Modes of Aβ toxicity in Alzheimer's disease

Jürgen Götz*, Anne Eckert, Miriam Matamales, Lars M. Ittner, Xin Liu

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

68 Citations (Scopus)


Alzheimer's disease (AD) is reaching epidemic proportions, yet a cure is not yet available. While the genetic causes of the rare familial inherited forms of AD are understood, the causes of the sporadic forms of the disease are not. Histopathologically, these two forms of AD are indistinguishable: they are characterized by amyloid-β (Aβ) peptide-containing amyloid plaques and tau-containing neurofibrillary tangles. In this review we compare AD to frontotemporal dementia (FTD), a subset of which is characterized by tau deposition in the absence of overt plaques. A host of transgenic animal AD models have been established through the expression of human proteins with pathogenic mutations previously identified in familial AD and FTD. Determining how these mutant proteins cause disease in vivo should contribute to an understanding of the causes of the more frequent sporadic forms. We discuss the insight transgenic animal models have provided into Aβ and tau toxicity, also with regards to mitochondrial function and the crucial role tau plays in mediating Aβ toxicity. We also discuss the role of miRNAs in mediating the toxic effects of the Aβ peptide.

Original languageEnglish
Pages (from-to)3359-3375
Number of pages17
JournalCellular and Molecular Life Sciences
Issue number20
Publication statusPublished - 1 Oct 2011
Externally publishedYes


  • Alzheimer
  • Amyloid
  • Frontotemporal dementia
  • Fyn
  • miRNA
  • Mitochondria
  • Oligomer
  • Proteomic
  • Tau
  • Transgenic

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