Alterations of proteolytic processing of synaptic adhesion molecules in Alzheimer disease
Project/Area Number |
24659028
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Research Category |
Grant-in-Aid for Challenging Exploratory Research
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Allocation Type | Multi-year Fund |
Research Field |
Biological pharmacy
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Research Institution | The University of Tokyo |
Principal Investigator |
TOMITA Taisuke 東京大学, 大学院・薬学系研究科, 准教授 (30292957)
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Project Period (FY) |
2012
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Project Status |
Completed (Fiscal Year 2012)
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Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2012: ¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
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Keywords | 神経細胞 / シナプス / 接着分子 |
Research Abstract |
In brain, each single neuron is connected to other neurons via synapses. Synapses can change their strength in response to neuronal activity, and synaptic adhesion molecules are implicated in the synapse plasticity. However, the metabolism of the synaptic adhesion molecules remains unknown. In the research, we found that neuroligin 1, which is associated with autism spectrum disorder, is sequentially processed by two proteases. This processing is modulated by synaptic activity and negatively regulates synapse formation in vivo.
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Report
(2 results)
Research Products
(19 results)
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[Journal Article] Effect of Helical Conformation and Side-Chain Structure on y-Secretase Inhibition by β-Peptide Foldamers : Insight into Substrate Recognition2013
Author(s)
Yuki Imamura, Naoki Umezawa, Satoko Osawa, Naoaki Shimada, Takuya Higo, Satoshi Yokoshima, Tohru Fukuyama, Takeshi Iwatsubo, Nobuki Kato, Taisuke Tomita, Tsunehiko Higuchi
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Journal Title
J. Med. Chem.
Volume: 56
Issue: 4
Pages: 1443-1454
DOI
Related Report
Peer Reviewed
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[Journal Article] Activity-dependent proteolytic cleavage of neuroligin-12012
Author(s)
Suzuki K, Hayashi Y, Nakahara S, Kumazaki H, Prox J, Horiuchi K, Zeng M, Tanimura S, Nishiyama Y, Osawa S, Sehara-Fujisawa A, Saftig P, Yokoshima S, Fukuyama T, Matsuki N, Koyama R, Tomita T, Iwatsubo T.
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Journal Title
Neuron
Volume: 76(2)
Issue: 2
Pages: 410-422
DOI
Related Report
Peer Reviewed
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