| First Author | Puzzo D | Year | 2017 |
| Journal | Elife | Volume | 6 |
| PubMed ID | 28696204 | Mgi Jnum | J:257152 |
| Mgi Id | MGI:6116932 | Doi | 10.7554/eLife.26991 |
| Citation | Puzzo D, et al. (2017) LTP and memory impairment caused by extracellular Abeta and Tau oligomers is APP-dependent. Elife 6:e26991 |
| abstractText | The concurrent application of subtoxic doses of soluble oligomeric forms of human amyloid-beta (oAbeta) 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 oAbeta and oTau share a common mechanism when they impair memory and LTP in mice. We found that as already shown for oAbeta, also oTau can bind to amyloid precursor protein (APP). Moreover, efficient intra-neuronal uptake of oAbeta and oTau requires expression of APP. Finally, the toxic effect of both extracellular oAbeta and oTau on memory and LTP is dependent upon APP since APP-KO mice were resistant to oAbeta- 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 Abeta and/or Tau. |
