| Project/Area Number |
17K15097
|
|---|
| Research Category |
Grant-in-Aid for Young Scientists (B)
|
| Allocation Type | Multi-year Fund |
|---|
| Research Field |
Functional biochemistry
|
|---|
| Research Institution | Japanese Foundation for Cancer Research |
|---|
Principal Investigator |
HAGA Yoshimi 公益財団法人がん研究会, がんプレシジョン医療研究センター がんオーダーメイド医療開発プロジェクト, 研究員 (40525789)
|
|---|
| Project Period (FY) |
2017-04-01 – 2019-03-31
|
| Project Status |
Completed (Fiscal Year 2018)
|
| Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2018: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
Fiscal Year 2017: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
|
|---|
| Keywords | 糖鎖 / 質量分析 / グライコプロテオミクス / 癌 / プロテオーム |
|---|
| Outline of Final Research Achievements |
To identify cancer-specific O-linked glycosylated proteins comprehensively, we developed a profiling technology that quantify and profile O-linked glycosylation sites in a very small amount of biological intact samples. We achieved high enrichment efficiency of O-glycopeptides and was able to identify plural unreported O-linked glycosylation sites on a model protein which was known to be multiply O-glycosylated. Furthermore, by the analysis using a cancer cell extract, we confirmed that cancer-related molecules such as mucins and NF-κB are certainly O-glycosylated.
|
| Academic Significance and Societal Importance of the Research Achievements |
糖鎖のうちN型糖鎖は付加部位のコンセンサス配列や基幹構造と呼ばれる共通の基礎構造があり、全N型糖鎖を遊離可能な酵素PNGase-Fも知られているため比較的研究がよく進んでいる。しかし、O型糖鎖はこれらの規則、ツールが全て無く、従来法や最新の質量分析計を駆使しても単一タンパク質のO型糖鎖付加部位を決定することさえ困難な状況であった。本開発技術は、あらゆる生体サンプル中から網羅的にO型糖鎖付加部位の同定と付加頻度の定量化を一度の質量分析で同時に可能とする世界初の分析手法である。
|
