BACKGROUND: Researches in recent years show that fibrillar amyloid-β peptide 1-42 can promote the accumulation of amyloid precursor protein in cell surface and lead to nerve injury.
OBJECTIVE: To explore the role of amyloid precursor protein signal pathway in neuronal cell injury induced by amyloid-β peptide 1-42.
METHODS: The cortical neurons were isolated from pregnant SD rats (17 to 18 days) and cultured. On the 7th day after cultivation, the neurons were incubated with 0 (normal control), 0.05, 0.5 and 5 mol/L fibrillar amyloid-β peptide 1-42 for 8 hours to construct cytotoxic model. Calcein content in the supernatant of neuron cell culture medium was determined by biochemical methods. The expression of amyloid precursor protein and Fe65 was detected by double-label immunofluorescence assays and western blotting.
RESULTS AND CONCLUSION: Compared with the normal control group, the calcein releasing was significantly increased after incubation with different concentrations of fibrillar amyloid-β peptide 1-42 for 8 hours. The co-localization and expression of amyloid precursor protein and Fe65 increased according to western blotting and immunofluorescence, respectively. These findings indicate that fibrillar amyloid-β peptide 1-42 can induce toxic injury in primary cultured cortical neurons, and the amyloid precursor protein-Fe65 signal pathway may be one of the mechanisms of cytotoxic activity.

Xing SL, Chen C, Shen DZ. Signal pathway of amyloid precursor protein in neuronal cell injury induced by amyloid-beta peptide 1-42. Zhongguo Zuzhi Gongcheng Yanjiu. 2012;16(15): 2797-2800.     [http://www.crter.cn  http://en.zglckf.com]