Degradation of Oligomer Tau by Autophagy

Background The specific pathological findings in Alzheimer’s disease (AD) brain are senile plaques composed of amyloid-β protein (Aβ) and neurofibrillary tangles (NFTs) highly phosphorylated tau protein. It has been suggested that autophagy may play an important role the degradation proteins. In this study, we investigated whether is involved oligomeric by immunohistochemistry using autopsied AD brains. Method Frozen brains were homogenized to produce lysates, Western blotting (WB) was performed anti-LC3 antibody, a marker autophagy. parietal lobes same autopsy used for immunohistochemical analysis anti-LC3, anti-P62, anti-oligomeric antibody (TOC-1) anti-phosphorylated (PHF-1). Result WB temporal lobe, LC3-II generally increased compared controls. addition, immunostaining showed (TOC1) LC3 coexisted control brains, tau, which stained faintly, found coexist with LC3, but not cytoplasm neurons serious (PHF-1) deposition. However, coexistence p62 remarkable. No or P62 staining observed neuropil thread. Conclusion These results suggest degraded also autophagy, no longer function when degree deposition serious.