Structural basis for molecular mechanism of heparanase mediated cancer cell invasion and metastasis
| Project/Area Number |
23790048
|
|---|
| Research Category |
Grant-in-Aid for Young Scientists (B)
|
| Allocation Type | Multi-year Fund |
|---|
| Research Field |
Physical pharmacy
|
|---|
| Research Institution | Kyushu University |
|---|
Principal Investigator |
TABATA Kaori 九州大学, 薬学研究科(研究院), 助教 (90464388)
|
|---|
| Project Period (FY) |
2011 – 2013
|
| Project Status |
Completed (Fiscal Year 2013)
|
| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2013: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2012: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2011: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
|
|---|
| Keywords | ヘパラナーゼ / X線結晶構造解析 / ガン転移 / 結晶構造解析 |
|---|
| Research Abstract |
Heparanase is an enzyme which involved in cancer cell invasion and metastasis. In this research, the purpose is to clarify the 3D-structure of heparanase.
I examined various protein expression systems using E. coli and silk worm, and succeeded in obtaining about 5 mg of the target protein from the 1L culture as a soluble fraction. The antibody was produced using the prepared recombinant protein as an antigen, and I confirmed that the antibody specifically recognized heparanase by ELISA. Then, I tried to crystallize complexes of heparanase with produced antibody, and succeeded in obtaining some micro crystals. Moreover, I also succeeded in obtaining the single crystals of beta-glucuronidase, which belongs to heparanase type enzyme.
|
Report
(4 results)
Research Products
(1 results)
