| Project/Area Number |
17591135
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Pediatrics
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| Research Institution | Institute for Developmental Research, Aichi Human Service Center |
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Principal Investigator |
TOKITA Yoshihito Institute for Developmental Research, Aichi Human Service Center, Institute for Developmental Research Department of Perinatology, Senior scientist (50291175)
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| Project Period (FY) |
2005 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥3,800,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥300,000)
Fiscal Year 2007: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2006: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 2005: ¥1,500,000 (Direct Cost: ¥1,500,000)
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| Keywords | Chondroitinsulfate / Proteoglycan / synapse / spine / developmental disorder / 神経細胞 / フィロポディア |
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| Research Abstract |
Neuroglycan C is a membrane-spanning chondroitin sulfate proteoglycan involved in presynaptic formation in early postnatal stages in vivo. Neuroglycan C is located dendritic filopodia and spines both in vitro and in vivo. In this study, we found that a treatment of an antibody against neuroglycan C ectodomain translocates neuroglycan C to neuronal cell body from dendritic spine in primary cultured neuron. Numerous immunopositive vesicles were observed in cell soma of cultured neurons after the antibody treatment. The finding suggests thats neuroglycan C with dimmer formation could act as other trancemembrane type receptors for signaling molecule. Actually, a dimer form of neuroglycan C is detected with a western blotting of rat brain. Therefore, we investigated the effect of anti-neuroglycan C antibody on spine shape and neurite morphogenesis in vitro. The antibody collapses phalloidin positive growth cone and dendritic spines of cultured neuron. In addition to this, long term treatment of the antibody results in the reduction of MAP2 positive neurites, dendrites.
These results suggest that an unknown ligand for neuroglycan C that could interact with neuroglycan C ectodomain stimulates reorganization of cytoskeleton such as actin fiber and also microtubules via dimer formation of Neuroglycan C. Neuroglycan C dimer may activate intracellular signalings linking to neurite retraction. Endogenous ligand for neuroglycan C should be clarified to understand physiological function of neuroglycan C.
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