative Disorders

Blue Books of Practical Neurology

Volumn 26, Issue C, 2002, Pages 143-174

  Tabrizi, Sarah J ^a   Schapira, Anthony H V ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

EID: 77957169293     PISSN: 18773419     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1877-3419(09)70064-9     Document Type: Article

References (248)

1. Halliwell B., and Gutteridge J.M.C. Free Radicals in Biology and Medicine. (1989), Oxford University Press, New York
2. Boveris A., and Chance B. The mitochondrial generation of hydrogen peroxide. Biochem J 134 (1973) 707-716
3. Freeman B.A., and Crapo J.D. Free radicals and tissue injury. Lab Invest 47 (1982) 412-426
4. Cadenas E., Boveris A., Ragan C.I., and Stoppani A. Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria. Arch Biochem Biophys 180 (1977) 248-257
5. Nohl H., and Jordan W. The mitochondrial site of superoxide formation. Biochem Biophys Res Commun 138 (1986) 533-539
6. Turrens J.F. Superoxide production by the mitochondrial respiratory chain. Biosci Rep 17 (1997) 3-8
7. Turrens J.F., and Boveris A. Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem J 191 (1980) 421-427
8. Beckman J.S., Carson M., Smith C.D., and Koppenol W.H. ALS, SOD and peroxynitrite. Nature 364 (1993) 584
9. Moncada S., Palmer R.M., and Higgs E.A. The biological significance of nitric oxide formation from L-arginine. Biochem Soc Trans 17 (1989) 642-644
10. Hobbs A.J., Higgs A., and Moncada S. Inhibition of nitric oxide synthase as a potential therapeutic target. Annu Rev Pharmacol Toxicol 39 (1999) 191-220
11. Lincoln J., Hoyle C.H.V., and Burnstock G. Nitric Oxide in Health and Disease: Biomedical Research Topics. (1997), Cambridge University Press, Cambridge UK
12. Simonian N.A., and Coyle J.T. Oxidative stress in neurodegenerative diseases. Annu Rev Pharmacol Toxicol 36 (1996) 83-106
13. Beckman J.S., and Tsai J.H. Reactions and diffusion of nitric oxide and peroxynitrite. Biochemist (1994) 8-10 Oct/Nov
14. Beckman J.S., Beckman T.W., Chen J., et al. Apparent hydroxyl radical production by peroxynitrite-implications for endothelial injury from nitric oxide and superoxide. Proc Natl Acad Sci U S A 87 (1990) 1620-1624
15. Vieral L., Ye Y.Z., Estevez A.G., and Beckman J.S. Immunohistochemical methods to detect nitrotyrosine. Methods Enzymol 301 (1999) 373-381
16. Halliwell B., and Gutteridge J.M.C. Oxygen radicals and the nervous system. Trends Neurosci 6 (1985) 22-26
17. Parkes T.L., Elia A.J., Dickinson D., et al. Extension of Drosophila lifespan by overexpression of human SOD1 in motorneurons. Nat Genet 19 (1998) 171-174
18. Rosen D.R., Siddique T., Patterson D., et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362 (1993) 59-62
19. Yim M.B., Kang J.H., Yim H.S., et al. A gain-of-function of an amyotrophic lateral sclerosis-associated CuZn-superoxide dismutase mutant: an enhancement of free radical formation due to a decrease in Km for hydrogen peroxide. Proc Natl Acad Sci U S A 93 (1996) 5709-5714
20. Cross C.E., Halliwell B., Borish E.T., et al. Oxygen radicals and human disease. Ann Intern Med 107 (1987) 526-545
21. Frei F., Kim M.C., and Ames B.N. Ubiquinol-10 is an effective lipid soluble antioxidant at physiological concentrations. Proc Natl Acad Sci U S A 84 (1990) 4879-4883
22. Finkel T., and Holbrook N.J. Oxidants, oxidative stress and the biology of ageing. Nature 408 (2000) 239-245
23. Beckman J.S. Peroxynitrite versus hydroxyl radical: the role of nitric oxide in superoxide-dependent cerebral injury. Ann N Y Acad Sci 738 (1994) 382-387
24. Brawn K., and Fridovich I. DNA strand scission by enzymatically generated oxygen free radicals. Arch Biochem Biophys 206 (1981) 414-419
25. Ames B.N. Endogenous DNA damage as related to cancer and ageing. Mutat Res 214 (1989) 41-46
26. Kasai H., Crain P.F., Kuchino Y., et al. Formation of 8-hydroxyguanine moiety in cellular DNA by agents producing oxygen radicals and evidence for its repair. Carcinogenesis 7 (1986) 1849-1851
27. Stadtman E.R. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu Rev Biochem 62 (1993) 797-821
28. Oliver C.N., Ahn B.W., Moerman E.J., et al. Age-related changes in oxidised proteins. J Biol Chem 262 (1987) 5488-5491
29. Mecocci P., MacGarvey U., Kaufman A.E., et al. Oxidative damage to mitochondrial DNA shows marked age-dependent increases in human brain. Ann Neurol 34 (1993) 609-616
30. Richter C., Park J.W., and Ames B.N. Normal oxidative damage to mitochondrial and nuclear DNA is extensive. Proc Natl Acad Sci U S A 85 (1988) 6465-6467
31. Trounce I., Byrne E., and Marzuki S. Decline in skeletal muscle mitochondrial respiratory chain function, possible factor in ageing. Lancet 1 (1989) 637-639
32. Wallace D.C. Mitochondrial DNA Mutations and Bioenergetic Defects in Aging and Neurodegenerative Diseases. In: Rosenberg R.N., Prusiner S.B., Di Mauro S., and Barchi R.L. (Eds). The Molecular and Genetic Basis of Neurological Disease. (1997), Butterworth-Heinemann, Boston 237-269
33. Melov S., Shoffner J.M., Kaufman A., and Wallace D.C. Marked increase in the number and variety of mitochondrial DNA rearrangements in aging human skeletal muscle. Nucleic Acids Res 23 (1995) 4122-4126
34. Corral-Debrinski M., Horton T., Lott M.T., et al. Mitochondrial DNA deletions in human brain: regional variability and increase with advanced age. Nat Genet 2 (1992) 324-329
35. Soong N.W., Hinton D.R., Cortopassi G., and Arnheim N. Mosaicism for a specific somatic mitochondrial DNA mutation in adult human brain. Nat Genet 2 (1992) 318-323
36. Cortopassi G.A., and Wong A. Mitochondria in organismal aging and degeneration. Biochimica Biophysica Acta 1410 (1999) 183-191
37. Hillered L., and Ernster L. Respiratory activity of isolated rat brain mitochondria following in vitro exposure to oxygen radicals. J Cereb Blood Flow Metab 3 (1983) 207-214
38. Zhang Y., Marcillat O., Giulivi C., et al. The oxidative inactivaton of mitochondrial electron transport chain components and ATP. J Biol Chem 265 (1990) 16330-16336
39. Benzi G., Curti D., Pastoris O., et al. Sequential damage in mitochondrial complexes by peroxidative stress. Neurochem Res 16 (1991) 1295-1302
40. Hartley A., Cooper J.M., and Schapira A. Iron induced oxidative stress and mitochondrial dysfunction: relevance to Parkinson's disease. Brain Res 627 (1993) 349-353
41. Thomas P.K., Cooper J.M., King R.H.M., et al. Myopathy in vitamin E deficient rats: muscle fibre necrosis associated with disturbances of mitochondrial function. J Anat 183 (1993) 451-461
42. Richter C., Gogvadze V., Laffranchi R., et al. Oxidants in mitochondria: from physiology to diseases. Biochim Biophys Acta 1271 (1995) 67-74
43. +) induces NADH dependent superoxide formation, and enhances NADH-dependent lipid peroxidation in bovine heart submitochondrial particles. Biochem Biophys Res Commun 170 (1990) 1049-1055
44. Esposito L.A., Melov S., Panov A., et al. Mitochondrial disease in mouse results in increased oxidative stress. Proc Natl Acad Sci U S A 96 (1999) 4820-4825
45. Li Y.B., Huang T.T., Carlson E.J., et al. Dilated cardiomyopathy and neonatal lethality in mutant mice lacing manganese superoxide dismutase. Nat Genet 11 (1995) 376-381
46. Lebovitz R.M., Zhang H., Vogel H., et al. Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice. Proc Natl Acad Sci U S A 93 (1996) 9782-9787
47. Melov S., Schneider J.A., Day B.J., et al. A novel neurological phenotype in mice lacking mitochondrial manganese superoxide dismutase. Nat Genet 18 (1998) 159-163
48. Melov S., Coskun P., Patel M., et al. Mitochondrial disease in superoxide dismutase 2 mutant mice. Proc Natl Acad Sci U S A 96 (1999) 846-851
49. Heales S.J., Bolanos J.P., Stewart V.C., et al. Nitric oxide, mitochondria and neurological disease. Biochim Biophys Acta 1410 (1999) 215-228
50. Cleeter M.J.W., Cooper J.M., Darley-Usmar V.M., et al. Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide. Implications for neurodegenerative diseases. FEBS Letts 345 (1994) 50-54
51. Bolanos J.P., Peuchen S., Heales S.J.R., et al. Nitric oxide-mediated inhibition of the mitochondrial respiratory chain in cultured astrocytes. J Neurochem 63 (1994) 910-916
52. Bolanos J.P., Heales S.J., Land J.M., and Clark J.B. Effect of peroxynitrite on the mitochondrial respiratory chain: differential susceptibility of neurones and astrocytes in primary culture. J Neurochem 64 (1995) 1965-1972
53. Soussi B., Idstrom J.P., Schersten T., and Bylund-Fellenius A.C. Cytochrome c oxidase and cardiolipin alterations in response to skeletal muscle ischaemia and reperfusion. Acta Physiol Scand 138 (1990) 107-114
54. Heales S.J., Bolanos J.P., Land J.M., and Clark J.B. Trolox protects mitochondrial complex IV from nitric oxide-mediated damage in astrocytes. Brain Res 668 (1994) 243-245
55. Brookes P.S., Land J.M., Clark J.B., and Heales S.J. Peroxynitrite and brain mitochondria: evidence for increased proton leak. J Neurochem 70 (1998) 2195-2202
56. Bolanos J.P., Almeida A., Stewart V., et al. Nitric oxide-mediated mitochondrial damage in the brain: mechanisms and implications for neurodegenerative diseases. J Neurochem 68 (1997) 2227-2240
57. Radi R., Rodriguez M., Castro L., and Telleri R. Inhibition of mitochondrial electron transport by peroxynitrite. Arch Biochem Biophys 308 (1994) 89-95
58. Olney J.W. Brain lesion, obesity and other disturbances in mice treated with monosodium glutamate. Science 164 (1969) 719-721
59. Olney J.W. Glutamate induced neuronal necrosis in the infant mouse hypothalamus. An electron microscopic study. J Neuropathol Exp Neurol 30 (1971) 75-90
60. Olney J.W., Ho O.L., and Rhee V. Cytotoxic effects of acidic and sulphur containing amino acids on the infant mouse central nervous system. Exp Brain Res 14 (1971) 16-76
61. Gasic G.P., and Hollmann M. Molecular neurobiology of glutamate receptors. Annu Rev Physiol 54 (1992) 507-536
62. Lipton S.A., and Rosenberg P.A. Excitatory amino acids as a final common pathway for neurological disorders. N Engl J Med 330 (1994) 613-622
63. Choi D.W., Maulucci-Gedde M., and Kriegstein A.R. Glutamate neurotoxicity in cortical cell culture. J Neurosci 7 (1987) 357-368
64. 2+ of NMDA responses in spinal cord neurones. Nature 309 (1984) 261-263
65. Nicholls D.G. Proteins, Transmitters and Synapses. (1994), Blackwells, London 155
66. McDermott A.B., Mayer M.L., Westbrook G.L., et al. NMDA-receptor activation increases cytoplasmic calcium concentration in cultured spinal cord neurones. Nature 321 (1986) 519-522
67. Orrenius S., Ankarcrona M., and Nicotera P. Mechanisms of calcium-related cell death. Adv Neurol 71 (1996) 137-151
68. Choi D.W. Glutamate neurotoxicity and diseases of the nervous system. Neuron 1 (1988) 623-634
69. Clark G.D., Happel L.T., Zorumski C.F., and Bazan N.G. Enhancement of hippocampal excitatory synaptic transmission by platelet-activating factor. Neuron 9 (1992) 1211-1216
70. 2+ in hippocampal neurons. Neuron 9 (1992) 285-294
71. Miller B., Sarantis M., Traynelis S.F., and Attwell D. Potentiation of NMDA receptor currents by arachidonic acid. Nature 355 (1992) 722-725
72. Volterra A., Trotti D., Cassutti P., et al. High sensitivity of glutamate uptake to extracellular free arachidonic acid levels in rat cortical synaptosomes and astrocytes. J Neurochem 59 (1992) 600-606
73. Lafon-Cazal M., Pietri S., Culcasi M., and Bockaert J. NMDA-dependent superoxide production and neurotoxicity. Nature 364 (1993) 535-537
74. Dawson V.L., Dawson T.M., London E.D., et al. Nitric oxide mediates glutamate neurotoxicity in primary cortical cultures. Proc Natl Acad Sci U S A 88 (1991) 6368-6371
75. Dawson V.L., Dawson T.M., Bartley D.A., et al. Mechanisms of nitric oxide-mediated neurotoxicity in primary brain cultures. J Neurosci 13 (1993) 2651-2661
76. Dawson V.L., Kizushi V.M., Huang P.L., et al. Resistance to neurotoxicity in cortical cultures from neuronal nitric oxide synthase-deficient mice. J Neurosci 16 (1996) 2479-2487
77. Swan J.H., and Meldrum B.S. Protection by NMDA antagonists against selective cell loss following transient ischaemia. J Cereb Blood Flow Metab 10 (1990) 343-351
78. Novelli A., Reilly J.A., Lysko P.G., and Henneberry R.C. Glutamate becomes neurotoxic via the N-methyl-D-aspartate receptor when intracellular energy levels are reduced. Brain Res 451 (1988) 205-212
79. Simpson J.R., and Isacson O. Mitochondrial impairment reduces the threshold for in vivo NMDA-mediated neuronal death in the striatum. Exp Neurol 121 (1993) 57-64
80. Zeevalk G.D., and Nicklas W.J. Mechanisms underlying initiation of excitotoxicity associated with metabolic inhibition. J Pharmacol Exp Ther 257 (1991) 870-878
81. Nowak L., Bregestovski P., Ascher P., et al. Magnesium gates glutamate-activated channels in mouse central neurones. Nature 307 (1984) 462-465
82. Zeevalk G.D., and Nicklas W.J. Chemically induced hypoglycaemia and anoxia: relationship to glutamate receptor-mediated toxicity in retina. J Pharmacol Exp Ther 253 (1990) 1285-1292
83. Reynolds I.J., and Hastings T.G. Glutamate induces the production of reactive oxygen species in cultured forebrain neurons following NMDA receptor activation. J Neurosci 15 (1995) 3318-3327
84. Dugan L.L., Sensi S.L., Canzoniero L.M., et al. Mitochondrial production of reactive oxygen species in cortical neurons following exposure to N-methyl-D-aspartate. J Neurosci 15 (1995) 6377-6388
85. Schinder A.F., Olson E.C., Spitzer N.C., and Montal M. Mitochondrial dysfunction is a primary event in glutamate neurotoxicity. J Neurosci 16 (1996) 6125-6133
86. White R.J., and Reynolds I.J. Mitochondrial depolarization in glutamate stimulated neurones-an early signal specific to excitotoxin exposure. J Neurosci 16 (1996) 5688-5697
87. Stout A.K., Raphael H.M., Kanterewicz B.I., et al. Glutamate-induced neuron death requires mitochondrial calcium uptake. Nat Neurosci 1 (1998) 366-373
88. Loeffler M., and Kroemer G. The mitochondrion in cell death control: certainties and incognita. Exp Cell Res 256 (2000) 19-26
89. Zamzami K., and Kroemer G. The mitochondrion in apoptosis: how Pandora's box opens. Nat Rev Mol Cell Biol 2 (2001) 67-71
90. Ferri K.F., and Kroemer G. Mitochondria-the suicide organelles. Bioassays 23 (2001) 111-115
91. Campuzano V., Montermini L., Molto M.D., et al. Friedreich's ataxia: autosomal recessive disease caused by an intronic GAA triplet repeat expansion. Science 271 (1996) 1423-1427
92. Campuzano V., Montermini L., Lutz Y., et al. Frataxin is reduced in Friedreich ataxia patients and is associated with mitochondrial membranes. Hum Mol Genet 6 (1997) 1771-1780
93. Cossee M., Durr A., Schmitt M., et al. Friedreich's ataxia: point mutations and clinical presentation of compound heterozygotes. Ann Neurol 45 (1999) 200-206
94. Priller J., Scherzer C.R., Faber P.W., et al. Frataxin gene of Friedreich's ataxia is targeted to mitochondria. Ann Neurol 42 (1997) 265-269
95. Koutnikova H., Campuzano V., Foury F., et al. Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin. Nat Genet 16 (1997) 345-351
96. Wilson R.B., and Roof D.M. Respiratory deficiency due to loss of mitochondrial DNA in yeast lacking the frataxin homologue. Nat Genet 16 (1997) 352-357
97. Radisky D.C., Babcock M.C., and Kaplan J. The yeast frataxin homologue mediates mitochondrial iron efflux. Evidence for a mitochondrial iron cycle. J Biol Chem 274 (1999) 4497-4499
98. Rotig A., De Lonlay P., Chretien D., et al. Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich ataxia. Nat Genet 17 (1997) 215-217
99. Bradley J.L., Blake J.C., Chamberlain S., et al. Clinical, biochemical and molecular genetic correlations in Friedreich's ataxia. Hum Mol Genet 9 (2000) 275-282
100. Hausladen A., and Fridovich I. Superoxide and peroxynitrite inactivates aconitases, but nitric oxide does not. J Biol Chem 269 (1994) 29405-29408
101. Castro L., Rodriguez M., and Radi R. Aconitase is readily inactivated by peroxynitrite, but not by its precursor nitric oxide. J Biol Chem 47 (1994) 29409-29415
102. Waldvogel D., vanGelderen P., and Hallett M. Increased iron in the dentate nucleus of patients with Friedreich's ataxia. Ann Neurol 46 (1999) 123-125
103. Wong A., Yang J., Cavadini P., et al. The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis. Hum Mol Genet 8 (1999) 425-430
104. Delatycki M.B., Camakaris J., Brooks H., et al. Direct evidence that mitochondrial iron accumulation occurs in Friedreich's ataxia. Ann Neurol 45 (1999) 673-675
105. Lodi R., Cooper J.M., Bradley J.L., et al. Deficit of in vivo mitochondrial ATP production in patients with Friedreich ataxia. Proc Natl Acad Sci U S A 96 (1999) 11492-11495
106. Johns D.R. Mitochondrial DNA and disease. N Engl J Med 333 (1995) 638-644
107. Gotoda T., Arita M., and Arai H. Adult-onset spinocerebellar dysfunction caused by a mutation in the gene for (alpha)-tocopherol-transfer protein. N Engl J Med 333 (1995) 1313-1318
108. Rustin P., von Kleist-Retzow J.C., Chantrel-Groussard K., et al. Effect of idebenone on cardiomyopathy in Friedreich's ataxia: a preliminary study. Lancet 354 (1999) 477-479
109. Lodi R., Hart P.E., Rajagopalan B., et al. Antioxidant treatment improves in vivo cardiac and skeletal muscle bioenergetics in patients with Friedreich's ataxia. Ann Neurol 49 5 (2001) 590-596
110. Casari G., De Fusco M., Ciarmaton S., et al. Spastic paraplegia and OXPHOS impairment caused by mutations in paraplegin, a nuclear-encoded mitochondrial metalloprotease. Cell 93 (1998) 973-983
111. Lutsenko S., and Cooper M.J. Localization of the Wilson's disease protein product to mitochondria. Proc Natl Acad Sci U S A 95 (1998) 6004-6009
112. Gu M., Cooper J.M., Butler P., et al. Oxidative-phosphorylation defects in liver of patients with Wilson's disease. Lancet 356 (2000) 469-474
113. Katzman R. Alzheimer's disease. N Engl J Med 314 (1986) 964-973
114. Goate A., Chartier-Harlin M.C., Mullan M., et al. Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease. Nature 349 (1991) 704-706
115. Levy-Lahad E., Wasco W., Poorkaj P., et al. Candidate gene for the chromosome 1 familial Alzheimer's disease locus. Science 269 (1995) 973-977
116. Sherrington R., Rogaev E.L., Liang Y., et al. Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature 375 (1995) 754-760
117. Bonilla E., Tanji K., Hirano M., et al. Mitochondrial involvement in Alzheimer's disease. Biochim Biophys Acta 1410 (1999) 171-182
118. 18Fluorodeoxyglucose positron emission tomography studies in presumed Alzheimer's cases, including 13 serial scans. Can J Neurol Sci 171 (1990) 1-11
119. Smith G.S., de Leon M.J., George A.E., et al. Topography of cross-sectional and longitudinal glucose metabolic deficits in Alzheimer's disease: pathophysiologic implications. Arch Neurol 49 (1992) 1142-1150
120. Reiman E.M., Caselli R.J., Yun L.S., et al. Preclinical evidence of Alzheimer's disease in persons homozygous for the e4 allele for apolipoprotein E. N Engl J Med 334 (1996) 752-758
121. Kish S.J., Bergeron C., Rajput A., et al. Brain cytochrome oxidase in Alzheimer's disease. J Neurochem 59 (1992) 776-779
122. Parker W.D., Mahr N.J., Filley C.M., et al. Reduced platelet cytochrome c oxidase activity in Alzheimer's disease. Neurology 44 (1994) 1086-1090
123. Parker W.D., Parks J., Filley C.M., and Kleinschmidt-DeMasters B.K. Electron transport chain defects in Alzheimer's disease. Neurology 44 (1994) 1090-1096
124. Mutisya E.M., Bowling A.C., and Beal M.F. Cortical cytochrome oxidase activity is reduced in Alzheimer's disease. J Neurochem 63 (1994) 2179-2184
125. Simonian N., and Hyman B.T. Functional alterations in Alzheimer's disease: diminution of cytochrome oxidase in the hippocampal formation. J Neuropathol Exp Neurol 52 (1993) 580-585
126. Hevner R.F., and Wong-Riley M.T. Neuronal expression of nuclear and mitochondrial genes for cytochrome oxidase (CO) subunits analyzed by in situ hybridization: comparison with CO activity and protein. J Neurosci 11 (1991) 1942-1958
127. Davis R.E., Miller S., Herrnstadt C., et al. Mutations in mitochondrial cytochrome c oxidase genes segregate with late-onset Alzheimer disease. Proc Natl Acad Sci U S A 94 (1997) 4526-4531
128. Truong D.D., Harding A.E., Scaravilli F., et al. Movement disorders in mitochondrial myopathies: a report of nine cases with two autopsy studies. Mov Disord 5 (1990) 109-117
129. Fahn S., Marsden C.D., and Calne D.B. Classification and Investigation of Dystonia. In: Fahn S., and Marsden C.D. (Eds). Movement Disorders 2, Neurology 7. (1987), Butterworth-Heinemann, Oxford, UK 332-355
130. Jun A.S., Brown M.D., and Wallace D.C. A mitochondrial DNA mutation at nucleotide pair 14459 of the NADH dehydrogenase subunit 6 gene associated with maternally inherited Leber hereditary optic neuropathy and dystonia. Proc Natl Acad Sci U S A 91 (1994) 6202-6210
131. Jun A.S., Trounce I.A., Brown M.D., et al. Use of transmitochondrial cybrids to assign a complex I defect to the mitochondrial DNA-encoded NADH dehydrogenase subunit 6 gene mutation at nucleotide pair 14459 that causes Leber hereditary optic neuropathy and dystonia. Mol Cell Biol 16 (1996) 771-777
132. De Vries D.D., Went L.N., Bruyn G.W., et al. Genetic and biochemical impairment of mitochondrial complex I activity in a family with Leber hereditary optic neuropathy and hereditary spastic dystonia. Am J Hum Genet 58 (1996) 703-711
133. Koehler C.M., Leuenberger D., Merchant S., et al. Human deafness dystonia syndrome is a mitochondrial disease. Proc Natl Acad Sci U S A 96 (1999) 2141-2146
134. Wallace D.C., and Murdock D.G. Mitochondria and dystonia: the movement disorder connection?. Proc Natl Acad Sci U S A 96 (1999) 1817-1819
135. Benecke R., Strümper P., and Weiss H. Electron transfer complex I defect in idiopathic dystonia. Ann Neurol 32 (1992) 683-686
136. Schapira A., Warner T., Gash M.T., et al. Complex I function in familial and sporadic dystonia. Ann Neurol 41 (1997) 556-559
137. Tabrizi S.J., Cooper J.M., and Schapira A. Mitochondrial DNA in focal dystonia: a cybrid analysis. Ann Neurol 44 (1998) 258-261
138. Cookson M.R., and Shaw P.J. Oxidative stress and motor neurone disease. Brain Pathol 9 (1999) 165-186
139. Beal M.F. Mitochondria and the pathogenesis of ALS. Brain 123 (2000) 1291-1292
140. Cudkowicz M.E., McKenna-Yasek D., Sapp P.E., et al. Epidemiology of mutations in superoxide dismutase in amyotrophic lateral sclerosis. Ann Neurol 41 (1997) 210-221
141. Shaw C.E., Enayat Z.E., Chioza B.A., et al. Mutations in all five exons of SOD-1 may cause ALS. Ann Neurol 43 (1998) 390-393
142. Siddique T., Nijhawan D., and Hentat A. Molecular genetic basis of familial ALS. Neurology 47 (1996) S27-S35
143. Crow J.P., Sampson J.B., Zhuang Y., et al. Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite. J Neurochem 69 (1997) 1936-1944
144. Estevez A.G., Crow J.P., Sampson J.B., et al. Induction of nitric oxide-dependant apoptosis in motor neurons by zinc-deficient superoxide dismutase. Science 286 (1999) 2498-2500
145. Gurney M.E., Pu H., Chiu A.Y., et al. Motor neuron degeneration in mice that express a human CuZn superoxide dismutase mutation. Science 264 (1994) 772-775
146. Wong P.C., Pardo C.A., Borchelt D.R., et al. An adverse property of a familiar ALS-linked SOD1 mutation causes motor neuron disease characterised by vacuolar degeneration of mitochondria. Neuron 14 (1995) 1105-1116
147. Bruijn L.I., Beal M.F., Becher M.W., et al. Elevated free nitrotyrosine levels, but not protein bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis. A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 72 (1993) 971-983
148. Nasir J., Floresco S.B., O'Kusky J.R., et al. Targeted disruption of the Huntington's disease gene results in embryonic lethality and behavioural changes in heterozygotes. Cell 81 (1995) 811-823
149. Zeitlin S., Liu J.P., Chapman D.L., et al. Increased apoptosis and early embryonic lethality in mice nullizygous for the Huntington's disease gene homolog. Nat Genet 11 (1995) 155-163
150. Rubinsztein D.C., Amos W., Leggo J., et al. Mutational bias provides a model for the evolution of Huntington's disease and predicts a general increase in disease prevalence. Nat Genet 7 (1994) 525-530
151. Strong T.V., Tagle D.A., Valdes J.M., et al. Widespread expression of the human and rat Huntington's disease gene in brain and non-neural tissues. Nat Genet 5 (1993) 259-265
152. Trottier Y., Devys D., Imbert G., et al. Cellular localization of the Huntington's disease protein and discrimination of the normal and mutated form. Nat Genet 10 (1995) 104-110
153. Cooper J.K., Schilling G., Peters M.F., et al. Truncated N-terminal fragments of huntingtin with expanded glutamine repeats form nuclear and cytoplasmic aggregates in cell culture. Hum Mol Genet 7 (1998) 783-790
154. Li S.H., and Li X.J. Aggregation of N-terminal huntingtin is dependent on the length of its glutamine repeats. Hum Mol Genet 7 (1998) 777-782
155. Martindale D., Hackam A., Wieczorek A., et al. Length of huntingtin and its polyglutamine tract influences localization and frequency of intracellular aggregates. Nat Genet 18 (1998) 150-154
156. Difiglia M., Sapp E., Chase K.O., et al. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277 (1997) 1990-1993
157. Davies S.W., Turmaine M., Cozens B.A., et al. Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell 90 (1997) 537-548
158. Beal M.F. Does impairment of energy metabolism result in excitotoxic neuronal death in neurodegenerative illnesses?. Ann Neurol 31 (1992) 119-130
159. Coyle J.T., and Schwarz R. Lesions of striatal neurones with kainic acid provides a model for Huntington's chorea. Nature 263 (1976) 244-246
160. McGeer E.G., and McGeer P.L. Duplication of biochemical changes of Huntington's chorea by intrastriatal injections of glutamic and kainic acids. Nature 263 (1976) 517-519
161. Schwarz R., Whetsell W.O., and Mangano R.M. Quinolinic acid: an endogenous metabolite that produces axon-sparing lesions in rat brain. Science 219 (1983) 316-318
162. Beal M.F., Kowell N.W., Ellison D.W., et al. Replication of the neurochemical characteristics of Huntington's disease by quinolinic acid. Nature 321 (1986) 168-171
163. Beal M.F., Kowell N.W., Ferrante R.J., and Cippolloni P.B. Quinolinic acid striatal lesions in primates as a model of Huntington's disease. Ann Neurol 26 (1989) 137
164. Sanberg P.R., Lehmann J., and Fibiger H.C. Impaired learning and memory after kainic acid lesions of the striatum, a behavior model of Huntington's disease. Brain Res 149 (1978) 546-551
165. Sanberg P.R., Calderon S.F., Guordana M., et al. The quinolinic acid model of Huntington's disease: locomotor abnormalities. Exp Neurol 105 (1989) 45-53
166. Storey E., Cipolloni P.B., Ferrante R.J., et al. Movement disorder following excitotoxin lesions in primates. Neuroreport 5 (1994) 1259-1261
167. Koh J.Y., Peters S., and Choi D.W. Neurons containing NADPH-diaphorase are selectively resistant to quinolinate toxicity. Science 234 (1986) 73-76
168. Taylor-Robinson S.D., Weeks R.A., Bryant D.J., et al. Proton magnetic resonance spectroscopy in Huntington's disease: evidence in favour of the glutamate excitotoxic theory. Mov Disord 11 (1996) 167-173
169. Young A.B., Greenmayre J.T., Hollingsworth Z., et al. NMDA receptor losses in putamen from patients with Huntington's disease. Science 241 (1988) 981-983
170. 3H]AMPA binding in layer VI of frontal cortex in Huntington's disease. Exp Neurol 127 (1994) 70-75
171. Myers R.H., Sax D.S., Koroshetz W.J., et al. Factors associated with slow progression in Huntington's disease. Arch Neurol 48 (1991) 800-804
172. Mann V.M., Cooper J.M., Javoy-Agid F., et al. Mitochondrial function and parental sex effect in Huntington's disease. Lancet 336 (1990) 749
173. Gu M., Cooper J.M., Gash M., et al. Mitochondrial defect in Huntington's disease caudate nucleus. Ann Neurol 39 (1996) 385-389
174. Browne S.E., Bowling A.C., MacGarvey U., et al. Oxidative damage and metabolic dysfunction in Huntington's disease: selective vulnerability of the basal ganglia. Ann Neurol 41 (1997) 646-653
175. Tabrizi S.J., Cleeter M., Xuereb J., et al. Biochemical abnormalities and excitotoxicity in Huntington's disease brain. Ann Neurol 45 (1999) 25-32
176. Patel M., Day B.J., Crapo J.D., et al. Requirement for superoxide in excitotoxic cell death. Neuron 16 (1996) 345-355
177. Brouillet E., Jenkins B.G., Hyman B.T., et al. Age-dependent vulnerability of the striatum to the mitochondrial toxin 3-nitropropionic acid. J Neurochem 60 (1993) 356-359
178. Beal M.F., Brouillet E., Jenkins B., et al. Neurochemical and histologic characterisation of excitotoxic lesions produced by the mitochondrial toxin 3-nitropropionic acid. J Neurosci 13 (1993) 4181-4192
179. Brouillet E., Hantraye P., Ferrante R.J., et al. Chronic mitochondrial energy impairment produces selective striatal degeneration and abnormal choreiform movements in primates. Proc Natl Acad Sci U S A 92 (1995) 7105-7109
180. Weller M., and Paul S.M. 3-nitroprionic acid is an indirect excitotoxin in cultured cerebellar granule neurons. Eur J Pharmacol 248 (1993) 223-228
181. Beal M.F., Brouillet E., Jenkins B., et al. Age-dependent striatal excitotoxic lesions produced by the endogenous mitochondrial inhibitor malonate. J Neurochem 61 (1993) 1147-1150
182. Greene J.G., Porter R.H.P., Eller R.V., and Greenmayre J.T. Inhibition of succinate dehydrogenase by malonic acid produces an "excitotoxic" lesion in rat striatum. J Neurochem 61 (1993) 1151-1154
183. Henshaw R., Jenkins B.G., Schulz J.B., et al. Malonate produces striatal lesions by indirect NMDA receptor activation. Brain Res 647 (1994) 161-166
184. Ludolph A.C., He F., Spencer P.S., et al. 3-nitropropionic acid: exogenous animal neurotoxin and possible human striatal toxin. Can J Neurol Sci 18 (1991) 492-498
185. Kuwert T., Lange H.W., Langer K.-J., et al. Cortical and subcortical glucose consumption measured by PET in patients with Huntington's disease. Brain 113 (1990) 1405-1423
186. Martin W.R.W., Clark C., Ammann W., et al. Cortical glucose metabolism in Huntington's disease. Neurology 42 (1992) 223-229
187. 1H NMR spectroscopy. Neurology 43 (1993) 2689-2695
188. 1H NMR spectroscopy studies in Huntington's disease: correlations with CAG repeat numbers. Neurology 5 (1998) 1357-1365
189. Hoang T.Q., Dubowitz D.J., Moats R., et al. Quantitative proton-decoupled P-31 MRS and H-1 MRS in the evaluation of Huntington's and Parkinson's disease. Neurology 50 (1998) 1033-1040
190. 10. Ann Neurol 41 (1997) 160-165
191. Arenas J., Campos Y., Ribacoba R., et al. Complex I defect in muscle from patients with Hunting-ton's disease. Ann Neurol 43 (1998) 397-400
192. Lodi R., Schapira A., Manners D., et al. Abnormal in vivo skeletal muscle energy metabolism in Huntington's disease and dentatorubropallidoluysian atrophy. Ann Neurol 48 (2000) 72-76
193. Mangiarini L., Sathasivam K., Seller M., et al. Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice. Cell 87 (1996) 493-506
194. Cha J.H.J., Kosinski C.M., Kerner J.A., et al. Altered brain neurotransmitter receptors in transgenic mice expressing a portion of an abnormal human Huntington disease gene. Proc Natl Acad Sci U S A 95 (1998) 6480-6485
195. Calabresi P., Pisani A., Mercuri N.B., and Bernardi G. The corticospinal projection: from synaptic plasticity to dysfunction of the basal ganglia. Trends Neurosci 19 (1996) 19-24
196. Petralia R.S., Wang Y.X., Niedzielski A.S., and Wenthold R.J. The metabotropic glutamate receptors, mGluR2 and mGluR3, show unique postsynaptic, presynaptic and glial localisation. Neuroscience 71 (1996) 949-976
197. Levine M.S., Chesselet M.F., Koppel A., et al. Enhanced sensitivity to glutamate receptor activation in mouse models of Huntington's disease. Soc Neurosci Abstr 24 (1998) 972
198. Tabrizi S.J., Mangiarini L., Workman J., et al. Biochemical abnormalities and excitotoxicity in the R6/2 HD transgenic mouse. Ann Neurol 47 (2000) 80-86
199. Sawa A., Wiegand G.W., Cooper J., et al. Increased apoptosis of Huntington disease lymphoblasts associated with repeat length-dependent mitochondrial depolarisation. Nat Med 5 (1999) 1194-1198
200. Ferrante R.J., Andreassen O.A., Jenkins B.G., et al. Neuroprotective effects of creatine in a transgenic mouse model of Huntington's disease. J Neurosci 20 (2000) 4389-4397
201. Polymeropoulos M.H., Lavedan C., Leroy E., et al. Mutation in the alpha-synuclein gene identified in families with Parkinson's disease. Science 276 (1997) 2045-2047
202. Kruger R., Kuhn W., Muller T., et al. Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease. Nat Genet 18 (1998) 106-108
203. Kitada T., Asakawa S., Hattori N., et al. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392 (1998) 605-608
204. Leroy E., Boyer R., Auburger G., et al. The ubiquitin pathway in Parkinson's disease. Nature 395 (1998) 451-452
205. Langston J.W., and Ballard P.A. Parkinsonism induced by 1-methyl-4-phenyl 1,2,3,6 tetrahydropyridine: implications for treatment and the pathophysiology of Parkinson's disease. Can J Neurol Sci 11 (1984) 160-165
206. +, a metabolic of MPTP, by brain synaptosomes. Biochem Biophys Res Commun 128 (1985) 1229-1232
207. Javitch J.A., and Snyder S.H. Uptake of MPTP (+) by dopamine neurons explains selectivity of parkinsonism-inducing neurotoxin, MPTP. Eur J Pharmacol 104 (1984) 455-456
208. +. Biochem Biophys Res Commun 134 (1986) 743-748
209. +, a metabolite of the neurotoxin MPTP. Life Sci 36 (1985) 2503-2508
210. Rossetti Z.L., Sotgiu A., Sharp D.E., et al. 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) and free radicals in vitro. Biochem Pharmacol 37 (1988) 4573-4574
211. Przedborski S., Kostic V., Jackson-Lewis V., et al. Transgenic mice with increased Cu/Zn-superoxide dismutase activity are resistant to N-methyl-4-phenyl 1,2,3,6 tetrahydropyridine-induced neurotoxicity. J Neurosci 12 (1992) 1658-1667
212. Schulz J.B., Matthews R.T., Mugit M.M.K., et al. Inhibition of neuronal nitric oxide synthase by 7-nitroindazole protects against MPTP-induced neurotoxicity in mice. J Neurochem 64 (1995) 936-939
213. Hantraye P., Brouillet E., Ferrante R., et al. Inhibition of neuronal nitric oxide synthase prevents MPTP-induced parkinsonism in baboons. Nat Med 2 (1996) 1017-1021
214. Przedborski S., Donaldson D., Murphy P.L., et al. Role of neuronal nitric oxide in 1-methyl-4-phenyl 1,2,3,6 tetrahydropyridine (MPTP)-induced dopaminergic neurotoxicity. Proc Natl Acad Sci U S A 93 (1996) 4565-4571
215. Betarbet R., Sherer T.B., MacKenzie G., et al. Chronic systemic pesticide exposure reproduces features of Parkinson's disease. Nat Neurosci 3 (2000) 1301-1306
216. Dexter D.T., Wells F.R., Lees A.J., et al. Increased nigral iron content and alterations in other metal ions occurring in brain in Parkinson's disease. J Neurochem 52 (1989) 1830-1836
217. Hirsch E.C., Brandel J.-P., Galle P., et al. Iron and aluminium increase in the substantia nigra of patients with Parkinson's disease: an x-ray microanalysis. J Neurochem 56 (1991) 446-451
218. Ben-Shachar D., and Youdim M.B.H. Intranigral iron injection induces behavioural and biochemical parkinsonism in rats. J Neurochem 57 (1991) 2133-2135
219. Sengstock G.J., Olanow C.W., Menzies R.A., et al. Infusion of iron into the rat substantia nigra: nigral pathology and dose-dependent loss of striatal dopaminergic markers. J Neurosci Res 35 (1993) 67-82
220. Sjöquist B., Eriksson A., and Winblad B. Salsolinol and catecholamines in human brain and their relation to alcoholism. Prog Clin Biol Res 90 (1982) 57-67
221. Niwa T., Takeda N., Yoshizumi H., et al. Presence of 2-methyl-6,7-dihydroxy 1,2,3,4 tetrahydroisoquinoline and 1,2-methyl-6,7-dihydroxy 1,2,3,4 tetrahydroisoquinoline, novel endogenous amines, in parkinsonian and normal human brains. Biochem Biophys Res Commun 177 (1991) 603-609
222. Naoi M., Maruyama W., Dostert P., et al. Dopamine-derived endogenous 1(R), 2(N)-dimethyl-6,7-dihydroxy-1,2,3,4-tetrahydroisoquinoline, N-methyl-(R)salsolinol, induced parkinsonism in rat: biochemical, pathological and behavioural studies. Brain Res 709 (1996) 285-295
223. Naoi M., Maruyama W., Dostert P., and Hashizume Y. N-methyl-(R)-salsolinol as a dopaminergic neurotoxin: from an animal model to an early marker of Parkinson's disease. J Neurol Transm 50 (1997) 89-105
224. Kotake Y., Tasaki Y., Makino Y., et al. 1-benzyl-1,2,3,4-tetrahydroisoquinoline as a parkinsonism-inducing agent-a novel endogenous amine in mouse brain and parkinsonian CSF. J Neurochem 65 (1995) 2633-2638
225. Yoshida M., Niwa T., and Nagatsu T. Parkinsonism in monkeys produced by chronic administration of an endogenous substance of the brain, tetrahydroisoquinoline-the behavioural and biochemical changes. Neurosci Lett 119 (1990) 109-113
226. Liptrot J., Holdup D., and Phillipson D. 1,2,3,4-tetrahydro-2-methyl-4,6,7-isoquinolinetriol depletes catecholamines in rat brain. J Neurochem 61 (1993) 2199-2206
227. McNaught K.S., Thull U., Carrupt P.A., et al. Inhibition of complex I by isoquinoline derivatives structurally related to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). Biochem Pharmacol 50 (1995) 1903-1911
228. McNaught K.S., Altomare C., Cellamare S., et al. Inhibition of α-ketoglutarate dehydrogenase by isoquinoline derivatives structurally related to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). Neuroreport 6 (1995) 1105-1108
229. McNaught K.S., Thull U., Carrupt P.A., et al. Toxicity to PC12 cells of isoquinoline derivatives structurally related to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine. Neurosci Letts 20 (1996) 37-40
230. Jenner P., and Olanow C.W. Understanding cell death in Parkinson's disease. Ann Neurol 44 (1998) S72-S84
231. Dexter D.T., Holley A.E., Flitter W.D., et al. Increased levels of lipid hydroperoxides in the Parkinsonian substantia nigra: an HPLC and ESR study. Mov Disord 9 (1994) 92-97
232. Alam Z.I., Jenner A., Daniel S.E., et al. Oxidative DNA damage in the parkinsonian brain: an apparent selective increase in 8-hydroxyguanine levels in substantia nigra. J Neurochem 69 (1997) 1196-1203
233. Alam Z.I., Daniel S.E., Lees A.J., et al. A generalised increase in protein carbonyls in the brain in Parkinson's but not incidental Lewy body disease. J Neurochem 69 (1997) 1326-1329
234. Olanow C.W. A radical hypothesis for neurodegeneration. Trends Neurosci 16 (1993) 439-444
235. Chance B., Sies H., and Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol Rev 59 (1979) 527-605
236. Sian J., Dexter D.T., Lees A.J., et al. Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia. Ann Neurol 36 (1994) 348-355
237. Sofic E., Lange K.W., Jellinger K., and Riederer P. Reduced and oxidised glutathione in the substantia nigra of patients with Parkinson's disease. Neurosci Lett 42 (1992) 128-130
238. Giasson B.I., Duda J.E., Murray I., et al. Oxidative damage linked to neurodegeneration by selective α-synuclein nitration in synucleinopathy lesions. Science 290 (2000) 985-989
239. Schapira A., Cooper J.M., Dexter D., et al. Mitochondrial complex I deficiency in Parkinson's disease. Lancet 1 (1989) 1269
240. Schapira A., Cooper J.M., Dexter D., et al. Mitochondrial complex I deficiency in Parkinson's disease. J Neurochem 54 (1990) 823-827
241. 1 reductase (complex I) deficiency in Parkinson's disease. J Neurochem 55 (1990) 2142-2145
242. Hattori N., Tanaka M., Ozawa T., and Mizuno Y. Immunohistochemical studies on complexes I, II, III and IV of mitochondria in Parkinson's disease. Ann Neurol 30 (1991) 563-571
243. Gu M., Gash M.T., Cooper J.M., et al. Mitochondrial respiratory chain function in multiple system atrophy. Mov Disord 12 (1997) 418-422
244. Schapira A. Mitochondrial Dysfunction in Neurodegenerative Disorders and Ageing. In: Schapira A., and DiMauro S. (Eds). Mitochondrial Disorders in Neurology. (1994), Butterworth-Heinemann, Oxford UK 227-244
245. Gu M., Cooper J.M., Taanman J.W., and Schapira A. Mitochondrial DNA transmission of the mitochondrial defect in Parkinson's disease. Ann Neurol 44 (1998) 177-186
246. Swerdlow R.H., Parks J.K., Miller S.W., et al. Origin and functional consequences of the complex I defect in Parkinson's disease. Ann Neurol 40 (1996) 663-671
247. Prezant T.R., Agapian J.V., Bohlman C., et al. Mitochondrial ribosomal RNA mutation associated with both antibiotic-induced and non-syndrome deafness. Nat Genet 4 (1993) 289-294
248. Schapira A. The 'new' mitochondrial disorders. J Neurol Neurosurg Psychiatry (2001) (in press)