DAMAGE AND REPAIR OF NERVE CELL DNA IN TOXIC STRESS*

REFERENCES

• Garruto R. M., Yase Y. Neurodegenerative disorders of the western Pacific: The search for mechanisms of pathogenesis. Trends Neurosci. 1986; 9: 368–375
   Web of Science ®Google Scholar
• Hirano A., Malamud N., Kurland L. T. Parkinsonism–dementia complex, an endemic disease on the island of Guam. II. Pathological features. Brain 1958; 84: 622–679
   Google Scholar
• Kurland L. T., Molgaard C. A. Guamanian ALS: Hereditary or acquired?. Human Motor Neuron Diseases, L. P. Rowland. Raven Press, New York 1982
   Google Scholar
• Stone R. Guam: Deadly disease dying out. Science 1994; 261: 424–426
   Web of Science ®Google Scholar
• Garruto R. M., Yanagihara R. Disappearance of high-incidence amyotrophic lateral sclerosis and parkinsonism-dementia on Guam. Neurology 1985; 35: 193–198
   PubMed Web of Science ®Google Scholar
• Garruto R. M., Yanagihara R., Gadjusek D. C., Arion D. M. Concentrations of heavy metals and essential minerals in garden soil and drinking water in the Western Pacific. Amyotrophic Lateral Sclerosis in Asia and Oceana, I. Chen, Y. Yase. National University, Taiwan 1984
   Google Scholar
• Spencer P. S., Ohta M., Palmer V. Cycad use and motor neuron disease in Kii peninsula of Japan. Lancet 1987; 2: 1462–1463
   PubMed Web of Science ®Google Scholar
• Spencer P. S., Palmer V., Herman A., Asmedi A. Cycad use and motor neuron disease in Irian Jaya. Lancet 1987; 2: 1273–1274
   PubMed Web of Science ®Google Scholar
• Figlewicz D. A., Garruto R. M., Krizus A., Yanagihara R., Rouleau G. A. The Cu/Zn superoxide dismutase gene in ALS and Parkinsonism–dementia of Guam. NeuroReport 1994; 5: 557–560
   PubMed Web of Science ®Google Scholar
• Gadjusek D. C., Salazar A. M. Amyotrophic lateral sclerosis and parkinsonian syndromes in high incidence among the Auyu and Jakai people of West New Guinea. Neurology 1982; 32: 107–126
   PubMed Web of Science ®Google Scholar
• Gibbs C. J., Gadjusek D. C. An update on long-term in vivo and in vitro studies designed to identify a virus as the cause of amyotrophic lateral sclerosis, parkinsonism–dementia, and Parkinson’s disease. Human Motor Neuron Diseases, L. P. Rowland. Raven Press, New York 1982
   Google Scholar
• Chen K. M., Yase Y. Parkinsonism–dementia, neurofibrillary tangles, and trace elements in the western Pacific. Senile Dementia of the Alzheimer Type, J. T. Hutlon, A. D. Kenny. Alan R. Liss Inc., New York 1985
   Google Scholar
• Ahlskog J. E., Waring S. C., Kurland L. T., Petersen R. C., Moyer T. P., Maraganore W. S., O’Brien P. C., Esteban-Santillan C., Bush V. Guamanian neurodegenerative disease: Investigation of the calcium metabolism/heavy metal hypothesis. Neurology 1995; 45: 1340–1344
   PubMed Web of Science ®Google Scholar
• Perl D., Gadjusek D. C., Garruto R. M. Intraneuronal aluminum accumulation in amyotrophic lateral sclerosis and Parkinsonism-dementia on Guam. Science 1982; 217: 1053–1055
   PubMed Web of Science ®Google Scholar
• Spencer P. S., Ross S. M., Kisby G., Roy D. N. Western Pacific amyotrophic lateral sclerosis: Putative role of cycad toxins. Amyotrophic Lateral Sclerosis: Concepts in Pathogenesis and Etiology, A. J. Hudson. University of Toronto Press, Toronto 1990
   Google Scholar
• Spencer P. S., Allen C. A., Kisby G. E., Ludolph A. C. On the etiology and pathogenesis of chemically induced neurodegenerative disorders. Neurobiol. Aging 1994; 15: 265–267
   PubMed Web of Science ®Google Scholar
• Reed D., Labarthe D., Chen K. M., Stallones R. A cohort study of amyotrophic lateral sclerosis and Parkinsonism–dementia on Guam and Rota. Am. J. Epidemiol. 1987; 125: 92–100
   PubMed Web of Science ®Google Scholar
• Duncan M. W., Steele J. C., Kopin I. J., Markey S. P. 2-Amino-3-(methylamino)-propanoic acid (BMAA) in cycad flour: An unlikely cause of amyotrophic lateral sclerosis and parkinsonism–dementia of Guam. Neurology 1990; 40: 767–772
   PubMed Web of Science ®Google Scholar
• Kisby G. E., Ellison M., Spencer P. S. Content of the neurotoxins cycasin (methylazoxymethanol β-D-glucoside) and BMAA (β-N-methylamino-L-alanine) in cycad flour prepared by Guam Chamorros. Neurology 1992; 42: 1336–1340
   PubMed Web of Science ®Google Scholar
• Kobayashi A. Cycasin in cycad materials used in Japan. Fed. Proc. 1972; 31: 1476–1477
   PubMedGoogle Scholar
• Zhang Z. X., Anderson D. W., Mantel N., Román G. C. Motor neuron disease on Guam: Geographic and familial occurrence, 1956–85. Acta Neurol. Scand. 1996; 94: 51–59
   PubMed Web of Science ®Google Scholar
• Hornabrook R. W. Essays on Kuru. Classey, Farindgon. Berkshire, Classey, U.K. 1976
   Google Scholar
• Anderson F. H., Richardson E. P., Okazaki H., Brody J. A. Neurofibrillary degeneration on Guam: Frequency in Chamorros and non Chamorros with no known neurological disease. Brain 1975; 102: 65–77
   Google Scholar
• Garruto R. M., Gadjusek D. C., Chen K.-M. Amyotrophic lateral sclerosis among Chamorro migrants from Guam. Ann. Neurol. 1980; 8: 612–619
   PubMed Web of Science ®Google Scholar
• Yase Y. The pathogenesis of amyotrophic lateral sclerosis. Lancet 1972; 2: 292–296
   PubMed Web of Science ®Google Scholar
• Shiraki H., Yase Y. Amyotrophic lateral sclerosis in Japan. Handbook of Clinical Neurology. Vol. 22. System Disorders and Atrophy, Part 2, P. J. Vinken, G. W. Bruyn. American Elsevier, New York 1975
   Google Scholar
• Jones M. M., Yang M., Mickelsen O. Effects of methylazoxymethanol glucoside and methylazoxymethanol acetate on the cerebellum of the postnatal Swiss albino mouse. Fed. Proc. 1972; 31: 1508–1511
   PubMedGoogle Scholar
• Spencer P. S., Kisby G. E. Slow toxins and western Pacific amyo-trophic lateral sclerosis. Handbook of Amyotrophic Lateral Sclerosis, R. A. Smith. Marcel Dekker, Inc., New York 1992
   Google Scholar
• Spencer P. S., Kisby G. E., Ludolph A. C. Slow toxins, biologic markers, and long-latency neurodegenerative disease in the western Pacific region. Neurology 1991; 41: 62–66
   PubMed Web of Science ®Google Scholar
• Kisby G. E., Ross S. M., Spencer P. S., Gold B. G., Nunn P. B., Roy D. N. Cycasin and BMAA: Candidate neurotoxins for western Pacific amyotrophic lateral sclerosis/Parkinsonism–dementia complex. Neurodegeneration 1992; 1: 73–82
   Google Scholar
• Spencer P. S., Nunn P. B., Hugon J., Ludolph A. C., Ross S. M., Roy D. N., Robertson R. C. Guam amyotrophic lateral sclerosis–parkinsonism–dementia linked to a plant excitant neurotoxin. Science 1987; 237: 517–522
   PubMed Web of Science ®Google Scholar
• Ross S. M., Spencer P. S. Specific antagonism of behavioral action of “uncommon” amino acids linked to motor-system diseases. Synapse 1987; 1: 248–253
   PubMed Web of Science ®Google Scholar
• Weiss J. H., Choi D. W. β-N-Methylamino-L-alanine neurotoxicity: Requirement for bicarbonate as a cofactor. Science 1988; 241: 973–975
   PubMed Web of Science ®Google Scholar
• Weiss J. H., Koh J. Y., Choi D. W. Neurotoxicity of β-N-methyl-amino-L-alanine (BMAA) and β-N-oxalylamino-L-alanine (BOAA) on cultured cortical neurons. Brain Res. 1989; 497: 64–71
   PubMed Web of Science ®Google Scholar
• Albin R. L., Greenamyre T. Alternative excitotoxic hypotheses. J. Am. Acad. Neurol. 1992; 42: 733–738
   PubMed Web of Science ®Google Scholar
• Allen C. N., Ross S. M., Spencer P. S. Properties of neurotoxic non- protein amino acids, β-N-methylamino-L-alanine (BMAA) and β-N-oxalyl-amino-L-alanine (BOAA). ALS, New Advances in Toxicology and Epidemiology, F. C. Rose, F. H. Norris. Smith Gordon, London 1990
   Google Scholar
• Copani A., Canonico P. L., Nicoletti F. β-N-Methylamino-L-alanine (L-BMAA) is a potent agonist of “metabolotropic” glutamate receptors. Eur. J. Pharmacol. 1990; 181: 327–328
   PubMed Web of Science ®Google Scholar
• Kisby G. E., Nottingham V., Kayton R., Roy D. N., Spencer P. S. Brain metabolism of β-N-methylamino-L-alanine (BMAA) and protection of excitotoxicity by GABA-uptake inhibitors. Soc. Neurosci. Abstr. 1992; 18: 82
   Google Scholar
• Seawright A. A., Brown A. W., Nolan C. C., Cavanagh J. B. Selective degeneration of cerebellar cortical neurons caused by cycad neurotoxin, L-β-methylaminoalanine (L-BMAA), in rats. Neuropathol. Appl. Neurobiol. 1990; 16: 153–169
   PubMed Web of Science ®Google Scholar
• Perry T. L., Bergeron C., Biro A. J., Hansen S. β-N-Methylamino-L-alanine. Chronic oral administration is not neurotoxic to mice. J. Neurol. Sci. 1989; 94: 173–180
   PubMed Web of Science ®Google Scholar
• Duncan M. W., Villacreses W. E., Pearson P. G., Wyatt L., Rapoport S. I., Kopin I., Markey S. P., Smith Q. R. 2-Amino-3-(methylamino)-propanoic acid (BMAA) pharmacokinetics and blood-barrier permeability in the rat. J. Pharmacol. Exp. Ther. 1991; 258: 27–35
   PubMed Web of Science ®Google Scholar
• Smith Q. R., Nagura H., Takada Y., Duncan M. W. Facilitated transport of the neurotoxin, β-N-methylamino-L-alanine, across the blood-brain barrier. J. Neurochem. 1992; 58: 1330–1337
   PubMed Web of Science ®Google Scholar
• Kabel J. F., Kisby G. E., Mako S. C., Glew R. H., Spencer P. S. Rodent brain metabolism of cycasin and DNA alkylation by methylazoxymethanol (MAM). Soc. Neurosci. Abstr. 1992; 18: 1249
   Google Scholar
• Matsuoka T., Nishizaki T., Kisby G. E. Na+-dependent and phlorizin-inhibitable transport of glucose and cycasin in brain endothelial cells. J. Neurochem. 1998; 70: 772–777
   PubMed Web of Science ®Google Scholar
• Nishizaki T., Kammesheidt A., Sumikawa K., Asada T., Okada Y. A sodium- and energy-dependent glucose transporter with similarities to SGLT1-2 is expressed in bovine cortical vessels. Neurosci. Res. 1995; 22: 13–22
   PubMed Web of Science ®Google Scholar
• Hirayama B., Hazama A., Loo D. F., Wright E. M., Kisby G. E. Transport of cycasin by the intestinal Na+/glucose cotransporter. Biochim. Biophys. Acta 1994; 1193: 151–154
   PubMed Web of Science ®Google Scholar
• Matsumoto H. Cycasin. CRC Handbook of Naturally Occurring Food Toxicants, M. J. Rechcigl. CRC Press, Boca RatonFL 1985
   Google Scholar
• Laqueur G. L., Matsumoto H. Neoplasms in female Fischer rats following intraperitoneal injection of methylazoxymethanol. J. Natl. Cancer Inst. 1967; 124: 691–697
   Google Scholar
• Laqueur G. L., Mickelson O., Shitney M. G., Kurland L. T. Carcinogenic properties of nuts from Cycas circinalis L. indigenous to Guam. J. Natl. Cancer Inst. 1963; 31: 919–959
   PubMed Web of Science ®Google Scholar
• Sieber S. M., Correa P., Dalgard D. W., McIntire K. R., Adamson R. H. Carcinogenicity and hepatotoxicity of cycasin and its aglycone methylazoxymethanol acetate in nonhuman primates. J. Natl. Cancer Inst. 1980; 65: 177–189
   PubMed Web of Science ®Google Scholar
• Yang M. G., Mickelsen O., Campbell M. E. Cycad flour used by Guamanians: Effects produced in rats by long-term feeding. J. Nutr. 1966; 90: 153–156
   PubMed Web of Science ®Google Scholar
• Shimiuz T., Yasuda N., Kono I., Yagi F., Tadera K., Kobayashi A. , Hepatic and spinal lesions in goats chronically intoxicated with cycasin. Jpn. J. Vet. Sci. 1986; 8: 1291–1295
   Google Scholar
• Dastur D. K. Cycad toxicity in monkeys: Clinical, pathological and biochemical aspects. Fed. Proc. 1964; 23: 1368–1369
   PubMedGoogle Scholar
• Dastur D. K., Palekar R. S. The experimental pathology of cycad toxicity with special reference to oncogenic effects. Indian J. Cancer 1974; 2: 33–49
   Google Scholar
• Whiting M. G. Toxicity of cycads. Econ. Bot. 1963; 17: 271–302
   Google Scholar
• Mason M. M., Fredrickson T. N. Derriengue investigations. The Fourth Conference on the Toxicity of Cycads. Toxicity of Cycads: Implications for Neurodegenerative Disease and Cancer. Transcripts of Four Cycad Conferences, M. G. Whiting. Medical Research Foundation, New York 1988
   Google Scholar
• Hooper P. T. Cycad poisoning. Handbook of Natural Toxins: Plant and Fungal Toxins, R. F. Keeler, A. T. Tu. Marcel Dekker, Inc., New York 1983
   Google Scholar
• Dastur D. K., Palekar R. S., Manghani D. K. Toxicity of various forms of Cycas circinalis in rhesus monkeys—pathology of brain, spinal cord and liver. ALS. New Advances in Toxicology and Epidemiology, F. C. Rose, F. H. Norris. Smith Gordon, London 1990
   Google Scholar
• Garcia-Ladona F. J., de Barry J., Girard C., Gombos G. Ectopic granule cell layer in mouse cerebellum after methylazoxymethanol (MAM) treatment. Exp. Brain Res. 1991; 86: 90–96
   PubMed Web of Science ®Google Scholar
• Lee M. H., Rabe A. Premature decline in Morris water maze performance of aging microencephalic rats. Neurotoxicol. Teratol. 1992; 14: 383–392
   PubMed Web of Science ®Google Scholar
• Ramakers G. M., Urban I. J.A., De Graan P. N.E., Di Luca M., Cattabeni F., Gispen W. H. The impaired long-term potentiation in the CA1 field of the hippocampus of cognitive deficient microencephalic rats is restored by D-serine. Neuroscience 1993; 54: 49–60
   PubMed Web of Science ®Google Scholar
• Kisby G. E., Sweatt C., McEvoy S., Spencer P. S. Potentiation of cycad toxin-induced DNA damage in brain tissue by DNA-repair inhibitors. Soc. Neurosci. Abstr. 1994; 20: 1649
   Google Scholar
• Williams G. M., Weisburger J. H. Chemical carcinogenesis. Toxicology, The Basic Science of Poisons, C. T. Klassen, M. O. Amdur, J. Doull. MacMillian, New York 1986
   Google Scholar
• Cimino M., Cattabeni F., Di Luca M., Peruzzi G., Andena M., Tirassa P., Angelucci F., Cozzari C., Aloe L. Levels of NGF, p75NGFR and ChAT immunoreactivity in brain of adult and aged microencephalic rats. Neurobiol. Aging 1996; 17: 137–142
   PubMed Web of Science ®Google Scholar
• Greiner P. O., Bonnet C. M., Angignard D., Dupont J. M., Herold M., Borzeix M. G. Neuropharmacological study of aged MAM-treated rats. Neurobiol. Aging 1992; 13: 527–529
   PubMed Web of Science ®Google Scholar
• Fischer M. H., Herm J. W., Waisman H. A. A preliminary biochemical examination of microencephalic rat brains. Biochem. Pharmacol. 1973; 22: 267–271
   PubMed Web of Science ®Google Scholar
• Fischer M. H., Welker C., Waisman H. A. Generalized growth retardation in rats induced by prenatal exposure to methylazoxymethyl acetate. Teratology 1972; 5: 223–232
   PubMedGoogle Scholar
• Balduini W., et al. Microencephalic rats as a model for cognitive disorders. Clin. Neuropharmacol. 1986; 9: S8–S18
   PubMed Web of Science ®Google Scholar
• Ferguson S. A., Racey F. D., Paule M. G., Holson R. R. Behavioral effects of methylazoxymethanol-induced microencephaly. Behav. Neurosci. 1993; 107: 1–10
   Google Scholar
• Gillies K., Price D. J. The fates of cells in the developing cerebral cortex of normal and methylazoxymethanol acetate-lesioned mice. Eur. J. Neurosci. 1993; 5: 73–84
   PubMed Web of Science ®Google Scholar
• Goldey E. S., O’Callaghan J. P., Stanton M. E., Barone S., Jr., Crofton K. M. Developmental neurotoxicity: Evaluation of testing procedures with methylazoxymethanol and methylmercury. Fundam. Appl. Toxicol. 1994; 23: 447–464
   PubMedGoogle Scholar
• Cattaneo E., Reinach B., Caputi A., Cattabeni F., Di Luca M. Selectivein in vitro blockade of neuroepithelial cell proliferation by methylazoxymethanol, a molecule capable of inducing long lasting functional impairments. J. Neurosci. Res. 1995; 41: 640–647
   PubMed Web of Science ®Google Scholar
• Johnston M. V., Coyle J. T. Histological and neurochemical effects of fetal treatment with methylazoxymethanol on rat neocortex in adulthood. Brain Res. 1979; 170: 135–155
   PubMed Web of Science ®Google Scholar
• Johnston M. V., Coyle J. T. Ontogeny of neurochemical markers for noradrenergic, GABAergic and cholinergic neurons in neocortex lesioned with methylazoxymethanol acetate. J. Neurochem. 1980; 34: 1429–1441
   PubMed Web of Science ®Google Scholar
• Eriksdotter-Nilsson M., Jonsson G., Dahl D., Bjorklund H. Astroglial development in microencephalic rat brain after fetal methylazoxymethanol treatment. J. Dev. Neurosci. 1986; 4: 353–362
   PubMed Web of Science ®Google Scholar
• Hoffman J. R., Boyne L. J., Levitt P., Fischer I. Short exposure of methylazoxymethanol causes a long-term inhibition of axonal outgrowth from cultured embryonic rat hippocampal neurons. J. Neurosci. Res. 1996; 46: 349–359
   PubMed Web of Science ®Google Scholar
• Esclaire F., Kisby G. E., Milne J., Lesort M., Spencer P., Hugon J. The Guam cycad toxin methylazoxymethanol damages neuronal DNA and modulates tau mRNA expression and excitotoxicity. Exp. Neurol. 1999; 155: 11–21
   PubMed Web of Science ®Google Scholar
• Mullaart E., Boerrigter M. E.T.I., Boer G. J., Vijg J. Spontaneous DNA breaks in the rat brain during development and aging. Mutat. Res. 1990; 237: 9–15
   PubMed Web of Science ®Google Scholar
• Mullaart E., Boerrigter M. E.T.I., Brouwer A., Berends F., Vijg J. Age-dependent accumulation of alkali-labile sites in DNA of post-mitotic but not in that of mitotic rat liver cells. Mech. Ageing Dev. 1988; 45: 41–49
   PubMed Web of Science ®Google Scholar
• Bhaskar M. S., Rao K. S. Altered conformation and increased strand breaks in neuronal and astroglial DNA of aging rat brain. Biochem. Mol. Biol. Int. 1994; 33: 377–384
   PubMedGoogle Scholar
• Mandavilli B. S., Rao K. S. Neurons in the cerebral cortex are most susceptible to DNA-damage in aging rat brain. Biochem. Mol. Biol. Int. 1996; 40: 507–514
   PubMedGoogle Scholar
• Mandavilli B. S., Rao K. S. Accumulation of DNA damage in aging neurons occurs through a mechanism other than apoptosis. J. Neurochem. 1996; 67: 1559–1565
   PubMed Web of Science ®Google Scholar
• Mecocci P., MacGarvey U., Kaufman A. E., Koontz D., Shoffner J. M., Wallace D. C., Beal M. F. Oxidative damage to mitochondrial DNA shows marked age-dependent increases in human brain. Ann. Neurol. 1993; 34: 609–616
   PubMed Web of Science ®Google Scholar
• Fitzmaurice P. S., Shaw I. C., Kleiner H. E., Miller R. T., Monks T. J., Lau S. S., Mitchell J. D., Lynch P. G. Evidence for DNA damage in amyotrophic lateral sclerosis. Muscle Nerve 1996; 19: 797–798
   PubMed Web of Science ®Google Scholar
• Ferrante R. J., Browne S. E., Shinobu L. A., Bowling A. C., Baik M. J., MacGarvey U., Kowall N. W., Brown R. H., Jr., Beal M. F. Evidence of increased oxidative damage in both sporadic and familial amyotrophic lateral sclerosis. J. Neurochem. 1997; 69: 2064–2074
   PubMed Web of Science ®Google Scholar
• Sanchez-Ramos J. R., Övervik E., Ames B. N. A marker of oxyradical-mediated DNA damage (8-hydroxy-2′-deoxyguanosine) is increased in nigro-striatum of Parkinson’s disease brain. Neurodegeneration 1994; 3: 197–204
   Google Scholar
• Alam Z. I., Jenner A., Daniel S. E., Lees A. J., Cairns N., Marsden C. D., Jenner P., Halliwell B. Oxidative DNA damage in the Parkinsonian brain: An apparent selective increase in 8-hydroxyguanine levels in substantia nigra. J. Neurochem. 1997; 69: 1196–1203
   PubMed Web of Science ®Google Scholar
• Mecocci P., MacGarvey U., Beal M. F. Oxidative damage to mitochondrial DNA is increased in Alzheimer’s disease. Ann. Neurol. 1994; 36: 747–751
   PubMed Web of Science ®Google Scholar
• Lyras L., Cairns N. J., Jenner A., Jenner P., Halliwell B. An assessment of oxidative damage to proteins, lipids, and DNA in brain from patients with Alzheimer’s disease. J. Neurochem. 1997; 68: 2061–2069
   PubMed Web of Science ®Google Scholar
• Gabbita S. P., Lovell M. A., Markesbery W. R. Increased nuclear DNA oxidation in the brain in Alzheimer’s disease. J. Neurochem. 1998; 71: 2034–2040
   PubMed Web of Science ®Google Scholar
• Aoki K., Nakatsuru Y., Sakurai J., Sato A., Masahito P., Ishikawa T. Age dependence of O6-methylguanine–DNA methyltransferase activity and its depletion after carcinogen treatment in the teleost medaka (Oryzias latopes). Mutat. Res. 1993; 293: 225–231
   PubMed Web of Science ®Google Scholar
• Cavanna M., Parodi S., Taningher M., Bolognesi C., Sciaba L., Brambilla G. DNA fragmentation in some organs of rats and mice treated with cycasin. Br. J. Cancer 1979; 39: 383–389
   PubMed Web of Science ®Google Scholar
• Damjanov I., Cox R., Sarma D. S. R., Farber E. Patterns of damage and repair of liver DNA induced by carcinogenic methylating agentsin in vivo. Cancer Res. 1973; 33: 2122–2128
   PubMed Web of Science ®Google Scholar
• Kidson C., Chen P., Imray F. P., Gipps E. Nervous system disease associated with dominant cellular radiosensitivity. Cellular Responses to DNA Damage, E. C. Friedberg, B. A. Bridges. Alan R. Liss, Inc., New York 1983
   Google Scholar
• Robbins J. H. Hypersensitivity to DNA-damaging agents in primary degenerations of excitable tissue. Cellular Responses to DNA Damage, E. C. Friedberg, B. A. Bridges. Alan R. Liss, Inc., New York 1983
   Google Scholar
• Taylor A. M. R., Harnden D. G., Arlett C. F., Harcourt S. A., Lehmann A. R., Stevens S., Bridges B. A. Ataxia-telangiectasia: A human mutation with abnormal radiation sensitivity. Nature 1975; 258: 427–429
   PubMed Web of Science ®Google Scholar
• Tan B. H., Bencsath A., Gaubatz J. W. Steady-state levels of 7-methylguanine increase in nuclear DNA of postmitotic mouse tissues during aging. Mutat. Res. 1990; 237: 229–238
   PubMed Web of Science ®Google Scholar
• Matsumoto H., Spatz M., Laqueur G. L. Quantitative changes with age in the DNA content of methylazoxymethanol-induced microencephalic rat brain. J. Neurochem. 1972; 19: 297–306
   PubMed Web of Science ®Google Scholar
• Richter C., Park J. W., Ames B. N. Normal oxidative damage to mitochondrial and nuclear DNA is extensive. Proc. Natl. Acad. Sci. USA 1988; 85: 6456–6467
   Google Scholar
• Ferrer I., Pozas E., Marti M., Blanco R., Planas A. M. Methylazoxymethanol acetate-induced apoptosis in the external granule cell layer of the developing cerebellum of the rat is associated with strong c-Jun expression and formation of high molecular weight c-Jun complexes. Neuropathol. Exp. Neurol. 1997; 56: 1–9
   PubMed Web of Science ®Google Scholar
• Ferrer I., Pozas E., Planas A. M. Ubiquitination of apoptotic cells in the developing cerebellum of the rat following ionizing radiation or methylazoxymethanol injection. Acta Neuropathol. 1997; 93: 402–407
   PubMed Web of Science ®Google Scholar
• Lafarga M., Lerga A., Andres M. A., Polanco J. I., Calle E., Berciano M. T. Apoptosis induced by methylazoxymethanol in developing rat cerebellum: Organization of the cell nucleus and its relationship to DNA and rRNA degradation. Cell Tissue Res. 1997; 289: 25–38
   PubMed Web of Science ®Google Scholar
• Wood K. A., Youle R. J. The role of free radicals and p53 in neuron apoptosisin in vivo. J. Neurosci. 1995; 15: 5851–5857
   PubMed Web of Science ®Google Scholar
• Van Den Berg H. W., Ball C. R. The effect of methylazoxymethanol acetate on DNA synthesis and cell proliferation of synchronous HeLa cells. Mutat. Res. 1972; 16: 381–390
   PubMed Web of Science ®Google Scholar
• Bedford A. J., Cooper E. H., Kenny T. E. A kinetic analysis of death and survival in HeLa cells following exposure to methylazoxymethanol acetate. Eur. J. Cancer 1974; 10: 713–720
   PubMed Web of Science ®Google Scholar
• Nagata Y., Matsumoto H. Studies on methylazoxymethanol: methylation of nucleic acids in the fetal rat brain. Proc. Soc. Exp. Biol. Med. 1969; 132: 383–385
   PubMed Web of Science ®Google Scholar
• Matsumoto H., Higa H. H. Studies on methylazoxymethanol, the aglycone of cycasin: Methylation of nucleic acidsin in vitro. Biochem. J. 1966; 98: 20C–22C
   PubMed Web of Science ®Google Scholar
• Nagasawa H. T., Shirota F. N., Matsumoto H. Decomposition of methylazoxymethanol, the aglycone of cycasin, in D2O. Nature 1972; 236: 234–235
   PubMed Web of Science ®Google Scholar
• Kisby G. E., Gold B. G., Austin D. R., Lystrup B., Spencer P. S. DNA damage in rodent brain tissue induced by cycad toxins. Soc. Neurosci. Abstr. 1993; 19: 196
   Google Scholar
• Kisby G. E., Eizirik D., Sweatt C., Spencer P. S. Reactive oxygen species produced by the cycad toxin methylazoxymethanol, a candidate etiological factor for western Pacific ALS/P-D. J. Cell Biochem. 1995; 21B: 99
   Google Scholar
• Augusto O., Netto L. E. S., Gomes L. F. DNA alkylation by carbon-centered radicals. Braz. J. Med. Biol. Res. 1992; 25: 1171–1183
   PubMed Web of Science ®Google Scholar
• Seeberg E., Eide L., Bjoras M. The base excision repair pathway. Trends Biochem. Sci. 1995; 20: 391–397
   PubMedGoogle Scholar
• Pegg A. E., Dolan M. E., Moschel R. C. Structure, function, and inhibition of O6-alkylguanine–DNA alkyltransferase. Prog. Nucleic Acid Res. Mol. Biol. 1995; 51: 167–223
   PubMed Web of Science ®Google Scholar
• Woodhead A. D., Merry B. J., Cao E.-H., Holehan A. M., Grist E., Carlson C. Levels of O6-methylguanine acceptor protein in tissues of rats and their relationship to carcinogenicity and aging. J. Natl. Cancer Inst. 1985; 75: 1141–1145
   PubMed Web of Science ®Google Scholar
• Wiestler O., Kleihues P., Pegg A. E. O6-alkylguanine–DNA alkyltransferase activity in human brain and brain tumors. Carcinogenesis 1984; 5: 121–124
   PubMed Web of Science ®Google Scholar
• Wilson T. M., Rivkees S. A., Deutsch W. A., Kelley M. R. Differential expression of the apurinic/apyrimidinic endonuclease (APE/ref-1) multifunctional DNA base excision repair gene during fetal development and in adult rat brain and testis. Mutat. Res. 1996; 362: 237–248
   PubMed Web of Science ®Google Scholar
• Duguid J. R., Eble J. N., Wilson T. M., Kelley M. R. Differential cellular and subcellular expression of the human multifunctional apurinic/apyrimidinic endonuclease (APE/ref-1) DNA repair enzyme. Cancer Res. 1995; 55: 6097–6102
   PubMed Web of Science ®Google Scholar
• Silber J. R., Blank A., Bobola M. S., Mueller B. A., Kostoe D. D., Ojemann G. A., Berger M. S. Lack of the DNA repair protein O6-methylguanine–DNA methyltransferase in histologically normal brain adjacent to primary human brain tumors. Proc. Natl. Acad. Sci. USA 1996; 93: 6941–6946
   PubMed Web of Science ®Google Scholar
• Silber J. R., Mueller B. A., Ewers T. G., Berger M. S. Comparison of O6-methylguanine–DNA methyltransferase activity in brain tumors and adjacent normal brain. Cancer Res. 1993; 53: 3416–3420
   PubMed Web of Science ®Google Scholar
• Ono Y., Watanabe M., Inoue Y., Ohmoto T., Akiyama K., Tsutsui K., Seki S. Developmental expression of APEX nuclease, a multifunctional DNA repair enzyme, in mouse brains. Dev. Brain Res. 1995; 86: 1–6
   PubMedGoogle Scholar
• Edwards M., Rassin D. K., Izumi T., Mitra S., Perez-Polo J. R. APE/Ref-1 responses to oxidative stress in aged rats. J. Neurosci. Res. 1998; 54: 635–638
   PubMed Web of Science ®Google Scholar
• Ambrosio S. M.D., Samuel M. J., Dutta-Choudury T. A., Wani A. A. O6-methylguanine–DNA methyltransferase in human fetal tissues: Fetal and maternal factors. Cancer Res. 1987; 47: 51–55
   PubMed Web of Science ®Google Scholar
• Grombacher T., Mitra S., Kaina B. Induction of the alkyltransferase (MGMT) gene by DNA damaging agents and the glucocorticoid dexamethasone and comparison with the response of base excision repair genes. Carcinogenesis 1996; 17: 2329–2336
   PubMed Web of Science ®Google Scholar
• Walton M., Lawlor P., Sirimanne E., Williams C., Gluckman P., Dragunow M. Loss of Ref-1 protein expression precedes DNA fragmentation in apoptotic neurons. Mol. Brain Res. 1997; 44: 167–170
   PubMedGoogle Scholar
• Fung H., Kow Y. W., Van Houten B., Taatjes D. J., Hatahet Z., Janssen Y. M.W., Vacek P., Faux S. P., Mossman B. T. Asbestos increases mammalian AP-endonuclease gene expression, protein levels, and enzyme activity in mesothelial cells. Cancer Res. 1998; 58: 189–194
   PubMed Web of Science ®Google Scholar
• Ramana C. V., Boldogh I., Izumi T., Mitra S. Activation of apurinic/apyrimidinic endonuclease in human cells by reactive oxygen species and its correlation with their adaptive response to genotoxicity of free radicals. Proc. Natl. Acad. Sci. USA 1998; 95: 5061–5066
   PubMed Web of Science ®Google Scholar
• Korr H., Schultz B. Unscheduled DNA synthesis in various types of cells of the mouse brain in vivo. Exp. Brain Res. 1989; 74: 573–578
   PubMed Web of Science ®Google Scholar
• LeDoux S. P., Williams B. A., Hollensworth B. S., Shen C., Thomale J., Rajewsky M. F., Brent T. P., Willson G. L. Glial cell-specific differences in repair of O6-methylguanine. Cancer Res. 1996; 56: 5615–5619
   PubMed Web of Science ®Google Scholar
• Kisby G. E., Milne J., Hugon J. G., Lesort M., Esclaire F., Spencer P. S. Methylazoxymethanol (MAM), a candidate etiological factor for Guam ALS, damages rat brain DNA and modulates its repair. Soc. Neurosci. Abstr. 1996; 22: 2141
   Google Scholar
• Kisby G. E., Springer N., Spencer P. S. In vitro neurotoxic and DNA-damage properties of nitrogen mustard (HN2). J. Appl. Toxicol., in press
   PubMedGoogle Scholar
• Eizirik D. L., Kisby G. E. Cycad toxin-induced damage of rodent and human pancreatic β-islet cells. Biochem. Pharmacol. 1995; 50: 355–365
   PubMed Web of Science ®Google Scholar
• Kisby G. E., Springer N., Claus A., Turker M., Spencer P. S. DNA damage, neurodegeneration and motor neuron disease. Soc. Neurosci. Abstr. 1997; 23: 215
   Google Scholar
• Lee V. M.Y., Trojanowski J. Q. Tau proteins and their significance in the pathobiology of Alzheimer’s disease. Pathobiology of Alzheimer’s Disease, A. M. Goate, F. Ashall. Academic Press Ltd, London 1995
   Google Scholar
• Hof P. R., Nimchinsky E. A., Bueé-Scherrer V., Bueé L., Nasrallah J., Hottinger A. F., Purohit D. P., Loerzel A. J., Steele J. C., Delacourte A., Bouras C., Morrison J. H., Perl D. P. Amyotrophic lateral sclerosis/parkinsonism–dementia complex of Guam: Quantitative neuropathology, immunohistochemical analysis of neuronal vulnerability, and comparison with related neurodegenerative disorders. Acta Neuropathol. 1994; 88: 397–404
   PubMed Web of Science ®Google Scholar
• Mawal-Dewan M., Schmidt M. L., Balin B., Perl D. P., Lee V. M.Y., Trojanowski J. Q. Identification of phosphorylation sites in PHF-tau from patients with Guam amyotrophic lateral sclerosis/parkinsonism– dementia complex. J. Neuropathol. Exp. Neurol. 1996; 55: 1051–1059
   PubMed Web of Science ®Google Scholar
• Bueé-Scherrer V., Bueé L., Hof P. R., Leveugle B., Gilles C., Loerzel A. J., Perl D. P., Delacourte A. Neurofibrillary degeneration in amyotrophic lateral sclerosis/parkinsonism–dementia complex of Guam—Immunochemical characterization of tau proteins. Am. J. Pathol. 1995; 146: 924–932
   PubMed Web of Science ®Google Scholar
• Gensler H. L., Bernstein H. DNA damge as the primary cause of aging. Quart. Rev. Biol. 1981; 56: 279–303
   PubMed Web of Science ®Google Scholar
• Hanawalt P. C., Sarasin A. Cancer-prone hereditary diseases with DNA processing abnormalities. Trends Genet. 1986; 2: 124–128
   Web of Science ®Google Scholar
• Rao K. S., Loeb L. A. DNA damage and repair in brain: Relationship to aging. Mutat. Res. 1992; 275: 317–329
   PubMed Web of Science ®Google Scholar
• Olkowski Z. L., Rosenfeld J. Abnormal DNA repair in patients with ALS. Soc. Neurosci. Abstr. 1995; 21: 1005
   Google Scholar
• Olkowski Z. L. Mutant AP endonuclease in patients with amyotrophic lateral sclerosis. NeuroReport 1998; 9: 239–242
   PubMed Web of Science ®Google Scholar
• Kisby G. E., Milne J., Sweatt C. Evidence of reduced DNA repair in amyotrophic lateral sclerosis brain tissue. NeuroReport 1997; 8: 1337–1340
   PubMed Web of Science ®Google Scholar
• Tan Z., Sun N., Schreiber S. S. Immunohistochemical localization of redox factor-1 (Ref-1) in Alzheimer’s hippocampus. NeuroReport 1998; 9: 2749–2752
   PubMed Web of Science ®Google Scholar
• Kisby G. E., Sweatt C., Spencer P. S. Evidence of reduced brain tissue DNA repair in neurodegenerative disease. Soc. Neurosci. Abstr. 1995; 21: 484
   Google Scholar
• Raji N. S., Rao K. S. Trisomy 21 and accelerated aging: DNA-repair parameters in peripheral lymphocytes of Down’s syndrome patients. Mech. Ageing Dev. 1998; 100: 85–101
   PubMed Web of Science ®Google Scholar
• Druzhyna N., Nair R. G., LeDoux S. P., Wilson G. L. Defective repair of oxidative damage in mitochondrial DNA in Down’s syndrome. Mutat. Res. 1998; 409: 81–89
   PubMed Web of Science ®Google Scholar
• Kisby G. E., Sweatt C., Spencer P. S. Role of DNA repair in protecting mature nervous tissue from DNA damage. J. Cell Biochem. 1995; 21A: 348
   Google Scholar
• Demple B., Harrison L. Repair of oxidative damage to DNA: Enzymology and biology. Annu. Rev. Biochem. 1994; 63: 915–948
   PubMed Web of Science ®Google Scholar
• Daniels L. B., Glew R. H. β-Glucosidase assays in the diagnosis of Gaucher’s disease. Clin. Chem. 1982; 28: 569–577
   PubMed Web of Science ®Google Scholar