Aggregates from mutant and wild-type α-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of β-sheet and amyloid-like filaments

Omar M.A. El-Agnaf, Ross Jakes, Martin D. Curran, Derek Middleton, Raffaele Ingenito, Elisabetta Bianchi, Antonello Pessi, David Neill, Andrew Wallace

Research output: Contribution to journalArticlepeer-review

325 Citations (Scopus)

Abstract

α-Synuclein (α-syn) protein and a fragment of it, called NAC, have been found in association with the pathological lesions of a number of neurodegenerative diseases. Recently, mutations in the α-syn gene have been reported in families susceptible to an inherited form of Parkinson's disease. We have shown that human wild-type α-syn, mutant α-syn(Ala30Pro) and mutant α-syn(Ala53Thr) proteins can self-aggregate and form amyloid-like filaments. Here we report that aggregates of NAC and α-syn proteins induced apoptotic cell death in human neuroblastoma SH-SY5Y cells. These findings indicate that accumulation of α-syn and its degradation products may play a major role in the development of the pathogenesis of these neurodegenerative diseases. Copyright (C) 1998 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)71-75
Number of pages5
JournalFEBS Letters
Volume440
Issue number1-2
DOIs
Publication statusPublished - Nov 27 1998
Externally publishedYes

Keywords

  • Amyloid
  • Lewy body
  • Neurodegenerative disease
  • Parkinson's disease
  • Toxicity
  • α-Synuclein

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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