Peroxiredoxin 1 – an antioxidant enzyme in cancer

Abstract Peroxiredoxins ( PRDX s), a ubiquitous family of redox‐regulating proteins, are reported of potential to eliminate various reactive oxygen species ( ROS ). As a major member of the antioxidant enzymes, PRDX 1 can become easily over‐oxidized on its catalytically active cysteine induced by a variety of stimuli in vitro and in vivo . In nucleus, oligomeric PRDX 1 directly associates with p53 or transcription factors such as c‐Myc, NF ‐κB and AR , and thus affects their bioactivities upon gene regulation, which in turn induces or suppresses cell death. Additionally, PRDX 1 in cytoplasm has anti‐apoptotic potential through direct or indirect interactions with several ROS ‐dependent (redox regulation) effectors, including ASK 1, p66 Shc , GST pi/ JNK and c‐Abl kinase. PRDX 1 is proven to be a versatile molecule regulating cell growth, differentiation and apoptosis. Recent studies have found that PRDX 1 and/or PRDX 1‐regulated ROS ‐dependent signalling pathways play an important role in the progression and metastasis of human tumours, particularly in breast, oesophageal and lung cancers. In this paper, we review the structure, effector functions of PRDX 1, its role in cancer and the pivotal role of ROS in anticancer treatment.