Possible involvement of endoplasmic reticulum protein degradation in Alzheimer's disease
Project/Area Number |
21790089
|
Research Category |
Grant-in-Aid for Young Scientists (B)
|
Allocation Type | Single-year Grants |
Research Field |
Biological pharmacy
|
Research Institution | Chiba Institute of Science |
Principal Investigator |
KANEKO Masayuki Chiba Institute of Science, 薬学部, 講師 (10322827)
|
Project Period (FY) |
2009 – 2010
|
Project Status |
Completed (Fiscal Year 2010)
|
Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2010: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2009: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
|
Keywords | 小胞体ストレス / ERAD / アルツハイマー病 / ユビキチンリガーゼ / APP / 小胞体 / ニューロン / 神経変性疾患 |
Research Abstract |
HRD1 promotes degradation of unfolded proteins in the endoplasmic reticulum as a ubiquitin ligase. In the present study, we suggest the possible involvement of oxidative stresses in the decrease of HRD1 protein, which promotes degradation of amyloid precursor protein (APP), in the brain of Alzheimer's disease (AD) patient. Furthermore, we evaluated whether HRD1 knockout mice exhibited the phenotypes of AD. In addition, we found another ubiquitin ligase, which is involved in the APP protein metabolism.
|
Report
(3 results)
Research Products
(54 results)
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[Journal Article] Activation of ceramidase and ceramide kinase by vanadate via a tyrosine kinase-mediated pathway2010
Author(s)
Tada, E., Toyomura, K., Nakamura, H., Sasaki, H., Saito, T., Kaneko, M., Okuma, Y., Murayama, T.
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Journal Title
J.Pharmacol.Sci. 114
Pages: 420-432
NAID
Related Report
Peer Reviewed
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[Journal Article] Loss of HRD1-mediated protein degradation causes amyloid precursor protein accumulation and amyloid-beta generation2010
Author(s)
Kaneko, M., Koike, H., Saito, R., Kitamura, Y., Okuma, Y., Nomura, Y.
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Journal Title
J.Neurosci. 30
Pages: 3924-3932
Related Report
Peer Reviewed
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