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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Effects of a human-based mixture of persistent organic pollutants on the in vivo exposed cerebellum and cerebellar neuronal cultures exposed in vitro
Hanne Friis Berntsen,Nur Duale,Cesilie Granum Bjørklund,Oscar D Rangel-Huerta,Kine Dyrberg,Tim Hofer,Kirsten Eline Rakkestad,Gunn Charlotte Østby,Ruth Halsne,Gudrun Seeberg Boge,Ragnhild E. Paulsen,Oddvar Myhre,Erik Ropstad +12 more
TL;DR: It is shown that early-life exposure to mixtures of POPs can cause adverse neurodevelopmental effects and differential expression of genes involved in apoptosis, oxidative stress, neurotransmission and cerebellar development are revealed.
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Peroxiredoxin 6 is a natural radioprotector.
Mars G. Sharapov,Sergey V. Gudkov,A. E. Gordeeva,O. E. Karp,V. E. Ivanov,O V Shelkovskaya,Vadim I. Bruskov,Vladimir I. Novoselov,E. E. Fesenko +8 more
TL;DR: In the irradiated animals, peroxiredoxin 6 decreased the severity of radiation-induced leucopenia, granulocytopenia, and thrombocytopensia, increased the number of blood corpuscles, and prevented the mass death of epithelial cells and the destruction of the small intestine.
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Involvement of retinoic acid-induced peroxiredoxin 6 expression in recovery of noise-induced temporary hearing threshold shifts.
TL;DR: Findings suggest that ATRA-induced Pr dx 6 expression may be associated with rapid recovery from temporary NIHL, and RA receptor α (RARα) functions as a transactivator of Prdx 6 gene expression.
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Antioxidants Special Issue: Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family.
TL;DR: The peroxiredoxins, first discovered about 30 years ago, are the most recently described family of ubiquitously expressed antioxidant enzymes.
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Peroxiredoxin 6 promotes upregulation of the prion protein (PrP) in neuronal cells of prion-infected mice
TL;DR: Besides its possible function as a novel marker protein in the diagnosis of TSEs, PDRX6 represents an attractive target molecule in putative pharmacological intervention strategies in the future.
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