Project/Area Number |
23658286
|
Research Category |
Grant-in-Aid for Challenging Exploratory Research
|
Allocation Type | Multi-year Fund |
Research Field |
Applied molecular and cellular biology
|
Research Institution | Shizuoka University |
Principal Investigator |
PARK Enoch Y. 静岡大学, グリーン科学技術研究所, 教授 (90238246)
|
Co-Investigator(Renkei-kenkyūsha) |
KATO Tatsuya 静岡大学, 農学研究科, 準教授 (00397366)
USUI Taichi 静岡大学, 理事 (50111802)
KATO Kouichi 名古屋市立大学, 薬学研究科, 教授 (20211849)
|
Project Period (FY) |
2011 – 2013
|
Project Status |
Completed (Fiscal Year 2013)
|
Budget Amount *help |
¥3,770,000 (Direct Cost: ¥2,900,000、Indirect Cost: ¥870,000)
Fiscal Year 2013: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2012: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2011: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
|
Keywords | バイオテクノロジー / 糖鎖 / タンパク質 / 昆虫 / 遺伝子 / N-アセチルグルコサミニダーゼ / ヒト型糖鎖型糖鎖 / ヒト型糖鎖 |
Research Abstract |
In order to provide an ability to synthesize sugar chains close to the complex type of mammalian cells from high mannose type of silkworm, we tried to modify the sugar chain synthetic pathway of silkworm. The activity of targeting N-acetylglucosaminidase in both Bm 5 cell and silkworm was decreased to 60% compared to control by adopting RNA silencing technology. As a test molecule IgG was expressed, and analyzed sugar chains. The paucimannose sugar chain of IgG accounted for 70% to 80% of the total, which suggests that silencing effect of N-acetylglucosaminidase was not enough to modify sugar chain synthetic pathway of silkworm. These results indicate that N-acetylglucosaminiltransferase may need to modify mannose type to complex type in silkworm.
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