Abstract
Dopamine (DA), or 3-hydroxytyramine, is a chemical species that has immense importance for the proper functioning of a number of the body’s organ systems. Perhaps DA exerts its most profound influence in its role as a neurotransmitter. DA is distributed in a rather discrete manner throughout the central nervous system (CNS), with its cell bodies originating in the mesencephalon. Its axonal processes ramify from here to many distant sites where DA participates in the process of neuronal communication. As a neurotransmitter, DA is known to mediate a wide-variety of physiological processes and behaviors including locomotor activity, modulation of the cardiovascular system, food-intake, regulation of body temperature, and neuroendocrine function, to mention but a few. DA also mediates the reinforcing effects of a number of psychostimulant drugs of abuse such as cocaine and the amphetamines. In a broader sense, DA is actually considered the neurotransmitter in the brain’s pleasure center (i.e., the nucleus accumbens) where it decodes the reinforcing effects of diverse stimuli. When the DA neuronal system does not function properly, it is possible that the ensuing disruption in higher-cognitive processes can lead to psychiatric illness. Furthermore, if the nigrostriatal DA system damaged or destroyed, the effects can manifest themselves as a neurological disorder, and Parkinson’s disease (PD) is the best known example of this. Therefore, the DA neuronal system is extremely important to brain function and it maintains a delicate balance between normal function and dysfunction.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Graham, D. G., Tiffany, S. M., Bell, W. R., Jr., and Gutknecht, W. F. (1978) Autoxidation versus covalent binding of quinones as the mechanism of toxicity of dopamine, 6hydroxydopamine, and related compounds toward C1300 neuroblastoma cells in vitro. Mol. Pharmacol. 14, 644–653.
Graham, D. G. (1978) Oxidative pathways for catecholamines in the genesis of neuromelanin and cytotoxic quinones. Mol. Pharmacol. 14, 633–643.
Hastings, T. G., Lewis, D. A., and Zigmond, M. J. (1996) Reactive dopamine metabolites and neurotoxicity: implications for Parkinson’s disease. Adv. Exp. Med. Biol. 387, 97–106.
Hastings, T. G. and Zigmond, M. J. (1994) Identification of catechol-protein conjugates in neostriatal slices incubated with [3H]dopamine: impact of ascorbic acid and glutathione. J. Neurochem. 63, 1126–1132.
Gieseg, S. P., Simpson, J. A., Charlton, T. S., Duncan, M. W., and Dean, R. T. (1993) Protein-bound 3,4-dihydroxyphenylalanine is a major reductant formed during hydroxyl radical damage to proteins. Biochemistry 32, 4780–4786.
Terland, O., Flatmark, T., Tangeras, A., and Gronberg, M. (1997) Dopamine oxidation generates an oxidative stress mediated by dopamine semiquinone and unrelated to reactive oxygen species. J. Mol. Cell. Cardiol. 29, 1731–1738.
Stokes, A. H., Brown, B. G., Lee, C. K., Doolittle, D. J., and Vrana, K. E. (1996) Tyrosinase enhances the covalent modification of DNA by dopamine. Brain Res. Mol. Brain Res. 42, 167–170.
Maker, H. S., Weiss, C., Silides, D. J., and Cohen, G. (1981) Coupling of dopamine oxidation (monoamine oxidase activity) to glutathione oxidation via the generation of hydrogen peroxide in rat brain homogenates. J. Neurochem. 36, 589–593.
Cohen, G., Farooqui, R., and Kesler, N. (1997) Parkinson disease: a new link between monoamine oxidase and mitochondrial electron flow. Proc. Natl. Acad. Sci. USA 94, 4890–4894.
Halliwell, B. (1992) Reactive oxygen species and the central nervous system. J. Neurochem. 59, 1609–1623.
Berman, S. B., Zigmond, M. J., and Hastings, T. G. (1996) Modification of dopamine transporter function: effect of reactive oxygen species and dopamine. J. Neurochem. 67, 593–600.
Berman, S. B. and Hastings, T. G. (1997) Inhibition of glutamate transport in synaptosomes by dopamine oxidation and reactive oxygen species. J. Neurochem. 69, 1185–1195.
Filloux, F. and Townsend, J. J. (1993) Pre-and postsynaptic neurotoxic effects of dopamine demonstrated by intrastriatal injection. Exp. Neurol. 119, 79–88.
Hastings, T. G., Lewis, D. A., and Zigmond, M. J. (1996) Role of oxidation in the neuro-toxic effects of intrastriatal dopamine injections. Proc. Natl. Acad. Sci. USA 93, 1956–1961.
Hoyt, K. R., Reynolds, I. J., and Hastings, T. G. (1997) Mechanisms of dopamine-induced cell death in cultured rat forebrain neurons: interactions with and differences from glutamate-induced cell death. Exp. Neurol. 143, 269–281.
Lai, C. T. and Yu, P. H. (1997) Dopamine-and L-beta-3,4-dihydroxyphenylalanine hydrochloride (L-Dopa)-induced cytotoxicity towards catecholaminergic neuroblastoma SH-SY5Y cells. Effects of oxidative stress and antioxidative factors. Biochem. Pharmacol. 53, 363–372.
Rosenberg, P. A. (1988) Catecholamine toxicity in cerebral cortex in dissociated cell culture. J. Neurosci. 8, 2887–2894.
Cadet, J. L. and Brannock, C. (1998) Free radicals and the pathobiology of brain dopamine systems. Neurochem. Int. 32, 117–131.
McCann, U. D., Wong, D. F., Yokoi, F., Villemagne, V., Dannals, R. F., and Ricaurte, G. A. (1998) Reduced striatal dopamine transporter density in abstinent methamphetamine and methcathinone users: evidence from positron emission tomography studies with [1 I C]WIN-35,428. J. Neurosci. 18, 8417–8422.
McCann, U. D., Szabo, Z., Scheffel, U., Dannals, R. F., and Ricaurte, G. A. (1998) Positron emission tomographic evidence of toxic effect of MDMA (“Ecstasy”) on brain serotonin neurons in human beings [see comments]. Lancet 352, 1433–1437.
Gibb, J. W., Johnson, M., Elayan, I., Lim, H. K., Matsuda, L., and Hanson, G. R. (1997) Neurotoxicity of amphetamines and their metabolites. NIDA Res. Monogr. 173, 128–145.
Schmidt, C. J., Ritter, J. K., Sonsalla, P. K., Hanson, G. R., and Gibb, J. W. (1985) Role of dopamine in the neurotoxic effects of methamphetamine. J. Pharmacol. Exp. Ther. 233, 539–544.
Stone, D. M., Johnson, M., Hanson, G. R., and Gibb, J. W. (1988) Role of endogenous dopamine in the central serotonergic deficits induced by 3,4-methylenedioxymethamphetamine. J. Pharmacol. Exp. Ther. 247, 79–87.
Gibb, J. W., Stone, D. M., Johnson, M., and Hanson, G. R. (1989) Role of dopamine in the neurotoxicity induced by amphetamines and related designer drugs, NIDA Res. Monogr. 94, 161–178.
Schmidt, C. J., Black, C. K., and Taylor, V. L. (1991) L-DOPA potentiation of the serotonergic deficits due to a single administration of 3,4-methylenedioxymethamphetamine, pchloroamphetamine or methamphetamine to rats. Eur. J. Pharmacol. 203, 41–49.
Aguirre, N., Barrionuevo, M., Lasheras, B., and Del Rio, J. (1998) The role of dopaminergic systems in the perinatal sensitivity to 3, 4-methylenedioxymethamphetamine-induced neurotoxicity in rats. J. Pharmacol. Exp. Ther. 286, 1159–1165.
Fumagalli, F., Gainetdinov, R. R., Wang, Y. M., Valenzano, K. J., Miller, G. W., and Caron, M. G. (1999) Increased methamphetamine neurotoxicity in heterozygous vesicular monoamine transporter 2 knock-out mice. J. Neurosci. 19, 2424–2431.
Cohen, G. (1994) Enzymatic/nonenzymatic sources of oxyradicals and regulation of antioxidant defenses. Ann. NY Acad. Sci. 738, 8–14.
Cubells, J. F., Rayport, S., Rajendran, G., and Sulzer, D. (1994) Methamphetamine neuro-toxicity involves vacuolation of endocytic organelles and dopamine-dependent intracellular oxidative stress. J. Neurosci. 14, 2260–2271.
Sulzer, D., Chen, T. K., Lau, Y. Y., Kristensen, H., Rayport, S., and Ewing, A. (1995) Amphetamine redistributes dopamine from synaptic vesicles to the cytosol and promotes reverse transport. J. Neurosci. 15, 4102–4108.
Fon, E. A., Pothos, E. N., Sun, B. C., Killeen, N., Sulzer, D., and Edwards, R. H. (1997) Vesicular transport regulates monoamine storage and release but is not essential for amphetamine action. Neuron 19, 1271–1283.
Rudnick, G. and Wall, S. C. (1992) The molecular mechanism of “ecstasy” [3,4methylenedioxy-methamphetamine (MDMA)]: serotonin transporters are targets for MDMA-induced serotonin release. Proc. Natl. Acad. Sci. USA 89, 1817–1821.
Schuldiner, S., Steiner-Mordoch, S., Yelin, R., Wall, S. C., and Rudnick, G. (1993) Amphetamine derivatives interact with both plasma membrane and secretory vesicle biogenic amine transporters. Mol. Pharmacol. 44, 1227–1231.
Pardo, B., Mena, M. A., Casarejos, M. J., Paino, C. L., and De Yebenes, J. G. (1995) Toxic effects of L-DOPA on mesencephalic cell cultures: protection with antioxidants. Brain Res. 682, 133–143.
Newcomer, T. A., Rosenberg, P. A., and Aizenman, E. (1995) Iron-mediated oxidation of 3,4-dihydroxyphenylalanine to an excitotoxin. J. Neurochem. 64, 1742–1748.
Cheng, N., Maeda, T., Kume, T., Kaneko, S., Kochiyama, H., Akaike, A., Goshima, Y., and Misu, Y. (1996) Differential neurotoxicity induced by L-DOPA and dopamine in cultured striatal neurons. Brain Res. 743, 278–283.
Basma, A. N., Morris, E. J., Nicklas, W. J., and Geller, H. M. (1995) L-dopa cytotoxicity to PC12 cells in culture is via its autoxidation. J. Neurochem. 64, 825–832.
Alexander, T., Sortwell, C. E., Sladek, C. D., Roth, R. H., and Steece-Collier, K. (1997) Comparison of neurotoxicity following repeated administration of 1-dopa, d-dopa and dopamine to embryonic mesencephalic dopamine neurons in cultures derived from Fisher 344 and Sprague-Dawley donors. Cell Transplant 6, 309–315.
Fahn, S (1998) Welcome news about levodopa, but uncertainty remains [editorial] [see comments]. Ann. Neurol. 43, 551–444.
Heikkila, R. E., Manzino, L., Cabbat, F. S., and Duvoisin, R. C. (1985) Studies on the oxidation of the dopaminergic neurotoxin 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine by monoamine oxidase B. J. Neurochem. 45, 1049–1054.
Shoulson, I. (1998) DATATOP: a decade of neuroprotective inquiry. Parkinson Study Group. Deprenyl and tocopherol antioxidative therapy of Parkinsonism. Ann. Neurol. 44, S160 - S166.
Giovanni, A., Liang, L. P., Hastings, T. G., and Zigmond, M. J. (1995) Estimating hydroxyl radical content in rat brain using systemic and intraventricular salicylate: impact of methamphetamine. J. Neurochem. 64, 1819–1825.
Shankaran, M., Yamamoto, B. K., and Gudelsky, G. A. (1999) Mazindol attenuates the 3,4-methylenedioxymethamphetamine-induced formation of hydroxyl radicals and longterm depletion of serotonin in the striatum. J. Neurochem. 72, 2516–2522.
Yamamoto, B. K. and Zhu, W. (1998) The effects of methamphetamine on the production of free radicals and oxidative stress. J. Pharmacol. Exp. Ther. 287, 107–114.
Deng, X. and Cadet, J. L. (1999) Methamphetamine administration causes overexpression of nNOS in the mouse striatum [In Process Citation]. Brain Res. 851, 254–257.
Zheng, Y. and Laverty, R. (1998) Role of brain nitric oxide in (+/-)3,4-methylenedioxymethamphetamine (MDMA)-induced neurotoxicity in rats. Brain Res. 795, 257–263.
Gudelsky, G. A. (1996) Effect of ascorbate and cysteine on the 3,4-methylenedioxymethamphetamine-induced depletion of brain serotonin. J. Neural. Transm. 103, 1397–1404.
Hom, D. G., Jiang, D., Hong, E. J., Mo, J. Q., and Andersen, J. K. (1997) Elevated expression of glutathione peroxidase in PC12 cells results in protection against methamphetamine but not MPTP toxicity. Brain Res. Mol. Brain Res. 46, 154–160.
Sheng, P., Cerruti, C., Ali, S., and Cadet, J. L. (1996) Nitric oxide is a mediator of methamphetamine (METH)-induced neurotoxicity. In vitro evidence from primary cultures of mesencephalic cells. Ann. NYAcad. Sci. 801, 174–186.
Itzhak, Y., Martin, J. L., and Ali, S. F. (1999) Methamphetamine-and 1-methyl-4-phenyl1,2,3,6-tetrahydropyridine-induced dopaminergic neurotoxicity in inducible nitric oxide synthase-deficient mice, Synapse 34, 305–312.
Itzhak, Y. and Ali, S. F. (1996) The neuronal nitric oxide synthase inhibitor, 7nitroindazole, protects against methamphetamine-induced neurotoxicity in vivo. J. Neurochem. 67, 1770–1773.
Ali, S. F. and Itzhak, Y. (1998) Effects of 7-nitroindazole, an NOS inhibitor on methamphetamine-induced dopaminergic and serotonergic neurotoxicity in mice. Ann. NYAcad. Sci. 844, 122–130.
Callahan, B. T. and Ricaurte, G. A. (1998) Effect of 7-nitroindazole on body temperature and methamphetamine-induced dopamine toxicity. NeuroReport 9, 2691–2695.
Di Monte, D. A., Royland, J. E., Jakowec, M. W., and Langston, J. W. (1996) Role of nitric oxide in methamphetamine neurotoxicity: protection by 7-nitroindazole, an inhibitor of neuronal nitric oxide synthase. J. Neurochem. 67, 2443–2450.
Jayanthi, S., Ladenheim, B., Andrews, A. M., and Cadet, J. L. (1999) Overexpression of human copper/zinc superoxide dismutase in transgenic mice attenuates oxidative stress caused by methylenedioxymethamphetamine (Ecstasy). Neuroscience 91, 1379–1387.
Jayanthi, S., Ladenheim, B., and Cadet, J. L. (1998) Methamphetamine-induced changes in antioxidant enzymes and lipid peroxidation in copper/zinc-superoxide dismutase transgenic mice. Ann. NYAcad. Sci. 844, 92–102.
Hirata, H., Asanuma, M., and Cadet, J. L. (1998) Superoxide radicals are mediators of the effects of methamphetamine on Zif268 (Egr-1, NGFI-A) in the brain: evidence from using CuZn superoxide dismutase transgenic mice. Brain Res. Mol. Brain Res. 58, 209–216.
Cadet, J. L., Ali, S. F., Rothman, R. B., and Epstein, C. J. (1995) Neurotoxicity, drugs and abuse, and the CuZn-superoxide dismutase transgenic mice. Mol. Neurobiol. 11, 155–163.
Cadet, J. L., Ladenheim, B., Hirata, H., Rothman, R. B., Ali, S., Carlson, E., Epstein, C., and Moran, T. H. (1995) Superoxide radicals mediate the biochemical effects of methylenedioxymethamphetamine (MDMA): evidence from using CuZn-superoxide dismutase transgenic mice. Synapse 21, 169–176.
Hirata, H., Ladenheim, B., Rothman, R. B., Epstein, C., and Cadet, J. L. (1995) Methamphetamine-induced serotonin neurotoxicity is mediated by superoxide radicals. Brain Res. 677, 345–347.
Cadet, J. L., Ladenheim, B., Baum, I., Carlson, E., and Epstein, C. (1994) CuZn-superoxide dismutase (CuZnSOD) transgenic mice show resistance to the lethal effects of methylenedioxyamphetamine (MDA) and of methylenedioxymethamphetamine (MDMA). Brain Res. 655, 259–262.
Cadet, J. L., Ali, S., and Epstein, C. (1994) Involvement of oxygen-based radicals in methamphetamine-induced neurotoxicity: evidence from the use of CuZnSOD transgenic mice. Ann. NYAcad. Sci. 738, 388–391.
Kita, T., Paku, S., Takahashi, M., Kubo, K., Wagner, G. C., and Nakashima, T. (1998) Methamphetamine-induced neurotoxicity in BALB/c, DBA/2N and C57BL/6N mice. Neuropharmacology 37, 1177–1184.
Beckman, J. S. and Koppenol, W. H. (1996) Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and the ugly. Am. J. Physiol. 271, C1424 - C1437.
Crow, J. P. and Beckman, J. S. (1995) The role of peroxynitrite in nitric oxide-mediated toxicity. Curr. Top. Microbiol. Immunol. 196, 57–73.
Crow, J. P. and Beckman, J. S. (1995) Reactions between nitric oxide, superoxide, and peroxynitrite: footprints of peroxynitrite in vivo. Adv. Pharmacol. 34, 17–43.
Koppenol, W. H., Moreno, J. J., Pryor, W. A., Ischiropoulos, H., and Beckman, J. S. (1992) Peroxynitrite, a cloaked oxidant formed by nitric oxide and superoxide. Chem. Res. Toxicol. 5, 834–842.
Beckman, J. S., Chen, J., Ischiropoulos, H., and Crow, J. P. (1994) Oxidative chemistry of peroxynitrite. Methods Enzymol. 233, 229–240.
Radi, R., Beckman, J. S., Bush, K. M., and Freeman, B. A. (1991) Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide. J. Biol. Chem. 266, 4244–4250.
Crow, J. P. and Ischiropoulos, H. (1996) Detection and quantitation of nitrotyrosine residues in proteins: in vivo marker of peroxynitrite. Methods Enzymol. 269, 185–194.
Souza, J M., Daikhin, E., Yudkoff, M., Raman, C. S., and Ischiropoulos, H. (1999) Factors determining the selectivity of protein tyrosine nitration. Arch. Biochem. Biophys. 371, 169–178.
van der Vliet, A., Eiserich, J. P., Kaur, H., Cross, C. E., and Halliwell, B. (1996) Nitrotyrosine as biomarker for reactive nitrogen species. Methods Enzymol. 269, 175–184.
Ischiropoulos, H. and al-Mehdi, A. B. (1995) Peroxynitrite-mediated oxidative protein modifications. FEBS Lett. 364, 279–282.
Smith, M. A., Richey Harris, P. L., Sayre, L. M., Beckman, J. S., and Perry, G. (1997) Widespread peroxynitrite-mediated damage in Alzheimer’s disease. J. Neurosci. 17, 2653–2657.
Crow, J. P. and Beckman, J. S. (1996) The importance of superoxide in nitric oxide-dependent toxicity: evidence for peroxynitrite-mediated injury. Adv. Exp. Med. Biol. 387, 147–161.
Ischiropoulos, H. (1998) Biological tyrosine nitration: a pathophysiological function of nitric oxide and reactive oxygen species. Arch. Biochem. Biophys. 356, 1–11.
Ara, J., Przedborski, S., Naini, A. B., Jackson-Lewis, V., Trifiletti, R. R., Horwitz, J., and Ischiropoulos, H. (1998) Inactivation of tyrosine hydroxylase by nitration following exposure to peroxynitrite and 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). Proc. Natl. Acad. Sci. USA 95, 7659–7663.
Imam, S. Z., Crow, J. P., Newport, G. D., Islam, F., Slikker, W., Jr., and Ali, S. F. (1999) Methamphetamine generates peroxynitrite and produces dopaminergic neurotoxicity in mice: protective effects of peroxynitrite decomposition catalyst. Brain Res. 837, 15–21.
Simonian, N. A. and Coyle, J. T. (1996) Oxidative stress in neurodegenerative diseases. Annu. Rev. Pharmacol. Toxicol. 36, 83–106.
Fahn, S and Cohen, G. (1992) The oxidant stress hypothesis in Parkinson’s disease: evidence supporting it. Ann. Neurol. 32, 804–812.
Tatton, W. G. and Olanow, C. W. (1999) Apoptosis in neurodegenerative diseases: the role of mitochondria [see comments]. Biochim. Biophys. Acta 1410, 195–213.
Gutteridge, J. M. (1994) Hydroxyl radicals, iron, oxidative stress, and neurodegeneration. Ann. NY Acad. Sci. 738, 201–213.
Zang, L. Y. and Misra, H. P. (1993) Generation of reactive oxygen species during the monoamine oxidase-catalyzed oxidation of the neurotoxicant, 1-methyl-4-phenyl-1,2,3,6tetrahydropyridine. J. Biol. Chem. 268, 16504–16512.
Zang, L. Y. and Misra, H. P. (1992) EPR kinetic studies of superoxide radicals generated during the autoxidation of 1-methyl-4-phenyl-2,3-dihydropyridinium, a bioactivated intermediate of parkinsonian-inducing neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine. J. Biol. Chem. 267, 23601–23608.
Zang, L. Y. and Misra, H. P. (1992) Superoxide radical production during the autoxidation of 1-methyl-4-phenyl-2,3-dihydropyridinium perchlorate. J. Biol. Chem. 267, 17547–17552.
Klivenyi, P., St. Clair, D., Wermer, M., Yen, H. C., Oberley, T., Yang, L., and Flint Beal, M. (1998) Manganese superoxide dismutase overexpression attenuates MPTP toxicity. Neurobiol. Dis. 5, 253–258.
Andrews, A. M., Ladenheim, B., Epstein, C. J., Cadet, J. L., and Murphy, D. L. (1996) Transgenic mice with high levels of superoxide dismutase activity are protected from the neurotoxic effects of 2’-NH2-MPTP on serotonergic and noradrenergic nerve terminals. Mol. Pharmacol. 50, 1511–1519.
Przedborski, S., Kostic, V., Jackson-Lewis, V., Naini, A. B., Simonetti, S., Fahn, S., et al. (1992) 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, 1658–1667.
Matthews, R. T., Beal, M. F., Fallon, J., Fedorchak, K., Huang, P. L., Fishman, M. C., and Hyman, B. T. (1997) MPP+ induced substantia nigra degeneration is attenuated in nNOS knockout mice. Neurobiol. Dis. 4, 114–121.
Przedborski, S., Jackson-Lewis, V., Yokoyama, R., Shibata, T., Dawson, V. L., and Dawson, T. M. (1996) Role of neuronal nitric oxide in 1-methyl-4-phenyl-1,2,3,6tetrahydropyridine (MPTP)-induced dopaminergic neurotoxicity. Proc. Natl. Acad. Sci. USA 93, 4565–4571.
Liberatore, G. T., Jackson-Lewis, V., Vukosavic, S., Mandir, A. S., Vila, M., McAuliffe, W. G., et al. (1999) Inducible nitric oxide synthase stimulates dopaminergic neurodegeneration in the MPTP model of Parkinson disease. Nature Med. 5, 1403–1409.
Hantraye, P., Brouillet, E., Ferrante, R., Palfi, S., Dolan, R., Matthews, R. T., and Beal, M. F. (1996) Inhibition of neuronal nitric oxide synthase prevents MPTP-induced parkinsonism in baboons [see comments], Nature Med. 2, 1017–1021.
Schulz, J. B., Matthews, R. T., Muqit, M. M., Browne, S. E., and Beal, M. F. (1995) Inhibition of neuronal nitric oxide synthase by 7-nitroindazole protects against MPTPinduced neurotoxicity in mice. J. Neurochem. 64, 936–939.
Golbe, L. I. (1993) Risk factors in young-onset Parkinson’s disease [editorial; comment]. Neurology 43, 1641–1643.
Hubble, J. P., Cao, T., Hassanein, R. E., Neuberger, J. S., and Koller, W. C. (1993) Risk factors for Parkinson’s disease [see comments]. Neurology 43, 1693–1697.
Semchuk, K. M., Love, E. J., and Lee, R. G. (1991) Parkinson’s disease and exposure t o rural environmental factors: a population based case-control study. Can. J. Neurol. Sci. 18, 279–286.
Seidler, A., Hellenbrand, W., Robra, B. P., Vieregge, P., Nischan, P., Joerg, J., et al. (1996) Possible environmental, occupational, and other etiologic factors for Parkinson’s disease: a case-control study in Germany. Neurology 46, 1275–1284.
Fleming, L., Mann, J. B., Bean, J., Briggle, T., and Sanchez-Ramos, J. R. (1994) Parkinson’s disease and brain levels of organochlorine pesticides. Ann. Neurol. 36, 100–103.
Semchuk, K. M., Love, E. J., and Lee, R. G. (1992) Parkinson’s disease and exposure to agricultural work and pesticide chemicals. Neurology 42, 1328–1335.
Koller, W., Vetere-Overfield, B., Gray, C., Alexander, C., Chin, T., Dolezal, J., et al. (1990) Environmental risk factors in Parkinson’s disease. Neurology 40, 1218–1221.
Barbeau, A., Dallaire, L., Buu, N. T., Poirier, J., and Rucinska, E. (1985) Comparative behavioral, biochemical and pigmentary effects of MPTP, MPP+ and paraquat in Rana pipiens. Life Sci. 37, 1529–1538.
Brooks, A. I., Chadwick, C. A., Gelbard, H. A., Cory-Slechta, D. A., and Federoff, H. J. (1999) Paraquat elicited neurobehavioral syndrome caused by dopaminergic neuron loss. Brain Res. 823, 1–10.
Wagner, S. R. and Greene, F. E. (1978) Dieldrin-induced alterations in biogenic amine content of rat brain. Toxicol. Appl. Pharmacol. 43, 45–55.
Heinz, G. H., Hill, E. F., and Contrera, J. F. (1980) Dopamine and norepinephrine depletion in ring doves fed DDE, dieldrin, and Aroclor 1254. Toxicol. Appl. Pharmacol. 53, 75–82.
Sanchez-Ramos, J., Facca, A., Basit, A., and Song, S. (1998) Toxicity of dieldrin for dopaminergic neurons in mesencephalic cultures. Exp. Neurol. 150, 263–271.
Bergen, W. G. (1971) The in vitro effect of dieldrin on respiration of rat liver mitochondria. Proc. Soc. Exp. Biol. Med. 136, 732–735.
Miller, G. W., Kirby, M. L., Levey, A. I., and Bloomquist, J. R. (1999) Heptachlor alters expression and function of dopamine transporters [In Process Citation]. Neurotoxicology 20, 631–637.
Vaccari, A. and Saba, P. (1995) The tyramine-labelled vesicular transporter for dopamine: a putative target of pesticides and neurotoxins. Eur. J. Pharmacol. 292, 309–314.
Ho, Y. S., Gargano, M., Cao, J., Bronson, R. T., Heimler, I., and Hutz, R. J. (1998) Reduced fertility in female mice lacking copper-zinc superoxide dismutase. J. Biol. Chem. 273, 7765–7769.
Huang, T. T., Yasunami, M., Carlson, E. J., Gillespie, A. M., Reaume, A. G., Hoffman, E. K., et al. (1997) Superoxide-mediated cytotoxicity in superoxide dismutase-deficient fetal fibroblasts. Arch. Biochem. Biophys. 344, 424–432.
Yang, W. and Sun, A. Y. (1998) Paraquat-induced free radical reaction in mouse brain microsomes. Neurochem. Res. 23, 47–53.
Yang, W. L. and Sun, A. Y. (1998) Paraquat-induced cell death in PC12 cells. Neurochem. Res. 23, 1387–1394.
Li, X. and Sun, A. Y. (1999) Paraquat induced activation of transcription factor AP-1 and apoptosis in PC12 cells. J. Neural. Transm. 106, 1–21.
Day, B. J., Patel, M., Calavetta, L., Chang, L. Y., and Stamler, J. S. (1999) A mechanism of paraquat toxicity involving nitric oxide synthase. Proc. Natl. Acad. Sci. USA 96, 12760–12765.
Kerry, N. and Rice-Evans, C. (1998) Peroxynitrite oxidises catechols to o-quinones. FEBS Lett. 437, 167–171.
Pannala, A. S., Razaq, R., Halliwell, B., Singh, S., and Rice-Evans, C. A. (1998) Inhibition of peroxynitrite dependent tyrosine nitration by hydroxycinnamates: nitration or electron donation? Free Radic. Biol. Med. 24, 594–606.
Hastings, T. G. and Zigmond, M. J. (1997) Loss of dopaminergic neurons in parkinsonism: possible role of reactive dopamine metabolites. J. Neural. Transm. (Suppl.)49, 103–110.
Stokes, A. H., Hastings, T. G., and Vrana, K. E. (1999) Cytotoxic and genotoxic potential of dopamine. J. Neurosci. Res. 55, 659–665.
LaVoie, M. J. and Hastings, T. G. (1999) Dopamine quinone formation and protein modification associated with the striatal neurotoxicity of methamphetamine: evidence against a role for extracellular dopamine. J. Neurosci. 19, 1484–1491.
Spencer, J. P., Jenner, P., Daniel, S. E., Lees, A. J., Marsden, D. C., and Halliwell, B. (1998) Conjugates of catecholamines with cysteine and GSH in Parkinson’s disease: possible mechanisms of formation involving reactive oxygen species. J. Neurochem. 71, 2112–2122.
Montine, T. J., Picklo, M. J., Amarnath, V., Whetsell, W. O., Jr., and Graham, D. G. (1997) Neurotoxicity of endogenous cysteinylcatechols. Exp. Neurol. 148, 26–33.
Rowe, D. B., Le, W., Smith, R. G., and Appel, S. H. (1998) Antibodies from patients with Parkinson’s disease react with protein modified by dopamine oxidation. J. Neurosci. Res. 53, 551–558.
Pfeiffer, S. and Mayer, B. (1998) Lack of tyrosine nitration by peroxynitrite generated at physiological pH. J. Biol. Chem. 273, 27280–27285.
Ohnishi, T., Yamazaki, H., Iyanagi, T., Nakamura, T., and Yamazaki, I. (1969) Oneelectron-transfer reactions in biochemical systems. II. The reaction of free radicals formed in the enzymic oxidation. Biochim. Biophys. Acta 172, 357–369.
Iyanagi, T. and Yamazaki, I. (1969) One-electron-transfer reactions in biochemical systems. 3. One-electron reduction of quinones by microsomal flavin enzymes. Biochim. Biophys. Acta 172, 370–381.
Iyanagi, T. and Yamazaki, I. (1970) One-electron-transfer reactions in biochemical systems. V. Difference in the mechanism of quinone reduction by the NADH dehydrogenase and the NAD(P)H dehydrogenase (DT-diaphorase). Biochim. Biophys. Acta 216, 282–294.
McCord, J. M. and Fridovich, I. (1969) Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244, 6049–6055.
Misra, H. P. and Fridovich, I. (1972) The role of superoxide anion in the autoxidation of epinephrine and a simple assay for superoxide dismutase. J. Biol. Chem. 247, 3170–3175.
Berman, S. B. and Hastings, T. G. (1999) Dopamine oxidation alters mitochondrial respiration and induces permeability transition in brain mitochondria: implications for Parkinson’s disease. J. Neurochem. 73, 1127–1137.
Kuhn, D. M., Arthur, R. E., Jr., Thomas, D. M., and Elferink, L. A. (1999) Tyrosine hydroxylase is inactivated by catechol-quinones and converted to a redox-cycling quinoprotein: possible relevance to Parkinson’s disease. J. Neurochem. 73, 1309–1317.
Kuhn, D. M., Aretha, C. W., and Geddes, T. J. (1999) Peroxynitrite inactivation of tyrosine hydroxylase: mediation by sulfhydryl oxidation, not tyrosine nitration. J. Neurosci. 19, 10289–10294.
Grima, B., Lamouroux, A., Blanot, F., Biguet, N. F., and Mallet, J. (1985) Complete coding sequence of rat tyrosine hydroxylase mRNA. Proc. Natl. Acad. Sci. USA 82, 617–621.
Andersson, K. K., Vassort, C., Brennan, B. A., Que, L., Jr., Haavik, J., Flatmark, T., et al. (1992) Purification and characterization of the blue-green rat phaeochromocytoma (PC 12) tyrosine hydroxylase with a dopamine-Fe(III) complex. Reversal of the endogenous feedback inhibition by phosphorylation of serine-40. Biochem. J. 284, 687–695.
Almas, B., Le Bourdelles, B., Flatmark, T., Mallet, J., and Haavik, J. (1992) Regulation of recombinant human tyrosine hydroxylase isozymes by catecholamine binding and phosphorylation. Structure/activity studies and mechanistic implications. Eur. J. Biochem. 209, 249–255.
Haavik, J., Martinez, A. and Flatmark, T. (1990) pH-dependent release of catecholamines from tyrosine hydroxylase and the effect of phosphorylation of Ser-40. FEBS Lett. 262, 363–365.
Haavik, J., Le Bourdelles, B., Martinez, A., Flatmark, T., and Mallet, J. (1991) Recombinant human tyrosine hydroxylase isozymes. Reconstitution with iron and inhibitory effect of other metal ions. Eur. J. Biochem. 199, 371–378.
Ramsey, A. J., Daubner, S. C., Ehrlich, J. I., and Fitzpatrick, P. F. (1995) Identification of iron ligands in tyrosine hydroxylase by mutagenesis of conserved histidinyl residues. Protein Sci. 4, 2082–2086.
Ribeiro, P., Wang, Y., Citron, B. A., and Kaufman, S. (1992) Regulation of recombinant rat tyrosine hydroxylase by dopamine. Proc. Natl. Acad. Sci. USA 89, 9593–9597.
Kuhn, D. M. and Arthur, R., Jr. (1998) Dopamine inactivates tryptophan hydroxylase and forms a redox-cycling quinoprotein: possible endogenous toxin to serotonin neurons. J. Neurosci. 18, 7111–7117.
Kato, T., Ito, S., and Fujita, K. (1986) Tyrosinase-catalyzed binding of 3,4dihydroxyphenylalanine with proteins through the sulfhydryl group. Biochim. Biophys. Acta 881, 415–421.
Paz, M. A., Fluckiger, R., Boak, A., Kagan, H. M., and Gallop, P. M. (1991) Specific detection of quinoproteins by redox-cycling staining. J. Biol. Chem. 266, 689–692.
Simpson, J. A., Narita, S., Gieseg, S., Gebicki, S., Gebicki, J. M., and Dean, R. T. (1992) Long-lived reactive species on free-radical-damaged proteins. Biochem. J. 282, 621–624.
Simpson, J. A., Gieseg, S. P., and Dean, R. T. (1993) Free radical and enzymatic mechanisms for the generation of protein bound reducing moieties. Biochim. Biophys. Acta 1156, 190–196.
Dean, R. T., Fu, S., Stocker, R., and Davies, M. J. (1997) Biochemistry and pathology of radical-mediated protein oxidation. Biochem. J. 324, 1–18.
Dean, R. T., Gebicki, J., Gieseg, S., Grant, A. J., and Simpson, J. A. (1992) Hypothesis: a damaging role in aging for reactive protein oxidation products? Mutat. Res. 275, 387–393.
Davies, M. J., Fu, S., Wang, H., and Dean, R. T. (1999) Stable mlarkers of oxidant damage to proteins and their application in the study of human disease Free Rad. Biol. Med. 27, 1151–1163.
Brunmark, A. and Cadenas, E. (1989) Redox and addition chemistry of quinoid compounds and its biological implications. Free Rad. Biol. Med. 7, 435–477.
Velez-Pardo, C., Jimenez Del Rio, M., Ebinger, G., and Vauquelin, G. (1996) Redox cycling activity of monoamine-serotonin binding protein conjugates. Biochem. Pharmacol. 51, 1521–1525.
Shen, X. M. and Dryhurst, G. (1996) Oxidation chemistry of (-)-norepinephrine in the presence of L-cysteine. J. Med. Chem. 39, 2018–2029.
Shen, X. M., Zhang, F. and Dryhurst, G. (1997) Oxidation of dopamine in the presence of cysteine: characterization of new toxic products. Chem. Res. Toxicol. 10, 147–155.
Liu, K. P., Gershon, M. D., and Tamir, H. (1985) Identification, purification, and characterization of two forms of serotonin binding protein from rat brain. J. Neurochem. 44, 1289–1301.
Tamir, H. and Liu, K. P. (1982) On the nature of the interaction between serotonin and serotonin binding protein: effect of nucleotides, ions, and sulfhydryl reagents. J. Neurochem. 38, 135–141.
Smythies, J. and Galzigna, L. (1998) The oxidative metabolism of catecholamines in the brain: a review. Biochim. Biophys. Acta 1380, 159–162.
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2002 Springer Science+Business Media New York
About this chapter
Cite this chapter
Kuhn, D.M. (2002). Dopamine and Its Modulation of Drug-Induced Neuronal Damage. In: Massaro, E.J. (eds) Handbook of Neurotoxicology. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-59259-165-7_7
Download citation
DOI: https://doi.org/10.1007/978-1-59259-165-7_7
Publisher Name: Humana Press, Totowa, NJ
Print ISBN: 978-1-61737-194-3
Online ISBN: 978-1-59259-165-7
eBook Packages: Springer Book Archive