Project/Area Number |
21590068
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Biological pharmacy
|
Research Institution | Iwate Medical University |
Principal Investigator |
|
Co-Investigator(Kenkyū-buntansha) |
二井 將光 岩手医科大学, 薬学部, 教授 (50012646)
後藤 奈緒美 岩手医科大学, 薬学部, 助教 (80403971)
|
Co-Investigator(Renkei-kenkyūsha) |
FUTAI Masamitsu 岩手医科大学, 薬学部, 教授 (50012646)
GOTO Naomi 岩手医科大学, 薬学部, 助教 (80403971)
|
Project Period (FY) |
2009 – 2011
|
Project Status |
Completed (Fiscal Year 2011)
|
Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2011: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2010: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2009: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
|
Keywords | プロトンポンプ / 一分子観察 / 破骨細胞 / 酸性環境 / 骨代謝 / 分泌 |
Research Abstract |
We have found that osteoclast-specific V-ATPase(vacuole-type proton-pumping ATPase) is composed of a3 and d2 isoforms. V-ATPase with a3 isoform is localized on lysosomal membrane, and is essential for traffic of lysosomes to plasmamembrane. Secretion of lysosomal enzymes and acidification outside osteoclasts are important for bone resorption. On the other hand, we have established experimental systems to observe subunit rotation of single molecule V-ATPase and to examine assembly of the catalytic domain and the proton pathway. These systems are essential to elucidate molecular mechanism that creates various acidic environments.
|