Magnetite-Amyloid-β deteriorates activity and functional organization in an in vitro model for Alzheimer's disease

Sci Rep. 2015 Nov 26:5:17261. doi: 10.1038/srep17261.

Abstract

The understanding of the key mechanisms behind human brain deterioration in Alzheimer' disease (AD) is a highly active field of research. The most widespread hypothesis considers a cascade of events initiated by amyloid-β peptide fibrils that ultimately lead to the formation of the lethal amyloid plaques. Recent studies have shown that other agents, in particular magnetite, can also play a pivotal role. To shed light on the action of magnetite and amyloid-β in the deterioration of neuronal circuits, we investigated their capacity to alter spontaneous activity patterns in cultured neuronal networks. Using a versatile experimental platform that allows the parallel monitoring of several cultures, the activity in controls was compared with the one in cultures dosed with magnetite, amyloid-β and magnetite-amyloid-β complex. A prominent degradation in spontaneous activity was observed solely when amyloid-β and magnetite acted together. Our work suggests that magnetite nanoparticles have a more prominent role in AD than previously thought, and may bring new insights in the understanding of the damaging action of magnetite-amyloid-β complex. Our experimental system also offers new interesting perspectives to explore key biochemical players in neurological disorders through a controlled, model system manner.

MeSH terms

  • Alzheimer Disease / pathology*
  • Amyloid beta-Peptides / toxicity*
  • Animals
  • Cell Aggregation / drug effects
  • Cells, Cultured
  • Ferrosoferric Oxide / toxicity*
  • Models, Biological*
  • Neurons / drug effects
  • Neurons / pathology*
  • Rats, Sprague-Dawley

Substances

  • Amyloid beta-Peptides
  • Ferrosoferric Oxide