DOPAMINE MERCAPTURATE CAN AUGMENT DOPAMINERGIC NEURODEGENERATION*

REFERENCES

• Lang A. E., Lozano A. M. Parkinson's disease. N. Engl. J. Med. 1998; 339: 1044–1053, 1130–1143
   PubMed Web of Science ®Google Scholar
• Corral-Debrinski M., Horton T., Lott M. T., Shoffner J. M., Beal M. F., Wallace D. C. Mitochondrial DNA deletions in human brain: regional variability and increase with advanced age. Nature Genet. 1992; 2: 324–329
   PubMed Web of Science ®Google Scholar
• Coyle J. T., Puttfarcken P. Oxidative stress, glutamate, and neurodegenerative disorders. Science 1993; 262: 689–695
   PubMed Web of Science ®Google Scholar
• Cohen G., Werner P. Free radicals, oxidative stress, and neurodegeneration. Neurodegenerative Diseases, D. B. Calne. W. B. Saunders, Philadelphia 1994; 139–162
   Google Scholar
• Jenner P. J., Olanow C. W. Understanding cell death in Parkinson's disease. Ann. Neurol. 1998; 44: S72–S84
   PubMed Web of Science ®Google Scholar
• Olanow C. W. Oxidative reactions in Parkinson's disease. Neurology 1990; 40: S32–S37
   Google Scholar
• Calne D. B. Treatment of Parkinson's disease. N. Engl. J. Med. 1993; 329: 1021–1027
   PubMed Web of Science ®Google Scholar
• Koller W. C. Neuroprotection for Parkinson's disease. Ann. Neurol. 1998; 44: S155–S159
   PubMed Web of Science ®Google Scholar
• Graham D. G. Oxidative pathways for catecholamines in the genesis of neuromelanin and cytotoxic quinones. Molec. Pharmacol. 1978; 14: 633–643
   PubMed Web of Science ®Google Scholar
• Graham D. G., Tiffany S. M., Bell W. R., Jr., Gutknecht W. F. Autoxidation versus covalent binding of quinones as the mechanism of toxicity of dopamine, 6-hydroxydopamine, and related compounds toward C1300 neuroblastoma cells in vitro. Molec. Pharmacol. 1978; 14: 644–653
   PubMed Web of Science ®Google Scholar
• Damier P., Hirsch E. C., Zhang P., Agid Y., Javoy-Agid F. Glutathione peroxidase, glial cells and Parkinson's disease. Neuroscience 1993; 52: 1–6
   PubMed Web of Science ®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-hydroxyguanosine levels in the substantia nigra. J. Neurochem. 1997; 69: 1196–1203
   PubMed Web of Science ®Google Scholar
• Dexter D. T., Carter C. J., Wells F. R., Javoy-Agid F., Agid Y., Lees A., Jenner P., Marsden C. D. Basal lipid peroxidation in substantia nigra is increased in Parkinson's disease. J. Neurochem. 1989; 52: 381–389
   PubMed Web of Science ®Google Scholar
• Halliwell B. Reactive oxygen species and the central nervous system. J. Neurochem. 1992; 59: 1609–1623
   PubMed Web of Science ®Google Scholar
• Jenner P., Dexter D. T., Sian J., Schapira A. H., Marsden C. D. Oxidative stress as a cause of nigral cell death in Parkinson's disease and incidental Lewy body disease. The Royal Kings and Queens Parkinson's Disease Research Group. Ann. Neurol. 1992; 32: S82–S87
   PubMed Web of Science ®Google Scholar
• The Parkinson's Disease Study Group, Effect of deprenyl on the progression of disability in early Parkinson's disease. N. Engl. J. Med. 1989; 321: 1364–1371
   PubMed Web of Science ®Google Scholar
• Fahn S. An open trial of high-dose antioxidants in early Parkinson's disease. Am. J. Clin. Nutr. 1991; 53: 380–382
   PubMed Web of Science ®Google Scholar
• Przedborski S., Jackson-Lewis V., Muthane U., Jiang H., Ferreira M., Naini A. B., Fahn S. Chronic levodopa administration alters cerebral mitochondrial respiratory chain activity. Neurology 1993; 34: 715–723
   Web of Science ®Google Scholar
• Mann D. M. A., Yates P. O. Possible role of neuromelanin in the pathogenesis of Parkinson's disease. Mech. Ageing Dev. 1983; 21: 193–203
   PubMed Web of Science ®Google Scholar
• Mann D. M., Yates P. O. Pathogenesis of Parkinson's disease. Arch. Neurol. 1982; 39: 545–549
   PubMedGoogle Scholar
• Hirsch E., Graybiel A. M., Agid Y. A. Melanized dopaminergic neurons are differentially susceptible to degeneration in Parkinson's disease. Nature 1988; 334: 345–348
   PubMed Web of Science ®Google Scholar
• Hirsch E. C. Why are nigral catecholaminergic neurons more vulnerable than other cells in Parkinson's disease?. Ann. Neurol. 1992; 32: S88–S93
   PubMed Web of Science ®Google Scholar
• Hastings T. G., Lewis D. A., Zigmond M. J. Role of oxidation in the neurotoxic effects of intrastriatal dopamine injections. Proc. Natl. Acad. Sci. USA 1996; 93: 1956–1961
   PubMed Web of Science ®Google Scholar
• Montine T. J., Underhill T. M., Linney E., Graham D. G. Fibroblasts that express aromatic amino acid decarboxylase have increased sensitivity to the synergistic cytotoxicity of L-dopa and manganese. Toxicol. Appl. Pharmacol. 1994; 128: 116–122
   PubMed Web of Science ®Google Scholar
• Montine T. J., Farris D. B., Graham D. G. Covalent crosslinking of neurofilament proteins by oxidized catechols as a potential mechanism of Lewy body formation. J. Neuropathol. Exp. Neurol. 1995; 54: 311–319
   PubMed Web of Science ®Google Scholar
• Picklo M. J., Amaranth V., Graham D. G., Montine T. J. Structure–function analysis of oxidative damage by endogenous catechol thioesters. Free Radical Biol. Med. 1999; 27: 271–277
   PubMedGoogle Scholar
• Shen X. M., Xia B., Wrona M. Z., Dryhurst G. Synthesis, redox properties in vivo formation, and neurobehavioral effects of N-acetylcysteinyl conjugates of dopamine: Possible metabolites of relevance to Parkinson's disease. Chem. Res. Toxicol. 1996; 9: 1117–1126
   PubMed Web of Science ®Google Scholar
• Monks T. J, Lau S. S. Toxicology of quinone-thioethers. Crit. Rev. Toxicol. 1992; 22: 243–270
   PubMed Web of Science ®Google Scholar
• Wang W, Ballatori N. Endogenous glutathione conjugates: occurrence and biological functions. Pharmacol. Rev. 1998; 50: 335–355
   PubMed Web of Science ®Google Scholar
• Monks T. J., Hanzlik R. P., Cohen G. M., Ross D. D. G. Graham, Quinone chemistry and toxicology. Toxicol. Appl. Pharmacol. 1992; 112: 2–16
   PubMed Web of Science ®Google Scholar
• Fornstedt B., Rosengren E., Carlsson A. Occurrence and distribution of 5-S-cysteinyl derivatives of dopamine, dopa, and dopac in the brains of eight mammalian species. Neuropharmacology 1986; 25: 451–454
   PubMed Web of Science ®Google Scholar
• Fornstedt B., Rosengren E., Carlsson A. The apparent autoxidation rate of catechols in dopamine-rich regions of human brains increases with degree of depigmentation of substantia nigra. J. Neural Transm. 1989; 1: 279–295
   Web of Science ®Google Scholar
• Fornstedt B., Pileblad E., Carlsson A. In vivo autoxidation of dopamine in guinea pig striatum increases with age. J. Neurochem. 1990; 55: 655–659
   PubMed Web of Science ®Google Scholar
• Spencer J. P. E., Jenner P., Daniel S. E., Lees A. J., Marsden D. C., Halliwell B. Conjugates of catecholamines with cysteine and GSH in Parkinson's disease: Possible mechanisms of formation involving reactive oxygen species. J. Neurochem. 1998; 71: 2112–2122
   PubMed Web of Science ®Google Scholar
• Sian J., Dexter D. T., Lees A. J. Glutathione related enzymes in brain in Parkinson's disease. Ann. Neurol. 1994; 36: 356–361
   PubMed Web of Science ®Google Scholar
• Miller R. T., Lau S. S., Monks T. J. Metabolism of 5-(glutathion-S-yl)-a-methyldopamine following intracerebroventricular administration to male Sprague–Dawley rats. Chem. Res. Toxicol. 1995; 8: 634–641
   PubMed Web of Science ®Google Scholar
• Shen X. M., Dryhurst G. Further insights into the influence of L-cysteine on the oxidation chemistry of dopamine: reaction pathways of potential relevance to Parkinson's disease. Chem. Res. Toxicol. 1996; 9: 751–763
   PubMed Web of Science ®Google Scholar
• Li H., Shen X. M., Dryhurst G. Brain mitochondria catalyze the oxidation of 7-(2-aminoethyl)-3,4-dihydro-5-hydroxy-2H-1,4-benzothiazine-3-carboxylic acid (DHBT-1) to intermediates that irreversibly inhibit complex I and scavenge glutathione: potential relevance to the pathogenesis of Parkinson's disease. J. Neurochem. 1998; 71: 2049–2062
   PubMed Web of Science ®Google Scholar
• Li H., Dryhurst G. Irreversible inhibition of mitochondrial complex I by 7-(2-aminoethyl)-3,4-dihydro-5-hydroxy-2H-1,4-benzothiazine-3-carboxylic acid (DHBT-1): A putative nigral endotoxin of relevance to Parkinson's disease. J. Neurochem. 1997; 69: 1530–1541
   PubMed Web of Science ®Google Scholar
• Montine T. J., Picklo M. J., Amarnath V., Whetsell W. O., Graham D. G. Neurotoxicity of endogenous cysteinylcatechols. Exp. Neurol. 1997; 148: 26–33
   PubMed Web of Science ®Google Scholar
• Le W. D., Colom L. V., Xie W. J., Smith R. G., Alexianu M., Appel S. H. Cell death induced by beta-amyloid 1–40 in MES 23.5 hybrid clone: The role of nitric oxide and NMDA-gated channel activation leading to apoptosis. Brain Res. 1995; 686: 49–60
   PubMed Web of Science ®Google Scholar
• Zhang J., Price J. O., Graham D. G., Montine T. J. Secondary excitotoxicity contributes to dopamine-induced apoptosis of dopaminergic neuronal cultures. Biochem. Biophys. Res. Commun. 1998; 248: 812–816
   PubMed Web of Science ®Google Scholar
• Green D. R., Reed J. C. Mitochondria and apoptosis. Science 1998; 281: 1309–1312
   PubMed Web of Science ®Google Scholar
• Kravtsov V. D., Fabian I. Automated monitoring of apoptosis in suspension cell cultures. Lab. Invest. 1996; 74: 557–570
   PubMed Web of Science ®Google Scholar
• Kravtsov V. D., Greer J. P., Whitlock J. A., Koury M. J. Use of the microculture kinetic assay of apoptosis to determine chemosensitivities to leukemias. Blood 1998; 92: 968–980
   PubMed Web of Science ®Google Scholar
• Aigner A., Jager M., Pasternack R., Weber P., Wienke D., Wolf S. Purification and characterization of cysteine-S-conjugate N-acetyltransferase from pig kidney. Biochem. J. 1996; 317: 213–218
   PubMed Web of Science ®Google Scholar
• Globus M. Y. T., Ginsberg M. D., Harik S. I., Busto R., Dietrich W. D. Role of dopamine in ischemic striatal injury. Neurology 1987; 37: 1712–1719
   PubMed Web of Science ®Google Scholar