| Project/Area Number |
11680746
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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 |
Nerve anatomy/Neuropathology
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| Research Institution | Azabu University (2000-2001)
The Institute of Physical and Chemical Research (1999) |
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Principal Investigator |
MURAYAMA Ohoshi Azabu University, Lab of Molecular Biol., College of Environmental Health Sciences, Associate Professor, 環境保健学部, 講師 (20301781)
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| Co-Investigator(Kenkyū-buntansha) |
TAKASHIMA Akihiko Azabu University, Lab for Alzheimer's Disease, BSI, RIKEN, Laboratory head, アルツハイマー病研究チーム, チームリーダー(研究職) (00154774)
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| Project Period (FY) |
1999 – 2001
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥2,600,000 (Direct Cost: ¥2,600,000)
Fiscal Year 2001: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 2000: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1999: ¥1,200,000 (Direct Cost: ¥1,200,000)
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| Keywords | Alzheimer's disease / FTDP-17 / tau protein / yeast two-hybrid / neuronal cell death / 酵母two-hybrid / 神経原繊維変化 / タウタンパク質 / Yeast Two-hybrid |
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| Research Abstract |
Neurofibrillary tangles (NFT) is one of the major pathological changes in brain of Alzheimer's disease patients. NFT is composed of the hyperphosphorylated tau observed in tauopathy. Recently tau mutation has been found in familial case of tauopathy, FTDP-17, which is characterized by NFT and loss of neurons. This finding suggests that the mutant tau protein causes NFT and neuronal death. Moreover, NFT-like pathological changes are present in cortex, hippicampus or spinal cord of transgenic mice expressing the mutant tau protein. These mice have shown behavioral disorders. Hence tau may be involved in developing the neurodegeneration of Alzheimer's disease and other tauopathies. However, a role of tau in neurodegeneration remains unclear. To understand the mechanism of neurodegeneration through tau, we screen proteins associating with tau protein by yeast two-hybrid system. Yeast (CG1945-T4R) expressing GAL4-DNA-BD/tau fusion proitein was transformed by human brain cDNA library constructed with pACT2, GAL4AD expression vector. Two positive clones associating with tau were selected on minimal SD plate without Trp, Leu and His. Interaction between tau and the expressed proteins of positive clones in culture cells were confirmed by immunoprecipitaion and immunostaining.
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