Prdx5, short for peroxiredoxin 5, is an enzyme that detoxifies reactive oxygen species. It is involved in multiple biological pathways such as DNA damage response (DDR), autophagy, and is associated with the regulation of signaling cascades including ATM/p53/Sirt2, and pathways related to Nrf2 [1,4,5,6]. Prdx5 is of great biological importance as it has implications in various diseases and cellular functions. Genetic models can be valuable for studying its functions in vivo.

Knockdown of Prdx5 led to DNA damage, manifested by induction of phosphorylated histone H2AX (γ -H2AX) and p53 -binding protein 1 (53BP1). Prdx5 regulates DDR through Plk1 -mediated phosphorylation of ATM kinase, increasing p53 acetylation at lysine 382, and inducing autophagy [1]. In castration -resistant prostate cancer, PRDX5 promotes AR inhibitor resistance and CRPC development, and its inhibition suppresses DTP cell proliferation [2]. In TSC2 mutant cells, drugs reducing Prdx5 levels made ER stress -induced cell death possible [3].

In conclusion, Prdx5 plays crucial roles in DNA damage response, autophagy, and is associated with diseases like castration -resistant prostate cancer and conditions related to TSC mutations. Studies using gene knockdown or inhibition models have revealed its functions in these biological processes and disease conditions, providing insights into potential therapeutic targets for relevant diseases.