2017 Fiscal Year Final Research Report
Acceleration of fracture healing by growth factor fused with tandem collagen-binding domains from Clostridium histolyticum collagenase
| Project/Area Number |
15K20015
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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 |
Orthopaedic surgery
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| Research Institution | Kitasato University |
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Principal Investigator |
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Keywords | 骨折治癒促進 / コラーゲン結合型成長因子 / コラーゲン結合ドメイン |
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| Outline of Final Research Achievements |
We examined the binding affinity of four collagen anchors derived fromthe two clostridial collagenases to H-Gly-Pro-Arg-Gly-(Pro-Hyp-Gly)12-NH2, a collagenous peptide, by surface plasmon resonance and found that tandem CBDs (s3a-s3b) have the highest affinity for the collagenous peptide.We also constructed four fusion proteins consisting of bFGF and s3 (bFGF-s3), s2b-s3b (bFGF-s2b-s3), s3b (bFGF-s3b), and s3a-s3b (bFGF-s3a-s3b) and compared their biological activities to those of a previous fusion construct (bFGF-s2b-s3) using a cell proliferation assay in vitro and a mouse femoral fracture model in vivo. Among these CB-bFGFs, bFGF-s3a-s3b showed the highest capacity to induce mesenchymal cell proliferation and callus formation in the mice fracture model. The poly(Pro-Hyp-Gly)10/bFGF-s3a-s3b
construct may therefore have the potential to promote bone formation in clinical settings.
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| Free Research Field |
整形外科学
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