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Original Research

Targeting α-synuclein oligomers by protein-fragment complementation for drug discovery in synucleinopathies

, PhD, , , , &

Bibliography

  • Irizarry MC, Growdon W, Gomez-Isla T, et al. Nigral and cortical Lewy bodies and dystrophic nigral neurites in Parkinson’s disease and cortical Lewy body disease contain alpha-synuclein immunoreactivity. J Neuropathol Exp Neurol 1998;57(4):334-7
  • Spillantini MG, Crowther RA, Jakes R, et al. Filamentous alpha-synuclein inclusions link multiple system atrophy with Parkinson’s disease and dementia with Lewy bodies. Neurosci Lett 1998;251(3):205-8
  • Spillantini MG, Schmidt ML, Lee VM, et al. Alpha-synuclein in Lewy bodies. Nature 1997;388(6645):839-40
  • Spillantini MG, Goedert M. The alpha-synucleinopathies: parkinson’s disease, dementia with Lewy bodies, and multiple system atrophy. Ann N Y Acad Sci 2000;920:16-27
  • Appel-Cresswell S, Vilarino-Guell C, Encarnacion M, et al. Alpha-synuclein p.H50Q, a novel pathogenic mutation for Parkinson’s disease. Mov Disord 2013;28(6):811-13
  • Chartier-Harlin MC, Kachergus J, Roumier C, et al. Alpha-synuclein locus duplication as a cause of familial Parkinson’s disease. Lancet 2004;364(9440):1167-9
  • Kiely AP, Asi YT, Kara E, et al. Alpha-Synucleinopathy associated with G51D SNCA mutation: a link between Parkinson’s disease and multiple system atrophy? Acta Neuropathol 2013;125(5):753-69
  • Kruger R, Kuhn W, Muller T, et al. Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson’s disease. Nat Genet 1998;18(2):106-8
  • Polymeropoulos MH, Lavedan C, Leroy E, et al. Mutation in the alpha-synuclein gene identified in families with Parkinson’s disease. Science 1997;276(5321):2045-7
  • Singleton AB, Farrer M, Johnson J, et al. alpha-Synuclein locus triplication causes Parkinson’s disease. Science 2003;302(5646):841
  • Zarranz JJ, Alegre J, Gomez-Esteban JC, et al. The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia. Ann Neurol 2004;55(2):164-73
  • Labbe C, Ross OA. Association studies of sporadic Parkinson’s disease in the genomic era. Curr Genomics 2014;15(1):2-10
  • Giasson BI, Duda JE, Quinn SM, et al. Neuronal alpha-synucleinopathy with severe movement disorder in mice expressing A53T human alpha-synuclein. Neuron 2002;34(4):521-33
  • Lauwers E, Debyser Z, Van Dorpe J, et al. Neuropathology and neurodegeneration in rodent brain induced by lentiviral vector-mediated overexpression of alpha-synuclein. Brain Pathol 2003;13(3):364-72
  • Van Uden E, Sagara Y, Van Uden J, et al. A protective role of the low density lipoprotein receptor-related protein against amyloid beta-protein toxicity. J Biol Chem 2000;275(39):30525-30
  • St Martin JL, Klucken J, Outeiro TF, et al. Dopaminergic neuron loss and up-regulation of chaperone protein mRNA induced by targeted over-expression of alpha-synuclein in mouse substantia nigra. J Neurochem 2007;100(6):1449-57
  • Kirik D, Rosenblad C, Burger C, et al. Parkinson-like neurodegeneration induced by targeted overexpression of alpha-synuclein in the nigrostriatal system. J Neurosci 2002;22(7):2780-91
  • Klein RL, King MA, Hamby ME, et al. Dopaminergic cell loss induced by human A30P alpha-synuclein gene transfer to the rat substantia nigra. Hum Gene Ther 2002;13(5):605-12
  • Lo Bianco C, Ridet JL, Schneider BL, et al. Alpha -Synucleinopathy and selective dopaminergic neuron loss in a rat lentiviral-based model of Parkinson’s disease. Proc Natl Acad Sci USA 2002;99(16):10813-18
  • Feany MB, Bender WW. A Drosophila model of Parkinson’s disease. Nature 2000;404(6776):394-8
  • Conway KA, Lee SJ, Rochet JC, et al. Accelerated oligomerization by Parkinson’s disease linked alpha-synuclein mutants. Ann N Y Acad Sci 2000;920:42-5
  • Danzer KM, Haasen D, Karow AR, et al. Different species of alpha-synuclein oligomers induce calcium influx and seeding. J Neurosci 2007;27(34):9220-32
  • Danzer KM, Ruf WP, Putcha P, et al. Heat-shock protein 70 modulates toxic extracellular alpha-synuclein oligomers and rescues trans-synaptic toxicity. Faseb J 2011;25(1):326-36
  • Kayed R, Sokolov Y, Edmonds B, et al. Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. J Biol Chem 2004;279(45):46363-6
  • Lashuel HA, Petre BM, Wall J, et al. Alpha-synuclein, especially the Parkinson’s disease-associated mutants, forms pore-like annular and tubular protofibrils. J Mol Biol 2002;322(5):1089-102
  • Sharon R, Bar-Joseph I, Frosch MP, et al. The formation of highly soluble oligomers of alpha-synuclein is regulated by fatty acids and enhanced in Parkinson’s disease. Neuron 2003;37(4):583-95
  • Volles MJ, Lee SJ, Rochet JC, et al. Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson’s disease. Biochemistry 2001;40(26):7812-19
  • Serpell LC, Berriman J, Jakes R, et al. Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation. Proc Natl Acad Sci USA 2000;97(9):4897-902
  • Uversky VN, M Cooper E, Bower KS, et al. Accelerated alpha-synuclein fibrillation in crowded milieu. FEBS Lett 2002;515(1-3):99-103
  • Wood SJ, Wypych J, Steavenson S, et al. alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson’s disease. J Biol Chem 1999;274(28):19509-12
  • Outeiro TF, Putcha P, Tetzlaff JE, et al. Formation of toxic oligomeric alpha-synuclein species in living cells. PLoS ONE 2008;3(4):e1867
  • Putcha P, Danzer KM, Kranich LR, et al. Brain-permeable small-molecule inhibitors of Hsp90 prevent alpha-synuclein oligomer formation and rescue alpha-synuclein-induced toxicity. J Pharmacol Exp Ther 2010;332(3):849-57
  • Kerppola TK. Visualization of molecular interactions by fluorescence complementation. Nat Rev Mol Cell Biol 2006;7(6):449-56
  • Remy I, Michnick SW. A highly sensitive protein-protein interaction assay based on Gaussia luciferase. Nat Methods 2006;3(12):977-9
  • Rozanov DV, Savinov AY, Golubkov VS, et al. Engineering a leucine zipper-TRAIL homotrimer with improved cytotoxicity in tumor cells. Mol Cancer Ther 2009;8(6):1515-25
  • Ghosh IH, Hamilton AD, Regan L. Antiparallel leucine zipper-directed protein reassembly: application to the green fluorescent protein. J Am Chem Soc 2000;122:5658-9
  • Hu CD, Chinenov Y, Kerppola TK. Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol Cell 2002;9(4):789-98
  • Morell M, Ventura S, Aviles FX. Protein complementation assays: approaches for the in vivo analysis of protein interactions. FEBS Lett 2009;583(11):1684-91
  • Dimant H, Kalia SK, Kalia LV, et al. Direct detection of alpha synuclein oligomers in vivo. Acta Neuropathol Commun 2013;1(1):6
  • Tetzlaff JE, Putcha P, Outeiro TF, et al. CHIP targets toxic alpha-Synuclein oligomers for degradation. J Biol Chem 2008;283(26):17962-8
  • Danzer KM, Kranich LR, Ruf WP, et al. Exosomal cell-to-cell transmission of alpha synuclein oligomers. Mol Neurodegener 2012;7:42
  • Auluck PK, Meulener MC, Bonini NM. Mechanisms of Suppression of {alpha}-Synuclein Neurotoxicity by Geldanamycin in Drosophila. J Biol Chem 2005;280(4):2873-8
  • Klucken J, Shin Y, Masliah E, et al. Hsp70 Reduces alpha-Synuclein Aggregation and Toxicity. J Biol Chem 2004;279(24):25497-502
  • McLean PJ, Klucken J, Shin Y, et al. Geldanamycin induces Hsp70 and prevents alpha-synuclein aggregation and toxicity in vitro. Biochem Biophys Res Commun 2004;321(3):665-9
  • Shen HY, He JC, Wang Y, et al. Geldanamycin induces heat shock protein 70 and protects against MPTP-induced dopaminergic neurotoxicity in mice. J Biol Chem 2005;280(48):39962-9
  • Jones DR, Moussaud S, McLean P. Targeting heat shock proteins to modulate alpha-synuclein toxicity. Ther Adv Neurol Disord 2014;7(1):33-51
  • Kalia LV, Kalia SK, McLean PJ, et al. alpha-Synuclein oligomers and clinical implications for Parkinson disease. Ann Neurol 2013;73(2):155-69
  • Magliery TJ, Regan L. Reassembled GFP: detecting protein-protein interactions and protein expression patterns. Methods Biochem Anal 2006;47:391-405
  • Anderson JP, Walker DE, Goldstein JM, et al. Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease. J Biol Chem 2006;281(40):29739-52
  • Fujiwara H, Hasegawa M, Dohmae N, et al. Alpha-Synuclein is phosphorylated in synucleinopathy lesions. Nat Cell Biol 2002;4(2):160-4
  • Ferrer I, Blanco R, Carmona M, et al. Active, phosphorylation-dependent mitogen-activated protein kinase (MAPK/ERK), stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK), and p38 kinase expression in Parkinson’s disease and Dementia with Lewy bodies. J Neural Transm 2001;108(12):1383-96
  • Ishii A, Nonaka T, Taniguchi S, et al. Casein kinase 2 is the major enzyme in brain that phosphorylates Ser129 of human alpha-synuclein: implication for alpha-synucleinopathies. FEBS Lett 2007;581(24):4711-17
  • Lee G, Tanaka M, Park K, et al. Casein kinase II-mediated phosphorylation regulates alpha-synuclein/synphilin-1 interaction and inclusion body formation. J Biol Chem 2004;279(8):6834-9
  • Martin ZS, Neugebauer V, Dineley KT, et al. alpha-Synuclein oligomers oppose long-term potentiation and impair memory through a calcineurin-dependent mechanism: relevance to human synucleopathic diseases. J Neurochem 2012;120(3):440-52
  • Okochi M, Walter J, Koyama A, et al. Constitutive phosphorylation of the Parkinson’s disease associated alpha-synuclein. J Biol Chem 2000;275(1):390-7
  • Wilms H, Rosenstiel P, Romero-Ramos M, et al. Suppression of MAP kinases inhibits microglial activation and attenuates neuronal cell death induced by alpha-synuclein protofibrils. Int J Immunopathol Pharmacol 2009;22(4):897-909
  • Hashimoto T, Adams KW, Fan Z, et al. Characterization of oligomer formation of amyloid-beta peptide using a split-luciferase complementation assay. J Biol Chem 2011;286(31):27081-91

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