In order to disclose the mechanisms, a high-throughput quantitative proteomics analysis was established to investigate the proteome profiles changes of hippocampus and temporal lobe of WT mice, APP/PS1 mice and rapamycin treated APP/PS1 mice.The extraction of proteins of hippocampus and temporal tissue employed liquid nitrogen grounding method, which was described as previous works of our laboratory and other laboratories [20, 21]. After fully and immediately grinding under the protection of liquid nitrogen, the products was dissolved by lysis buffer (8 M urea and 1  cocktail in PBS, pH = 8.0) prepared in ice ahead of schedule and then the solutions were transferred to a 1.5-mL tube in ice. Cellular debris was removed by centrifugation (12,000 rpm, 15 min, 4 °C) and the liquid supernatant was transferred into a fresh 1.5-mL tube and immediately stored at -80 °C. The protein concentration of the supernatant was detected by Nanodrop 2000 (Thermo Scientific, NJ, USA) following the manufacture instructions.