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Treating Oxidative Neural Injury: Methionine Sulfoxide Reductase Therapy for Parkinson’s Disease

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Oxidative Neural Injury

Part of the book series: Contemporary Clinical Neuroscience ((CCNE))

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Abstract

Parkinson’s disease is a common neurodegenerative disease that is characterized by loss of dopaminergic neurons in the substantia nigra and impaired motor function. The disease is multifactorial but oxidative injury is associated with the pathology and contributes to neuronal injury. Fibrillations of α-synuclein are present in pathological lesions in this disease. Oxidation of the sulfur moieties of methionine residues on α-synuclein can contribute to α-synuclein fibrillation. An anti-oxidant enzyme methionine sulfoxide reductase can reverse the methionine oxidation on α-synuclein and act as a sink scavenging reactive oxygen species. Thus, boosting methionine sulfoxide reductase activity may prevent oxidative injury in dopaminergic neurons that contributes to neurodegeneration and impaired neuronal function in Parkinson’s disease. One promising approach to augmenting methionine sulfoxide reductase activity in neurons is to provide a naturally occurring substrate for methionine sulfoxide reductase A, S-methyl-l-cysteine. Recent work in our lab with this compound supports the promise of this substance in preventing or delaying motor dysfunction in multiple model systems of Parkinson’s disease.

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References

  1. Huse DM, Schulman K, Orsini L, Castelli-Haley J, Kennedy S, Lenhart G. Burden of illness in Parkinson's disease. Mov Disord. 2005 Nov;20(11):1449–1454.

    Google Scholar 

  2. de Lau LM, Breteler MM. Epidemiology of Parkinson's disease. Lancet Neurol. 2006 Jun;5(6):525–535.

    Google Scholar 

  3. Gorell JM, Johnson CC, Rybicki BA, Peterson EL, Richardson RJ. The risk of Parkinson's disease with exposure to pesticides, farming, well water, and rural living. Neurology. 1998 May;50(5):1346–1350.

    Google Scholar 

  4. Alexander GE, Crutcher MD. Functional architecture of basal ganglia circuits: neural substrates of parallel processing. Trends Neurosci. 1990 Jul;13(7):266–271.

    Google Scholar 

  5. Hawkes CH, Del Tredici K, Braak H. Parkinson's disease: a dual-hit hypothesis. Neuropathol Appl Neurobiol. 2007 Dec;33(6):599–614.

    Google Scholar 

  6. Spillantini MG, Schmidt ML, Lee VM, Trojanowski JQ, Jakes R, Goedert M. α-Synuclein in Lewy bodies. Nature. 1997 Aug 28;388(6645):839–840.

    Google Scholar 

  7. Cooper AA, Gitler AD, Cashikar A, Haynes CM, Hill KJ, Bhullar B, Liu K, Xu K, Strathearn KE, Liu F, Cao S, Caldwell KA, Caldwell GA, Marsischky G, Kolodner RD, Labaer J, Rochet JC, Bonini NM, Lindquist S. α-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models. Science. 2006 Jul 21;313(5785):324–328.

    Google Scholar 

  8. Giasson BI, Murray IV, Trojanowski JQ, Lee VM. A hydrophobic stretch of 12 amino acid residues in the middle of α-synuclein is essential for filament assembly. J Biol Chem. 2001 Jan 26;276(4):2380–2386.

    Google Scholar 

  9. Polymeropoulos MH, Lavedan C, Leroy E, Ide SE, Dehejia A, Dutra A, Pike B, Root H, Rubenstein J, Boyer R, Stenroos ES, Chandrasekharappa S, Athanassiadou A, Papapetropoulos T, Johnson WG, Lazzarini AM, Duvoisin RC, Di Iorio G, Golbe LI, Nussbaum RL. Mutation in the α-synuclein gene identified in families with Parkinson's disease. Science. 1997 Jun 27;276(5321):2045–2047.

    Google Scholar 

  10. Singleton AB, Farrer M, Johnson J, Singleton A, Hague S, Kachergus J, Hulihan M, Peuralinna T, Dutra A, Nussbaum R, Lincoln S, Crawley A, Hanson M, Maraganore D, Adler C, Cookson MR, Muenter M, Baptista M, Miller D, Blancato J, Hardy J, Gwinn-Hardy K. α-Synuclein locus triplication causes Parkinson's disease. Science. 2003 Oct 31;302(5646):841.

    Google Scholar 

  11. Chartier-Harlin MC, Kachergus J, Roumier C, Mouroux V, Douay X, Lincoln S, Levecque C, Larvor L, Andrieux J, Hulihan M, Waucquier N, Defebvre L, Amouyel P, Farrer M, Destee A. α-Synuclein locus duplication as a cause of familial Parkinson's disease. Lancet. 2004 Sep 25–Oct 1;364(9440):1167–1169.

    Google Scholar 

  12. Grundemann J, Schlaudraff F, Haeckel O, Liss B. Elevated α-synuclein mRNA levels in individual UV-laser-microdissected dopaminergic substantia nigra neurons in idiopathic Parkinson's disease. Nucleic Acids Res. 2008;36(7):e38.

    Google Scholar 

  13. Braak E, Braak H. Silver staining method for demonstrating Lewy bodies in Parkinson's disease and argyrophilic oligodendrocytes in multiple system atrophy. J Neurosci Methods. 1999 Feb 1;87(1):111–115.

    Google Scholar 

  14. Paleologou KE, Irvine GB, El-Agnaf OM. α-synuclein aggregation in neurodegenerative diseases and its inhibition as a potential therapeutic strategy. Biochem Soc Trans. 2005 Nov;33(Pt 5):1106–1110.

    Google Scholar 

  15. Wood SJ, Wypych J, Steavenson S, Louis JC, Citron M, Biere AL. α-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease. J Biol Chem. 1999 Jul 9;274(28):19509–19512.

    Google Scholar 

  16. Kahle PJ, Neumann M, Ozmen L, Muller V, Jacobsen H, Schindzielorz A, Okochi M, Leimer U, van Der Putten H, Probst A, Kremmer E, Kretzschmar HA, Haass C. Subcellular localization of wild-type and Parkinson's disease-associated mutant α-synuclein in human and transgenic mouse brain. J Neurosci. 2000 Sep 1;20(17):6365–6373.

    Google Scholar 

  17. Masliah E, Rockenstein E, Veinbergs I, Mallory M, Hashimoto M, Takeda A, Sagara Y, Sisk A, Mucke L. Dopaminergic loss and inclusion body formation in α-synuclein mice: implications for neurodegenerative disorders. Science. 2000 Feb 18;287(5456):1265–1269.

    Google Scholar 

  18. van der Putten H, Wiederhold KH, Probst A, Barbieri S, Mistl C, Danner S, Kauffmann S, Hofele K, Spooren WP, Ruegg MA, Lin S, Caroni P, Sommer B, Tolnay M, Bilbe G. Neuropathology in mice expressing human α-synuclein. J Neurosci. 2000 Aug 15;20(16):6021–6029.

    Google Scholar 

  19. Wakamatsu M, Ishii A, Iwata S, Sakagami J, Ukai Y, Ono M, Kanbe D, Muramatsu S, Kobayashi K, Iwatsubo T, Yoshimoto M. Selective loss of nigral dopamine neurons induced by overexpression of truncated human α-synuclein in mice. Neurobiol Aging. 2008 Apr;29(4):574–585.

    Google Scholar 

  20. Lo Bianco C, Ridet JL, Schneider BL, Deglon N, Aebischer P. α-synucleinopathy and selective dopaminergic neuron loss in a rat lentiviral-based model of Parkinson's disease. Proc Natl Acad Sci U S A. 2002 Aug 6;99(16):10813–10818.

    Google Scholar 

  21. Nuber S, Petrasch-Parwez E, Winner B, Winkler J, von Horsten S, Schmidt T, Boy J, Kuhn M, Nguyen HP, Teismann P, Schulz JB, Neumann M, Pichler BJ, Reischl G, Holzmann C, Schmitt I, Bornemann A, Kuhn W, Zimmermann F, Servadio A, Riess O. Neurodegeneration and motor dysfunction in a conditional model of Parkinson's disease. J Neurosci. 2008 Mar 5;28(10):2471–2484.

    Google Scholar 

  22. Hashimoto M, Hsu LJ, Xia Y, Takeda A, Sisk A, Sundsmo M, Masliah E. Oxidative stress induces amyloid-like aggregate formation of NACP/α-synuclein in vitro. Neuroreport. 1999 Mar 17;10(4):717–721.

    Google Scholar 

  23. Uversky VN, Li J, Fink AL. Pesticides directly accelerate the rate of α-synuclein fibril formation: a possible factor in Parkinson's disease. FEBS Lett. 2001 Jul 6;500(3):105–108.

    Google Scholar 

  24. Glaser CB, Yamin G, Uversky VN, Fink AL. Methionine oxidation, α-synuclein and Parkinson's disease. Biochim Biophys Acta. 2005 Jan 17;1703(2):157–169.

    Google Scholar 

  25. Uversky VN, Yamin G, Souillac PO, Goers J, Glaser CB, Fink AL. Methionine oxidation inhibits fibrillation of human α-synuclein in vitro. FEBS Lett. 2002 Apr 24;517(1–3):239–244.

    Google Scholar 

  26. Norris EH, Giasson BI, Hodara R, Xu S, Trojanowski JQ, Ischiropoulos H, Lee VM. Reversible inhibition of α-synuclein fibrillization by dopaminochrome-mediated conformational alterations. J Biol Chem. 2005 Jun 3;280(22):21212–21219.

    Google Scholar 

  27. Yamin G, Glaser CB, Uversky VN, Fink AL. Certain metals trigger fibrillation of methionine-oxidized alpha-synuclein. J Biol Chem. 2003 Jul 25;278(30):27630–27635.

    Google Scholar 

  28. Vogt W. Oxidation of methionyl residues in proteins: tools, targets, and reversal. Free Radic Biol Med. 1995 Jan;18(1):93–105.

    Google Scholar 

  29. Weissbach H, Resnick L, Brot N. Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage. Biochim Biophys Acta. 2005 Jan 17;1703(2):203–212.

    Google Scholar 

  30. Rahman MA, Nelson H, Weissbach H, Brot N. Cloning, sequencing, and expression of the Escherichia coli peptide methionine sulfoxide reductase gene. J Biol Chem. 1992 Aug 5;267(22):15549–15551.

    Google Scholar 

  31. St John G, Brot N, Ruan J, Erdjument-Bromage H, Tempst P, Weissbach H, Nathan C. Peptide methionine sulfoxide reductase from Escherichia coli and Mycobacterium tuberculosis protects bacteria against oxidative damage from reactive nitrogen intermediates. Proc Natl Acad Sci U S A. 2001 Aug 14;98(17):9901–9906.

    Google Scholar 

  32. Marchetti MA, Lee W, Cowell TL, Wells TM, Weissbach H, Kantorow M. Silencing of the methionine sulfoxide reductase A gene results in loss of mitochondrial membrane potential and increased ROS production in human lens cells. Exp Eye Res. 2006 Nov;83(5):1281–1286.

    Google Scholar 

  33. Moskovitz J, Bar-Noy S, Williams WM, Requena J, Berlett BS, Stadtman ER. Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals. Proc Natl Acad Sci U S A. 2001 Nov 6;98(23):12920–12925.

    Google Scholar 

  34. Picot CR, Petropoulos I, Perichon M, Moreau M, Nizard C, Friguet B. Overexpression of MsrA protects WI-38 SV40 human fibroblasts against H2O2-mediated oxidative stress. Free Radic Biol Med. 2005 Nov 15;39(10):1332–1341.

    Google Scholar 

  35. Yermolaieva O, Xu R, Schinstock C, Brot N, Weissbach H, Heinemann SH, Hoshi T. Methionine sulfoxide reductase A protects neuronal cells against brief hypoxia/reoxygenation. Proc Natl Acad Sci U S A. 2004 Feb 3;101(5):1159–1164.

    Google Scholar 

  36. Moskovitz J, Flescher E, Berlett BS, Azare J, Poston JM, Stadtman ER. Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress. Proc Natl Acad Sci U S A. 1998 Nov 24;95(24):14071–14075.

    Google Scholar 

  37. Prentice HM, Moench IA, Rickaway ZT, Dougherty CJ, Webster KA, Weissbach H. MsrA protects cardiac myocytes against hypoxia/reoxygenation induced cell death. Biochem Biophys Res Commun. 2008 Feb 15;366(3):775–778.

    Google Scholar 

  38. Brand AH, Manoukian AS, Perrimon N. Ectopic expression in Drosophila. Methods Cell Biol. 1994;44:635–654.

    Article  PubMed  CAS  Google Scholar 

  39. Ruan H, Tang XD, Chen ML, Joiner ML, Sun G, Brot N, Weissbach H, Heinemann SH, Iverson L, Wu CF, Hoshi T. High-quality life extension by the enzyme peptide methionine sulfoxide reductase. Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2748–2753.

    Google Scholar 

  40. Raj HG, Sharma RK, Garg BS, Parmar VS, Jain SC, Goel S, Tyagi YK, Singh A, Olsen CE, Wengel J. Mechanism of biochemical action of substituted 4-methylbenzopyran-2-ones. Part 3: A novel mechanism for the inhibition of biological membrane lipid peroxidation by dioxygenated 4-methylcoumarins mediated by the formation of a stable ADP-Fe-inhibitor mixed ligand complex. Bioorg Med Chem. 1998 Nov;6(11):2205–2212.

    Google Scholar 

  41. Ossowska K, Wardas J, Smialowska M, Kuter K, Lenda T, Wieronska JM, Zieba B, Nowak P, Dabrowska J, Bortel A, Kwiecinski A, Wolfarth S. A slowly developing dysfunction of dopaminergic nigrostriatal neurons induced by long-term paraquat administration in rats: an animal model of preclinical stages of Parkinson's disease? Eur J Neurosci. 2005 Sep;22(6):1294–1304.

    Google Scholar 

  42. Hoshi T, Heinemann S. Regulation of cell function by methionine oxidation and reduction. J Physiol. 2001 Feb 15;531(Pt 1):1–11.

    Google Scholar 

  43. Levine RL, Mosoni L, Berlett BS, Stadtman ER. Methionine residues as endogenous antioxidants in proteins. Proc Natl Acad Sci U S A. 1996 Dec 24;93(26):15036–15040.

    Google Scholar 

  44. Yao Y, Yin D, Jas GS, Kuczer K, Williams TD, Schoneich C, Squier TC. Oxidative modification of a carboxyl-terminal vicinal methionine in calmodulin by hydrogen peroxide inhibits calmodulin-dependent activation of the plasma membrane Ca-ATPase. Biochemistry. 1996 Feb 27;35(8):2767–2787.

    Google Scholar 

  45. Hansel A, Kuschel L, Hehl S, Lemke C, Agricola H-J, Hoshi T, Heinemann SH. Mitochondrial targeting of the human peptide methionine sulfoxide reductase (MSRA), an enzyme involved in the repair of oxidized proteins. FASEB J. 2002;16:911–913.

    PubMed  CAS  Google Scholar 

  46. Haenold R, Wassef R, Hansel A, Heinemann SH, Hoshi T. Identification of a new functional splice variant of the enzyme methionine sulphoxide reductase A (MSRA) expressed in rat vascular smooth muscle cells. Free Radic Res. 2007 Sep 28:1–13.

    Google Scholar 

  47. Chiueh CC, Andoh T, Lai AR, Lai E, Krishna G. Neuroprotective strategies in Parkinson's disease: protection against progressive nigral damage induced by free radicals. Neurotox Res. 2000;2(2–3):293–310.

    Article  PubMed  CAS  Google Scholar 

  48. Gabbita SP, Aksenov MY, Lovell MA, Markesbery WR. Decrease in peptide methionine sulfoxide reductase in Alzheimer's disease brain. J Neurochem. 1999;73(4):1660–1666.

    Article  PubMed  CAS  Google Scholar 

  49. Muqit MM, Feany MB. Modelling neurodegenerative diseases in Drosophila: a fruitful approach? Nat Rev Neurosci. 2002 Mar;3(3):237–243.

    Google Scholar 

  50. Whitworth AJ, Wes PD, Pallanck LJ. Drosophila models pioneer a new approach to drug discovery for Parkinson's disease. Drug Discov Today. 2006 Feb;11(3–4):119–126.

    Google Scholar 

  51. Coulom H, Birman S. Chronic exposure to rotenone models sporadic Parkinson's disease in Drosophila melanogaster. J Neurosci. 2004 Dec 1;24(48):10993–10998.

    Google Scholar 

  52. Feany MB, Bender WW. A Drosophila model of Parkinson's disease. Nature. 2000 Mar 23;404(6776):394–398.

    Google Scholar 

  53. Polymeropoulos MH. Autosomal dominant Parkinson's disease and α-synuclein. Ann Neurol. 1998 Sep;44(3 Suppl 1):S63–64.

    Google Scholar 

  54. Kruger R, Kuhn W, Muller T, Woitalla D, Graeber M, Kosel S, Przuntek H, Epplen JT, Schols L, Riess O. Ala30Pro mutation in the gene encoding α-synuclein in Parkinson's disease. Nat Genet. 1998 Feb;18(2):106–108.

    Google Scholar 

  55. Le Bourg E, Lints FA. Hypergravity and aging in Drosophila melanogaster. 4. Climbing activity. Gerontology. 1992;38(1–2):59–64.

    Article  PubMed  Google Scholar 

  56. Braak H, Del Tredici K, Rub U, de Vos RA, Jansen Steur EN, Braak E. Staging of brain pathology related to sporadic Parkinson's disease. Neurobiol Aging. 2003 Mar–Apr;24(2):197–211.

    Google Scholar 

  57. Wassef R, Haenold R, Hansel A, Brot N, Heinemann SH, Hoshi T. Methionine sulfoxide reductase A and a dietary supplement S-methyl-L-cysteine prevent Parkinson's-like symptoms. J Neurosci. 2007 Nov 21;27(47):12808–12816.

    Google Scholar 

  58. Pesah Y, Burgess H, Middlebrooks B, Ronningen K, Prosser J, Tirunagaru V, Zysk J, Mardon G. Whole-mount analysis reveals normal numbers of dopaminergic neurons following misexpression of α-synuclein in Drosophila. Genesis. 2005 Apr;41(4):154–159.

    Google Scholar 

  59. Williams JA, Sehgal A. Molecular components of the circadian system in Drosophila. Annu Rev Physiol. 2001;63:729–755.

    Google Scholar 

  60. Helfrich-Forster C. Differential control of morning and evening components in the activity rhythm of Drosophila melanogaster– sex-specific differences suggest a different quality of activity. J Biol Rhythms. 2000 Apr;15(2):135–154.

    Google Scholar 

  61. Krishnan B, Dryer SE, Hardin PE. Circadian rhythms in olfactory responses of Drosophila melanogaster. Nature. 1999 Jul 22;400(6742):375–378.

    Google Scholar 

  62. Fernandez JR, Grant MD, Tulli NM, Karkowski LM, McClearn GE. Differences in locomotor activity across the lifespan of Drosophila melanogaster. Exp Gerontol. 1999 Aug;34(5):621–631.

    Google Scholar 

  63. Kordower JH, Chu Y, Hauser RA, Freeman TB, Olanow CW. Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease. Nat Med. 2008 Apr 6.

    Google Scholar 

  64. Li JY, Englund E, Holton JL, Soulet D, Hagell P, Lees AJ, Lashley T, Quinn NP, Rehncrona S, Bjorklund A, Widner H, Revesz T, Lindvall O, Brundin P. Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation. Nat Med. 2008 May;14(5):501–503.

    Google Scholar 

  65. Sugiyama K, Kumazawa A, Zhou H, Saeki S. Dietary methionine level affects linoleic acid metabolism through phosphatidylethanolamine N-methylation in rats. Lipids. 1998 Mar;33(3):235–242.

    Google Scholar 

  66. Sugiyama K, Yamakawa A, Kumazawa A, Saeki S. Methionine content of dietary proteins affects the molecular species composition of plasma phosphatidylcholine in rats fed a cholesterol-free diet. J Nutr. 1997 Apr;127(4):600–607.

    Google Scholar 

  67. Hirche F, Schroder A, Knoth B, Stangl GI, Eder K. Methionine-induced elevation of plasma homocysteine concentration is associated with an increase of plasma cholesterol in adult rats. Ann Nutr Metab. 2006;50(2):139–146.

    Google Scholar 

  68. Hirche F, Schroder A, Knoth B, Stangl GI, Eder K. Effect of dietary methionine on plasma and liver cholesterol concentrations in rats and expression of hepatic genes involved in cholesterol metabolism. Br J Nutr. 2006 May;95(5):879–888.

    Google Scholar 

  69. Moskovitz J, Weissbach H, Brot N. Cloning the expression of a mammalian gene involved in the reduction of methionine sulfoxide residues in proteins. Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2095–2099.

    Google Scholar 

  70. Yeh YY, Liu L. Cholesterol-lowering effect of garlic extracts and organosulfur compounds: human and animal studies. J Nutr. 2001 Mar;131(3s):989S–993S.

    Google Scholar 

  71. Takada N, Yano Y, Wanibuchi H, Otani S, Fukushima S. S-methylcysteine and cysteine are inhibitors of induction of glutathione S-transferase placental form-positive foci during initiation and promotion phases of rat hepatocarcinogenesis. Jpn J Cancer Res. 1997 May;88(5):435–442.

    Google Scholar 

  72. Hsu CC, Yen HF, Yin MC, Tsai CM, Hsieh CH. Five cysteine-containing compounds delay diabetic deterioration in Balb/cA mice. J Nutr. 2004 Dec;134(12):3245–3249.

    Google Scholar 

  73. Agarwal B, Rao CV, Bhendwal S, Ramey WR, Shirin H, Reddy BS, Holt PR. Lovastatin augments sulindac-induced apoptosis in colon cancer cells and potentiates chemopreventive effects of sulindac. Gastroenterology. 1999 Oct;117(4):838–847.

    Google Scholar 

  74. Juge N, Mithen RF, Traka M. Molecular basis for chemoprevention by sulforaphane: a comprehensive review. Cell Mol Life Sci. 2007 May;64(9):1105–1127.

    Google Scholar 

  75. Lowther WT, Brot N, Weissbach H, Matthews BW. Structure and mechanism of peptide methionine sulfoxide reductase, an “anti-oxidation” enzyme. Biochemistry. 2000;39(44):13307–13312.

    Article  PubMed  CAS  Google Scholar 

  76. Lowther WT, Weissbach H, Etienne F, Brot N, Matthews BW. The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB. Nat Struct Biol. 2002 May;9(5):348–352.

    Google Scholar 

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Acknowledgments

The authors’ laboratories are supported in part by grants from NIH and IZKF Jena.

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  1. Department of Physiology, University of Pennsylvania, Philadelphia, PA 19104, USA

    Ramez Wassef & Toshinori Hoshi

  2. Department of Biophysics, Center for Molecular Biomedicine, Friedrich Schiller University Jena, Jena, Germany

    Stefan H. Heinemann

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    Wassef, R., Heinemann, S.H., Hoshi, T. (2009). Treating Oxidative Neural Injury: Methionine Sulfoxide Reductase Therapy for Parkinson’s Disease. In: Veasey, S. (eds) Oxidative Neural Injury. Contemporary Clinical Neuroscience. Humana Press. https://doi.org/10.1007/978-1-60327-342-8_12

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