| Project/Area Number |
25430071
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Neurochemistry/Neuropharmacology
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| Research Institution | Kitasato University |
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Principal Investigator |
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| Co-Investigator(Renkei-kenkyūsha) |
KOTERA Yoshio 北里大学, 理学部, 准教授 (60265733)
YAMAMORI Saori 北里大学, 医学部, 講師 (30464803)
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| Research Collaborator |
NAGATA Etsuko 北里大学, 医学部, 技術員
SUGAYA Tsukiko 北里大学, 医学部, 技術員
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| Project Period (FY) |
2013-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2015: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2014: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2013: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | NMDA受容体 / スパイン / タンパク質輸送 / D-セリン / ケタミン / FRAP / 樹状突起スパイン / プロテインキナーゼG / シナプス可塑性 / プロテインキナーゼＧ / シナプスタグ |
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| Outline of Final Research Achievements |
Newly synthesized proteins are thought to reconstitute PSD by substituting PSD components during establishment of sustained synaptic plasticity. We investigated transport from dendrites into spines of synaptic protein involved in the PSD reconstitution such as Homer1-a, and found 2 pathways. NMDA receptor-dependent Ca2+ influx triggered the synaptic activity-dependent transport, which depended on protein kinase G and was available for Homer1-a, but not for EGFP. The other is the D-serine pathway. D-serine activated transport of both EGFP and Homer1-a even when activity-dependent transport was inhibited. It was blocked by D-serine site antagonists and ketamine, which was respectively restored by application of D-serine. We conclude that NMDA receptor has a constitutive activity by which D-serine regulates protein transport in spines, and suggested that D-serine regulates protein-protein interaction between NMDA receptor and intraspinal protein transport components.
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