| pubmed-article:12914801 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12914801 | lifeskim:mentions | umls-concept:C0033164 | lld:lifeskim |
| pubmed-article:12914801 | lifeskim:mentions | umls-concept:C0007600 | lld:lifeskim |
| pubmed-article:12914801 | lifeskim:mentions | umls-concept:C0684336 | lld:lifeskim |
| pubmed-article:12914801 | lifeskim:mentions | umls-concept:C0521390 | lld:lifeskim |
| pubmed-article:12914801 | lifeskim:mentions | umls-concept:C0038838 | lld:lifeskim |
| pubmed-article:12914801 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:12914801 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:12914801 | pubmed:dateCreated | 2003-8-13 | lld:pubmed |
| pubmed-article:12914801 | pubmed:abstractText | Previous studies have reported a neuroprotective role for cellular prion protein (PrP(C)) against apoptosis induced by serum deprivation in an immortalized prion protein gene (Prnp)-deficient neuronal cell line, but the mechanisms remain unclear. In this study, to investigate the mechanisms by which PrP(C) prevents apoptosis, the authors compared apoptosis of Prnp(-/-) cells with that of Prnp(-/-) cells expressing the wild-type PrP(C) or PrP(C) lacking N-terminal octapeptide repeat region under serum-free conditions. Re-introduction of Prnp rescued cells from apoptosis, upregulated superoxide dismutase (SOD) activity, enhanced superoxide anion elimination, and inhibited caspase-3/9 activation. On the other hand, N-terminally truncated PrP(C) enhanced apoptosis accompanied by potentiation of superoxide production and caspase-3/9 activation due to inhibition of SOD. These results suggest that PrP(C) protects Prnp(-/-) cells from apoptosis via superoxide- and caspase-3/9-dependent pathways by upregulating SOD activity. Furthermore, the octapeptide repeat region of PrP(C) plays an essential role in regulating apoptosis and SOD activity. | lld:pubmed |
| pubmed-article:12914801 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12914801 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12914801 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12914801 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12914801 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12914801 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12914801 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12914801 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12914801 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12914801 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12914801 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12914801 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12914801 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:12914801 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:12914801 | pubmed:author | pubmed-author:ItoharaShigey... | lld:pubmed |
| pubmed-article:12914801 | pubmed:author | pubmed-author:MatsumotoYosh... | lld:pubmed |
| pubmed-article:12914801 | pubmed:author | pubmed-author:OnoderaTakash... | lld:pubmed |
| pubmed-article:12914801 | pubmed:author | pubmed-author:InoueKeiichiK | lld:pubmed |
| pubmed-article:12914801 | pubmed:author | pubmed-author:NakamuraYukoY | lld:pubmed |
| pubmed-article:12914801 | pubmed:author | pubmed-author:SaekiKeiichiK | lld:pubmed |
| pubmed-article:12914801 | pubmed:author | pubmed-author:SakudoAkikazu... | lld:pubmed |
| pubmed-article:12914801 | pubmed:author | pubmed-author:LeeDeug-chanD... | lld:pubmed |
| pubmed-article:12914801 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12914801 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:12914801 | pubmed:volume | 308 | lld:pubmed |
| pubmed-article:12914801 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12914801 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12914801 | pubmed:pagination | 660-7 | lld:pubmed |
| pubmed-article:12914801 | pubmed:dateRevised | 2006-11-28 | lld:pubmed |
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| pubmed-article:12914801 | pubmed:meshHeading | pubmed-meshheading:12914801... | lld:pubmed |
| pubmed-article:12914801 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12914801 | pubmed:articleTitle | Impairment of superoxide dismutase activation by N-terminally truncated prion protein (PrP) in PrP-deficient neuronal cell line. | lld:pubmed |
| pubmed-article:12914801 | pubmed:affiliation | Department of Molecular Immunology, School of Agricultural and Life Sciences, University of Tokyo, Japan. | lld:pubmed |
| pubmed-article:12914801 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12914801 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:12914801 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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