Apoptosis mediated neurotoxicity induced by chronic application of β amyloid fragment 25-35

Gianluigi Forloni, Roberto Chiesa, Simona Smiroldo, Laura Verga, Mario Salmona, Fabrizio Tagliavini, Nadia Angeretti

Research output: Contribution to journalArticlepeer-review


To investigate whether and how amyloid-P protein (Aβ) is involved in the neurodegenerative changes characteristic of Alzheimer's disease (AD), primary hippocampal neurones from foetal rat brain were exposed acutely and chronically to micromolar concentrations of a synthetic peptide homologous to residues 25-35 of Aβ (β 25-35). A single application of this peptide (25-100 µM) was ineffective but when the neuronal cultures were exposed to β 25-35 (25-100 (µM) repeatedly every two days for ten days, cell survival was dramatically reduced. The structural changes and the DNA fragmentation of cells chronically exposed to the peptide suggested that neuronal death occurred by apoptosis. Furthermore, β 25-35 showed the intrinsic ability to polymerize into amyloidlike fibrils in vitro. These results confirm the potential pathogenic role of Ap in AD, and indicate that amyloid fibrils may induce neuronal death through a specific programmed process.

Original languageEnglish
Pages (from-to)523-526
Number of pages4
Issue number5
Publication statusPublished - 1993


  • Alzheimer's disease
  • Fibrils
  • Programmed cell death
  • Senile plaques
  • β-amyloid

ASJC Scopus subject areas

  • Neuroscience(all)


Dive into the research topics of 'Apoptosis mediated neurotoxicity induced by chronic application of β amyloid fragment 25-35'. Together they form a unique fingerprint.

Cite this