Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family

Edited by
May 2019
152 pages
  • ISBN978-3-03897-934-0 (Paperback)
  • ISBN978-3-03897-935-7 (PDF)

This book is a reprint of the Special Issue Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family that was published in

Biology & Life Sciences

The peroxiredoxin family was discovered approximately 30 years ago and is now recognized as one of the most important families of enzymes related to antioxidant defense and cellular signaling. Peroxiredoxin 6 shares the basic enzymatic functions that characterize this family, but also exhibits several unique and crucial activities. These include the ability to reduce phospholipid hydroperoxides, phospholipase A2 activity, and an acyl transferase activity that is important in phospholipid remodeling. This book describes the available models for investigating the unique functions of PRDX6 and its role in normal physiological function, as well its roles in the pathophysiology of diseases including cancer, diseases of the eye, and male fertility.

  • Paperback
© 2019 by the authors; CC BY-NC-ND license
glutathione peroxidase; phospholipase A2; inflammation; lipid peroxidation; NADPH (nicotinamide adenine dinucleotide phosphate) oxidase; phospholipid hydroperoxide; spermatozoa; oxidative stress; reactive oxygen species; fertilization; sperm capacitation; Prdx6; cornea; Fuchs’ endothelial corneal dystrophy; lipid peroxidation; mitochondrial membrane potential; peroxiredoxin 6; surfactant protein A; phospholipase A2; drug delivery; liposomes; substrate binding; sulfinic acid; Prdx6 structure; mass spectroscopic analysis; peroxiredoxin 6; ionizing radiation; radioprotection; antioxidant activity; peroxidatic cysteine; thioredoxin fold; sulfonic/sulfinic acid; phospholipase A2 activity; reactive oxygen species; Peroxiredoxin; Prdx6; PLA2 activity; 1-Cys Prdx; phospholipase A2; glutathione peroxidase; reactive oxygen species; redox balance; endothelium; inflammation; diabetes; peroxidase; phospholipase A2; lipid peroxidation; phospholipid hydroperoxide; knockout mouse; knock-in mouse; membrane repair; n/a