Prdx2, a characteristic 2-Cys enzyme, is one of the most effective scavenger proteins against reactive oxygen species (ROS) and hydrogen peroxide (H₂O₂), protecting cells from oxidative stress. It is involved in multiple signaling pathways and is crucial for maintaining cellular redox balance. Dysregulation of Prdx2 can lead to increased ROS levels and oxidative stress, which are implicated in various diseases [1].

In non-alcoholic steatohepatitis (NASH) research, liver-specific Prdx2 knockout (Prdx2 LKO) female mice fed a methionine-choline deficient diet (MCD) showed a significant increase in hepatic lipid accumulation, inflammation, circulating levels of aspartate aminotransferase (AST), and pro-inflammatory signaling pathways within the liver. There was also an increase in lipid peroxidation, suggesting a protective role of Prdx2 in NASH [2]. In colorectal cancer cells, removal of Prdx2 using short-hairpin RNA vector inhibited cell-cycle progression and autophagy, and Prdx2 promoted cell-cycle progression via activation of the p38 MAPK pathway [3].

In conclusion, Prdx2 is essential for maintaining cellular redox balance and is involved in multiple biological processes. The use of Prdx2 knockout mouse models has revealed its protective role in NASH and its promoting role in colorectal cancer cell-cycle progression. Understanding Prdx2's functions provides insights into the mechanisms of related diseases and may offer potential therapeutic targets.