Preparation of functional glyco-polymers and analysis of their cellular immune activities to develop anti-pollinosis drugs(Fostering Joint International Research)
Project/Area Number |
15KK0282
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Research Category |
Fund for the Promotion of Joint International Research (Fostering Joint International Research)
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Allocation Type | Multi-year Fund |
Research Field |
Applied molecular and cellular biology
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Research Institution | Okayama University |
Principal Investigator |
MAEDA Megumi 岡山大学, 環境生命科学研究科, 准教授 (20434988)
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Research Collaborator |
VAN DAMME Els J.M. Faculty of Bioscience Engineering, Ghent University, Department of Molecular Biotechnology, Prof.
Rahman Ziaur Institute of Food and Radiation Biology, Atomic Energy Research Establishment, Bangladesh Atomic Energy Commission
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Project Period (FY) |
2015 – 2017
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Project Status |
Completed (Fiscal Year 2017)
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Budget Amount *help |
¥14,040,000 (Direct Cost: ¥10,800,000、Indirect Cost: ¥3,240,000)
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Keywords | 遊離N-グリカン / 糖鎖結合タンパク質 / レクチン / 糖鎖ポリマー / PNGase / ENGase / 小胞体品質管理 / ルイスa抗原 / FNGs / ハイマンノース型糖鎖 / 複合型糖鎖 / ポリ-γ-L-グルタミン酸 / 核細胞質レクチン / 環境ストレス / aPNGase / pseudomonas syringae / 遊離型N-グリカン / 糖鎖 / 蛋白質 / 生体分子 / シグナル伝達 / 免疫学 |
Outline of Final Research Achievements |
Naturally occurring free N-glycans (FNGs) derived from glycoproteins/glycopeptides by the action of peptide: N-glycanase (PNGase) and endo-β-N-acetylglucosaminidase (ENGase) have been postulated to act as signaling molecules stimulating plant growth or fruit ripening. To elucidate the physiological role of FNGs in plants, we have analyzed the sensitivity of the A.thaliana mutants, ENGase-DKO and acidic PNGase-DKO, to abiotic (NaCl treatment) and biotic (P. syringae infection) stresses. Since it is believed that nucleocytoplasmic lectins function in the plant stress response, synthesized glycopolymers were used to study the interaction between FNGs and lectins in plant cells.
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Report
(4 results)
Research Products
(34 results)
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[Journal Article] Molecular characterization of tomato α1,3/4-fucosidase, a member of glycosyl hydrolase family 29, involved in degradation of plant complex type N-glycans.2017
Author(s)
Rahman, M.D., Maeda, M., Itano, S., Hossain, M.A., Ishimizu, T., Kimura, Y.
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Journal Title
J. Biochem.
Volume: 161
Pages: 421-432
DOI
NAID
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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