| Project/Area Number |
09480225
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Neurochemistry/Neuropharmacology
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| Research Institution | Tokyo Medical University |
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Principal Investigator |
MOCHIDA Sumiko Tokyo Medical University, Physiology, Associate professor, 医学部, 助教授 (30096341)
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| Co-Investigator(Kenkyū-buntansha) |
TAKAHASHI Masami Mitsubishi kasei Life Science Institute, Project Leader, 脳神経科学部, プロジェクトリーダー
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| Project Period (FY) |
1997 – 1999
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| Project Status |
Completed (Fiscal Year 1999)
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| Budget Amount *help |
¥10,500,000 (Direct Cost: ¥10,500,000)
Fiscal Year 1999: ¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1998: ¥3,800,000 (Direct Cost: ¥3,800,000)
Fiscal Year 1997: ¥4,600,000 (Direct Cost: ¥4,600,000)
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| Keywords | synaptic vesicles / neurotransmitter / exocytosis / prosynaptic proteins / CaィイD12+ィエD1-binding proteins / CaィイD12+ィエD1 channels / Ca^<2+>チャネル |
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| Research Abstract |
To examine roles for presynaptic protein-protein interactions in neurotransmitter release, synapses formed between rat superior cervical ganglion neurons in culture were employed. The synaptic protein interaction site of several presynaptic proteins were synthesized and introduced into the presynaptic neurons through a glass patch pipette, while measuring synaptic transmission evoked by presynaptic action potentials. The change in postsynaptic responses, we speculated the function of the proteins as follows.
1)CaィイD12+ィエD1-binding protein
(A)synaptotagmin : trigger of synaptic vesicle fusion, promotion of endocytosis.
(B)Doc2α-Munc 13 interacion : synaptic vesicle translocation to the release site.
2)SNARE-associating proteins
(A)N-type CaィイD12+ィエD1 channels : involved in synchronous transmitter release, voltage-dependent enhancement of transmitter release.
(B)P/Q-type CaィイD12+ィエD1 channels : involved in neurotransmitter release.
cSnapin : modulation of synaptotagmin-SNARE complex interaction.
(D)Syntaphilin : control of SNARE complex assembly by syntaxin-1 clamping.
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