Characterization of a double (amyloid precursor protein-tau) transgenic: Tau phosphorylation and aggregation

M. Pérez, E. Ribe, A. Rubio, F. Lim, M. A. Morán, P. Gómez Ramos, I. Ferrer, M. T G Isla, J. Avila

Research output: Contribution to journalArticlepeer-review


A double transgenic mouse expressing the amyloid precursor protein, bearing the Swedish mutations, and expressing tau protein containing three of the mutations present in frontotemporal dementia linked to chromosome 17 (FTDP-17), has been characterized. In the double transgenic mouse an increase in tau phosphorylation at serine S262 and S422 was observed compared with that found in simple transgenic mice. The phosphorylation at S262 was also found, in a much lower level, in the single transgenic mouse expressing amyloid precursor protein (APP), and it was absent in that overexpressing tau variant. Additionally, in the double transgenic mouse a slight increase in the amount of sarkosyl insoluble tau polymers was observed in comparison with that found in single transgenic tau mouse. Also, wider tau filaments were found in the double transgenic mouse compared with those found in the single transgenic mouse. Our results suggest that β-amyloid peptide could facilitate the phosphorylation of tau at a site not directed by proline, such as serine 262, and that modification could facilitate tau aberrant aggregation. Also, they suggest that different types of tau filamentous polymers can occur in different mouse models for tauopathies, like those used for Alzheimer's disease or FTDP-17.

Original languageEnglish
Pages (from-to)339-347
Number of pages9
Issue number2
Publication statusPublished - 2005


  • Alzheimer's disease
  • beta-amyloid aggregates
  • FTDP-17
  • kinases
  • phosphorylation
  • tau polymers

ASJC Scopus subject areas

  • Neuroscience(all)


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