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Conjugates of Catecholamines with Cysteine and GSH in Parkinson's Disease: Possible Mechanisms of Formation Involving Reactive Oxygen Species
Open accessAbstract
Abstract: Oxidation of l ‐3,4‐dihydroxyphenylalanine ( l ‐DOPA) and dopamine (DA) to generate semiquinones/quinones, oxygen radicals, and other reactive oxygen species may play a role in neuronal cell death in Parkinson's disease (PD). In particular, semiquinones/quinones can form conjugates with thiol compounds such as GSH and cysteine. Exposure of l ‐DOPA, DA, and other catecholamines to a system generating O 2 •− radical led to O 2 •− ‐dependent depletion of added GSH (or cysteine), accompanied by the formation of thiol‐DA or ‐DOPA adducts as detected by HPLC. Superoxide could additionally cause destruction of these adducts. Iron or copper ions could also promote conjugate formation between GSH or cysteine and DA and l ‐DOPA, especially if H 2 O 2 was present. We applied HPLC to measure glutathionyl and cysteinyl conjugates of l ‐DOPA, DA, and 3,4‐dihydroxyphenylacetic acid (DOPAC) in postmortem brain samples from PD patients and normal control subjects. Conjugates were detected in most brain areas examined, but levels were highest in the substantia nigra and putamen. In most regions, adduct levels were lower in PD, but there were significant increases in cysteinyl adducts of l ‐DOPA, DA, and DOPAC in PD substantia nigra, suggesting that acceleration of l ‐DOPA/DA oxidation occurs in PD, although we cannot say if this is a primary feature of the disease or if it is related to therapy with l ‐DOPA. In vitro, conjugate formation could be inhibited by the dithiol dihydrolipoate but not by its oxidised form, lipoic acid.
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“Observation of cysteinyl adducts of dopamine in substantia nigra postmortem samples confirmed severe oxidation process occurring in PD brain. (Spencer et al. 1998).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Spencer et al. 1998
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- Halliwell B. and Gutteridge J. M. C. (1989) Free Radicals in Biol- ogy and Medicine, 2nd edit. Clarendon Press, Oxford.
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Items 201–300 of 374
Jiang, X., Wrona, M. Z., & Dryhurst, G. (1999) · Chemical Research in Toxicology · doi:10.1021/tx9801615 · Cited by 32
A functionalized hydroxydopamine quinone links thiol modification to neuronal cell death
Farzam, A., Chohan, K. L., Strmiskova, M., Hewitt, S. J., Park, D. S., Pezacki, J. P., & Özcelik, D. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101377 · Cited by 31
Smythies, J., Iuliis, A. D., Zanatta, L., & Galzigna, L. (2002) · Neurotoxicity Research · doi:10.1080/10298420290007655 · Cited by 31
“This has been confirmed by Spencer et al. (1998) who showed that in the PD SNpc, there are increased levels of cysteinyl adducts of dopamine, L-DOPA and DOPAC, suggesting increased levels of oxidation of L-DOPA and of dopamine.”
BackgroundEnhancement of Dopaminergic Neurotoxicity by the Mercapturate of Dopamine
Zhang, J., Kravtsov, V., Amarnath, V., Picklo, M. J., Graham, D. G., & Montine, T. J. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0740970.x · Cited by 32
“The concentrations of glutathionyl and cysteinyl catechol thioethers are up to 3% of total dopamine (Fornstedt et al., 1986; Spencer et al., 1998 ); however, conditions that increase extravesicular dopamine also increase the amount of dopamine converted to Cysdopamine (Hastings et al., 1996a,b).”
BackgroundZhou, Z., & Lim, T. M. (2009) · Nature Precedings · doi:10.1007/s11064-010-0247-7 · Cited by 30
“Furthermore, when compared with aged controls, the highest level of GSH-DA conjugates were detected in the SN and putamen of postmortem PD patients [26].”
BackgroundHarnessing the Therapeutic Potential of the Nrf2/Bach1 Signaling Pathway in Parkinson’s Disease
Ahuja, M., Kaidery, N. A., Dutta, D., Attucks, O. C., Kazakov, E. H., Gazaryan, I. G., Matsumoto, M., Igarashi, K., Sharma, S. M., & Thomas, B. (2022) · Antioxidants · doi:10.3390/antiox11091780 · Cited by 34
“nigra of PD patients, suggesting the cytotoxic nature of DA oxidation products [28].”
BackgroundHoltz, W. A., Turetzky, J. M., & O’Malley, K. L. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.639 · Cited by 30
Common anti-inflammatory drugs are potentially therapeutic for Parkinson’s disease?
Asanuma, M., & Miyazaki, I. (2007) · Experimental Neurology · doi:10.1016/j.expneurol.2007.05.006 · Cited by 30
Modulation of D1-like dopamine receptor function by aldehydic products of lipid peroxidation
Shin, Y., White, B. H., Uh, M., & Sidhu, A. (2003) · Brain Research · doi:10.1016/s0006-8993(02)04279-8 · Cited by 30
Jia, Z., Zhu, H., Misra, B. R., Li, Y., & Misra, H. P. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9670-4 · Cited by 29
“For example, the endogenous cellular antioxidant glutathione (GSH) and the phase 2 enzyme NAD(P)H:quinone oxidoreductase 1 (NQO1) have recently been demonstrated to play critical roles in protecting neuronal cells against dopamine or 6-OHDA-induced oxidative stress and electrophilic cellular damage [5, 6 ]. In this co…”
BackgroundDopamine Prevents Nitration of Tyrosine Hydroxylase by Peroxynitrite and Nitrogen Dioxide
Park, S. U., Geddes, T. J., Javitch, J. A., & Kuhn, D. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304362200 · Cited by 29
Myoglobin Modification by Enzyme‐Generated Dopamine Reactive Species
Nicolis, S., Zucchelli, M., Monzani, E., & Casella, L. (2008) · Chemistry - A European Journal · doi:10.1002/chem.200801014 · Cited by 29
Neuroprotection for Parkinson’s disease: a new approach for a new millennium
Drukarch, B., & Muiswinkel, F. L. V. (2001) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.10.10.1855 · Cited by 29
“It is interesting to note, therefore, that in addition to depletion of GSH, the level of cysteinyl conjugates of DA is increased in the substantia nigra of Parkinsonian patients [37].”
Background5-S-Cysteinyl-dopamine effect on the human dopaminergic neuroblastoma cell line SH-SY5Y
Mosca, L., Lendaro, E., D’Erme, M., et al. (2006) · Neurochemistry International · doi:10.1016/j.neuint.2006.01.023 · Cited by 27
Saleem, U., Raza, Z., Anwar, F., Chaudary, Z., & Ahmad, B. (2019) · BMC Complementary and Alternative Medicine · doi:10.1186/s12906-019-2772-5 · Cited by 26
“These reactive metabolites of dopamine can form the cysteinyl adducts at substantia nigra of PD patient thus induces the neurodegeneration [42].”
BackgroundHurben, A. K., & Tretyakova, N. Y. (2022) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.2c00193 · Cited by 25
Agrahari, S., Singh, A. K., Gautam, R. K., et al. (2022) · Environmental Science and Pollution Research · doi:10.1007/s11356-022-23660-y · Cited by 25
Glial metabolism of quercetin reduces its neurotoxic potential
Vafeiadou, K., Vauzour, D., Rodriguez‐Mateos, A., Whiteman, M., Williams, R. J., & Spencer, J. P. E. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.07.014 · Cited by 25
Self-citationButterfield, D. A., Palmieri, E. M., & Castegna, A. (2016) · Expert Review of Proteomics · doi:10.1586/14789450.2016.1149470 · Cited by 25
“Since dopamine’s oxidation to its reactive metabolites, ROS and DA quinone (DAQ), may also contribute to the oxidative stress and mitochondrial dysfunction seen in PD by altering mitochondrial respiration and inducing permeability transition in brain mitochondria [146,147], exposure of isolated mitochondria to dopamin…”
The Role of Iron in Parkinson Disease and 1-Methyl-4-Phenyl-1,2,3,6-Tetrahydropyridine Toxicity
Yantiri, F., & Andersen, J. K. (1999) · IUBMB Life · doi:10.1080/713803493 · Cited by 25
Asanuma, M., & Miyazaki, I. (2006) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.6.9.1313 · Cited by 28
Evidence for covalent lipoyl adduction with dopaquinone following tyrosinase-catalyzed oxidation
Tsuji, K., Hatani, T., Okada, T., et al. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.02.118 · Cited by 25
“[17] have shown that DHLA, but not LA, inhibits the formation of the 5-S-cysteinyl- and 5-S-glutathionyl-catecholamine adducts in a system generating O 2 , proposing this as a model of oxidative stress for nervous system in general, and suggesting that DHLA may achieve these inhibitory effects by competing with either…”
BackgroundWeingarten, P., Bermak, J. C., & Zhou, Q. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00190.x · Cited by 24
Khan, F. H., Sen, T., & Chakrabarti, S. (2003) · Free Radical Research · doi:10.1080/1071576031000115651 · Cited by 24
“quinones are equally deleterious for the cells especially in causing mitochondrial dysfunction or inhibition of important enzymes.([3,4]) We have recently reported that in rat brain crude synaptoso-”
BackgroundDOPA pheomelanin is increased in nigral neuromelanin of Parkinson’s disease
Cai, W., Wakamatsu, K., Zucca, F. A., Wang, Q., Yang, K., Honarvar, N. M., Srivastava, P., Tanaka, H., Holly, G., Casella, L., et al. (2023) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2023.102414 · Cited by 24
“also detected significant increases in cysteinyl adducts of DOPA in addition to cysteinyl adducts of DA in PD SN (Spencer et al., 1998).”
Antioxidant Effect of Alpha-Lipoic Acid in 6-Hydroxydopamine Unilateral Intrastriatal Injected Rats
Andreeva-Gateva, P. A., Traikov, L. L., Sabit, Z., Bakalov, D. V., & Tafradjiiska-Hadjiolova, R. K. (2020) · Antioxidants · doi:10.3390/antiox9020122 · Cited by 24
“DA is easily oxidized both spontaneously and enzymatically to produce DA quinone species, which are able to covalently modify cellular nucleophiles, such as GSH, proteins cysteinyl residues, α-synuclein, parkin and other proteins, which are all implicated in the pathophysiology of PD [9].”
BackgroundSidell, K. R., Olson, S. J., Ou, J. J., Zhang, Y., Amarnath, V., & Montine, T. J. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00586.x · Cited by 23
“Previous studies have reported elevated Cys-DA levels in midbrain and basal ganglia from PD patients (Spencer et al. 1998).”
BackgroundResultInfluentialLiu, X., Zheng, Z., Xue, C., Wang, X., Li, J., Liu, Z., Xin, W., Xu, X., Zhou, D., Yao, L., et al. (2025) · Inflammation · doi:10.1007/s10753-025-02291-8 · Cited by 26
Brain Damage - Bridging Between Basic Research and Clinics
González-Quevedo, A. (2012) · InTech eBooks · doi:10.5772/2174 · Cited by 21
Patsoukis, N., Papapostolou, I., Zervoudakis, G., Georgiou, C. D., Matsokis, N. A., & Panagopoulos, N. T. (2004) · Neuroscience Letters · doi:10.1016/j.neulet.2004.11.019 · Cited by 21
Ilundáin, R. L., Valls, J. V. F., Rueda, J. J. V., Guerrero, D., & Fraile, P. (2001) · Revista Española de Salud Pública · doi:10.1590/s1135-57272001000100006 · Cited by 21
Pathways of dopamine oxidation mediated by nitric oxide
Rettori, D., Tang, Y., Dias, L. C., & Cadenas, E. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00953-x · Cited by 21
Voshavar, C., Shah, M. M., Xu, L., & Dutta, A. K. (2015) · Neurotoxicity Research · doi:10.1007/s12640-015-9548-6 · Cited by 21
“Conjugation of glutathione and its amino acid (cysteine) with oxidized products of DA, L-DOPA, DOPAC (dopamine metabolite), and other catecholamines has been also suggested to result in decrease of reduced glutathione levels (Linert and Jameson 2000; Shen and Dryhurst 1996; Spencer et al. 1998).”
Pandey, S., Singh, A. K., Chaudhari, N., Nampoothiri, L. P., & Kumar, G. N. (2015) · Current Microbiology · doi:10.1007/s00284-014-0763-9 · Cited by 20
Srivastava, J. P., Kushwaha, A., & Singh, M. (2018) · NANO · doi:10.1142/s179329201850131x · Cited by 20
Çakır, S., Biçer, E., & Eleman, A. (2001) · Transition Metal Chemistry · doi:10.1023/a:1007119907894 · Cited by 20
Immune cell metabolic dysfunction in Parkinson’s disease
Mark, J. R., & Tansey, M. G. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00827-y · Cited by 25
“Recent studies have revealed increased ROS levels [75], reduced function of antioxidant peroxidases [76], and decreased levels of glutathione, the primary endogenous antioxidant molecule, in the SNpc of PD patients relative to age-matched controls [77] (Fig.”
Protective Effects of Curcumin on Manganese-Induced BV-2 Microglial Cell Death
Park, E., & Chun, H. S. (2017) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b17-00160 · Cited by 19
Mitochondrial proteomics as a selective tool for unraveling Parkinson’s disease pathogenesis
Pienaar, I. S., Dexter, D. T., & Burkhard, P. R. (2010) · Expert Review of Proteomics · doi:10.1586/epr.10.8 · Cited by 19
Antibacterial effect of singlet oxygen depending on bacteria surface charge
Bae, I. K., Shin, J.-Y., Son, J.-H., et al. (2022) · Photodiagnosis and Photodynamic Therapy · doi:10.1016/j.pdpdt.2022.102975 · Cited by 18
Li, Y., Luo, F., Wei, L., Liu, Z., & Xu, P. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2010.09.070 · Cited by 18
Costa, V. M., Ferreira, L. M., Branco, P. S., et al. (2008) · Chemical Research in Toxicology · doi:10.1021/tx8002577 · Cited by 18
Neurorescue by a ROS Decomposition Catalyst
Soll, M., Am, O. B., Mahammed, A., et al. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00144 · Cited by 17
Z-Ligustilide Potentiates the Cytotoxicity of Dopamine in Rat Dopaminergic PC12 Cells
Qi, H., Zhao, J., Han, Y., Lau, A. S. Y., & Rong, J. (2012) · Neurotoxicity Research · doi:10.1007/s12640-012-9319-6 · Cited by 17
“In contrast, recent studies suggest that dopamine-derived thioethers may be potent neurotoxins in brain (Spencer et al. 1998; Zhang et al. 2000; Sidell et al. 2001; Montine et al. 2002).”
ResultWang, J., Wang, Y., Lv, H., Hui, F., Ma, Y., Lu, S., Sha, Q., & Wang, E. (2006) · Journal of Electroanalytical Chemistry · doi:10.1016/j.jelechem.2006.05.021 · Cited by 17
Taurine inhibition of metal-stimulated catecholamine oxidation
Dawson, R., Baker, D., Eppler, B., et al. (2000) · Neurotoxicity Research · doi:10.1007/bf03033322 · Cited by 17
“Quinones formed from dopamine oxidation form adducts with thiols such as cysteine and significant increases in cysteinyl adducts of L-dopa and dopamine have been found in the substantia nigra of Parkinson's patients (Spencer et al., 1998).”
BackgroundFarooqui, T. (2007) · The Neuroscientist · doi:10.1177/10738584070130040501 · Cited by 17
TNFα increases activity of γ‐glutamyl transpeptidase in cultured rat astroglial cells
Ruedig, C., & Dringen, R. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10878 · Cited by 17
“, 2002b) is a GT substrate (Wang and Ballatori, 1998); thus, an elevated activity of GT could contribute to the formation of 5-cysteinyl dopamine that was found in significantly higher concentrations in the substantia nigra of PD patients compared to that in controls (Spencer et al., 1998).”
ResultKim, S. Y., Park, E., Park, J. A., Choi, B.-S., Kim, S., Jeong, G., Kim, C., Kim, D. K., Kim, S.-J., & Chun, H. S. (2010) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf903294x · Cited by 16
Transsulfuration pathway: a targeting neuromodulator in Parkinson’s disease
Corona-Trejo, A., Gonsebatt, M. E., Trejo‐Solís, C., Campos‐Peña, V., Granados, L. I. Q., Villegas‐Vázquez, E. Y., Reyes‐Hernández, O. D., Hernández-Abad, V. J., Figueroa‐González, G., & Silva‐Adaya, D. (2023) · Reviews in the Neurosciences · doi:10.1515/revneuro-2023-0039 · Cited by 17
“The levels of cysteinyl adducts of L-DOPA, dopamine, and DOPAC, significantly increase in the substantia nigra of PD patients (Spencer et al. 1998).”
BackgroundDopamine-induced death of PC12 cells is prevented by a substituted tetrahydronaphthalene
Song, J. H., Slot, A. J., Ryan, R. W. J., & Ross, G. M. (2004) · Neuropharmacology · doi:10.1016/j.neuropharm.2004.01.001 · Cited by 16
A peptide disrupting the D2R-DAT interaction protects against dopamine neurotoxicity
Su, P., & Liu, F. (2017) · Experimental Neurology · doi:10.1016/j.expneurol.2017.05.010 · Cited by 16
“Studies in PD patients reported significant increase of cysteinyl adduct of dopamine in substantia nigra, indicating neurotoxicity of dopamine and its involvement in PD (Spencer et al., 1998).”
BackgroundPeralta-Rincón, J. R., Escudero, G., & Edelaar, P. (2017) · Journal of Orthoptera Research · doi:10.3897/jor.26.14550 · Cited by 16
“2012) and to Parkinson’s disease in the brain (Spencer et al. 1998).”
BackgroundLiu, J., Tan, F., Liu, X., Yi, R., & Zhao, X. (2020) · RSC Advances · doi:10.1039/c9ra09863a · Cited by 16
Weinberg, A., Nylander, K. D., Yan, C., et al. (2004) · Brain Research · doi:10.1016/j.brainres.2004.03.048 · Cited by 16
Pan, T.-M., Lin, L.-A., Ding, H., Her, J.-L., & Pang, S. (2024) · Talanta · doi:10.1016/j.talanta.2024.126178 · Cited by 16
Pathology of Neurodegenerative Diseases
Kim, Y. S., Kim, Y.-K., Hwang, O., & Dong, J. (2012) · InTech eBooks · doi:10.5772/38028 · Cited by 16
Kato, Y., Peskin, A. V., Dickerhof, N., Harwood, D. T., & Kettle, A. J. (2012) · Chemical Research in Toxicology · doi:10.1021/tx300218f · Cited by 13
Vauzour, D., Pinto, J. T., Cooper, A. J. L., & Spencer, J. P. E. (2014) · Biochemical Journal · doi:10.1042/bj20131519 · Cited by 13
Self-citationDOPAMINE MERCAPTURATE CAN AUGMENT DOPAMINERGIC NEURODEGENERATION*
Montine, T. J., Amarnath, V., Picklo, M. J., Sidell, K. R., Zhang, J., & Graham, D. G. (2000) · Drug Metabolism Reviews · doi:10.1081/dmr-100102339 · Cited by 12
Shen, X.-M., & Dryhurst, G. (2001) · Tetrahedron · doi:10.1016/s0040-4020(00)00953-4 · Cited by 12
Betharia, S., Rondón-Ortiz, A. N., & Brown, D. A. (2019) · Neurochemical Research · doi:10.1007/s11064-019-02823-3 · Cited by 10
Direct Ring Conjugation of Catecholamines and Their Immunological Interactions
Mitchell, J. S., Wu, Y., Cook, C. J., et al. (2006) · Bioconjugate Chemistry · doi:10.1021/bc0602174 · Cited by 12
Wang, C., & Zhang, Z. (2020) · ChemElectroChem · doi:10.1002/celc.202000867 · Cited by 11
Inactivation of Aconitase by Tetrahydrobiopterin in DArgic Cells: Relevance to PD
Yoon, N. S., Cho, Y., Lee, S. Y., Choi, H. J., & Hwang, O. (2010) · Experimental Neurobiology · doi:10.5607/en.2010.19.1.23 · Cited by 11
V63 and N65 of overexpressed α-synuclein are involved in mitochondrial dysfunction
Zhang, H., Liu, J., Wang, X., Duan, C., Wang, X., & Yang, H. (2016) · Brain Research · doi:10.1016/j.brainres.2016.04.002 · Cited by 11
The Mercapturomic Profile of Health and Non-Communicable Diseases
Dias, C. G., Morelló, J., Semedo, V. A. R., Correia, M. J., Coelho, N. R., Monteiro, E. C., Antunes, A. M. M., & Pereira, S. A. (2019) · Microarrays · doi:10.3390/ht8020010 · Cited by 11
“Assess Cys- and GSH-conjugates of DA, DOPA and DOPAC in brain tissue and changes on their levels in PD Ref [74] Postmortem brain samples from six PD patients with PD (mean age 77 yo, L-DOPA therapy) and six CTLs (mean age 81 yo); Brains were dissected into 11 regions Detectable conjugates in most brain regions, with h…”
BackgroundResultEvaluation of GSH adducts of adrenaline in biological samples
Silva, R., Boldt, S., Costa, V. M., et al. (2007) · Biomedical Chromatography · doi:10.1002/bmc.796 · Cited by 11
“, 2001, 2002, 2004) and neurotoxicity (Spencer et al., 1998; Smythies et al., 2002).”
BackgroundMethodInfluentialGreco, G., Panzella, L., Pezzella, A., Napolitano, A., & d’Ischia, M. (2010) · Tetrahedron · doi:10.1016/j.tet.2010.03.103 · Cited by 12
Oxidative Stress and Parkinson Disease
Lim, K., Graham, D. G., & Ng, X. (2011) · Wiley eBooks · doi:10.1002/9781118148143.ch10 · Cited by 11
Mondal, K., Ghanty, R., Mahadevan, A., Waghmare, G., Santhoshkumar, R., Nandeesh, B. N., & Datta, I. (2025) · Stem Cell Research & Therapy · doi:10.1186/s13287-025-04573-2 · Cited by 12
Characterization of catechol‐thioether‐induced apoptosis in human SH‐SY5Y neuroblastoma cells
Mosca, L., Tempera, I., Lendaro, E., et al. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21536 · Cited by 10
“dopamine concentration is documented in the substantia nigra along with a depigmentation of this cerebral area (Fornstedt et al., 1989; Spencer et al., 1998).”
BackgroundInfluentialPotential repositioning of exemestane as a neuroprotective agent for Parkinson’s disease
Son, H. J., Han, S. H., Lee, J. A., Shin, E. J., & Hwang, O. (2017) · Free Radical Research · doi:10.1080/10715762.2017.1353688 · Cited by 10
“NO (C) and ROS (D) levels in the cell medium were determined after 24 h. Data obtained from three independent experiments are expressed as percent of LPS-treated control ± SEM; p< .05 and p< .01 versus LPS-treated control. induce the antioxidant enzyme genes in dopaminergic neuronal cells.”
BackgroundInfluentialFornstedt, B. (2024) · Journal of Neural Transmission · doi:10.1007/s00702-023-02718-2 · Cited by 10
“S -cysteinyl adducts of DA, DOPA and DOPAC have been detected in DA-rich brain regions in several mammalian species including humans (Rosengren et al. 1985; Fornstedt et al. 1986, 1990a; Spencer et al. 1998), and 5-”
Molecular and Cellular Events Regulating Dopamine Neuron Survival
Corsini, G. U., Maggio, R., & Vaglini, F. (2002) · Handbook of experimental pharmacology · doi:10.1007/978-3-662-06765-9_11 · Cited by 9
Fishman-Jacob, T., & Youdim, M. B. H. (2023) · Journal of Neural Transmission · doi:10.1007/s00702-023-02687-6 · Cited by 7
Reduced DNA oxidation in aged prostaglandin H synthase-1 knockout mice
Jeng, W., Ramkissoon, A., & Wells, P. G. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.11.016 · Cited by 8
Fluid interface-mediated nanoparticle membrane as an electrochemical sensor
Ali, M. A., Barman, K., Jasimuddin, S., & Ghosh, S. K. (2014) · RSC Advances · doi:10.1039/c4ra12149j · Cited by 8
Badillo‐Ramírez, I., Landeros‐Rivera, B., de la O-Cuevas, E., et al. (2019) · New Journal of Chemistry · doi:10.1039/c9nj03781k · Cited by 8
Gille, G., Radad, K., Reichmann, H., & Rausch, W. (2005) · Journal of Neural Transmission · doi:10.1007/s00702-005-0369-2 · Cited by 8
“Moreover, L-dopa or DA autooxidation can lead to the formation of the respective quinones which are able to deplete GSH or to react with sulfhydryl groups, predominantly of cysteine, resulting in the formation of 5-S-cysteinyl L-dopa=5-S-cysteinyl DA and subsequent protein malfunction (Asanuma et al., 2003; Spencer et…”
BackgroundLiving Under the Volcano: Effects on the Nervous System and Human Health
Navarro‐Sempere, A., Cobo, R., Camarinho, R., Garcia, P., Rodrigues, A., Garcı́a, M., & Segovia, Y. (2025) · Environments · doi:10.3390/environments12020049 · Cited by 8
Synthesis of catecholamine conjugates with nitrogen-centered bionucleophiles
Siopa, F., Pereira, A. S., Ferreira, L. M., et al. (2012) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2012.05.002 · Cited by 7
Liu, P.-Y., Sun, S.-C., Chen, Y.-S., et al. (2015) · Electrochimica Acta · doi:10.1016/j.electacta.2015.10.168 · Cited by 7
Yoo, H., Ahn, G.-Y., Lee, E.-J., et al. (2017) · Molecular & Cellular Toxicology · doi:10.1007/s13273-017-0034-5 · Cited by 7
Dopamine thioethers: Formation in brain and neurotoxicity
Montine, K. S., Sidell, K. R., Zhang, J., et al. (2002) · Neurotoxicity Research · doi:10.1080/1029842021000045435 · Cited by 7
“Thus, it has been proposed that oxidized DA could be a proneurotoxin that is activated to a more potent neurotoxin by a similar MAP in pathway in brain ( Spencer et al., 1998; Zhang et al., 2000; Sidell et al., 2001).”
BackgroundDryhurst, G. (2001) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-0667-6_61 · Cited by 7
Ophthalmate is a new regulator of motor functions via CaSR: implications for movement disorders
Alhassen, S., Hogenkamp, D. J., Nguyen, H. A., et al. (2024) · Brain · doi:10.1093/brain/awae097 · Cited by 6
Adrenaline and Noradrenaline: Partners and Actors in the Same Play"
Marisa, V., Carvalho, F. D., de Lourdes, M., Albuquerque, R., Carvalho, M. X. E. R., & Remião, F. (2012) · InTech eBooks · doi:10.5772/36070 · Cited by 5
Fei, Q., Shen, K., Ke, H., et al. (2023) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2023.129563 · Cited by 5
Systems biology and network medicine: An integrated approach to redox biology and pathobiology
Lee, L. Y.-H., & Loscalzo, J. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-818606-0.00003-1 · Cited by 5
Initiation of symptomatic therapy in Parkinson's disease: dopamine agonists versus levodopa
Lev, N., Djaldetti, R., & Melamed, E. (2007) · Journal of Neurology · doi:10.1007/s00415-007-5004-8 · Cited by 5
“Furthermore, the quinone products of levodopa metabolism can bind to and deplete levels of reduced glutathione, thereby depriving the brain of an important antioxidant, levels of which are already decreased in the brains of PD patients [56, 58].”
BackgroundLau, F. C., Joseph, J. A., & Shukitt‐Hale, B. (2005) · Oxidative stress and disease · doi:10.1201/9781420026559.ch22 · Cited by 5
Saha, C., Kumari, P., Mgenge, L., et al. (2025) · Biochemical Engineering Journal · doi:10.1016/j.bej.2025.109755 · Cited by 4
Zhang, L., Min, Y., Fu, W., et al. (2022) · Scientia Sinica Chimica · doi:10.1360/ssc-2022-0069 · Cited by 4
Cytosolic dopamine determines hypersensitivity to blunt force trauma
Zuurbier, K. R., Fonseca, R. S., Arneaud, S. L. B., Tatge, L., Otuzoglu, G., Wall, J. M., & Douglas, P. M. (2024) · iScience · doi:10.1016/j.isci.2024.110094 · Cited by 4
Molecular Mechanisms Involved in the Neuroprotective Action of Phytochemicals
Sunkaria, A., Yadav, A., Sharma, S. K., & Sandhir, R. (2017) · Wiley eBooks · doi:10.1002/9781119155195.ch27 · Cited by 4
Neurotoxicity: A Complex Multistage Process Involving Different Mechanisms
Niedzielska, E., Rospond, B., Pomierny-Chamioło, L., Sadakierska−Chudy, A., & Filip, M. (2021) · Springer eBooks · doi:10.1007/978-3-030-71519-9_159-1 · Cited by 3
Redox Pioneer: Professor Barry Halliwell
Pervaiz, S. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3518 · Cited by 3
Dopamine and Neurodegeneration
Gille, G., & Riederer, P. F. (2005) · Humana Press eBooks · doi:10.1007/978-1-59259-852-6_18 · Cited by 3
Parkinson’s disease managing reversible neurodegeneration
Hinz, M., Stein, A. L., Cole, T., McDougall, B., & Westaway, M. (2016) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s98367 · Cited by 3
“L-dopa-associated glutathione depletion.(37) 20.”
Retracted
Metadata
- Authors
- Spencer, J. P. E., Jenner, P., Daniel, S. E., Lees, A. J., Marsden, D. C., & Halliwell, B.
- Affiliations
- University of London (GB)
- King's College London (GB)
- Parkinson's UK (GB)
- Corresponding author
- Spencer, Jeremy P. E.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 1998-11
- Volume
- 71
- Issue
- 5
- Pages
- 2112-2122
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W2165866163
- Cited by
- 373
- References
- 0
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 6 · 2023: 9 · 2022: 8 · 2021: 7 · 2020: 8 · 2019: 10 · 2018: 2 · 2017: 11 · 2016: 10 · 2015: 14 · 2014: 15 · 2013: 12 · 2012: 19
- FWCI
- 12.67
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Neurochemistry (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Topics
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Keywords
- Parkinson's disease, catecholamines, L-DOPA, dopamine, glutathione conjugates, cysteine conjugates, reactive oxygen species, superoxide, semiquinone, quinones, oxidative stress, neuronal cell death, substantia nigra, putamen, alpha-lipoic acid, postmortem brain
- MeSH terms
- Aged, Aged, 80 and over, Chromatography, High Pressure Liquid, Copper, Cysteine, Dihydroxyphenylalanine, Dopamine, Glutathione, Humans, Iron, Parkinson Disease, Reference Values, Superoxides, 3,4-Dihydroxyphenylacetic Acid, 8,11,14-Eicosatrienoic Acid, Reactive Oxygen Species, Hypoxanthine, Xanthine
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