| Project/Area Number |
21390491
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Morphological basic dentistry
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| Research Institution | Osaka University |
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Principal Investigator |
TOYOSAWA Satoru 大阪大学, 大学院・歯学研究科, 教授 (30243249)
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| Co-Investigator(Kenkyū-buntansha) |
NAKANO Takayoshi 大阪大学, 大学院・工学系研究科, 教授 (30243182)
SAEKI Makio 大阪大学, 大学院・歯学研究科, 講師 (30273692)
SATO Sunao 大阪大学, 大学院・歯学研究科, 講師 (70335660)
KISHINO Mitunobu 大阪大学, 大学院・歯学研究科, 助教 (60346161)
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| Co-Investigator(Renkei-kenkyūsha) |
KAGAWA Ryousuke 大阪大学, 歯学部附属病院, 医員 (40448147)
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| Project Period (FY) |
2009 – 2011
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| Project Status |
Completed (Fiscal Year 2011)
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| Budget Amount *help |
¥17,290,000 (Direct Cost: ¥13,300,000、Indirect Cost: ¥3,990,000)
Fiscal Year 2011: ¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2010: ¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2009: ¥8,450,000 (Direct Cost: ¥6,500,000、Indirect Cost: ¥1,950,000)
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| Keywords | 分子進化 / 生体内石灰化 / リン酸化 / 酸性リン蛋白質 / カゼインキナーゼ / 生体内石化化 / DMP1 / 石灰化 / 骨形成 |
|---|
| Research Abstract |
Dentin matrix protein 1(DMP1), which is a one of the acidic phosphoproteins composed of the bone. Molecular evolution study of DMP1 indicated that phosphorylation by casein kinase(CK) might be related to the DMP1 function. Highly phosphorylated DMP1 by CK has a large number of acidic domains. Because of its highly acidic nature, it is supposed that negative-charged DMP1 can bind to calcium, thereby regulating matrix mineralization. In this study, we found that Ser residues of DMP1 were phosphorylated in the bone and cultured osteoblast and that osteoblast-derived CK might phosphorylate DMP1. Culture experiment with CK inhibitor indicated that mineralization was controlled by inhibition of the CK activity. Therefore, it was supposed when DMP1 was phosphorylated by CK, and did negative-charged DMP1 promoted mineralization.
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