LTP and memory impairment caused by extracellular Aβ and Tau oligomers is APP-dependent

Roberto Piacentini, Domenica Donatella Li Puma, Claudio Grassi, Sara Cocco, Daniela Puzzo, Mauro Fá, Walter Gulisano, Agnes Staniszewski, Hong Zhang, Maria Rosaria Tropea, Agostino Palmeri, Paul Fraser, Luciano D’Adamio, Ottavio Arancio

Research output: Contribution to journalArticlepeer-review

65 Citations (Scopus)


The concurrent application of subtoxic doses of soluble oligomeric forms of human amyloid-beta (oAβ) and Tau (oTau) proteins impairs memory and its electrophysiological surrogate long-term potentiation (LTP), effects that may be mediated by intra-neuronal oligomers uptake. Intrigued by these findings, we investigated whether oAβ and oTau share a common mechanism when they impair memory and LTP in mice. We found that as already shown for oAβ, also oTau can bind to amyloid precursor protein (APP). Moreover, efficient intra-neuronal uptake of oAβ and oTau requires expression of APP. Finally, the toxic effect of both extracellular oAβ and oTau on memory and LTP is dependent upon APP since APP-KO mice were resistant to oAβ- and oTau-induced defects in spatial/associative memory and LTP. Thus, APP might serve as a common therapeutic target against Alzheimer's Disease (AD) and a host of other neurodegenerative diseases characterized by abnormal levels of Aβ and/or Tau.
Original languageEnglish
Pages (from-to)N/A-N/A
Number of pages21
Publication statusPublished - 2017


  • APP
  • Alzheimer's disease
  • amyloid-beta
  • memory
  • mouse
  • neuroscience
  • synaptic plasticity
  • tau


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