2012 Fiscal Year Final Research Report
Study of the molecular mechanisms of abnormal prion protein (PrP) production by exploration of PrP-interacting molecules.
| Project/Area Number |
23780313
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Applied veterinary science
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| Research Institution | National Agriculture and Food Research Organization |
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Principal Investigator |
IWAMARU Yoshifumi 独立行政法人農業・食品産業技術総合研究機構, 動物衛生研究所・プリオン病研究センター, 主任研究員 (20355142)
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| Project Period (FY) |
2011 – 2012
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| Keywords | プリオン / 界面活性剤不溶膜画分 / ラフト |
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| Research Abstract |
Prion diseases are transmissible, fatal, neurodegenerative disorders. One of the hallmarks of prion diseases is progressive accumulation of a misfolded and protease-resistant isoform (PrP^<Sc>) of protease-sensitive prion protein (PrP^C) which is a host-encoded glycoprotein attached to the lipid-raft on the membrane. The conversion of PrPC into PrPSc seems to take place at the cell surface or along the endocytic pathway, however, the molecular basis of the conversion remains unclear, particularly regarding role of other cellular factors in prion replication.In this study, to understand the molecular events in the conversion, we analyzed what molecules interact with PrP^C in lipid-raft enriched detergent resistant microdomains (DRM) using the enzyme-mediated activation of radical sources (EMARS), a newly established biochemical labeling method for cell surface molecules. We demonstrated that neuronal microtubule regulatoryphosphoprotein, Sthatmin2 was colocalized with PrP in N2a cells.
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