| Project/Area Number |
04670706
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
Psychiatric science
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| Research Institution | Nagoya City University |
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Principal Investigator |
SUZUKI Tatsuo Nagoya City University. Medical School Associate Professor, 医学部, 助教授 (80162965)
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| Co-Investigator(Kenkyū-buntansha) |
TANAKA Ryo Nagoya City University. Medical School Professor, 医学部, 教授 (90094383)
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| Project Period (FY) |
1992 – 1993
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| Project Status |
Completed (Fiscal Year 1993)
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| Budget Amount *help |
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1993: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 1992: ¥1,200,000 (Direct Cost: ¥1,200,000)
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| Keywords | Calmodulin kinaseII / Protein kinase C / autophosphorylation / long-term potentiation / calpain / calcium / tramslocation / カルモジュリンキナーゼII / Cキナーゼ |
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| Research Abstract |
1. A specific substrate for protein kinase C, distinct from contaminating myelin basic protein, was found in the postsynaptic density fraction prepared form rat cerebrum.
2. The cubstrate (250 kDa) of calmodulin kinase II associated with postsynaptic density was found to be related to P _<400> protein, and that of 200 kDa related to myosin.
3. We prepared an antibody that stecifically reacts with calmodulin kinase II autophosphorylated at Thr286/287 site. The antibody is a powerful tool to detect an active form of calmodulin kinase II both in vivo and in vitro.
4. Immunohistochemical analysis was done on rat brains using sntibody specifically reacting autophosphrylated CaMKII.Neurons in all subregions of hippocampus were stained in the rat in which kindling was established. Especially the somas and dendrites of CA1 region were strongly immunoreactive. The results suggest that activation of aclmodulin kinase II is involved in the development and maintenance of kindling.
5. We found elevation of Ca^<2+>-independent protein kinase C activity in the supermatant fraction and, concomitantly, limited proteolysis of protein linase C in the particulate fraction of rat hippocampi in which lang-term potentiation was induced. The experiment suggested that proteolytic conversion of protein kinase C may contribute to the maintenance of long0term patentiation. We also suggest that calpain is redponsible for the production of Ca_<2+>-indepadent form of protein kinase C.
6. We found that calmodulin kinase II, both alpha and beta/beta', artificially translocate into postsynaptic density after decapitation. The experiment suggested that the concentration of calmodulin kinase II in the PSD in vivo is not high as has been believed previously.
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