Genetically augmenting tau levels does not modulate the onset or progression of Abeta pathology in transgenic mice

J Neurochem. 2007 Aug;102(4):1053-63. doi: 10.1111/j.1471-4159.2007.04607.x. Epub 2007 Apr 30.

Abstract

The two hallmark pathologies of Alzheimer's disease (AD) are amyloid plaques, composed of the small amyloid-beta (Abeta) peptide, and neurofibrillary tangles, comprised aggregates of the microtubule binding protein, tau. The molecular linkage between these two lesions, however, remains unknown. Based on human and mouse studies, it is clear that the development of Abeta pathology can trigger tau pathology, either directly or indirectly. However, it remains to be established if the interaction between Abeta and tau is bidirectional and whether the modulation of tau will influence Abeta pathology. To address this question, we used the 3xTg-AD mouse model, which is characterized by the age-dependent buildup of both plaques and tangles. Here we show that genetically augmenting tau levels and hyperphosphorylation in the 3xTg-AD mice has no effect on the onset and progression of Abeta pathology. These data suggest that the link between Abeta and tau is predominantly if not exclusively unidirectional, which is consistent with the Abeta cascade hypothesis and may explain why tauopathy-only disorders are devoid of any Abeta pathology.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Age Factors
  • Alzheimer Disease / genetics
  • Alzheimer Disease / metabolism
  • Alzheimer Disease / pathology*
  • Amyloid Precursor Protein Secretases / genetics
  • Amyloid beta-Peptides / genetics
  • Amyloid beta-Peptides / metabolism*
  • Animals
  • Antibodies, Monoclonal / metabolism
  • Disease Models, Animal*
  • Disease Progression
  • Enzyme-Linked Immunosorbent Assay
  • Gene Expression Regulation, Enzymologic / physiology
  • Humans
  • Mice
  • Mice, Transgenic
  • Microscopy, Electron, Transmission / methods
  • Neurofibrillary Tangles / metabolism
  • Neurofibrillary Tangles / pathology
  • Neurofibrillary Tangles / ultrastructure
  • Phosphoprotein Phosphatases / metabolism
  • Phosphorylation
  • Plaque, Amyloid / metabolism
  • Plaque, Amyloid / pathology
  • Plaque, Amyloid / ultrastructure
  • tau Proteins / genetics
  • tau Proteins / metabolism*

Substances

  • Amyloid beta-Peptides
  • Antibodies, Monoclonal
  • PHF-1 monoclonal antibody
  • tau Proteins
  • Phosphoprotein Phosphatases
  • Amyloid Precursor Protein Secretases