Peroxiredoxin 6: a bifunctional enzyme with glutathione peroxidase and phospholipase A₂ activities.
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TLDR
Peroxiredoxin 6 (Prdx6) is the prototype and the only mammalian 1-Cys member of the Prdx family and has important roles in both antioxidant defense and homeostasis based on its ability to generate lysophospholipid substrate for the remodeling pathway of phospholipids synthesis.Abstract:
Peroxiredoxin 6 (Prdx6) is the prototype and the only mammalian 1-Cys member of the Prdx family. Major differences from 2-Cys Prdxs include the use of glutathione (GSH) instead of thioredoxin as the physiological reductant, heterodimerization with πGSH S-transferase as part of the catalytic cycle, and the ability either to reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or to hydrolyze the sn-2 ester (alkyl) bond of phospholipids (phospholipase A(2) [PLA(2)] activity). The bifunctional protein has separate active sites for peroxidase (C47, R132, H39) and PLA(2) (S32, D140, H26) activities. These activities are dependent on binding of the protein to phospholipids at acidic pH and to oxidized phospholipids at cytosolic pH. Prdx6 can be phosphorylated by MAP kinases at T177, which markedly increases its PLA(2) activity and broadens its pH-activity spectrum. Prdx6 is primarily cytosolic but also is targeted to acidic organelles (lysosomes, lamellar bodies) by a specific targeting sequence (amino acids 31-40). Oxidant stress and keratinocyte growth factor are potent regulators of Prdx6 gene expression. Prdx6 has important roles in both antioxidant defense based on its ability to reduce peroxidized membrane phospholipids and in phospholipid homeostasis based on its ability to generate lysophospholipid substrate for the remodeling pathway of phospholipid synthesis.read more
Citations
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Redox Mechanisms in Neurodegeneration: From Disease Outcomes to Therapeutic Opportunities.
TL;DR: Redox regulated events that are disrupted in neurodegenerative disorders and whose modulation affords therapeutic opportunities are reviewed and may provide avenues for novel therapeutics.
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Coherent correlation networks among protein biomarkers of beef tenderness: What they reveal.
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Curcumin abates hypoxia-induced oxidative stress based-ER stress-mediated cell death in mouse hippocampal cells (HT22) by controlling Prdx6 and NF-κB regulation
TL;DR: It is proposed that using curcumin to reinforce the naturally occurring Prdx6 expression and attenuate ROS-based ER stress and NF-κB-mediated aberrant signaling improves cell survival and may provide an avenue to treat and/or postpone diseases associated with ROS or ER stress.
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Peroxiredoxin 6, a Novel Player in the Pathogenesis of Diabetes
Francesca Pacifici,Roberto Arriga,Gian Pio Sorice,Barbara Capuani,Maria Giovanna Scioli,Donatella Pastore,Giulia Donadel,Alfonso Bellia,Sara Caratelli,Andrea Coppola,Francesca Ferrelli,Massimo Federici,Giuseppe Sconocchia,Manfredi Tesauro,Paolo Sbraccia,David Della-Morte,Andrea Giaccari,Augusto Orlandi,Davide Lauro +18 more
TL;DR: It is demonstrated that PRDX6 is a key mediator of overt hyperglycemia in T2D glucose metabolism, opening new perspectives for targeted therapeutic strategies in diabetes care.
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Peroxiredoxin 6 phospholipid hydroperoxidase activity in the repair of peroxidized cell membranes.
Aron B. Fisher,Jose P. Vasquez-Medina,Chandra Dodia,Elena M. Sorokina,Jian-Qin Tao,Sheldon I. Feinstein +5 more
TL;DR: An important role for Prdx6 in recovery from membrane lipid peroxidation is confirmed and reduction of H2O2 or short chain hydroperoxides does not play a role in the recovery process.
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