Discovery of ER-endomannosidase and its importance on glycoprotein quality control
| Project/Area Number |
25560420
|
|---|
| Research Category |
Grant-in-Aid for Challenging Exploratory Research
|
| Allocation Type | Multi-year Fund |
|---|
| Research Field |
Chemical biology
|
|---|
| Research Institution | Seikei University |
|---|
Principal Investigator |
|
|---|
| Project Period (FY) |
2013-04-01 – 2016-03-31
|
| Project Status |
Completed (Fiscal Year 2015)
|
| Budget Amount *help |
¥3,770,000 (Direct Cost: ¥2,900,000、Indirect Cost: ¥870,000)
Fiscal Year 2015: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2014: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2013: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
|
|---|
| Keywords | 糖鎖 / 酵素 / 合成化学 / タンパク質品質管理 / 糖タンパク質品質管理 / 阻害剤 / 基質 / エンドマンノシダーゼ / カルネキシンサイクル / 合成糖鎖プローブ |
|---|
| Outline of Final Research Achievements |
We previously have found an endomannosidase (EM) activity in the endoplasmic reticulum (ER). Since ER-EM will play important roles for releasing unfolded glycoproteins from the folding system, calnexin/calreticulin cycle, herein we synthesized inhibitors and substrates contributing functional analysis of this enzyme. To explore the origin of ER-EM activity, we examined blue native PAGE with MS/MS analysis. Moreover, we generated a recombinant enzyme of ER-EM candidate, resulted in the ER-localization of the candidate enzyme was also elucidated. Additionally, specificity analyses of calreticulin and UGGT that are related to functions of ER-EM, were also carried out.
|
Report
(4 results)
Research Products
(38 results)
