| Project/Area Number |
16590387
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Virology
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| Research Institution | Nagasaki University |
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Principal Investigator |
SAKAGUCHI Suehiro Nagasaki University, Graduate School of Biomedical Sciences, Associate Professor, 大学院・医歯薬学総合研究科, 助教授 (60274635)
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| Project Period (FY) |
2004 – 2005
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| Project Status |
Completed (Fiscal Year 2005)
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| Budget Amount *help |
¥3,100,000 (Direct Cost: ¥3,100,000)
Fiscal Year 2005: ¥1,500,000 (Direct Cost: ¥1,500,000)
Fiscal Year 2004: ¥1,600,000 (Direct Cost: ¥1,600,000)
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| Keywords | prion protein / yeast two-hybrid / binding molecule / prion / prion disease / cell death / aggregate / yeast-two hyb |
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| Research Abstract |
To elucidate the normal function of cellular isoform of prion protein, designated PrP^c, we tried to identify a PrP^c-binding molecule(s) by a yeast two-hybrid screening using a mouse brain cDNA library. A splicing variant of synaptic glycoprotein 2 (Gpsn2), named sGpsn2, was isolated as a PrP^c-binding molecule. In sGpsn2, the forth exon encoding 15 amino acids was splicing out. Interestingly, transient expression of sGpsn2 markedly induced death of COS-7 cells and the cell death was blocked by co-expression of PrP^c. We do not know whether Gpsn2 also could induce similar cell death in COS-7 cells. On Western blotting of the cells expressing sGpsn2, smearing signals for sGpsn2 were detected with molecular weights higher than 250 kDa, suggesting that sGpsn2 might be aggregated in the cells. Taken together, these results suggest that PrP^c could be involved in the cellular protection from the abnormal protein aggregate-induced cell death.
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