Abstract: Objective To study the distribution and modification of α-synuclein (α-syn) in α-synuclein A53T transgenic mice. Methods The α-syn A53T transgenic mice were used as Parkinson's disease (PD) model mice. Western blot was used to detect the expression and abnormal aggregation of α-syn in the stomach, substantia nigra and striatum of A53T transgenic mice and wild-type C57BL/6 mice. Results Compared with wild-type mice, the expressions of total α-syn (C-20) and nitrosylated α-syn (n-syn) in the stomach, substantia nigra and striatum of A53T transgenic mice increased. The content of phosphorylated α-syn (p-syn) in the stomach and substantia nigra decreased, while the content of p-syn in the striatum increased. The content of α-syn (5G4) in the form of oligomers in the substantia nigra and striatum increased, but decreased in the stomach. Among them, n-syn had the highest content in stomach tissues, α-syn in the form of oligomers had the highest content in the substantia nigra, and p-syn had the highest content in the striatum. Conclusion The total α-syn protein in A53T transgenic mice increases, and the content of abnormally modified and aggregated α-syn varies in different organs, suggesting that the pathological changes of the organs are specific in the pathogenesis of PD.

Key words: Parkinson's disease, A53T transgenic mice, α-synuclein (α-syn), abnormal form