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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2003-8-13
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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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, Serum-Free,
http://linkedlifedata.com/resource/pubmed/chemical/PrPC Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Prions,
http://linkedlifedata.com/resource/pubmed/chemical/Prnp protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-bcl-2,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxide Dismutase,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxides
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
308
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
660-7
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pubmed:dateRevised |
2006-11-28
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pubmed:meshHeading |
pubmed-meshheading:12914801-Amyloid,
pubmed-meshheading:12914801-Animals,
pubmed-meshheading:12914801-Apoptosis,
pubmed-meshheading:12914801-Caspases,
pubmed-meshheading:12914801-Cell Line,
pubmed-meshheading:12914801-Culture Media, Serum-Free,
pubmed-meshheading:12914801-Enzyme Activation,
pubmed-meshheading:12914801-Male,
pubmed-meshheading:12914801-Mice,
pubmed-meshheading:12914801-Mice, Inbred C57BL,
pubmed-meshheading:12914801-Mice, Knockout,
pubmed-meshheading:12914801-Neurons,
pubmed-meshheading:12914801-PrPC Proteins,
pubmed-meshheading:12914801-Prions,
pubmed-meshheading:12914801-Protein Precursors,
pubmed-meshheading:12914801-Proto-Oncogene Proteins c-bcl-2,
pubmed-meshheading:12914801-Repetitive Sequences, Amino Acid,
pubmed-meshheading:12914801-Sequence Deletion,
pubmed-meshheading:12914801-Superoxide Dismutase,
pubmed-meshheading:12914801-Superoxides
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pubmed:year |
2003
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pubmed:articleTitle |
Impairment of superoxide dismutase activation by N-terminally truncated prion protein (PrP) in PrP-deficient neuronal cell line.
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pubmed:affiliation |
Department of Molecular Immunology, School of Agricultural and Life Sciences, University of Tokyo, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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