| Project/Area Number |
22570111
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Structural biochemistry
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| Research Institution | Ochanomizu University |
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Principal Investigator |
OGAWA Haruko お茶の水女子大学, 大学院・人間文化創成科学研究科, 教授 (90143700)
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| Co-Investigator(Renkei-kenkyūsha) |
KAWASAKI Nana 国立医薬品食品衛生研究所, 生物薬品部, 部長 (20186167)
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| Project Period (FY) |
2010 – 2012
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| Project Status |
Completed (Fiscal Year 2012)
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| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2012: ¥260,000 (Direct Cost: ¥200,000、Indirect Cost: ¥60,000)
Fiscal Year 2011: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2010: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
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| Keywords | 膵臓酵素 / 糖鎖認識 / 糖質消化 / 糖質吸収 / 外分泌調節 / 糖尿病 / α-アミラーゼの糖結合性 / トリプシノーゲンの糖結合性 / リパーゼの糖結合性 / トリプシンの糖結合性 / 血糖値恒常性 / DPP4 / SGLT1 / 糖鎖認識の意義 / 消化・吸収 / 糖代謝 / Na^+-Glc共輸送体1(SGLT1) / α-アミラーゼ / Na+-Glc共輸送体1(SGLT1) |
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| Research Abstract |
We found novel carbohydrate-binding activities of pancreatic enzymes; -amylase, trypsinogen/trypsin, and lipase, etc. The carbohydrate-binding sites of bovine trypsinogen and trypsin were identified by cocrystallization with Me -GalNAc, and X-ray crystallography. Expression, purification, and refolding methods of recombinant human pancreatic lipase were established for the first time using Escherichia coli. The interaction between -amylase and N-glycans in the BBM activated starch degradation to produce much more Glc on one hand, while suppressing a sharp increase in Glc absorption on the other. Therefore, the carbohydrate recognition of α-amylase was shown to playa key role in regulating Glc assimilation to maintain blood homeostasis in the intestine.
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