Source:http://linkedlifedata.com/resource/pubmed/id/14706620
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2004-1-6
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pubmed:abstractText |
Prion protein (PrP) binds copper and exhibits superoxide dismutase-like activity, while the roles of PrP in copper homeostasis remain controversial. Using Zeeman graphite furnace atomic absorption spectroscopy, we quantified copper levels in immortalized PrP gene (Prnp)-deficient neuronal cells transfected with Prnp and/or Prnd, which encodes PrP-like protein (PrPLP/Dpl), in the presence or absence of oxidative stress induced by serum deprivation. In the presence of serum, copper levels were not significantly affected by the expression of PrP and/or PrPLP/Dpl, whereas serum deprivation induced a decrease in copper levels that was inhibited by PrP but not by PrPLP/Dpl. The inhibitory effect of PrP on the decrease of copper levels was prevented by overexpression of PrPLP/Dpl. These findings indicate that PrP specifically stabilizes copper homeostasis, which is perturbed under oxidative conditions, while PrPLP/Dpl overexpression prevents PrP function in copper homeostasis, suggesting an interaction of PrP and PrPLP/Dpl and distinct functions between PrP and PrPLP/Dpl on metal homeostasis. Taken together, these results strongly suggest that PrP, in addition to its antioxidant properties, plays a role in stabilizing cellular copper homeostasis under oxidative conditions.
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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/Copper,
http://linkedlifedata.com/resource/pubmed/chemical/GPI-Linked Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Manganese,
http://linkedlifedata.com/resource/pubmed/chemical/PrPC Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Prions,
http://linkedlifedata.com/resource/pubmed/chemical/Prnd protein, mouse
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0006-291X
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pubmed:author |
pubmed-author:ItoharaShigeyoshiS,
pubmed-author:LeeDeug-chanDC,
pubmed-author:LehmannSylvainS,
pubmed-author:MatsumotoYoshitsuguY,
pubmed-author:NagasakaSeijiS,
pubmed-author:NittaKayakoK,
pubmed-author:OnoderaTakashiT,
pubmed-author:SaekiKeiichiK,
pubmed-author:SakaguchiSuehiroS,
pubmed-author:SakudoAkikazuA,
pubmed-author:YoshimuraEtsuroE
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
313
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
850-5
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:14706620-Animals,
pubmed-meshheading:14706620-Antioxidants,
pubmed-meshheading:14706620-Cell Line,
pubmed-meshheading:14706620-Copper,
pubmed-meshheading:14706620-GPI-Linked Proteins,
pubmed-meshheading:14706620-Homeostasis,
pubmed-meshheading:14706620-Male,
pubmed-meshheading:14706620-Manganese,
pubmed-meshheading:14706620-Mice,
pubmed-meshheading:14706620-Mice, Knockout,
pubmed-meshheading:14706620-Oxidation-Reduction,
pubmed-meshheading:14706620-PrPC Proteins,
pubmed-meshheading:14706620-Prions,
pubmed-meshheading:14706620-Transfection
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pubmed:year |
2004
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pubmed:articleTitle |
Prion protein suppresses perturbation of cellular copper homeostasis under oxidative conditions.
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pubmed:affiliation |
Department of Molecular Immunology, School of Agricultural and Life Sciences, University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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