An unbalanced synaptic transmission: Cause or consequence of the amyloid oligomers neurotoxicity?

Miriam Sciaccaluga, Alfredo Megaro, Giovanni Bellomo, Gabriele Ruffolo, Michele Romoli, Eleonora Palma, Cinzia Costa

Research output: Contribution to journalReview articlepeer-review


Amyloid-β (Aβ) 1-40 and 1-42 peptides are key mediators of synaptic and cognitive dysfunction in Alzheimer’s disease (AD). Whereas in AD, Aβ is found to act as a pro-epileptogenic factor even before plaque formation, amyloid pathology has been detected among patients with epilepsy with increased risk of developing AD. Among Aβ aggregated species, soluble oligomers are suggested to be responsible for most of Aβ’s toxic effects. Aβ oligomers exert extracellular and intracellular toxicity through different mechanisms, including interaction with membrane receptors and the formation of ion-permeable channels in cellular membranes. These damages, linked to an unbalance between excitatory and inhibitory neurotransmission, often result in neuronal hy-perexcitability and neural circuit dysfunction, which in turn increase Aβ deposition and facilitate neurodegeneration, resulting in an Aβ-driven vicious loop. In this review, we summarize the most representative literature on the effects that oligomeric Aβ induces on synaptic dysfunction and network disorganization.

Original languageEnglish
Article number5991
Number of pages21
JournalInternational Journal of Molecular Sciences
Issue number11
Publication statusPublished - Jun 1 2021


  • Aβ oligomers
  • Calcium homeostasis
  • Excitatory/inhibitory unbalance
  • Hyperexcitability
  • Network dysfunction
  • Neurotoxicity
  • Synaptic plasticity

ASJC Scopus subject areas

  • Catalysis
  • Molecular Biology
  • Spectroscopy
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry


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