| Project/Area Number |
10672037
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Biological pharmacy
|
|---|
| Research Institution | CHIBA UNIVERSITY |
|---|
Principal Investigator |
NAKAMURA Tatsunosuke CHIBA UNIVERSITY PHARMACEUTICAL SCIENCES RESEARCH ASSOCIATE, 薬学部, 助手 (20114308)
|
|---|
| Project Period (FY) |
1998 – 2000
|
| Project Status |
Completed (Fiscal Year 2000)
|
| Budget Amount *help |
¥2,500,000 (Direct Cost: ¥2,500,000)
Fiscal Year 2000: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1999: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 1998: ¥1,000,000 (Direct Cost: ¥1,000,000)
|
|---|
| Keywords | TRP / cation channel / Escherichia coli / capsaicin receptor / K^+ channel / structure and function / mammalian cultured cells / イオン選択性 / チャネル / Na^+排出 / K^+輸送系 / トランスポーター / antiporter / イオン輸送系 / 蛋白発現 / クロストーク / ポア構造 |
|---|
| Research Abstract |
TRP (transient receptor rotential) homologue of mouse function as cation channel that passes Ca^<2+> and Na^+. When TRP homologue gene was transformed in Escherichia coli mutant strain TO114 which lacks all Na^+/H^+ antiporters, this strain became sensitive to Na^+ suggesting that it functions in E.coli membrane. We detected His tagged TRP homologue expressed in membrane fraction of E.coli. TRP probably has common structure with VR1, capsaicin receptor, but those structures are not known. TRP/VR1 were suggested to have homology with Shaker type K^+ channels with 6 transmembrane regions, though there are no experimental reports. We started experiment for TRP structure using bacterial system and got some results. We are doing further experiment using mammalian cultured cells to confirm the TRP structure that got from bacterial system.
|
