BMP-induced bone formation in binding site between p65 subunit of NF-kB and Smad4
| Project/Area Number |
26861556
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Functional basic dentistry
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| Research Institution | Kyushu University (2015-2016)
Kyushu Dental College (2014) |
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Principal Investigator |
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥3,770,000 (Direct Cost: ¥2,900,000、Indirect Cost: ¥870,000)
Fiscal Year 2015: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2014: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | SMAD4 / NF-kB / BMP2 / NF-κB / BMP / 結合領域 / BMPシグナル / NF-kBシグナル |
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| Outline of Final Research Achievements |
Bone morphogenic proteins (BMPs) are essential for bone formation in vivo and osteoblast differentiation in vitro via a Smad signaling pathway. The transcription factor NF-kB plays a key role in immune and inflammatory responses, proliferation and tumorigenesis. Recent findings revealed the importance of NF-kB in osteoblast differentiation and bone formation. We also showed that NF-kB inhibits BMP-induced osteoblast differentiation via interaction between MH1 domain (MH1) of Smad4 and TA2 domain (TA2) of NF-kB, p65 subunit. To identify the binding site between Smad4-MH1 and p65-TA2, we investigated interaction of these molecules using purified recombinant proteins of Smad4-MH1 and p65-TA2. We revealed that each molecules are directly bound. The peptide which based amino acid sequence of binding region of TA2 inhibited the suppression of BMP signal by p65, suggesting that the peptide is able to be a novel target protein of osteoblast differentiation.
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Report
(4 results)
Research Products
(3 results)
