Peroxiredoxin-6 (Prdx6) is a unique member of the peroxiredoxin family of antioxidant enzymes. Unlike other peroxiredoxins, Prdx6 contains only one conserved cysteine residue and exhibits three types of activities: peroxidase activity, phospholipase A2 (PLA2) activity, and lysolecithin acyltransferase (LPCAT) activity. These activities are crucial for antioxidant defense, cellular phospholipid balance, and the generation of superoxide anion via activation of NADPH oxidase signaling cascades. The regulation of Prdx6 activities is influenced by subcellular localization, substrate binding, and post-translational modifications. Prdx6 plays a significant role in the reduction of peroxidized membrane phospholipids and in the phospholipid homeostasis by generating lysophospholipid substrates for the remodeling pathway of phospholipid synthesis. Prdx6 is closely associated with the pathogenesis of various diseases, including cancer, inflammatory diseases, ischemic stroke, traumatic brain injury, and neurodegenerative diseases. Moreover, Prdx6 has been implicated in the repair of peroxidized cell membranes and cell signaling, highlighting its importance in maintaining cellular integrity and function. The enzyme's ability to reduce oxidized sn-2 fatty acyl groups of phospholipids and to hydrolyze the sn-2 ester bond of phospholipids contributes to its bifunctional role in antioxidant defense and phospholipid homeostasis.
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