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

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dc.contributor.author Hudson, Amanda en_US
dc.contributor.author Sotirchos, Irene en_US
dc.contributor.author Dayey, Mw en_US
dc.contributor.editor en_US
dc.date.accessioned 2012-10-12T03:34:20Z
dc.date.available 2012-10-12T03:34:20Z
dc.date.issued 2011 en_US
dc.identifier 2010004744 en_US
dc.identifier.citation Hudson Amanda, Sotirchos Irene, and Dayey Mw 2011, 'The Activity And Hydrogen Peroxide Sensitivity Of The Peroxiredoxins From The Parasitic Nematode Haemonchus Contortus', Elsevier Science Bv, vol. 176, no. 1, pp. 17-24. en_US
dc.identifier.issn 0166-6851 en_US
dc.identifier.other C1 en_US
dc.identifier.uri http://hdl.handle.net/10453/18534
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. en_US
dc.language en_US
dc.publisher Elsevier Science Bv en_US
dc.relation.isbasedon http://dx.doi.org/10.1016/j.molbiopara.2010.11.006 en_US
dc.title The Activity And Hydrogen Peroxide Sensitivity Of The Peroxiredoxins From The Parasitic Nematode Haemonchus Contortus en_US
dc.parent Molecular And Biochemical Parasitology en_US
dc.journal.volume 176 en_US
dc.journal.number 1 en_US
dc.publocation Amsterdam en_US
dc.identifier.startpage 17 en_US
dc.identifier.endpage 24 en_US
dc.cauo.name SCI.Faculty of Science en_US
dc.conference Verified OK en_US
dc.for 110803 en_US
dc.personcode 030905 en_US
dc.personcode 99068203 en_US
dc.personcode 0000069969 en_US
dc.percentage 100 en_US
dc.classification.name Medical Parasitology en_US
dc.classification.type FOR-08 en_US
dc.edition en_US
dc.custom en_US
dc.date.activity 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.staffid en_US


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