| Project/Area Number |
11670942
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Psychiatric science
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| Research Institution | Osaka University |
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Principal Investigator |
NAKAMURA Yu Osaka University Graduate School of Medicine, Assistant professor, 医学系研究科, 助手 (70291440)
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| Co-Investigator(Kenkyū-buntansha) |
TANAKA Toshihisa Osaka University Graduate School of Medicine, Assistant Professor, 医学系研究科, 助手 (10294068)
KUDO Takashi Osaka University Graduate School of Medicine, Lecturer, 医学系研究科, 講師 (10273632)
TAKEDA Masatoshi Osaka University Graduate School of Medicine, Professor, 医学系研究科, 教授 (00179649)
YOSHIDA Shigefaka Nara Institute of Science and Technology Graduate School of Biological Science Associate Professor, バイオサイエンス科, 助教授 (20230740)
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| Project Period (FY) |
1999 – 2000
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| Project Status |
Completed (Fiscal Year 2000)
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| Budget Amount *help |
¥3,300,000 (Direct Cost: ¥3,300,000)
Fiscal Year 2000: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 1999: ¥2,500,000 (Direct Cost: ¥2,500,000)
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| Keywords | neurofilament / phosphorylation / PKA / PKC / Alzheimer / phoshorylation / Rh0 |
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| Research Abstract |
Long-term potentiation (LTP) is a cellular model of neuronal plasticity that is thought to involve the phosphorylation of various proteins. NF-L is considered a possible substrate for phosphorylation. First, we prepared site-specific phosphorylation-dependent antibodies (abNFL26) against the phosphorylation site Ser-26 of Rho-kinase. The in vitro specificity of those antibodies were appreciated by dot and western blot analyses. During LTP stimulation of mouse hippocampal slices, the series of the site-specific phosphorylation-dependent antibodies against the phosphorylation sites, Ser-26, -51, -55, -57, demonstrates the increase in the phosphorylation level of Ser57 in NF-L, and the visualization of the localized distribution of Ser57 phosphorylation in a subpopulation of apical dendrites of the pyramidal neurons. Furthermore, Ser57 phosphorylation during LTP is suggested to be mediated by CaMKII.We show that NF-L is phosphorylated by CaMKII in a subpopulation of the apical dendrites during LTP, indicating that Ser57 is a novel phosphorylation site of NF-L in vivo related to the neuronal signal transduction. And these data implies that the phosphorylation of NF-L by CaMKII might be influenced, resulting in memory dysfuctions.
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