The Activity And Hydrogen Peroxide Sensitivity Of The Peroxiredoxins From The Parasitic Nematode Haemonchus Contortus

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Show simple item record Hudson, AL Sotirchos, IM Dayey, M 2012-10-12T03:34:20Z 2011-01
dc.identifier.citation Molecular And Biochemical Parasitology, 2011, 176 (1), pp. 17 - 24
dc.identifier.issn 0166-6851
dc.identifier.other C1 en_US
dc.description.abstract The requirement of aerobic organisms to control damage caused by reactive oxygen species has led to the evolution of the antioxidant systems. Peroxiredoxins are a large family of peroxidases which detoxify hydrogen peroxide at the expense of thiols. The parasitic nematode Haemonchus contortus contains two peroxiredoxins, HcPrx1 a mitochondrial protein and HcPrx2 a cytoplasmic protein. Although both peroxiredoxins contain the conserved eukaryotic motifs 'GGLG' and 'YF', identified as critical for hydrogen peroxide instability, both were stable to high concentrations of hydrogen peroxide, demonstrating different functions to their mammalian counterparts. H. contort-us also contains two thioredoxin reductases and five different thioredoxin-like proteins. The activity of both peroxiredoxins was specific for the thioredoxin system; however, both could also be regenerated by the glutathione system when coupled to the nematode specific thioredoxin HcTrx5. Analysis of homologous genes in Caenorhabditis elegans showed that only CePrx2, which is secreted, was sensitive to the external oxidant hydrogen peroxide. However, both peroxiredoxins KO C. elegans were sensitive to intracellular free radicals and both peroxiredoxins protected DNA from free radical attack. The results demonstrate that the hydrogen peroxide detoxification and the antioxidant activity of the peroxiredoxins are separate activities that are independent of the 'GGLG' and 'YF' motifs.
dc.publisher Elsevier Science Bv
dc.relation.isbasedon 10.1016/j.molbiopara.2010.11.006
dc.title The Activity And Hydrogen Peroxide Sensitivity Of The Peroxiredoxins From The Parasitic Nematode Haemonchus Contortus
dc.type Journal Article
dc.parent Molecular And Biochemical Parasitology
dc.journal.volume 1
dc.journal.volume 176
dc.journal.number 1 en_US
dc.publocation Amsterdam en_US
dc.identifier.startpage 17 en_US
dc.identifier.endpage 24 en_US SCI.Faculty of Science en_US
dc.conference Verified OK en_US
dc.for 110803 Medical Parasitology
dc.personcode 030905
dc.percentage 100 en_US Medical Parasitology en_US
dc.classification.type FOR-08 en_US
dc.edition en_US
dc.custom en_US en_US
dc.location.activity WOS:000287284800003 en_US
dc.description.keywords Thioredoxin Reductase; Escherichia-Coli; Biochemical-Characterization; Glutathione-Peroxidase; Substrate-Specificity; 2-Cys Peroxiredoxins; Schistosoma-Mansoni; Antioxidant; Systems; Protein en_US
dc.description.keywords Thioredoxin Reductase
dc.description.keywords Escherichia-Coli
dc.description.keywords Biochemical-Characterization
dc.description.keywords Glutathione-Peroxidase
dc.description.keywords Substrate-Specificity
dc.description.keywords 2-Cys Peroxiredoxins
dc.description.keywords Schistosoma-Mansoni
dc.description.keywords Antioxidant
dc.description.keywords Systems
dc.description.keywords Protein
pubs.embargo.period Not known
pubs.organisational-group /University of Technology Sydney
pubs.organisational-group /University of Technology Sydney/Faculty of Science
utslib.copyright.status Closed Access 2015-04-15 12:17:09.805752+10
utslib.collection.history Closed (ID: 3)

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