2004 Fiscal Year Final Research Report Summary
Functional analyses of Exip, a new splicing variant of p38 which binds to anti-inflammatory drug.
| Project/Area Number |
15510188
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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 |
Living organism molecular science
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| Research Institution | RIKEN |
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Principal Investigator |
SUDO Tatsuhiko RIKEN, Antibiotics Laboratory, Senior Research Scientist, 長田抗生物質研究室, 先任研究員 (30260227)
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| Project Period (FY) |
2003 – 2004
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| Keywords | p38 / Exip / Tollip / IL-1 / IRAK / Innate immunity / Inflammatory / Splicing |
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| Research Abstract |
Based on the plan, the experiments were conducted and the results mentioned below were obtained.
1.Analysis of an Exip binding protein
By using yeast two-hybrid screening, we found that Exip, but not p38α, binds to Tollip (Toll interacting protein) which is involved in Interleukin-1(IL-1) signaling pathway as a component of the receptor proximal complex and impaired NF-κB activity. Moreover, Exip binds to another component of the complex, IRAK (IL-1 associating kinase). Exogenous-expression of Exip resulted in down-regulation of NF-κB activities both in HeLa and HEK293T cells. Together, these results demonstrate that Exip can be a new component of NF-κB pathway, and contribute to a comprehensive understanding of the signal transduction pathway in the inflammatory responses
2.Regulation of Exip expression
By using newly raised antibody specific for Exip, we identified that the antibody specifically recognize Exip in HL-60 and THP-1 in addition to exogenously expressed Exip. Its expression was enhanced by heat treatment but not by inflammatory cytokines.
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Research Products
(12 results)
