O-GalNAz glycan imaging to understand amyloid beta generation
| Project/Area Number |
25840043
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Functional biochemistry
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| Research Institution | Institute of Physical and Chemical Research |
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Principal Investigator |
TACHIDA YURIKO 国立研究開発法人理化学研究所, 疾患糖鎖研究チーム, 技師 (70392024)
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2015: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2013: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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| Keywords | 糖鎖 / アルツハイマー病 / Clickケミストリー / O-結合型糖鎖 / APP / O結合型糖鎖 / Aβ |
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| Outline of Final Research Achievements |
Deposition of amyloid β-peptide (Aβ) in the brain parenchyma and cerebral vessels is closely associated with Alzheimer’s disease (AD). Aβ is generated from the amyloid precursor protein (APP) by multiple proteases. Our previous analysis of endothelial APP770 has shown that its O-glycosylated form is preferentially processed to generate Ab. In this study, we have visualized O-glycan with GalNAz and observed the intracellular trafficking of O-glycosylated APP770 by super-resolution microscopic analysis.
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Report
(4 results)
Research Products
(6 results)
