References(104)
1.
Benninger DH, Thees S, Kollias SS, Bassetti CL, Waldvogel D. Morphological differences in Parkinson’s disease with and without rest tremor. J Neurol. 2009;256(2):256–263.
2.
Hughes AJ, Daniel SE, Kilford L, Lees AJ. Accuracy of clinical diagnosis of idiopathic Parkinson’s disease: a clinico-pathological study of 100 cases. J Neurol Neurosurg Psychiatry. 1992;55(3):181–184.
3.
Berardelli A, Rothwell JC, Thompson PD, Hallett M. Pathophysiology of bradykinesia in Parkinson’s disease. Brain. 2001;124(Pt 11):2131–2146.
4.
Santens P, Boon P, Van Roost D, Caemaert J. The pathophysiology of motor symptoms in Parkinson’s disease. Acta Neurol Belg. 2003;103(3):129–134.
5.
Pankratz N, Foroud T. Genetics of Parkinson disease. Genet Med. 2007;9(12):801–811.
6.
Wirdefeldt K, Adami HO, Cole P, Trichopoulos D, Mandel J. Epidemiology and etiology of Parkinson’s disease: a review of the evidence. Eur J Epidemiol. 2011;26 Suppl 1:S1–S58.
7.
Hancock DB, Martin ER, Mayhew GM, et al. Pesticide exposure and risk of Parkinson’s disease: a family-based case-control study. BMC Neurol. 2008;8:6.
8.
Betarbet R, Sherer TB, MacKenzie G, Garcia-Osuna M, Panov AV, Greenamyre JT. Chronic systemic pesticide exposure reproduces features of Parkinson’s disease. Nat Neurosci. 2000;3(12):1301–1306.
9.
Sherer TB, Kim JH, Betarbet R, Greenamyre JT. Subcutaneous rotenone exposure causes highly selective dopaminergic degeneration and alpha-synuclein aggregation. Exp Neurol. 2003;179(1):9–16.
10.
Rascol O, Lozano A, Stern M, Poewe W. Milestones in Parkinson’s disease therapeutics. Mov Disord. 2011;26(6):1072–1082.
11.
Mallory M, Honer W, Hsu L, Johnson R, Rockenstein E, Masliah E. In vitro synaptotrophic effects of Cerebrolysin in NT2N cells. Acta Neuropathol. 1999;97(5):437–446.
12.
Hartbauer M, Hutter-Paier B, Skofitsch G, Windisch M. Antiapoptotic effects of the peptidergic drug cerebrolysin on primary cultures of embryonic chick cortical neurons. J Neural Transm. 2001;108(4):459–473.
13.
Ladurner G, Kalvach P, Moessler H; Cerebrolysin Study Group. Neuroprotective treatment with cerebrolysin in patients with acute stroke: a randomised controlled trial. J Neural Transm. 2005;112(3):415–428.
14.
Ren J, Sietsma D, Qiu S, Moessler H, Finklestein SP. Cerebrolysin enhances functional recovery following focal cerebral infarction in rats. Restor Neurol Neurosci. 2007;25(1):25–31.
15.
Heiss WD, Brainin M, Bornstein NM, Tuomilehto J, Hong Z; Cerebrolysin Acute Stroke Treatment in Asia (CASTA) Investigators. Cerebrolysin in patients with acute ischemic stroke in Asia: results of a double-blind, placebo-controlled randomized trial. Stroke. 2012;43(3):630–636.
16.
Wong GK, Zhu XL, Poon WS. Beneficial effect of cerebrolysin on moderate and severe head injury patients: result of a cohort study. Acta Neurochir Suppl. 2005;95:59–60.
17.
Ruther E, Ritter R, Apecechea M, Freitag S, Windisch M. Efficacy of Cerebrolysin in Alzheimer’s disease. In: Jellinger KA, Ladurner G, Windisch M, editors. New Trends in the Diagnosis and Therapy of Alzheimer’s Disease. Vienna: Springer-Verlag; 1994:131–141.
18.
Alvarez XA, Cacabelos R, Laredo M, et al. A 24-week, double-blind, placebo-controlled study of three dosages of Cerebrolysin in patients with mild to moderate Alzheimer’s disease. Eur J Neurol. 2006;13(1):43–54.
19.
Damulin IV, Koberskaya NN, Mkhitaryan EA. Effects of cerebrolysin on moderate cognitive impairments in cerebral vascular insufficiency (a clinical-electrophysiological study). Neurosci Behav Physiol. 2008;38(6):639–645.
20.
Allegri RF, Guekht A. Cerebrolysin improves symptoms and delays progression in patients with Alzheimer’s disease and vascular dementia. Drugs Today (Barc). 2012;48 Suppl A:25–41.
21.
Bajenaru O, Tiu C, Moessler H, et al. Efficacy and safety of Cerebrolysin in patients with hemorrhagic stroke. J Med Life. 2010;3(2):137–143.
22.
Thome J, Doppler E. Safety profile of Cerebrolysin: clinical experience from dementia and stroke trials. Drugs Today (Barc). 2012;48 Suppl A:63–69.
23.
Rockenstein E, Adame A, Mante M, Moessler H, Windisch M, Masliah E. The neuroprotective effects of Cerebrolysin in a transgenic model of Alzheimer’s disease are associated with improved behavioral performance. J Neural Transm. 2003;110(11):1313–1327.
24.
Safarova ER, Shram SI, Grivennikov IA, Myasoedov NF. Trophic effects of nootropic peptide preparations cerebrolysin and semax on cultured rat pheochromocytoma. Bull Exp Biol Med. 2002;133(4):401–403.
25.
Sharma HS, Zimmermann-Meinzingen S, Sharma A, Johanson CE. Cerebrolysin attenuates blood–brain barrier and brain pathology following whole body hyperthermia in the rat. Acta Neurochir Suppl. 2010;106:321–325.
26.
Sharma HS, Zimmermann-Meinzingen S, Johanson CE. Cerebrolysin reduces blood-cerebrospinal fluid barrier permeability change, brain pathology, and functional deficits following traumatic brain injury in the rat. Ann N Y Acad Sci. 2010;1199:125–137.
27.
Zhang C, Chopp M, Cui Y, et al. Cerebrolysin enhances neurogenesis in the ischemic brain and improves functional outcome after stroke. J Neurosci Res. 2010;88(15):3275–3281.
28.
Menon PK, Muresanu DF, Sharma A, Mössler H, Sharma HS. Cerebrolysin, a mixture of neurotrophic factors induces marked neuroprotection in spinal cord injury following intoxication of engineered nanoparticles from metals. CNS Neurol Disord Drug Targets. 2012;11(1):40–49.
29.
Formichi P, Radi E, Battisti C, Di Maio G, Muresanu D, Federico A. Cerebrolysin administration reduces oxidative stress-induced apoptosis in lymphocytes from healthy individuals. J Cell Mol Med. 2012;16(11):2840–2843.
30.
Miller RL, James-Kracke M, Sun GY, Sun AY. Oxidative and inflammatory pathways in Parkinson’s disease. Neurochem Res. 2009;34(1):55–65.
31.
Paget GE, Barnes JM. Toxicity testing. In: Laurence DR, Bacharach AL, editors. Evaluation of Drug Activities Pharmacometics. London: Academic Press; 1964:134–166.
32.
Ruiz-Larrea MB, Leal AM, Liza M, Lacort M, de Groot H. Antioxidant effects of estradiol and 2-hydroxyestradiol on iron-induced lipid peroxidation of rat liver microsomes. Steroids. 1994;59(6):383–388.
33.
Ellman GL. Tissue sulfhydryl groups. Arch Biochem Biophys. 1959;82(1):70–77.
34.
Moshage H, Kok B, Huizenga JR, Jansen PL. Nitrite and nitrate determination in plasma: a critical evaluation. Clin Chem. 1995; 41(6 Pt 1):892–896.
35.
Higashino K, Takahashi Y, Yamamura Y. Release of phenyl acetate esterase from liver microsomes by carbon tetrachloride. Clin Chim Acta. 1972;41:313–320.
36.
Watson AD, Berliner JA, Hama SY, et al. Protective effect of high density lipoprotein associated paraoxonase. Inhibition of the biological activity of minimally oxidized low density lipoprotein. J Clin Invest. 1995;96(6):2882–2891.
37.
Ellman GL, Courtney KD, Andres V Jr, Feather-Stone RM. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem Pharmacol. 1961;7:88–95.
38.
Gorun V, Proinov I, Baltescu V, Balaban G, Barzu O. Modified Ellman procedure for assay of cholinesterases in crude enzymatic preparations. Anal Biochem. 1978;86(1):324–326.
39.
Feng Y, Liang ZH, Wang T, Qiao X, Liu HJ, Sun SG. alpha-Synuclein redistributed and aggregated in rotenone-induced Parkinson’s disease rats. Neurosci Bull. 2006;22(5):288–293.
40.
Sherer TB, Betarbet R, Testa CM, et al. Mechanism of toxicity in rotenone models of Parkinson’s disease. J Neurosci. 2003;23(34):10756–10764.
41.
Testa CM, Sherer TB, Greenamyre JT. Rotenone induces oxidative stress and dopaminergic neuron damage in organotypic substantia nigra cultures. Brain Res Mol Brain Res. 2005;134(1):109–118.
42.
Meister A. Glutathione metabolism and its selective modification. J Biol Chem. 1988;263(33):17205–17208.
43.
Cotgreave IA, Gerdes RG. Recent trends in glutathione biochemistry – glutathione-protein interactions: a molecular link between oxidative stress and cell proliferation? Biochem Biophys Res Commun. 1998;242(1):1–9.
44.
Dringen R. Metabolism and functions of glutathione in brain. Prog Neurobiol. 2000;62(6):649–671.
45.
Bains JS, Shaw CA. Neurodegenerative disorders in humans: the role of glutathione in oxidative stress-mediated neuronal death. Brain Res Brain Res Rev. 1997;25(3):335–358.
46.
Kaur D, Lee D, Ragapolan S, Andersen JK. Glutathione depletion in immortalized midbrain-derived dopaminergic neurons results in increases in the labile iron pool: implications for Parkinson’s disease. Free Radic Biol Med. 2009;46(5):593–598.
47.
Jha N, Jurma O, Lalli G, et al. Glutathione depletion in PC12 results in selective inhibition of mitochondrial complex I activity. Implications for Parkinson’s disease. J Biol Chem. 2000;275(34):26096–26101.
48.
Schulz JB, Lindenau J, Seyfried J, Dichgans J. Glutathione, oxidative stress and neurodegeneration. Eur J Biochem. 2000;267(16):4904–4911.
49.
Dean OM, van den Buuse M, Bush AI, et al. A role for glutathione in the pathophysiology of bipolar disorder and schizophrenia? Animal models and relevance to clinical practice. Curr Med Chem. 2009;16(23):2965–2976.
50.
Gawryluk JW, Wang JF, Andreazza AC, Shao L, Young LT. Decreased levels of glutathione, the major brain antioxidant, in post-mortem prefrontal cortex from patients with psychiatric disorders. Int J Neuropsychopharmacol. 2011;14(1):123–130.
51.
Sofic E, Lange KW, Jellinger K, Riederer P. Reduced and oxidized glutathione in the substantia nigra of patients with Parkinson’s disease. Neurosci Lett. 1992;142(2):128–130.
52.
Sian J, Dexter DT, Lees AJ, et al. Alterations in glutathione levels in Parkinson’s disease and other neurodegenerative disorders affecting basal ganglia. Ann Neurol. 1994;36(3):348–355.
53.
Fitzmaurice PS, Ang L, Guttman M, Rajput AH, Furukawa Y, Kish SJ. Nigral glutathione deficiency is not specific for idiopathic Parkinson’s disease. Mov Disord. 2003;18(9):969–976.
54.
Sechi G, Deledda MG, Bua G, et al. Reduced intravenous glutathione in the treatment of early Parkinson’s disease. Prog Neuropsychopharmacol Biol Psychiatry. 1996;20(7):1159–1170.
55.
Wei T, Chen C, Hou J, Xin W, Mori A. Nitric oxide induces oxidative stress and apoptosis in neuronal cells. Biochim Biophys Acta. 2000; 1498(1):72–79.
56.
Bal-Price A, Brown GC. Inflammatory neurodegeneration mediated by nitric oxide from activated glia-inhibiting neuronal respiration, causing glutamate release and excitotoxicity. J Neurosci. 2001;21(17):6480–6491.
57.
Förstermann U, Sessa WC. Nitric oxide synthases: regulation and function. Eur Heart J. 2012;33(7):829–837, 837a–837d.
58.
Kovac A, Erickson MA, Banks WA. Brain microvascular pericytes are immunoactive in culture: cytokine, chemokine, nitric oxide, and LRP-1 expression in response to lipopolysaccharide. J Neuroinflammation. 2011;8:139.
59.
Abdel-Salam OME, Omara EA, El-Shamarka MES, Hussein JS. Nigrostriatal damage after systemic rotenone and/or lipopolysaccharide and the effect of cannabis. Comparative Clinical Pathology. 2013;1–16.
60.
Bashkatova V, Alam M, Vanin A, Schmidt WJ. Chronic administration of rotenone increases levels of nitric oxide and lipid peroxidation products in rat brain. Exp Neurol. 2004;186(2):235–241.
61.
Schmidt WJ, Alam M. Controversies on new animal models of Parkinson’s disease pro and con: the rotenone model of Parkinson’s disease (PD). J Neural Transm Suppl. 2006;(70):273–276.
62.
Moncada S, Palmer RM, Higgs EA. Nitric oxide: physiology, pathophysiology, and pharmacology. Pharmacol Rev. 1991;43(2):109–142.
63.
Wink DA, Mitchell JB. Chemical biology of nitric oxide: Insights into regulatory, cytotoxic, and cytoprotective mechanisms of nitric oxide. Free Radic Biol Med. 1998;25(4–5):434–456.
64.
Korhonen R, Lahti A, Kankaanranta H, Moilanen E. Nitric oxide production and signaling in inflammation. Curr Drug Targets Inflamm Allergy. 2005;4(4):471–479.
65.
Mander P, Borutaite V, Moncada S, Brown GC. Nitric oxide from inflammatory-activated glia synergizes with hypoxia to induce neuronal death. J Neurosci Res. 2005;79(1–2):208–215.
66.
He Y, Imam SZ, Dong Z, et al. Role of nitric oxide in rotenone-induced nigro-striatal injury. J Neurochem. 2003;86(6):1338–1345.
67.
Abdel-Salam OME, Khadrawy YA, Youness ER, et al. Effect of a single intrastriatal rotenone injection on oxidative stress and neurodegeneration in the rat brain. Comparative Clinical Pathology. 2013;1–11.
68.
La Du BN. Human serum paraoxonase: arylesterase. In: Kalow W, editor. Pharmacogenetics of Drug Metabolism. New York: Pergamon Press; 1992:51–91.
69.
Draganov DI, La Du BN. Pharmacogenetics of paraoxonases: a brief review. Naunyn Schmiedebergs Arch Pharmacol. 2004;369(1):78–88.
70.
Furlong CE. Paraoxonases: An Historical Perspective. In: Mackness B, Mackness M, Aviram M, Paragh G, editors. The Paraoxonases: Their Role in Disease Development and Xenobiotic Metabolism. Dordrecht: Springer; 2008:3–31.
71.
Kondo I, Yamamoto M. Genetic polymorphism of paraoxonase 1 (PON1) and susceptibility to Parkinson’s disease. Brain Res. 1998;806(2):271–273.
72.
Carmine A, Buervenich S, Sydow O, Anvret M, Olson L. Further evidence for an association of the paraoxonase 1 (PON1) Met-54 allele with Parkinson’s disease. Mov Disord. 2002;17(4):764–766.
73.
Belin AC, Ran C, Anvret A, et al. Association of a protective paraoxonase 1 (PON1) polymorphism in Parkinson’s disease. Neurosci Lett. 2012;522(1):30–35.
74.
Lee PC, Rhodes SL, Sinsheimer JS, Bronstein J, Ritz B. Functional paraoxonase 1 variants modify the risk of Parkinson’s disease due to organophosphate exposure. Environ Int. 2013;56:42–47.
75.
Wehr H, Bednarska–Makaruk M, Graban A, et al. Paraoxonase activity and dementia. J Neurol Sci. 2009;283(1–2):107–108.
76.
Zengi O, Karakas A, Ergun U, Senes M, Inan L, Yucel D. Urinary 8-hydroxy-2′-deoxyguanosine level and plasma paraoxonase 1 activity with Alzheimer’s disease. Clin Chem Lab Med. 2011;50(3):529–534.
77.
Jamroz-Wisniewska A, Beltowski J, Stelmasiak Z, Bartosik-Psujek H. Paraoxonase 1 activity in different types of multiple sclerosis. Mult Scler. 2009;15(3):399–402.
78.
Nguyen SD, Hung ND, Cheon-Ho P, Ree KM, Dai-Eun S. Oxidative inactivation of lactonase activity of purified human paraoxonase 1 (PON1). Biochim Biophys Acta. 2009;1790(3):155–160.
79.
Thornberry NA, Lazebnik Y. Caspases: enemies within. Science. 1998;281(5381):1312–1316.
80.
Budihardjo I, Oliver H, Lutter M, Luo X, Wang X. Biochemical pathways of caspase activation during apoptosis. Annu Rev Cell Dev Biol. 1999;15:269–290.
81.
Yuan J, Yankner BA. Apoptosis in the nervous system. Nature. 2000;407(6805):802–809.
82.
Wang X, Qin ZH, Leng Y, et al. Prostaglandin A1 inhibits rotenone-induced apoptosis in SH-SY5Y cells. J Neurochem. 2002;83(5):1094–1102.
83.
Ahmadi FA, Linseman DA, Grammatopoulos TN, et al. The pesticide rotenone induces caspase-3-mediated apoptosis in ventral mesencephalic dopaminergic neurons. J Neurochem. 2003;87(4):914–921.
84.
Hartmann A, Hunot S, Michel PP, et al. Caspase-3: A vulnerability factor and final effector in apoptotic death of dopaminergic neurons in Parkinson’s disease. Proc Natl Acad Sci U S A. 2000;97(6):2875–2880.
85.
Tatton NA. Increased caspase 3 and Bax immunoreactivity accompany nuclear GAPDH translocation and neuronal apoptosis in Parkinson’s disease. Exp Neurol. 2000;166(1):29–43.
86.
Shimizu S, Narita M, Tsujimoto Y. Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature. 1999;399(6735):483–487.
87.
Zhai D, Jin C, Huang Z, Satterthwait AC, Reed JC. Differential regulation of Bax and Bak by anti-apoptotic Bcl-2 family proteins Bcl-B and Mcl-1. J Biol Chem. 2008;283(15):9580–9586.
88.
Susnow N, Zeng L, Margineantu D, Hockenbery DM. Bcl-2 family proteins as regulators of oxidative stress. Semin Cancer Biol. 2009;19(1):42–49.
89.
Hochman A, Sternin H, Gorodin S, et al. Enhanced oxidative stress and altered antioxidants in brains of Bcl-2-deficient mice. J Neurochem. 1998;71(2):741–748.
90.
Amstad PA, Liu H, Ichimiya M, et al. BCL-2 is involved in preventing oxidant-induced cell death and in decreasing oxygen radical production. Redox Rep. 2001;6(6):351–362.
91.
Longoni B, Boschi E, Demontis GC, Marchiafava PL, Mosca F. Regulation of Bcl-2 protein expression during oxidative stress in neuronal and in endothelial cells. Biochem Biophys Res Commun. 1999;260(2):522–526.
92.
Mennicken F, Maki R, de Souza EB, Quirion R. Chemokines and chemokine receptors in the CNS: a possible role in neuroinflammation and patterning. Trends Pharmacol Sci. 1999;20(2):73–78.
93.
Sozzani S, Locati M, Zhou D, et al. Receptors, signal transduction, and spectrum of action of monocyte chemotactic protein-1 and related chemokines. J Leukoc Biol. 1995;57(5):788–794.
94.
Orlikowski D, Chazaud B, Plonquet A, et al. Monocyte chemoattractant protein 1 and chemokine receptor CCR2 productions in Guillain-Barré syndrome and experimental autoimmune neuritis. J Neuroimmunol. 2003;134(1–2):118–127.
95.
Thompson WL, Karpus WJ, Van Eldik LJ. MCP-1-deficient mice show reduced neuroinflammatory responses and increased peripheral inflammatory responses to peripheral endotoxin insult. J Neuroinflammation. 2008;5:35.
96.
Yang G, Meng Y, Li W, et al. Neuronal MCP-1 mediates microglia recruitment and neurodegeneration induced by the mild impairment of oxidative metabolism. Brain Pathol. 2011;21(3):279–297.
97.
Everitt BJ, Robbins TW. Central cholinergic systems and cognition. Annu Rev Psychol. 1997;48:649–684.
98.
Aosaki T, Miura M, Suzuki T, Nishimura K, Masuda M. Acetylcholine-dopamine balance hypothesis in the striatum: an update. Geriatr Gerontol Int. 2010;10 Suppl 1:S148–S157.
99.
Fox SH. Non-dopaminergic treatments for motor control in Parkinson’s disease. Drugs. 2013;73(13):1405–1415.
100.
Ullrich C, Humpel C. Rotenone induces cell death of cholinergic neurons in an organotypic co-culture brain slice model. Neurochem Res. 2009;34(12):2147–2153.
101.
McCoy MK, Tansey MG. TNF signaling inhibition in the CNS: implications for normal brain function and neurodegenerative disease. J Neuroinflammation. 2008;5:45.
102.
Mogi M, Togari A, Tanaka K, Ogawa N, Ichinose H, Nagatsu T. Increase in level of tumor necrosis factor (TNF)-alpha in 6-hydroxydopamine-lesioned striatum in rats without influence of systemic L-DOPA on the TNF-alpha induction. Neurosci Lett. 1999;268(2):101–104.
103.
Sriram K, Matheson JM, Benkovic SA, Miller DB, Luster MI, O’Callaghan JP. Mice deficient in TNF receptors are protected against dopaminergic neurotoxicity: implications for Parkinson’s disease. FASEB J. 2002;16(11):1474–1476.
104.
De Lella Ezcurra AL, Chertoff M, Ferrari C, Graciarena M, Pitossi F. Chronic expression of low levels of tumor necrosis factor-alpha in the substantia nigra elicits progressive neurodegeneration, delayed motor symptoms and microglia/macrophage activation. Neurobiol Dis. 2010;37(3):630–640.