| Project/Area Number |
02670520
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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) |
1990 – 1991
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| Project Status |
Completed (Fiscal Year 1991)
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| Budget Amount *help |
¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1991: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1990: ¥1,200,000 (Direct Cost: ¥1,200,000)
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| Keywords | Postsynaptic Density / Calmodulin Kinase II / C Kinase / Long-Term Potentiation / キナ-ゼC |
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| Research Abstract |
Long-term potentiation(LTP)is an experimental model for memory and learning of higher animals. It is a well-known fact that intracellular rise in Ca^<2+> is essential requirement for generation of LTP. Little is known about the synaptic modulation triggered by the intracellular Ca^<2+> rise, though the involvement of protein kinase C, Ca^<2+>/calmodulin-dependent protein kinase 11(CaM KII), and/or calpain are indicated experimentally. For the purpose of making the synaptic change clearer we tried to characterize the substrates for the protein kinases associated with isolated postsynaptic density(PSD)-enriched fractions. Four major groups of substrates for the CaM KII(250k Mr, 200k Mr, 180k Mr, and 140k Mr)and one for kinase C(17k Mri were identified. Tlie 250k Mr substrate resembled P_<400> protein, IP_3 receptor, in structure. The 17k Mr substrate was different from myelin basic protein which was electrophoresed nearly at the same distance. We made an antibody against the 140k Mr substrates to obtain biological and physicochemical properties of the protein. We also made an antibody specific to the Thr_<286>-autophosphorylated and autonomous form of CaM KII. The latter antibody is an extremely useful reagent to understand the biological functions of the CaM KII, especially the role of kinase autophoshorylation in the modulation of the synaptic function such as in LTP.
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