| Project/Area Number |
08670247
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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 |
Experimental pathology
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
NAMBA Yuziro KYOTO UNIVERSITY,Institute for Professor Virus Research, ウイルス研究所, 教授 (50027322)
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| Project Period (FY) |
1996 – 1997
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| Project Status |
Completed (Fiscal Year 1997)
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| Budget Amount *help |
¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1997: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1996: ¥1,500,000 (Direct Cost: ¥1,500,000)
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| Keywords | T lymphocyte / protein phosphorylation / cytoskeleton / growth signal |
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| Research Abstract |
The effect of phosphorylation of 1-plastin on its activity to bundle filamentous actin (F-actin) was investigated using highly purified 1-plastin obtained from a human T cell leukemia cell line. The experimental results indicated that the regulatory role of Ca ion on the actin-bundling activity of 1-plastin was substantially abolished by phosphorylation and the activity was extremely diminished even in very low concentration of Ca ion. It was presumed that in T lymphocytes phosphrylation of 1-plastin induced by IL-2 stimulation dissociate actin bundles and enhances the rearrangement of micrifilaments.
The protein kinase which phosphorylate 1-plastin was searched for in human leukemia cell line using the synthetic oligopeptide identical to the N-terminal portion of 1-plastin as the substrate of kinase assay. The results indicated that casein kinase 2 is the candidate that phosphorylate 1-plastin under IL-2 stimulation.
Using the monoclonal antibody which spesifically reacts with 1-plastin the localization of this protein in IL-2 dependent human T cell line was investigated. Under IL-2 free condition 1-plastin was localized in actin stress fiber. The distribution of this protein rapidly changed by IL-2 stimulation. Under this condition 1-plastin was distributed diffusely with relatively dense distribution in pseudopod indicating that the phosphorylation of 1-plastin contributes to the rearrangement of actin cytoskeleton.
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