Structural and functional analyses of vascular smooth muscle-type ATP-sensitive K+ channels
| Project/Area Number |
16K19020
|
|---|
| Research Category |
Grant-in-Aid for Young Scientists (B)
|
| Allocation Type | Multi-year Fund |
|---|
| Research Field |
General pharmacology
|
|---|
| Research Institution | Saga University |
|---|
Principal Investigator |
|
|---|
| Project Period (FY) |
2016-04-01 – 2018-03-31
|
| Project Status |
Completed (Fiscal Year 2017)
|
| Budget Amount *help |
¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2017: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2016: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
|
|---|
| Keywords | 薬理学 / 血管平滑筋 / イオンチャネル / ATP感受性カリウムチャネル / Proximity ligation assay |
|---|
| Outline of Final Research Achievements |
Immunohistochemical analyses were performed to investigate the molecular subunit composition of vascular smooth muscle-type KATP channels.
In single smooth muscle cells dispersed from mouse portal vein, an in situ Proximity Ligation Assay (PLA) using primary antibodies against SUR2B and KIR6.1 detected positive signals of immunofluorescence, suggesting that SUR2B and KIR6.1 subunit proteins were closely co-localized. In contrast, immunofluorescence signals were not detected when PLA was performed in which the primary antibodies were omitted. Moreover, immunofluorescence signals were not detected when PLA was carried out in the presence of selective blocking peptides for the SUR2B and KIR6.1 proteins.
These results strongly suggest that native KATP channels in mouse portal vein myocytes are likely to be composed of SUR2B and KIR6.1 subunit proteins.
|
Report
(3 results)
Research Products
(4 results)
