| Project/Area Number |
02807031
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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 |
Pathological medical chemistry
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| Research Institution | Hamamatsu University School of Medicine |
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Principal Investigator |
FUJITA Michiya Hamamatsu University School of Medicine, Department of Biochemistry, Professor, 医学部・生化学第二, 教授 (60014031)
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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 |
¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 1991: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1990: ¥1,100,000 (Direct Cost: ¥1,100,000)
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| Keywords | calmodulin / adenylate cyclase / calmodulin-binding proteins / beta-adrenergic agents / synaptosomal membranes / CaM-kinase II / カルモデュリン結合タンパク貭 / 神経伝達 / ド-パミン作動性神経系 / カルモヂュリン / 協調的反強効果 / βアドレノセプタ- |
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| Research Abstract |
The calmodulin-binding proteins in rat striatal synaptosomal membranes were investigated with 12 5I-calmodulin overlay method after SDS-PAGE. Possible phosphorylation of the calmodulin-binding proteins and its effect on the affinity of the calmodulinbinding were also examined.
The above investigations produced the following results. Protein kinase A activity and its substrate(s)and a substrate(s)to calmodulin kinase II were detected in the synaptosomal membranes. ^<32>-P-autoradiography and ^<125>-I-calmodulin overlay demonstrated several calmodulin-binding proteins on SDS-PAGE.
Calmodulin-binding proteins were found to consist of Ca-dependent and -independent components. The recovery of the Ca-dependent component was not affected by the presence of Ca in the preparation medium, while that of the Ca-independent ones was reduced in the presence of Ca.
These findings demonstrated that the present synaptosomal membrane preparation could be used as a system suitable for the study of the roles of calmodulin in brain neuronal membranes.
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