Animal models of Parkinson's disease and their applications

References

• Fearnley JM, Lees AJ. Ageing and Parkinson’s disease: substantia nigra regional selectivity. Brain. 1991;114:2283–2301.
   PubMed Web of Science ®Google Scholar
• Marsden CD. Parkinson’s disease. J Neurol Neurosurg Psychiatry. 1994;57:672–681.
   PubMed Web of Science ®Google Scholar
• Fahn S. Description of Parkinson’s disease as a clinical syndrome. Ann N Y Acad Sci. 2003;991:1–14.
   PubMed Web of Science ®Google Scholar
• Yacoubian TA, Standaert DG. Targets for neuroprotection in Parkinson’s disease. Biochim Biophys Acta. 2009;1792:676–687.
   PubMed Web of Science ®Google Scholar
• Jankovic J. Motor fluctuations and dyskinesias in Parkinson’s disease: clinical manifestations. Mov Disord. 2005;20:S11–S16.
   PubMed Web of Science ®Google Scholar
• Olanow CW, Damier P, Goetz CG, et al. Multicenter, open-label, trial of sarizotan in Parkinson disease patients with levodopa-induced dyskinesias (the Splendid Study). Clin Neuropharmacol. 2004;27:58–62.
   PubMed Web of Science ®Google Scholar
• Cummings JL. Depression and Parkinson’s disease: a review. Am J Psychiatry. 1992;149:443–454.
   PubMed Web of Science ®Google Scholar
• Walsh K, Bennett G. Parkinson’s disease and anxiety. Postgrad Med J. 2001;77:89–93.
   PubMed Web of Science ®Google Scholar
• Maricle RA, Nutt JG, Valentine RJ, et al. Dose-response relationship of levodopa with mood and anxiety in fluctuating Parkinson’s disease: a double-blind, placebo-controlled study. Neurology. 1995;45:1757–1760.
   PubMed Web of Science ®Google Scholar
• Funkiewiez A, Ardouin C, Cools R, et al. Effects of levodopa and subthalamic nucleus stimulation on cognitive and affective functioning in Parkinson’s disease. Mov Disord. 2006;21:1656–1662.
   PubMedGoogle Scholar
• Decamp E, Schneider JS. Interaction between nicotinic and dopaminergic therapies on cognition in a chronic Parkinson model. Brain Res. 2009;1262:109–114.
   Web of Science ®Google Scholar
• Jackson-Lewis V, Blesa J, Przedborski S. Animal models of Parkinson’s disease. Parkinsonism Relat Disord. 2012;18 (Suppl 1):S183–S185.
   Web of Science ®Google Scholar
• Xu Y, Deng YL, Qing H. The phosphorylation of α-synuclein: development and implication for the mechanism and therapy of the Parkinson’s disease. J Neurochem. 2015;135:4–18.
   PubMed Web of Science ®Google Scholar
• Tufekci KU, Genc S, Genc K. The endotoxin-induced neuroinflammation model of Parkinson’s disease. Parkinsons Dis. 2011;2011:487450.
   PubMed Web of Science ®Google Scholar
• Dawson TM, Ko HS, Dawson VL. Genetic animal models of Parkinson’s disease. Neuron. 2010;66:646–661.
   PubMed Web of Science ®Google Scholar
• Cohen G. Oxy-radical toxicity in catecholamine neurons. Neurotoxicology. 1984;5:77–82.
   PubMed Web of Science ®Google Scholar
• Soto-Otero R, Méndez-Álvarez E, Hermida-Ameijeiras Á, et al. Autoxidation and neurotoxicity of 6-hydroxydopamine in the presence of some antioxidants: potential implication in relation to the pathogenesis of Parkinson’s disease. J Neurochem. 2000;74:1605–1612.
   PubMed Web of Science ®Google Scholar
• Blandini F, Armentero MT, Martignoni E. The 6-hydroxydopamine model: news from the past. Parkinsonism Relat Disord. 2008;14 (Suppl 2):S124–S129.
   Google Scholar
• Alves da Costa C, Dunys J, Brau F, et al. 6-Hydroxydopamine but not 1-methyl-4-phenylpyridinium abolishes α-synuclein anti-apoptotic phenotype by inhibiting its proteasomal degradation and by promoting its aggregation. J Biol Chem. 2006;281:9824–9831.
   Web of Science ®Google Scholar
• Crowther RA, Daniel SE, Goedert M. Characterisation of isolated α-synuclein filaments from substantia nigra of Parkinson’s disease brain. Neurosci Lett. 2000;292:128–130.
   PubMed Web of Science ®Google Scholar
• Ungerstedt U. 6-Hydroxy-dopamine induced degeneration of central monoamine neurons. Eur J Pharmacol. 2006;281:9824–9831.
   Google Scholar
• Schwarting RKW, Huston JP. The unilateral 6-hydroxydopamine lesion model in behavioral brain research. Analysis of functional deficits, recovery and treatments. Prog Neurobiol. 1996;49:215–266.
   PubMed Web of Science ®Google Scholar
• Curtius HC, Wolfensberger M, Steinmann B, et al. Mass fragmentography of dopamine and 6-hydroxydopamine: application to the determination of dopamine in human brain biopsies from the caudate nucleus. J Chromatogr A. 1974;99:529–540.
   PubMed Web of Science ®Google Scholar
• Andrew R, Watson DG, Best SA, et al. The determination of hydroxydopamines and other trace amines in the urine of parkinsonian patients and normal controls. Neurochem Res. 1993;18:1175–1177.
   PubMed Web of Science ®Google Scholar
• Terzioglu M, Galter D. Parkinson’s disease: genetic versus toxin-induced rodent models. FEBS J. 2008;275:1384–1391.
   PubMed Web of Science ®Google Scholar
• Bové J, Perier C. Neurotoxin-based models of Parkinson’s disease. Neuroscience. 2012;211:51–76.
   PubMed Web of Science ®Google Scholar
• Heikkila RE, Hess A, Duvoisin RC. Dopaminergic neurotoxicity of 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine in mice. Science. 1984;224:1451–1453.
   PubMed Web of Science ®Google Scholar
• Nicklas WJ, Vyas I, Heikkila RE. Inhibition of NADH-linked oxidation in brain mitochondria by 1-methyl-4-phenyl-pyridine, a metabolite of the neurotoxin, 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine. Life Sci. 1985;36:2503–2508.
   PubMed Web of Science ®Google Scholar
• McCormack AL, Mak SK, Shenasa M, et al. Pathological modifications of α-synuclein in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-treated squirrel monkeys. Neuropathol Exp Neurol. 2008; 67:793–802.
   Web of Science ®Google Scholar
• Purisai MG, McCormack AL, Langston WJ, et al. α-Synuclein expression in the substantia nigra of MPTP-lesioned non-human primates. Neurobiol Dis. 2005;20:898–906.
   Web of Science ®Google Scholar
• Collier TJ, Kanaan NM, Kordower JH. Aging as a primary risk factor for Parkinson’s disease: evidence from studies of non-human primates. Nat Rev Neurosci. 2011;12:359–366.
   PubMed Web of Science ®Google Scholar
• Eriksen N, Stark AK, Pakkenberg B. Age and Parkinson’s disease-related neuronal death in the substantia nigra pars compacta. J Neural Transm Suppl. 2009;73:203–213.
   Google Scholar
• McCormack AL, Mak SK, Henderson JM, et al. α-Synuclein suppression by targeted small interfering RNA in the primate substantia nigra. PLoS One. 2010;5:e12122.
   PubMed Web of Science ®Google Scholar
• Agid Y, Javoy-Agid F, Ruberg M. Biochemistry of neurotransmitter in Parkinson’s disease. In: Marsden CD, Fahn S, editors. Movement Disorders, Vol 2. London: Butterworths; 1987:166–230.
   Google Scholar
• Langston JW, Forno LS, Tetrud J, et al. Evidence of active nerve cell degeneration in the substantia nigra of human years after 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine exposure. Ann Neurol. 1999;46:598–605.
   PubMed Web of Science ®Google Scholar
• Dhillon AS, Tarbutton GL, Levin JL, et al. Pesticide/environmental exposures and Parkinson’s disease in East Texas. J Agromed. 2008;13:37–48.
   PubMedGoogle Scholar
• Greenamyre JT, Cannon JR, Drolet R, Mastroberardino PG. Lessons from the rotenone model of Parkinson’s disease. Trends Pharmacol Sci. 2010;31:141–142.
   PubMed Web of Science ®Google Scholar
• Wu YN, Johnson SW. Dopamine oxidation facilitates rotenone-dependent potentiation of N-methyl-d-aspartate currents in rat substantia nigra dopamine neurons. Neuroscience. 2011;195:138–144.
   Web of Science ®Google Scholar
• Berry C, Vecchia CL, Nicotera P. Paraquat and Parkinson’s disease. Cell Death Differ. 2010;17:1115–1125.
   PubMed Web of Science ®Google Scholar
• Miller GW. Paraquat: the red herring of Parkinson’s disease research. Toxicol Sci. 2007;100:1–2.
   Web of Science ®Google Scholar
• Brooks AI, Chadwick CA, Gelbard HA, et al. Paraquat elicited neurobehavioral syndrome caused by dopaminergic neuron loss. Brain Res. 1999;823:1–10.
   PubMed Web of Science ®Google Scholar
• Prasad K, Tarasewicz E, Mathew J, et al. Toxicokinetics and toxicodynamics of paraquat accumulation in mouse brain. Exp Neurol. 2009;215:358–367.
   PubMed Web of Science ®Google Scholar
• Manning-Bog AB, McCormack AL, Li J, et al. The herbicide paraquat causes up-regulation and aggregation of α-synuclein in mice. Paraquat and α-synuclein. J Biol Chem. 2002;277:1641–1644.
   PubMed Web of Science ®Google Scholar
• Trulson ME, Cannon MS, Faegg TS, Raese JD. Effects of chronic methamphetamine on the nigral-striatal dopamine system in rat brain: tyrosine hydroxylase immunochemistry and quantitative light microscopic studies. Brain Res Bull. 1985;15:569–577.
   Web of Science ®Google Scholar
• Cashaw JL. Tetrahydropapaveroline in brain regions of rats after acute ethanol administration. Alcohol. 1993;10:133–138.
   Web of Science ®Google Scholar
• Nagatsu T. Isoquinoline neurotoxin in the brain and Parkinson’s disease. Neurosci Res. 1997;29:99–111.
   PubMed Web of Science ®Google Scholar
• Storch A, Ott S, Hwang YI, et al. Selective dopaminergic neurotoxicity of isoquinoline derivatives related to Parkinson’s disease: studies using heterologous expression systems of the dopamine transporter. Biochem Pharmacol. 2002;63:909–920.
   PubMed Web of Science ®Google Scholar
• Barbeau A. Manganese and extrapyramidal disorders. Neurotoxicology. 1984;5:13–35.
   PubMed Web of Science ®Google Scholar
• Corti O, Lesage S, Brice A. What genetics tells us about the causes and mechanisms of Parkinson’s disease. Physiol Rev. 2011;91:1161–1218.
   PubMed Web of Science ®Google Scholar
• Polymeropoulos MH, Lavedan C, Leroy E, et al. Mutation in the alpha-synuclein gene identified in families with Parkinson’s disease. Science. 1997;276:2045–2047.
   PubMed Web of Science ®Google Scholar
• Lees AJ, Hardy J, Revesz T. Parkinson’s disease. Lancet. 2009;373:2055–2066.
   PubMed Web of Science ®Google Scholar
• Singleton AB. Altered alpha-synuclein homeostasis causing Parkinson’s disease: the potential roles of dardarin. Trends Neurosci. 2005;28:416–421.
   Web of Science ®Google Scholar
• Fornai F, Schlüter OM, Lenzi P, et al. Parkinson-like syndrome induced by continuous MPTP infusion: convergent roles of the ubiquitin proteasome system and α-synuclein. Proc Nat Acad Sci U S A. 2005;102:3413–3418.
   PubMed Web of Science ®Google Scholar
• Cannon JR, Tapias VM, Na HM, et al. A highly reproducible rotenone model of Parkinson’s disease. Neurobiol Dis. 2009;34:279–290.
   PubMed Web of Science ®Google Scholar
• Abeliovich A, Schmitz Y, Fariñas I, et al. Mice lacking alpha-synuclein display functional deficits in the nigrostriatal dopamine system. Neuron. 2000;25:239–252.
   PubMed Web of Science ®Google Scholar
• Thiruchelvam MJ, Powers JM, Cory-Slechta DA, Richfield RK. Risk factors for dopaminergic neuron loss in human α-synuclein transgenic mice. Eur J Neurosci. 2004;19:845–854.
   Web of Science ®Google Scholar
• Nuber S, Petrasch-Parwez, Winner B, et al. Neurodegeration and motor dysfunction in a conditional model of Parkinson’s disease. J Neurosci. 2008;28:2471–2484.
   Web of Science ®Google Scholar
• Iwatsubo T. Pathological biochemistry of alpha-synucleinopathy. Neuropathology. 2007:27;474–478.
   Web of Science ®Google Scholar
• Foulds PG, Mitchell JD, Parker A, et al. Phosphorylated alpha-synuclein can be detected in blood plasma and is potentially a useful biomarker for Parkinson’s disease. FASEB J. 2011;25:4127–4137.
   PubMed Web of Science ®Google Scholar
• Wang Y, Shi M, Chung KA, et al. Phosphorylated alpha-synuclein in Parkinson’s disease. Sci Transl Med. 2012;4:121ra20.
   PubMed Web of Science ®Google Scholar
• Biskup S, Moore DJ, Celsi F, et al. Localization of LRRK2 to membranous and vesicular structures in mammalian brain. Ann Neurol. 2006;60:557–569.
   PubMed Web of Science ®Google Scholar
• Zimprich A, Biskup S, Leitner P, Lichtner P. Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology. Neuron. 2001;44:601–607.
   Google Scholar
• Greggio E, Jain S, Kingsbury A, et al. Kinase activity is required for the toxic effects of mutant LRRK2/dardarin. Neurobiol Dis. 2006;23:329–341.
   PubMed Web of Science ®Google Scholar
• Albrecht M. LRRK2 mutations and Parkinsonism. Lancet. 2005;365:12–30.
   Google Scholar
• Ross OA, Toft M, Whittle AJ, et al. Lrrk2 and Lewy body disease. Ann Neurol. 2006;59:388–393.
   PubMed Web of Science ®Google Scholar
• Smith WW, Pei Z, Jiang H, et al. Kinase activity of mutant LRRK2 mediates neuronal toxicity. Nat Neurosci. 2006;9:1231–1233.
   PubMed Web of Science ®Google Scholar
• Wang D, Tang B, Zhao G, et al. Dispensable role of Drosophila ortholog of LRRK2 kinase activity in survival of dopaminergic neurons. Mol Neurodegener. 2008;3:3.
   PubMed Web of Science ®Google Scholar
• Ramirez A, Heimbach A, Gründemann J, et al. Hereditary parkinsonism with dementia is caused by mutations in ATP13A2, encoding a lysosomal type 5 P-type ATPase. Nat Genet. 2006;38:1184–1191.
   PubMed Web of Science ®Google Scholar
• Lücking CB, Dürr A, Bonifati V, et al. Association between early-onset Parkinson’s disease and mutations in the Parkin Gene. N Engl J Med. 2000;342:1560–1567.
   PubMed Web of Science ®Google Scholar
• Gasser T. Molecular pathogenesis of Parkinson disease: insights from genetic studies. Expert Rev Mol Med. 2009;11:e22.
   PubMed Web of Science ®Google Scholar
• Heutink P. PINK-1 and DJ-1 - new genes for autosomal recessive Parkinson’s disease. J Neural Transm Suppl. 2006;70:215–219.
   Google Scholar
• Shimura H, Hattori N, Kubo S, et al. Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase. Nat Genet. 2000;25:302–305.
   PubMed Web of Science ®Google Scholar
• Moore DJ, Dawson TM. Value of genetic models in understanding the cause and mechanisms of Parkinson’s disease. Curr Neurol Neurosci. 2008;8:288–296.
   Web of Science ®Google Scholar
• Shin JH, Ko HS, Kang H, et al. PARIS (ZNF746) repression of PGC-1α contributes to neurodegeneration in Parkinson’s disease. Cell. 2011;144:689–702.
   PubMed Web of Science ®Google Scholar
• Silvestri L, Caputo V, Bellacchio E, et al. Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism. Hum Mol Genet. 2005;14:3477–3492.
   PubMed Web of Science ®Google Scholar
• Gandhi S, Wood-Kaczmar A, Yao Z, et al. PINK1-associated Parkinson’s disease is caused by neuronal vulnerability to calcium-induced cell death. Mol Cell. 2009;33:627–638.
   PubMed Web of Science ®Google Scholar
• Gautier CA, Kitada T, Shen J, et al. Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress. Proc Nat Acad Sci U S A. 2008;105:11364–11369.
   PubMed Web of Science ®Google Scholar
• Deng H, Dodson MW, Huang H, Guo M. The Parkinson’s disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila. Proc Nat Acad Sci U S A. 2008;105:14503–14508.
   PubMed Web of Science ®Google Scholar
• Narendra DP, Jin SM, Tanaka A, et al. PINK1 is selectively stabilized on impaired mitochondria to activate parkin. PLoS Biol. 2010;8:e1000298.
   PubMed Web of Science ®Google Scholar
• Zhang L, Shimoji M, Thomas B, et al. Mitochondrial localization of the Parkinson’s disease related protein DJ-1: implications for pathogenesis. Hum Mol Genet. 2005;14:2063–2073.
   PubMed Web of Science ®Google Scholar
• Andres-Mateos E, Perier C, Zhang L, et al. DJ-1 gene deletion reveals that DJ-1 is an atypical peroxiredoxin-like peroxidase. Proc Nat Acad Sci U S A. 2007;104:14807–14812.
   PubMed Web of Science ®Google Scholar
• Bonifati V, Rizzu P, van Baren MJ, et al. Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism. Science. 2003;299:256–259.
   PubMed Web of Science ®Google Scholar
• Dehay B, Ramirez A, Martinez-Vicente M, et al. Loss of P-type ATPase ATP13A2/PARK9 function induces general lysosomal deficiency and leads to Parkinson disease neurodegeneration. Proc Natl Acad Sci U S A. 2012;9:9611–9616.
   Google Scholar
• Usenovic M, Tresse E, Mazzulli JR, et al. Deficiency of ATP13A2 leads to lysosomal dysfunction, α-synuclein accumulation, and neurotoxicity. J Neurosci. 2012;32:4240–4246.
   PubMed Web of Science ®Google Scholar
• Hefti F, Melamed E, Wurtman RJ. Partial lesions of the dopaminergic nigrostriatal system in rat brain: biochemical characterization. Brain Res. 1980;195:123–137.
   PubMed Web of Science ®Google Scholar
• Sheikh N, Ahm A, Siripurapu KB, et al. Effect of Bacopa monniera on stress induced changes in plasma corticosterone and brain monoamines in rats. J Ethnopharmacol. 2007;111:671–676.
   PubMed Web of Science ®Google Scholar
• Newcomer JW, Krystal JH. NMDA receptor regulation of memory and behavior in humans. Hippocampus. 2001;11:529–542.
   PubMed Web of Science ®Google Scholar
• Buter TC, van den Hout A, Matthews FE, et al. Dementia and survival in Parkinson disease: a 12-year population study. Neurology. 2008;70:1017–1022.
   PubMed Web of Science ®Google Scholar
• Visanji NP, O’Neill MJ, Duty S. Nicotine, but neither the alpha4beta2 ligand RJR2403 nor an alpha7 nAChR subtype selective agonist, protects against a partial 6-hydroxydopamine lesion of the rat median forebrain bundle. Neuropharmacology. 2006;51:506–516.
   Web of Science ®Google Scholar
• Szeto HH. Development of mitochondria-targeted aromatic-cationic peptides for neurodegenerative diseases. Ann N Y Acad Sci. 2008; 1147:112–121.
   PubMed Web of Science ®Google Scholar
• Ho YJ, Ho SC, Pawlak CR, Yeh KY. Effects of d-cycloserine on MPTP-induced behavioral and neurological changes: potential for treatment of Parkinson’s disease dementia. Behav Brain Res. 2011;219:280–290.
   PubMed Web of Science ®Google Scholar
• Hussain G, Manyam BV. Mucuna pruriens proves more effective than L-DOPA in Parkinson’s disease animal model. Phytother Res. 1997;11:419–423.
   Web of Science ®Google Scholar
• Choi HS, Park MS, Kim SH, et al. Neuroprotective effects of herbal ethanol extracts from Gynostemma pentaphyllum in the 6-hydroxydopamine-lesioned rat model of Parkinson’s disease. Molecules. 2010;15:2814–2824.
   Web of Science ®Google Scholar
• Zbarsky V, Datla KP, Parkar S, et al. Neuroprotective properties of the natural phenolic antioxidants curcumin and naringenin but not quercetin and fisetin in a 6-OHDA model of Parkinson’s disease. Free Radic Res. 2005;39:1119–1125.
   PubMed Web of Science ®Google Scholar
• Guo SH, Yan JQ, Yang TB, et al. Protective effects of green tea polyphenols in the 6-OHDA rat model of Parkinson’s disease through inhibition of ROS-NO pathway. Biol Psychiatry. 2007;62:1353–1362.
   PubMed Web of Science ®Google Scholar
• Li LY, Zhao XL, Fei XF, et al. Bilobalide inhibits 6-OHDA-induced activation of NF-kB and loss of dopaminergic neurons in rat substantia nigra. Acta Pharmacol Sin. 2008;29:539–547.
   PubMed Web of Science ®Google Scholar
• Wu WR, Zhu XZ. Involvement of monoamine oxidase inhibition in neuroprotective and neurorestorative effects of Ginkgo biloba extract against MPTP-induced nigrostriatal dopaminergic toxicity in C57 mice. Life Sci. 1999;65:157–164.
   PubMed Web of Science ®Google Scholar
• Schmidt N, Ferger B. Neuroprotective effects of (±)-Kavain in the MPTP mouse model of Parkinson’s disease. Synapse. 2001;40:47–54.
   PubMed Web of Science ®Google Scholar
• Chen XC, Chen Y, Zhu YG, et al. Protective effect of ginsenoside Rg1 against MPTP-induced apoptosis in mouse substantia nigra neurons. Acta Pharmacol Sin. 2002;23:829–834.
   PubMed Web of Science ®Google Scholar
• Geng XC, Tian XF, Tu PF, Pu XP. Neuroprotective effects of echinacoside in the mouse MPTP model of Parkinson’s disease. Eur J Pharmacol. 2007;564:66–74.
   PubMed Web of Science ®Google Scholar
• Cleren C, Calingasan NY, Chen J, Beal MF. Celastrol protects against MPTP- and 3-nitropropionic acid-induced neurotoxicity. J Neurochem. 2005;94:995–1004.
   PubMed Web of Science ®Google Scholar
• Liu HQ, Zhang WY, Luo XT, Ye Y, Zhu XZ. Paeoniflorin attenuates neuroinflammation and dopaminergic neurodegeneration in the MPTP model of Parkinson’s disease by activation of adenosine A1 receptor. Br J Pharmacol. 2006;148:314–325.
   Web of Science ®Google Scholar
• Lu KT, Ko MC, Chen BY, et al. Neuroprotective effects of resveratrol on MPTP-induced neuron loss mediated by free radical scavenging. J Agric Food Chem. 2008;56:6910–6913.
   PubMed Web of Science ®Google Scholar
• Blanchet J, Longpré F, Bureau G, et al. Resveratrol, a red wine polyphenol, protects dopaminergic neurons in MPTP-treated mice. Prog Neuropsychopharmacol Biol Psychiatry. 2008;32:1243–1250.
   PubMed Web of Science ®Google Scholar
• Cheng YX, He GR, Mu X, et al. Neuroprotective effect of baicalein against MPTP neurotoxicity: behavioral, biochemical and immunohistochemical profile. Neurosci Lett. 2008;441:16–20.
   PubMed Web of Science ®Google Scholar
• Wang P, Niu L, Gao L, et al. Neuroprotective effect of gypenosides against oxidative injury in the substantia nigra of a mouse model of Parkinson’s disease. J Int Med Res. 2010;38:1084–1092.
   Web of Science ®Google Scholar
• Fujikawa T, Miguchi S, Kanada N, et al. Acanthopanax senticosus Harms as a prophylactic for MPTP-induced Parkinson’s disease in rats. J Ethnopharmacol. 2005;97:375–381.
   PubMed Web of Science ®Google Scholar
• Sankar SR, Manivasagam T, Krishnamurti A, Ramanathan M. The neuroprotective effect of Withania somnifera root extract in MPTP-intoxicated mice: an analysis of behavioral and biochemical variables. Cell Mol Biol Lett. 2007;12:473–481.
   PubMed Web of Science ®Google Scholar
• Moneim AEA. The neuroprotective effects of Purslane (Portulaca oleracea) on rotenone-induced biochemical changes and apoptosis in brain of rat. CNS Neurol Disord Drug Targets. 2013;12:830–841.
   Web of Science ®Google Scholar
• Fujikawa T, Kanada N, Shimada A, et al. Effect of sesamin in Acanthopanax senticosus HARMS on behavioral dysfunction in rotenone-induced parkinsonian rats. Biol Pharm Bull. 2005;28:169–172.
   Web of Science ®Google Scholar
• Shin KS, Zhao TT, Choi HS, et al. Effects of gypenosides on anxiety disorders in MPTP-lesioned mouse model of Parkinson’s disease. Brain Res. 2014;1567:57–65.
   Web of Science ®Google Scholar
• Snow BJ, Macdonald L, Mcauley D, Wallis W. The effect of amantadine on levodopa-induced dyskinesias in Parkinson’s disease: a double-blind, placebo-controlled study. Clin Neuropharmacol. 2000;23:82–85.
   PubMed Web of Science ®Google Scholar
• Sieradzan KA, Fox SH, Hill M, et al. Cannabinoids reduce levodopa-induced dyskinesia in Parkinson’s disease: a pilot study. Neurology. 2001;5:2108–2111.
   Google Scholar
• Meco G, Stirpe P, Edito F, et al. Aripiprazole in L-dopa-induced dyskinesias: a one-year open-label pilot study. J Neural Transm. 2009;116:881–884.
   PubMed Web of Science ®Google Scholar
• van der Stelt M, Fox SH, Hill M, et al. A role for endocannabinoids in the generation of parkinsonism and levodopa-induced dyskinesia in MPTP-lesioned non-human primate models of Parkinson’s disease. FASEB J. 2005;19:1140–1142.
   PubMed Web of Science ®Google Scholar
• Mo J, Zhang H, Yu LP, et al. L-Stepholidine reduced L-DOPA-induced dyskinesia in 6-OHDA-lesioned rat model of Parkinson’s disease. Neurobiol Aging. 2010;31:926–936.
   PubMed Web of Science ®Google Scholar
• Shin KS, Zhao TT, Park KH, et al. Gypenosides attenuate the development of L-DOPA-induced dyskinesia in 6-hydroxydopamine-lesioned rat model of Parkinson’s disease. BMC Neurosci. 2015;16:23.
   Web of Science ®Google Scholar
• Kaur H, Chauhan S, Sandhir R. Protective effect of lycopene on oxidative stress and cognitive decline in rotenone induced model of Parkinson’s disease. Neurochem Res. 2011;36:1435–1443.
   PubMed Web of Science ®Google Scholar