Copper- and iron-induced differential fibril formation in α-synuclein: TEM study

Neuroscience Letters

Volumn 424, Issue 2, 2007, Pages 78-82

  Bharathi, ^a   Indi, S S ^b   Rao, K S J ^a  

^a CENTRAL FOOD TECHNOLOGICAL RESEARCH INSTITUTE   (India)

^b INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

Synuclein; Copper; Electron microscopy; Fibrils; Iron; Parkinson's disease

Indexed keywords

COPPER; IRON; SYNUCLEIN;

ARTICLE; CELL INCLUSION; CELL TYPE; NERVE DEGENERATION; NEUROFIBRILLARY TANGLE; NEUROPATHOLOGY; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN INDUCTION; PROTEIN PROTEIN INTERACTION; TRANSMISSION ELECTRON MICROSCOPY; WILD TYPE;

ALPHA-SYNUCLEIN; COPPER; HUMANS; IRON; MICROSCOPY, ELECTRON, TRANSMISSION; MUTATION; PROTEIN BINDING; TIME FACTORS;

EID: 34548021006     PISSN: 03043940     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neulet.2007.06.052     Document Type: Article

References (44)

1. Armstrong R.A., Lantos P.L., and Cairns N.J. Spatial patterns of α-synuclein positive glial cytoplasmic inclusions in multiple system atrophy. Mov. Disord. 19 (2004) 109-112
2. Bucciantini M., Giannoni E., Chiti F., Baroni F., Formigli L., Zurdo J., Taddei N., Ramponi G., Dobson C.M., and Stefani M. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416 (2002) 507-511
3. Conway K.A., Harper J.D., and Lansbury Jr. P.T. Accelerated in vitro fibril formation by a mutant alpha synuclein linked to early-onset Parkinsons disease. Nat. Med. 4 (1998) 1318-1320
4. Conway K.A., Harper J.D., and Lansbury Jr. P.T. Fibrils formed in vitro from α-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid. Biochemistry 39 (2000) 2552-2563
5. Conway K.A., Lee S.J., Rochet J.C., Ding T.T., Williamson R.E., and Lansbury Jr. P.T. Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy. Proc. Natl. Acad. Sci. 97 (2000) 571-576
6. Dexter D.T., Wells F.R., Lees A.J., Agid F., Jenner Y., and Marsden C.D. Increased nigral iron content and alterations in other metals ions occurring in brain in parkinson's disease. J. Neurochem. 52 (1989) 1830-1836
7. Goedert M. Filamentous nerve cell inclusions in neurodegenerative diseases: Tauopathies and α-synucleinopathies. Philos. Trans. R. Soc. Lond. B Biol. Sci. 354 (1999) 1101-1118
8. Goedert M. α-Synuclein and neurodegenerative diseases. Nat. Rev. Neurosci. 2 (2001) 492-501
9. Goers J., Uversky V.N., and Fink A.L. Polycation-induced oligomerization and accelerated fibrillation of human α-synuclein in vitro. Protein Sci. 12 (2003) 702-707
10. Golts N., Snyder H., Frasier M., Theisler C., Choi P., and Wolozin B. Magnesium inhibits spontaneous and iron-induced aggregation of α-synuclein. J. Biol. Chem. 277 (2002) 16116-16123
11. Hoyer W., Antony T., Cherny D., Heim G., Jovin T.M., and Subramaniam V. Dependence of α-synuclein aggregate morphology on solution conditions. J. Mol. Biol. 322 (2002) 383-393
12. Iseki E. Dementia with Lewy bodies: Reclassification of pathological subtypes and boundary with Parkinson's disease or Alzheimer's disease. Neuropathology 24 (2004) 72-78
13. Iwai A., Masliah E., Yoshimoto M., Ge N., Flanagan L., de Silva H.A., Kittel A., and Saitoh T. The precursor protein of non-Aβ component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system. Neuron 14 (1995) 467-475
14. Jensen P.H., and Gai W.P. α-Synuclein. Axonal transport, ligand interaction and neurodegeneration. Adv. Exp. Med. Biol. 487 (2001) 129-134
15. Jiminez-Jiminez F.J., Molina J.A., Aguilar M.V., Meseguer I., Mateos-Vega C.J., Gonzalez-Munoz M.J., de Bustos F., Martinez-Salio A., Orti-Pareja M., Zurdo M., and Martinez M.C. Cerebrospinal fluid levels of transition metals in patients with Parkinson's disease. J. Neural Transm. 105 (1998) 497-505
16. Krishnan S., Chi E.Y., Wood S.J., Kendrick B.S., Li C., Garzon-Rodriguez W., Wypych J., Randolph T.W., Narhi L.O., Biere A.L., Citron M., and Carpenter J.F. Oxidative dimer formation is the critical rate-limiting step for Parkinson's disease α-synuclein fibrillogenesis. Biochemistry 42 (2003) 829-837
17. Kruger R., Kuhn W., Muller T., Woitalla D., Graeber M., Kosel S., Przuntek H., Epplen J.T., Schols L., and Riess O. Ala30Pro mutation in the gene encoding α-synuclein in Parkinson's disease. Nat. Genet. 18 (1998) 106-108
18. Lashuel H.A., Petre B.M., Wall J., Simon M., Nowak R.J., Walz T., and Lansbury Jr. P.T. α-synuclein, especially the Parkinson's disease associated mutants, forms pore-like annular and tubular protofibrils. J. Mol. Biol. 322 (2002) 1089-1102
19. Li J., Uversky V.N., and Fink A.L. Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties of aggregation, and fibrillation of human-alpha synuclein. Biochemistry 40 (2001) 11604-11613
20. Lowe R., Poutney D.L., Jensen P.H., Gai W.P., and Voelcker N.H. Calcium(II) selectively induces alpha synuclein annular oligomers via interaction with the C-terminal domain. Protein Sci. 13 (2004) 3245-3252
21. Maroteaux L., Campanelli J.T., and Scheller R.H. Synuclein: a neuron specific protein localized to the nucleus and presynaptic nerve terminal. J. Neurosci. 8 (1998) 2804-2815
22. Narhi L., Wood S.J., Stevenson S., Jung Y., Wu G.M., Anafi D., Kaufman S.A., Martin F., Sitney K., Denis P., Louis J.C., Wypych J., Biere A.L., and Citron M. Both familial Parkinson's disease mutations accelerate alpha-synuclein aggregation. J. Biol. Chem. 274 (1999) 9843-9846
23. Ostrerova-Golts N., Petrucelli L., Hardy J., Lee J.M., Farer M., and Wolozin B. The A53T alpha-synuclein mutation increases iron-dependent aggregation and toxicity. J. Neurosci. 20 (2000) 6048-6054
24. Paik S.R., Shin H.J., and Lee J.H. Metal-catalyzed oxidation of α-synuclein in the presence of copper(II) and hydrogen peroxide. Arch. Biochem. Biophys. 378 (2000) 269-277
25. Paik S.R., Shin H.J., Lee J.H., Chang C.S., and Kim J. Copper(II) induced self-oligomerisation of α-synuclein. Biochem. J. 340 (1999) 821-828
26. Perrin R.J., Woods W.S., Clayton D.F., and George J.M. Exposure to long chain polyunsaturated fatty acids triggers rapid multimerization of synucleins. J. Biol. Chem. 276 (2001) 41958-41962
27. Polymeropoulos M.H., Lavedan C., Leroy E., Ide S.E., Dehejia A., Dutra A., Pike B., Root H., Rubenstein J., Boyer R., Stenroos E.S., Chandrasekharappa S., Athanassiadou A., Papapetropoulos T., Johnson W.G., Lazzarini A.M., Duvoism R.C., Di Iorio G., Golbe L.I., and Nussbaum R.L. Mutation in the α-synuclein gene identified in families with Parkinson's disease. Science 276 (1997) 2045-2047
28. Rasia R.M., Bertoncini C.W., Marsh D., Hoyer W., Cherny D., Zweckstetter M., Griesinger C., Jovin T.M., and Fernandez C.O. Structural characterization of copper(II) binding to alpha-synuclein: Insights into the bioinorganic chemistry of Parkinson's disease. Proc. Natl. Acad. Sci. U.S.A. 102 (2005) 4294-4299
29. Rochet J.C., Conway K.A., and Lansbury Jr. P.T. Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein. Biochemistry 39 (2000) 10619-10626
30. Serpell L.C., Berriman J., Jakes R., Goedert M., and Crowther R.A. Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross β conformation. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 4897-4902
31. Singleton A.B., 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 M.R., Muenter M., Baptista M., Miller D., Blancato J., Hardy J., and Gwinn-Hardy K. α-synuclein locus triplication causes Parkinson's disease. Science 302 (2003) 841
32. Souza J.M., Giasson B.I., Chen Q., Lee V.M., and Ischiropoulos H. Dityrosine cross-linking promotes formation of stable α-synuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies. J. Biol. Chem. 275 (2000) 18344-18349
33. Spillantini M.G., Crowther R.A., Jakes R., Hasegawa M., and Goedert M. α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with Lewy bodies. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 6469-6473
34. Spillantini M.G., Schimdt M.L., Lee V.M., Trojanowski J.Q., Jakes R., and Goedert M. α-Synuclein in Lewy bodies. Nature 388 (1997) 839-840
35. Totterdell S., Hanger D., and Meredith G.E. The ultrastructural distribution of α-synuclein-like protein in normal mouse brain. Brain Res. 1004 (2004) 61-72
36. Trojanowski J.Q., and Lee V.M. Parkinson's disease and related α-synucleinopathies are brain amyloidoses. Ann. NY Acad. Sci. 991 (2003) 107-110
37. Uversky V.N. Natively unfolded proteins: a point where biology waits where biology waits for physics. Protein Sci. 11 (2002) 739-756
38. Uversky V.N. What does it mean to be natively unfolded?. Eur. J. Biochem. 269 (2002) 2-12
39. Uversky V.N. A protein-chameleon: conformational plasticity of α-synuclein, a disordered protein involved in neurodegenerative disorders. J. Biomol. Struct. Dyn. 21 (2003) 211-234
40. Uversky V.N., Li J., and Fink A.L. Metal-triggered structural transformations, aggregation, and fibrillation of human α-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure. J. Biol. Chem. 276 (2001) 44284-44296
41. Weinreb P.H., Zhen W., Poon A.W., Conway K.A., and Lansbury Jr. P.T. NACP a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 35 (1996) 13709-13715
42. Yamin G., Glaser C.B., Uversky V.N., and Fink A.L. Certain metal trigger fibrillation of methionine-oxidized alpha synuclein. J. Biol. Chem. 278 (2003) 27630-27635
43. Zarranz J.J., Alegre J., Gomez-Esteban J.C., Lezcano E., Ros R., Ampuero I., Vidal L., Hoenicka J., Rodriguez O., Atares B., Llorens V., Gomez Tortosa E., del Ser T., Munoz D.G., and de Yebenes J.G. The new mutation, E46K, of α-synuclein causes Parkinson and Lewy body dementia. Ann. Neurol. 55 (2004) 164-173
44. Zecca L., Stroppolo A., Gatti A., Tampellini D., Toscani M., Gallorini M., Giaveri G., Arosio P., Santambrogio P., Fariello R.G., Karatekin E., Kleinman M.H., Turro N., Hornykiewicz O., and Zucca F.A. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 9843-9848