Ultramicrostructural analysis of biomineralization processes of DMP1
| Project/Area Number |
24390409
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (B)
|
| Allocation Type | Partial Multi-year Fund |
|---|
| Section | 一般 |
|---|
| Research Field |
Morphological basic dentistry
|
|---|
| Research Institution | Osaka University |
|---|
Principal Investigator |
TOYOSAWA Satoru 大阪大学, 歯学研究科(研究院), 教授 (30243249)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
YASUDA Hidehiro 大阪大学, 学内共同利用施設, 教授 (60210259)
MIURA Ichirou 大阪大学, 歯学部附属病院, 助教 (70437383)
ISHIMOTO Takuya 大阪大学, 工学研究科, 助教 (50508835)
SAEKI Makio 大阪大学, 工学研究科, 助教 (30273692)
USA Yu 大阪大学, 歯学部附属病院, 助教 (80444579)
|
|---|
| Co-Investigator(Renkei-kenkyūsha) |
KAGAWA Ryousuke 大阪大学, 歯学部附属病院, 医員 (40448147)
|
|---|
| Project Period (FY) |
2012-04-01 – 2015-03-31
|
| Project Status |
Completed (Fiscal Year 2014)
|
| Budget Amount *help |
¥15,990,000 (Direct Cost: ¥12,300,000、Indirect Cost: ¥3,690,000)
Fiscal Year 2014: ¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2013: ¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2012: ¥7,280,000 (Direct Cost: ¥5,600,000、Indirect Cost: ¥1,680,000)
|
|---|
| Keywords | 生体内石灰化 / dentin matrix protein 1 / 翻訳後修飾 / 超微構造 / 骨細胞 / リン酸化 / Fam20C |
|---|
| Outline of Final Research Achievements |
DMP1 (dentin matrix protein 1) is a non-collagenous matrix protein produced by osteocytes buried in bone matrix. DMP1 has a large number of phosphorylation sites and these regions become highly negative-charged domain after phosphorylation. The highly phosphorylated, negative-charged DMP1 may play an important role in the bone mineralization by recruiting Ca2+ and subsequent mineral deposition. In this study, ultramicrostructural analysis suggested DMP1 did not participate in initial calcification in the osteoid. Immunohistochemical analysis suggested after post-translational cleavage, DMP1 had a tendency to be localized at perilacunar matrix as an NH2-terminal fragment and at pericanalicular matrix as a COOH-terminal fragment. Further, COOH-terminal fragment at pericanalicular matrix was demonstrated to be highly phosphorylated. Therefore, highly phosphorylated, negative-charged COOH-terminal fragment at pericanalicular matrix may play an important role in the bone mineralization.
|
Report
(4 results)
Research Products
(9 results)
