| Project/Area Number |
13672318
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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 |
Biological pharmacy
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| Research Institution | Nippon Veterinary and Animal Science University |
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Principal Investigator |
TATE Naoko Nippon Veterinary and Animal Science University, Veterinary, Associate, 獣医学部, 助教授 (00201955)
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| Project Period (FY) |
2001 – 2003
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| Project Status |
Completed (Fiscal Year 2003)
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| Budget Amount *help |
¥4,000,000 (Direct Cost: ¥4,000,000)
Fiscal Year 2003: ¥1,100,000 (Direct Cost: ¥1,100,000)
Fiscal Year 2002: ¥1,500,000 (Direct Cost: ¥1,500,000)
Fiscal Year 2001: ¥1,400,000 (Direct Cost: ¥1,400,000)
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| Keywords | neuron / Reelin / complex / structure / 円偏光二色性 / 層構造 |
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| Research Abstract |
Reelin is a key molecule of ordered neuronal alignment in the brain. I demonstrated that Rsslin molecules assembled with each other to form a huge protein complex both in vitro and in vivo, which is inhibited by the function-blocking CR-50 antibody (Proc. Natl. Acad. Sci., USA).
In this study, I first showed that the N-terminal 370 amino acids of Reelin that is an epitope against CR-50 antibody played an important role in order to form Reelin-Reelin interaction and this domain consisted of a-helix (20%) and β-sheet (40%) structure. This structure was important for the formation of Reelin complex. Secondary I examined the structure of the F-spondin-like domain which stayed up-stream of CR-50 epitope domain by circular dichroism spectroscopy. The result is that the the F-spondin-like domain had an a-helix (20%) and β-sheet (50%). Then, I analyzed this domain by analitycal gel filtration chromatography. The elution profile showed that the F-spondin-like domain form a homopolymer. Therefore, not only CR-50 epiope but also F-spondin-like domain was thought to contribute to form Reelin complex.
Then, in order to get the information of Reelin molecule structure by nuclear magnetic resonance (NMR) spectroscopy, I explored a new measurement technique of NMR spetroscopy.
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