Destabilization of non-pathological variants of ataxin-3 by metal ions results in aggregation/fibrillogenesis. (Articolo in rivista)

Type
Label
  • Destabilization of non-pathological variants of ataxin-3 by metal ions results in aggregation/fibrillogenesis. (Articolo in rivista) (literal)
Anno
  • 2007-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.biocel.2007.01.012 (literal)
Alternative label
  • Ricchelli F; Fusi P; Tortora P; Valtorta M; Riva M; Tognon G; Chieregato K; Bolognin S; Zatta P. (2007)
    Destabilization of non-pathological variants of ataxin-3 by metal ions results in aggregation/fibrillogenesis.
    in International journal of biochemistry & cell biology
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Ricchelli F; Fusi P; Tortora P; Valtorta M; Riva M; Tognon G; Chieregato K; Bolognin S; Zatta P. (literal)
Pagina inizio
  • 966 (literal)
Pagina fine
  • 977 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 39 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 5 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Institute of Biomedical Technologies- CNR- Department of Biology, University of Padua (literal)
Titolo
  • Destabilization of non-pathological variants of ataxin-3 by metal ions results in aggregation/fibrillogenesis. (literal)
Abstract
  • Ataxin-3 (AT3), a protein that causes spinocerebellar ataxia type 3, has a C-terminus containing a polyglutamine stretch, the length of which can be expanded in its pathological variants. Here, we report on the role of Cu(2+), Mn(2+), Zn(2+) and Al(3+) in the induction of defective protein structures and subsequent aggregation/fibrillogenesis of three different non-pathological forms of AT3, i.e. murine (Q6), human non-expanded (Q26) and human moderately expanded (Q36). AT3 variants showed an intrinsic propensity to misfolding/aggregation; on the other hand, Zn(2+) and Al(3+) strongly stimulated the amplitude and kinetics of these conformational conversions. While both metal ions induced a time-dependent aggregation into amyloid-like fibrillar forms, only small oligomers and/or short protofibrillar species were detected for AT3s alone. The rate and extent of the metal-induced aggregation/fibrillogenesis processes increased with the size of the polyglutamine stretch. Mn(2+) and Cu(2+) had no effect on (Q6) or actually prevented (Q26 and Q36) the AT3 structural transitions. (literal)
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