Source:http://linkedlifedata.com/resource/pubmed/id/12715897
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
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| pubmed:dateCreated |
2003-4-28
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| pubmed:abstractText |
Cellular defense systems against reactive oxygen species (ROS) include thioredoxin reductase (TrxR) and glutathione reductase (GR). They generate sulfhydryl-reducing systems which are coupled to antioxidant enzymes, the thioredoxin and glutathione peroxidases (TPx and GPx). The fruit fly Drosophila lacks a functional GR, suggesting that the thioredoxin system is the major source for recycling glutathione. Whole genome in silico analysis identified two non-selenium containing putative GPx genes. We examined the biochemical characteristics of one of these gene products and found that it lacks GPx activity and functions as a TPx. Transgene-dependent overexpression of the newly identified Glutathione peroxidase homolog with thioredoxin peroxidase activity (Gtpx-1) gene increases resistance to experimentally induced oxidative stress, but does not compensate for the loss of catalase, an enzyme which, like GTPx-1, functions to eliminate hydrogen peroxide. The results suggest that GTPx-1 is part of the Drosophila Trx antioxidant defense system but acts in a genetically distinct pathway or in a different cellular compartment than catalase.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Catalase,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Peroxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Paraquat,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxidases,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxiredoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Reactive Oxygen Species
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| pubmed:status |
MEDLINE
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| pubmed:month |
Mar
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| pubmed:issn |
1431-6730
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
384
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
463-72
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| pubmed:dateRevised |
2007-11-15
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| pubmed:meshHeading |
pubmed-meshheading:12715897-Animals,
pubmed-meshheading:12715897-Animals, Genetically Modified,
pubmed-meshheading:12715897-Base Sequence,
pubmed-meshheading:12715897-Catalase,
pubmed-meshheading:12715897-Drosophila melanogaster,
pubmed-meshheading:12715897-Gene Expression,
pubmed-meshheading:12715897-Genes, Insect,
pubmed-meshheading:12715897-Glutathione Peroxidase,
pubmed-meshheading:12715897-Hyperoxia,
pubmed-meshheading:12715897-In Situ Hybridization,
pubmed-meshheading:12715897-Longevity,
pubmed-meshheading:12715897-Molecular Sequence Data,
pubmed-meshheading:12715897-Neoplasm Proteins,
pubmed-meshheading:12715897-Oxidative Stress,
pubmed-meshheading:12715897-Paraquat,
pubmed-meshheading:12715897-Peroxidases,
pubmed-meshheading:12715897-Peroxiredoxins,
pubmed-meshheading:12715897-Reactive Oxygen Species,
pubmed-meshheading:12715897-Sequence Alignment,
pubmed-meshheading:12715897-Transgenes
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| pubmed:year |
2003
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| pubmed:articleTitle |
A putative glutathione peroxidase of Drosophila encodes a thioredoxin peroxidase that provides resistance against oxidative stress but fails to complement a lack of catalase activity.
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| pubmed:affiliation |
Abteilung Molekulare Entwicklungsbiologie, Max-Planck-Institut für biophysikalische Chemie, Am Fassberg, D-37077 Göttingen, Germany.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|