| Project/Area Number |
23590260
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Multi-year Fund |
|---|
| Section | 一般 |
|---|
| Research Field |
General physiology
|
|---|
| Research Institution | Kagawa University |
|---|
Principal Investigator |
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
OHIRA Tetsuya 福島県立医科大学, 医学部疫学講座, 主任教授 (50448031)
KITAMURA Akihiko 大阪がん循環器病予防センター (80450922)
山下 哲生 香川大学, 医学部, 助教 (80444727)
|
|---|
| Project Period (FY) |
2011 – 2013
|
| Project Status |
Completed (Fiscal Year 2013)
|
| Budget Amount *help |
¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2013: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2012: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2011: ¥3,510,000 (Direct Cost: ¥2,700,000、Indirect Cost: ¥810,000)
|
|---|
| Keywords | 細胞死 / ミトコンドリア / カスパーゼ非依存性細胞死 / 膜結合様式 / 分子機序 / ＡＩＦ / AIF |
|---|
| Research Abstract |
To elucidate exact membrane-binding manner of AIF, we contracted recombinant E. coli strains which overexpressed mouse AIFs, mitochondria-type AIF (delta 1-53) or cleaved-type AIF (delta 1-102). We found that more than 80% of mitochondria-type AIF was associated to the membrane when the ionic strength (I) of preparation buffer was the same as a physiological conditions (I = 150 mM). While, at high conditions (I = 300 mM), most enzyme (95%) was dissociated from the membrane. It is noteworthy that cleaved-type AIF partly associated to the membrane (about 50%) at low I, and was also dissociated by increasing I. These results suggest that the N-terminal region (residues 67-85) of AIF is involved in the membrane-binding but is not absolutely necessary and the binding manner of AIF to the membrane may be an ion bond.
|
