| Project/Area Number |
16300111
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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 |
Nerve anatomy/Neuropathology
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| Research Institution | Shiga University of Medical Science |
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Principal Investigator |
TOOYAMA Ikuo Shiga University of Medical Science, Molecular Neuroscience Research Center, Professor, 分子神経科学研究センター, 教授 (20207533)
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| Co-Investigator(Kenkyū-buntansha) |
KIMURA Hiroshi Shiga University of Medical Science, Molecular Neuroscience Research Center, Professor, 分子神経科学研究センター, 教授 (40079736)
MATSUO Akinori Shiga University of Medical Science, Molecular Neuroscience Research Center, Research Assosiate, 分子神経科学研究センター, 助手 (20324585)
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| Project Period (FY) |
2004 – 2006
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| Project Status |
Completed (Fiscal Year 2006)
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| Budget Amount *help |
¥9,200,000 (Direct Cost: ¥9,200,000)
Fiscal Year 2006: ¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 2005: ¥2,700,000 (Direct Cost: ¥2,700,000)
Fiscal Year 2004: ¥4,300,000 (Direct Cost: ¥4,300,000)
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| Keywords | acetylcholine / cholinergic neurons / alternative splicing / antibody / learning / memory / alternative splicin |
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| Research Abstract |
Although most ChAT antibodies clearly stain central cholinergic neurons, it is difficult to reveal peripheral cholinergic system. The difficulty suggests that different forms of ChAT may exist in peripheral tissues. To test the hypothesis, we investigated the rat pterygopalatine ganglion, which is a structure that contains many cholinergic neurons sending their axons peripherally to cerebral vessels. From the experiments, we found a splice variant of ChAT mRNA expressed, not in the brain, but in the pterygopalatine. According to the genomic structure of ChAT, the variant lacks exons 6, 7, 8 and 9. The cDNA sequence has no frame shift and preserves regions of the ChAT protein which are essential for its catalytic function. Since the variant is expressed preferentially in peripheral tissues, we termed the form as pChAT(peripheral type of ChAT). And we termed the known ChAT as cChAT (common type of ChAT).
In this study, we investigated the structure of cChAT ad pChAT of human and monkey. We cloned cDNAs of cChAT and pChAT from the placenta of human and monkey. In the second step of our experiments, we produced antisera specific to cChAT and pChAT. Using these antisera, we investigated localizations of cChAT and pChAT proteins in the brain of rat, monkey and human. We have published the results in eleven papers of international journals (List in the next page). Findings of pChAT should facilitate investigations of cholinergic mechanism in the central and peripheral nervous system.
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