1. Hyperphosphorylation of microtubule-associated tau protein plays dual role in neurodegeneration and neuroprotection 
Yao Zhang, Qing Tian, Qi Zhang, Xinwen Zhou, Shijie Liu, Jian-Zhi Wang 
Pathophysiology 
Volume 16, Issue 4, Pages (October 2009)
DOI: /j.pathophys
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2. Fig. 1
The N2a cells transfected with GSK-3β are more resistant to staurosporine-induced apoptosis than those transfected with the vector. Triple-labeling of the cells with PHF-1, activated form of caspase-3 and Hochest after treatment with 1μM staurosporine for 12h (n=5, scale bar=20μm). An obvious dissociation of PHF-1 (hyperphosphorylated tau) from activated caspase-3/fragmented nuclei (apoptotic markers) was observed in addition to the significantly decreased apoptosis in cells transfected with GSK-3β.
Pathophysiology  , DOI: ( /j.pathophys )
Copyright © 2009 Elsevier Ireland Ltd Terms and Conditions

3. Fig. 2
The anti-apoptotic effect of tau hyperphosphorylation and the possible underlying mechanisms. GSK-3β phosphorylates both tau and β-catenin (β-cat). Phosphorylation of β-cat stimulates the proteolysis in the cytoplasma and dephosphorylated β-cat is allocated to the nuclei where it regulates the expression of cell survival-stimulating proteins. The hyperphosphorylation of tau can preserve β-cat, which may indicate the protective effects of tau hyperphosphorylation to the induced apoptosis (Li et al. [65]).
Pathophysiology  , DOI: ( /j.pathophys )
Copyright © 2009 Elsevier Ireland Ltd Terms and Conditions