Peroxiredoxin2

Peroxiredoxin2, often abbreviated as PRDX2, is a protein belonging to the peroxiredoxin family. These proteins are ubiquitously found in eukaryotes and play a crucial role in cellular defense against oxidative stress. PRDX2 is a thiol-specific antioxidant enzyme, meaning it utilizes cysteine residues to reduce reactive oxygen species (ROS).

In humans, PRDX2 is encoded by the PRDX2 gene and is widely expressed in various tissues, with high levels found in erythrocytes (red blood cells). This high expression in red blood cells is significant because these cells are particularly vulnerable to oxidative damage due to their continuous exposure to oxygen.

The primary function of PRDX2 is to catalyze the reduction of hydrogen peroxide (H2O2) and organic hydroperoxides. This detoxification process involves a catalytic cycle where PRDX2 is oxidized by the peroxide and then reduced back to its active form by thioredoxin. This mechanism helps protect cells from the harmful effects of ROS, which can damage DNA, proteins, and lipids, contributing to aging and various diseases.

Beyond its antioxidant role, PRDX2 has been implicated in other cellular processes, including cell proliferation, differentiation, and apoptosis. Its involvement in these diverse pathways suggests a multifaceted role in cellular homeostasis. Aberrant PRDX2 expression or activity has been linked to several human diseases, including cancer and neurodegenerative disorders, highlighting its importance in maintaining cellular health.