| Project/Area Number |
05454668
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Neurochemistry/Neuropharmacology
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| Research Institution | Kumamoto University |
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Principal Investigator |
MIYAMOTO Eishichi Kumamoto University, Pharmacology, Professor, 医学部, 教授 (50109659)
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| Co-Investigator(Kenkyū-buntansha) |
YAMAMOTO Hideyuki Kumamoto University, Pharmacology, Assistant Professor, 医学部, 講師 (60191433)
FUKUNAGA Kohji Kumamoto University, Pharmacology, Associate Professor, 医学部, 助教授 (90136721)
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| Project Period (FY) |
1993 – 1994
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| Project Status |
Completed (Fiscal Year 1994)
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| Budget Amount *help |
¥6,600,000 (Direct Cost: ¥6,600,000)
Fiscal Year 1994: ¥1,900,000 (Direct Cost: ¥1,900,000)
Fiscal Year 1993: ¥4,700,000 (Direct Cost: ¥4,700,000)
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| Keywords | Calcium mobilization / CaM kinase II / Neuron / Glia / Enzyme activation / Glutamate receptor / Long-term potentiation / Culturesd cell / プロテインホスファターゼ / 蛋白質燐酸化反応 |
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| Research Abstract |
Nerve impulses, various neurotransmitters, and growth hormones exert their effects through elevation of the intracellular concentration of calcium ion (Ca^<2+>). Ca^<2+> is involved in several types of neuronal functions including biosynthesis of neurotransmitters, stimulus-secretion coupling of neurotransmitters and hormones, microtubule assembly-diassembly cycle, synaptic plasticity, gene expression and many metabolic reactions. These include the short-term and long-term events with respect to time course. Although the precise molecular mechanisms mediating the actions of Ca^<2+> in the brain diverse, accumulating evidence suggests the effects of Ca^<2+> are mediated through Ca^<2+>-binding proteins. Furthermore, many of the functions are ultimately conducted by protein kinases and protein phosphatases in a Ca^<2+>-dependent manner. In an attempt to elucidate the functions in the central nervous system through calcium signaling pathways, we have been examining the dynamic state of activation of Ca^<2+>/calmodulin-dependent protein kinase II (CaM kinase II) in primary cultures of neurons and glias and established cell systems. We found that CaM kinase II is activated through elevation of intracellular Ca^<2+> in response to the extracellular stimuli. Firthermore, with concomitant activation of the enzyme, phosphorylation of endogenous substrates, activation of the enzyme and long-term potentiation were observed.
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