2011 Fiscal Year Final Research Report
A possible mechanism for PrP^<Sc> formation through modification with a lipid peroxidation product hydroxylnonenal at the membrane interface
| Project/Area Number |
22658095
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Single-year Grants |
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| Research Field |
Applied veterinary science
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| Research Institution | Hokkaido University |
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Principal Investigator |
INABA Mutsumi 北海道大学, 大学院・獣医学研究科, 教授 (00183179)
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| Co-Investigator(Kenkyū-buntansha) |
SATO Kota 北海道大学, 大学院・獣医学研究科, 准教授 (50283974)
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| Project Period (FY) |
2010 – 2011
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| Keywords | 脂質過酸化 / ヒドロキシノネナール / 膜 / プリオン病 / 病態 |
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| Research Abstract |
Pathogenesis of prion diseases involves transition of PrP^C into PrP^<Sc>. The purpose of this study was to examine if the lipid peroxidation product, 4-hydroxy nonenal(HNE) would modify the structure of PrP^C through formation of PrP^C-HNE adducts and trigger the formation of insoluble PrP^<Sc>. The mass spectrometry analysis showed that PrP^C was accessible to HNE modification when the cells expressing PrP^Cwere exposed to exogenous HNE. However, the content of proteinase K-resistant PrP bearing HNE adducts was negligible, indicating that HNE modification would not be a sole cause for PrP^<Sc> formation.
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[Journal Article] Parallel reductions in stomatin and Na, K-ATPase through the exosomal pathway during reticulocyte maturation in dogs : stomatin as a genotypic and phenotypic marker of high K^+and low K^+red cells2010
Author(s)
Komatsu, T., Sato, K., Otsuka, Y., Arashiki, N., Tanaka, K., Tamahara, S., Ono, K., and Inaba, M.
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Journal Title
J. Vet. Med. Sci.
Volume: 72
Pages: 893-901
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[Journal Article] Covalent modification of spectrin in red cell membranes by the lipid peroxidation product 4-hydroxy-2-nonenal.2010
Author(s)
Arashiki, N., Otsuka, Y., Ito, D., Yang, M., Komatsu, T., Sato, K., and Inaba, M.
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Journal Title
Biochem. Biophys. Res. Commun.
Volume: 391
Pages: 1543-1547
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