| Project/Area Number |
18500242
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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 |
Neuroscience in general
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| Research Institution | Kobe University |
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Principal Investigator |
TANIGUCHI Taizo Kobe University, バイオシグナル研究センター, Visiting Medical Scientist (70346253)
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| Project Period (FY) |
2006 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥4,010,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥510,000)
Fiscal Year 2007: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
Fiscal Year 2006: ¥1,800,000 (Direct Cost: ¥1,800,000)
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| Keywords | Dementia / Animal model of dementia / Behavioral analysis / Brain and neural function / Medicine / Bioinformatics / Proteome analysis / 疾患モデル |
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| Research Abstract |
Proteome analysis of hippocampal proteins from dementia model mice SJLB
Proteins from the hippocampus of dementia model. mice SJLB and control mice are differentiated by 2D gel. Expression level or phosphorylation level of proteins were compared. Several proteins more or less expressed or phosphorylated in SJLB were found and identified by TOF-MS. The results were reported at the Neuro2007 and The 80^th Annual Meeting of The Japanese Pharmacological Science.
Proteome analysis of hippocampal proteins from SJLB before and after donepezil administration.
Proteins from the hippocampus of SJLB before and after donepezil administration were also analyzed. Several proteins changing the level of expression or phosphorylation were identified by TOF-MS. The results were reported at The 81^st Annual Meeting of The Japanese Pharmacological Science.
Analysis of the filament formation mechanism for the tau protein.
The heparin-induced self-aggregation of four repeat peptides (R1-R4) in an acidic solution
… More
(pH = 4.5) were investigated by fluorescence and circular dichroism (CD) measurements and compared with those in a neutral solution (pH = 7.5). The R1 peptide showed resistive behaviour for filament formation in the acidic solution. This is the first report on the markedly different self-aggregation behaviours of the repeat peptides and published in Biochem. Biophys. Res. Commun. 327, 712-718 (2006); J Biochem. 142, 49-54 (2007)
To examine the linkage-dependent contribution of each repeat peptide (R1-R4) to filament formation of the three- or four-repeat microtubule-binding domain (MBD) in the tau protein, four two-repeat peptides (R12, R13, R23 and R34) and two three-repeat peptides (R123 and R234) were prepared, and their in vitro self-aggregation was investigated. Systematic studies of the linkage-dependent contribution of each repeat peptide to the paired helical filament formation were carried out and the essential information for understanding the mechanism of the filament formation was reported in FEBS J. 275, 1529-39 (2008) Less
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