Source:http://linkedlifedata.com/resource/pubmed/id/11369504
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
10
|
| pubmed:dateCreated |
2001-5-22
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| pubmed:abstractText |
Prion diseases are fatal neurodegenerative disorders resulting from conformational changes in the prion protein from its normal cellular isoform, PrPC, to the infectious scrapie isoform, PrP(Sc). In spite of many studies, the physiological function of PrPC remains unknown. Recent work shows that PrPC binds Cu2+, internalizing it into the cytoplasm. Since many antioxidant enzymes depend on Cu2+ (e.g., Cu/ZnSOD), their function could be affected in prion diseases. Here we investigate a possible relationship between PrP(C) and the cellular antioxidant systems in different structures isolated from PrPC knockout and wild-type mice by determining oxidative damage in protein and lipids and activity of antioxidant enzymes (CAT, SOD) and stress-adaptive enzymes (ODC). Our results show that, in the absence of PrPC, there is an increased oxidation of lipid and protein in all structures investigated. Decreased SOD activity and changes in CAT/ODC activities were also observed. Taking into account these results, we suggest that the physiological function of PrP(C) is related to cellular antioxidant defenses. Therefore, during development of prion diseases, the whole organism becomes more sensitive to ROS injury, leading to a progressive oxidative disruption of tissues and vital organs, especially the central nervous system.
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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/Antioxidants,
http://linkedlifedata.com/resource/pubmed/chemical/Catalase,
http://linkedlifedata.com/resource/pubmed/chemical/Ornithine Decarboxylase,
http://linkedlifedata.com/resource/pubmed/chemical/PrPC Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Reactive Oxygen Species,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxide Dismutase,
http://linkedlifedata.com/resource/pubmed/chemical/Thiobarbituric Acid Reactive...
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| pubmed:status |
MEDLINE
|
| pubmed:month |
May
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| pubmed:issn |
0891-5849
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
30
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1137-44
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| pubmed:dateRevised |
2010-4-8
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| pubmed:meshHeading |
pubmed-meshheading:11369504-Animals,
pubmed-meshheading:11369504-Antioxidants,
pubmed-meshheading:11369504-Brain,
pubmed-meshheading:11369504-Catalase,
pubmed-meshheading:11369504-Gene Deletion,
pubmed-meshheading:11369504-Lipid Peroxidation,
pubmed-meshheading:11369504-Liver,
pubmed-meshheading:11369504-Male,
pubmed-meshheading:11369504-Mice,
pubmed-meshheading:11369504-Mice, Inbred C57BL,
pubmed-meshheading:11369504-Mice, Inbred Strains,
pubmed-meshheading:11369504-Myocardium,
pubmed-meshheading:11369504-Ornithine Decarboxylase,
pubmed-meshheading:11369504-Oxidation-Reduction,
pubmed-meshheading:11369504-Oxidative Stress,
pubmed-meshheading:11369504-PrPC Proteins,
pubmed-meshheading:11369504-Reactive Oxygen Species,
pubmed-meshheading:11369504-Superoxide Dismutase,
pubmed-meshheading:11369504-Thiobarbituric Acid Reactive Substances
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| pubmed:year |
2001
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| pubmed:articleTitle |
Imbalance of antioxidant defense in mice lacking cellular prion protein.
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| pubmed:affiliation |
Laboratório de Estresse Oxidativo, Departamento de Bioquímica, ICBS-Universidade Federal do Rio Grande do Sul, Porto Alegre, Brazil. fklamt@zaz.com.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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