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

H Zhao, R Chang, H Che, J Wang, L Yang, W Fang… - Neuroscience …, 2013 - Elsevier
H Zhao, R Chang, H Che, J Wang, L Yang, W Fang, Y Xia, N Li, Q Ma, X Wang
Neuroscience letters, 2013Elsevier
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 …
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.
Elsevier