Hyperphosphorylation of tau protein by calpain regulation in retina of Alzheimer's disease transgenic mouse

Neurosci Lett. 2013 Sep 13:551:12-6. doi: 10.1016/j.neulet.2013.06.026. Epub 2013 Jun 25.

Abstract

Aim to investigate phosphorylated tau expression and its pathogenic mechanism in eye of Alzheimer's disease (AD) transgenic mice. Levels of tau, phosphorylated tau and other related factors (p35/p25, Cyclin-dependent kinase 5 (Cdk5), calpain) were observed by western blot. β-Amyloid (Aβ) plaques and neuron-fibrillary tangles (NFTs) in APP/PS1 double transgenic mice were detected by immuno-histochemistry. We found that hyper-expression of phosphorylated tau was detected in retina, and only a few or no expressed in optic nerve, cornea and lens of transgenic mice. Increased senile plaques (Aβ) and NFTs were observed in transgenic mice accompanying with increased tau phosphorylation. The increased tau phosphorylation was associated with a significant increase in production of p35 and p25, and up-regulation of calpain. In conclusion, phosphorylated tau level was highly expressed in retina of AD transgenic mice. The pathogenic mechanism of AD was triggered by accelerating tau pathology via calpain-mediated tau hyper-phosphorylation in retina of an AD mice model.

Keywords: Alzheimer disease; Calpain; Cdk5; Phosphorylated tau; Tau pathology.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alzheimer Disease / metabolism*
  • Alzheimer Disease / pathology*
  • Animals
  • Calpain / metabolism*
  • Disease Models, Animal
  • Mice
  • Mice, Transgenic
  • Neurofibrillary Tangles / metabolism
  • Phosphorylation
  • Plaque, Amyloid / metabolism
  • Retina / metabolism*
  • Retina / pathology*
  • tau Proteins / metabolism*

Substances

  • tau Proteins
  • Calpain