Updated on 2025/03/14

写真a

 
MAEDA Megumi
 
Organization
Faculty of Environmental, Life, Natural Science and Technology Professor
Position
Professor
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Degree

  • 農学 ( 岡山大学 )

Research Interests

  • サイトカイン

  • アスベスト

  • Th2免疫応答

  • 抗腫瘍免疫

  • 食物アレルゲン

  • 糖鎖ポリマー

  • 植物抗原性糖鎖

  • レクチン

  • N-glycan

  • 花粉アレルゲン

Research Areas

  • Life Science / Applied biochemistry

  • Life Science / Immunology

Education

  • Okayama University   自然科学研究科 博士後期課程   生命分子化学専攻

    2003.4 - 2006.3

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    Country: Japan

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  • Okayama University   自然科学研究科博士前期課程   生物資源化学専攻

    2001.4 - 2003.3

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    Country: Japan

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  • Okayama University   農学部   総合農業科学科

    1997.4 - 2001.3

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    Country: Japan

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Research History

  • Faculty of Environmental, Life, Natural Science and Technology, Okayama University

    2023.4

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  • Faculty of Environmental and Life Science, Okayama University

    2021.4 - 2023.3

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  • Graduate School of Environmental and Life Science Okayama University

    2017.3 - 2021.3

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  • ベルギー国ゲント大学 博士研究員

    2016.4 - 2016.10

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  • 岡山大学大学院 環境生命科学研究科 助教

    2014.4 - 2017.2

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Professional Memberships

Committee Memberships

  •   糖鎖生命科学連携ネットワーク型拠点コラボレイティブフェロー  

    2024.4 - 2026.3   

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  • 第42回日本糖質学会 (鳥取)   Advisory Board  

    2023.2 - 2023.9   

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  •   第62回日本生化学会中国・四国支部例会 実行委員  

    2021.11   

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Papers

  • Construction of tomato plants with suppressed endo-β-N-acetylglucosaminidase activity using CRISPR-Cas9 mediated genome editing. Reviewed International journal

    Naoko Okamoto, Megumi Maeda, Chiharu Yamamoto, Reo Kodama, Koichi Sugimoto, Yoshihito Shinozaki, Hiroshi Ezura, Yoshinobu Kimura

    Plant physiology and biochemistry : PPB   190   203 - 211   2022.11

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    Language:English   Publishing type:Research paper (scientific journal)  

    High mannose-type free N-glycans with a single N-acetyl-D-glucosamine (GlcNAc) residue at the reducing end (GN1-HMT-FNGs) are produced by cytosolic endo-β-N-acetylglucosaminidase (EC:3.2.1.96) (ENGase) and are ubiquitous in differentiating and growing plant cells. To elucidate the physiological functions of HMT-FNGs in plants, we identified the ENGase gene in tomato (Solyc06g050930) and detected ENGase activity and increased production of GN1-HMT-FNGs during tomato fruit maturation. However, the precise role of GN1-HMT-FNGs in fruit maturation remains unclear. In this study, we established tomato ENGase mutants with suppressed ENGase activity via CRISPR/Cas9 genome editing technology. DNA sequencing of the Δeng mutants (T0 and T1 generations) revealed that they had the same mutations in the genomic DNA around the target sequences. Three null CRISPR/Cas9 segregant plants of the T1 generation (Δeng1-2, -22, and -26) were used to measure ENGase activity and analyze the structural features of HMT-FNGs in the leaves. The Δeng mutants did not exhibit ENGase activity and produced GN2-HMT-FNGs bearing tow GlcNAc residues at the reducing end side instead of GN1-HMT-FNGs. The Δeng mutants lack the N-terminal region of ENGase, indicating that the N-terminal region is important for full ENGase activity. The fruits of Δeng mutants (T2 generation) also showed loss of ENGase activity and similar structural features of HMT-FNGs of the T1 generation. However, there was no significant difference in fruit maturation between the T2 generation of the Δeng mutants and the wild type. The Δeng mutants rich in GN2-HMT-FNGs could be offered as a new tomato that is different from wild type containing GN1-HMT-FNGs.

    DOI: 10.1016/j.plaphy.2022.08.009

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  • Structural features of free N-glycans in α1,3/4-fucosidase-deficient Arabidopsis thaliana: deletion of α1,3/4-fucosidase activity induced accumulation of plant complex type GN1 free N-glycans. Reviewed International journal

    Shun Takata, Megumi Hayashi, Megumi Maeda, Takeshi Ishimizu, Yoshinobu Kimura

    Bioscience, biotechnology, and biochemistry   86 ( 10 )   1413 - 1416   2022.9

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    Language:English   Publishing type:Research paper (scientific journal)  

    Deletion of α-1,3/4-fucosidase activity in Arabidopsis thaliana resulted in the accumulation of GN1-type free N-glycans with the Lewis a epitope (GN1-FNG). This suggests that the release of α-fucose residue(s) may trigger rapid degradation of the plant complex-type (PCT) GN1-FNG. The fact that PCT-GN1-FNG has rarely been detected to date is probably due to its easier degradation compared with PCT-GN2-FNG.

    DOI: 10.1093/bbb/zbac120

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  • Improved method for preparation and purification of recombinant α-synuclein: high-mannose-type free N-glycan prepared from an edible bean (Vigna angulari, Azuki bean) inhibits α-synuclein aggregation. Reviewed International journal

    Shota Kosaka, Makoto Katsube, Megumi Maeda, Yoshinobu Kimura

    Bioscience, biotechnology, and biochemistry   86 ( 6 )   770 - 774   2022.5

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    Language:English   Publishing type:Research paper (scientific journal)  

    Parkinson's disease is characterized by the accumulation of amyloid, which consists of α-synuclein (α-Syn). To screen compounds with amyloid aggregation inhibitory activity, an effective method for the preparation of α-Syn is a prerequisite. We established a simpler method for α-Syn preparation using freeze-thaw treatment of transformed Escherichia coli. Furthermore, we found that the high-mannose type free N-glycans could prevent α-Syn aggregation.

    DOI: 10.1093/bbb/zbac040

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  • Improved assay system for acidic peptide: N-glycanase (aPNGase) activity in plant extracts. Reviewed International journal

    Chiharu Yamamoto, Mikako Ogura, Ryota Uemura, Maeda Megumi, Hiroyuki Kajiura, Ryo Misaki, Kazuhito Fujiyama, Yoshinobu Kimura

    Analytical biochemistry   634   114367 - 114367   2021.12

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    Language:English   Publishing type:Research paper (scientific journal)  

    Plant acidic peptide: N-glycanase (aPNGase) release N-glycans from glycopeptides during the degradation process of glycoproteins in developing or growing plants. We have previously developed a new method to detect the aPNGase activity in crude extracts, which is prerequisite for the construction of aPNGase knockout or overexpression lines. However, this method has the disadvantage of requiring de-sialylation treatment and a lectin chromatography. In this study, therefore, we improved the simple and accurate method for detecting aPNGase activity using anion-exchange HPLC requiring neither the desialylation treatment nor the lectin affinity chromatography.

    DOI: 10.1016/j.ab.2021.114367

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  • Large-scale preparation of sialyl-Tn antigen-containing peptides from mucin-like glycoproteins in boar seminal gel. Reviewed International journal

    Ryota Takeuchi, Megumi Maeda, Miran Nakano, Hiroaki Funahashi, Yoshinobu Kimura

    Bioscience, biotechnology, and biochemistry   85 ( 9 )   2022 - 2025   2021.8

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    Language:English   Publishing type:Research paper (scientific journal)  

    Sialyl-Tn antigen, a tumor antigen, is a valuable ligand for the purification of proteins that specifically bind to it. Here, we developed a new method for the preparation of large amounts of sialyl-Tn antigen-containing peptides from an unused resource, boar seminal gel. The glycopeptides were prepared from the actinase E digests by a combination of gel filtration and hydrophilic partitioning.

    DOI: 10.1093/bbb/zbab114

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Books

  • Sugar Chain Analysis by Enzymatic Digenstion and 2D Mapping by HPLC.. Experimental Glycoscience, Glycochemistry

    Springer 

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  • Sugar Chain Analysis by Enzymatic Digenstion and 2D Mapping by HPLC.「Experimental Glycoscience, Glycochemistry」

    Springer 

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MISC

  • 「花粉-食物アレルギー症候群の病態と治療」に寄せる スギ・ヒノキ花粉アレルゲンに結合したN-グリカンの構造特性と免疫活性解析に向けた新技術

    前田恵, 木村万里子, 木村吉伸

    月刊アレルギーの臨床   ( 511 )   2018

  • Ginkgo biloba α-fucosidase with activity towards plant complex type N-glycans containing the Lewis a epitope: Purification and characterization

    Itano Satsuki, Maeda Megumi, Md. Ziaur Rahman, Kimura Yoshinobu

    Scientific Reports of the Faculty of Agriculture, Okayama University   106   5 - 12   2017

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    Language:English  

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  • Structural features of free N-glycans occurring in plants and functional features of de-N-glycosylation enzymes, ENGase, and PNGase: the presence of unusual plant complex type N-glycans International journal

    Megumi Maeda, Yoshinobu Kimura

    FRONTIERS IN PLANT SCIENCE   5   429 - 429   2014.9

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    Language:English   Publisher:FRONTIERS RESEARCH FOUNDATION  

    Free N-glycans (FNGs) are present at micromolar concentrations in plant cells during their differentiation, growth, and maturation stages. It has been postulated that these FNGs are signaling molecules involved in plant development or fruit ripening. However, the hypothetical biochemical and molecular function of FNGs has not been yet established.The structure of FNGs found ubiquitously in plant tissues such as hypocotyls, leaves, roots, developing seeds, or fruits can be classified into two types: high-mannose type and plant complex type; the former, in most cases, has only one GIcNAc residue at the reducing end (GNI type), while the latter has the chitobiosyl unit at the reducing end (GN2 type). These findings suggest that endo-13-N-acetylglucosaminidase (ENGase) must be involved in the production of GN1 type FNGs, whereas only peptide:N-glycanase (PNGase) is involved in the production of GN2 type FNGs. It has been hypothesized that cytosolic PNGase (cPNGase) and ENGase in animal cells are involved in the production of high-mannose type FNGs in order to release N-glycans from the misfolded glycoproteins in the protein quality control systems. In the case of plants, it is well known that another type of PNGase, the acidic PNGase (aPNGase) is involved in the production of plant complex type FNGs in an acidic organelle, suggesting the de-N-glycosylation mechanism in plants is different from that in animal cells. To better understand the role of these FNGs in plants, the genes encoding these N-glycan releasing enzymes (ENGase and PNGase) were first identified, and then structure of FNGs in ENGase knocked-out plants were analyzed.These transgenic plants provide new insight into the plant-specific de-N-glycosylation mechanism and putative physiological functions of FNGs. In this review, we focus on the structural features of plant FNGs, as well as functional features of cPNGase/ENGase and plant specific PNGase, and putative functions of FNGs are also discussed.

    DOI: 10.3389/fpls.2014.00429

    Web of Science

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  • Changes in Glycinin‒Digesting Protease Activity During Soybean Germination.

    Md. Akhtaruzzaman, Maeda Megumi, Kitagawa Keiko, Takagi Shigeaki, Kimura Yoshinobu

    岡山大学農学部学術報告   103   1 - 4   2014.2

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    Language:English   Publisher:岡山大学農学部  

    Changes in glycinin-digesting protease activity during soybean germination have been investigated.The glycinin-digesting protease activities of imbibed or germinated soybean seed were assayed byRP‒HPLC using a tryptic peptide from CM‒glycinin or by SDS‒PAGE using CM‒glycinin as the endogenoussubstrate. Proteolytic activities of the germinated soybean seeds were found through the wholeperiod of germination, the activities were maintained significantly unchanged during germination for 4days, and then those specific activities declined slowly. AE‒HPLC analysis of the glycinin-digestingprotease in the imbibed or germinated soybean seeds showed unchanged peaks corresponding to glycinin-digesting activity, suggesting that the glycinin-digesting protease was not induced during germinationbut had already been synthesized during seed maturation. 大豆発芽期におけるグリシニン分解酵素 (98 kDa SBP) の活性変動を解析した.大豆種子を4時間水で膨潤後, 25℃ 暗黒下で発芽させた.経時的にサンプリングを行い,2M NaCl を含むトリス緩衝液 (㏗ 7.0) により粗酵素を抽出後,グリシニン由来のトリプシン分解ペプチドを基質としてグリシニン分解酵素の活性変動を逆相 HPLC により追跡した.その結果,種子膨潤後4日間比活性はほぼ一定の値を保ち,以後徐々に低下することが分かった.次いで,粗酵素溶液からイオン交換 HPLC により98 kDa SBP を部分精製するとともに,発芽期における 98 kDa SBP の消長を解析したところ,98 kDa SBP は乾燥種子及び各発芽段階の種子中全てに認められ,かつグリシン分解活性もグリシニン由来のトリプシン分解ペプチド基質に対する活性と同様に認められた.以上の結果から,98 kDa SBP は種子発芽に伴い誘導されるプロテアーゼではなく,種子貯蔵型のプロテアーゼであることが明らかになった.

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  • Suppression of cytosolic and acidic peptide: N-glycanase (PNGase) in Arabidopsis thaliana

    Tsuyoshi Akiyama, Megumi Maeda, Yoshinobu Kimura

    GLYCOBIOLOGY   23 ( 11 )   1378 - 1378   2013.11

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    Language:English   Publishing type:Research paper, summary (international conference)   Publisher:OXFORD UNIV PRESS INC  

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Presentations

  • 酸性及び細胞質ペプチド: N-グリカナーゼ二重欠損 A. thaliana遊離N-グリカン構造解析

    奥村陸, 白井佐保子, 三﨑亮, 梶浦裕之, 藤山和仁, 木村吉伸, 前田恵

    学会創立100周年記念 中四国支部・西日本支部合同大会(第66回 講演会)(高知)  2023.9.22 

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    Event date: 2023.9.21 - 2023.9.22

    Presentation type:Oral presentation (general)  

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  • 植物糖鎖を多価結合したネオ複合糖質の自然免疫応答に及ぼす免疫活性解析

    板野紗月, 沓野那緒, 藤原美智子, 加来田博貴, 木村吉伸, 前田恵

    第42回日本糖質学会年会(鳥取) 

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    Event date: 2023.9.7 - 2023.9.9

    Presentation type:Poster presentation  

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  • 遊離糖鎖の機能解明を目的とした酸性PNGase 欠損トマトの構築およびオーキシンへの結合性解析

    井口 夢香, 堀口 星, 前田 恵, 木村 吉伸

    第95回日本生化学会大会(名古屋) 

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    Event date: 2022.11.9 - 2022.11.11

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  • 組換えα-synucleinの遊離N-グリカンのアミロイド形成抑制活性

    中野海藍, 小坂将太, 前田恵, 木村吉伸

    第95回日本生化学会大会(名古屋) 

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    Event date: 2022.11.9 - 2022.11.11

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  • ピーナッツアレルギー発症に関わるAra h1の N末端ドメインの消化酵素に対する抵抗性の検討

    石橋 里菜, Asaduzzaman Md, 前田 恵, 木村 吉伸

    第95回日本生化学会大会(名古屋) 

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    Event date: 2022.11.9 - 2022.11.11

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Awards

  • 研究集会助成事業

    2022.12   公益財団法人八雲環境科学振興財団  

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  • 両備檉園記念財団 生物学研究奨励賞

    2021.10  

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  • 49th Society of Toxicology (USA); Immunotoxicology Specialty Section, HESI Immunotoxicology, Young Investigator Travel Award

    2010.3  

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  • 2006年度日本農芸化学会大会B.B.B.論文賞 Glycoform analysis of Japanese cedar pollen allergen, Cry j1 Biosci. Biotechnol. Biochem., 69, 1700-1705 (2005)

    2007  

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    Country:Japan

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  • 第18回日本農芸化学会中四国支部講演会 2007年度農芸化学会中四国支部奨励賞 植物糖タンパク質糖鎖の代謝機構とアレルゲン糖鎖の構造・機能解析.

    2007  

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    Country:Japan

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Research Projects

  • ヒノキ科花粉症に対する次世代アレルゲン免疫療法の開発

    Grant number:JP24ek0410129  2024.07 - 2027.03

    国立研究開発法人 日本医療研究開発機構  【重点領域】アレルゲン免疫療法の開発または改善に資する研究

    岡野 光博, 前田 恵ら

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    Authorship:Coinvestigator(s) 

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  • 新規食品素材「アクアファバ」に含まれる遊離型オリゴ糖・ペプチドの構造と機能解析

    Grant number:21K02101  2021.04 - 2024.03

    日本学術振興会  科学研究費助成事業 基盤研究(C)  基盤研究(C)

    木村 万里子, 前田 恵, 山下 弘高, 吉田 和利, 藤田 裕之

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    Grant amount:\4160000 ( Direct expense: \3200000 、 Indirect expense:\960000 )

    ①豆煮汁からの遊離型オリゴ糖の精製および化学構造解析:6種の豆類(大豆,ひよこまめ, 手亡, 小豆, えんどう, レンズまめ)から,一般的な餡の製造工程に準じて2時間加熱して煮汁を調製し,それらの凍結乾燥物を得た。次に,各凍結乾燥物から,50%エタノール分画,陽イオン交換によりオリゴ糖画分を調製し,順相HPLC-RI及びLC-ESI-MSでラフィノース族オリゴ糖の定量分析を行った。その結果,ひよこまめ煮汁はラフィノースの,大豆,ひよこまめ,小豆およびえんどうの煮汁はスタキオースの良い供給源として利用できる可能性が認められた。小豆と手亡の煮汁中にN-グリカン(M8,M3FX)の存在も認められたものの,今回定量には至らなかった。
    ②豆煮汁由来オリゴ糖の機能性解析:豆煮汁オリゴ糖画分のプレバイオティック効果は,4種のビフィズス菌において有意に認められたものの(p<0.01),N-グリカンの増殖活性は認められなかった。
    ③ 豆煮汁からのACE阻害ペプチドの精製および化学構造・機能解析:6種の豆煮汁から,上述①と同じ手法でペプチド画分を調製し,さらにODSカラムと逆相HPLCに供してACE阻害活性ペプチドを単離した。活性ペプチドの構造解析は,MS/MS分析,プロテインシークエンサーにより行った。ACE阻害活性測定は,合成基質から遊離する馬尿酸をHPLCで定量する手法により行った。
    ④ 各種「アクアファバ」の泡の物性および嗜好性:3種(ひよこ豆、小豆、手亡)の豆煮汁を一定条件下で泡立て光学顕微鏡観察を行ったところ,豆の種類により泡沫の状態(安定性や泡直径など)が異なることが認められた。

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  • Synthesis of functional glycopolymers and analysis of their immuno-suppression activity involved in pollen allergen specific Th2 immune response

    Grant number:18K05559  2018.04 - 2021.03

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (C)  Grant-in-Aid for Scientific Research (C)

    Maeda Megumi

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    Grant amount:\4420000 ( Direct expense: \3400000 、 Indirect expense:\1020000 )

    Japanese cedar and cypress pollen allergens occur Lewis a antigen-containing N-glycans. Although the core structure of plant antigenic N-glycans, M3FX, suppress Th2 immune response, the immune activity of Lewis a antigen-containing N-glycans has not been elucidated. In this study, we purified a large amount of Lewis a antigen-containing N-glycans from glycoproteins expressed in Egeria densa and synthesized a multivalent glycopolymer. It was suggested that the glycopolymers suppressed antigen presentation by dendritic cell-like cell lines and may contribute to the suppression of Th2 immune responses.

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  • Preparation of functional glyco-polymers and analysis of their cellular immune activities to develop anti-pollinosis drugs

    Grant number:15K07841  2015.04 - 2018.03

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (C)  Grant-in-Aid for Scientific Research (C)

    MAEDA Megumi, KIMURA Yoshinobu, OKANO Mitsuhiro

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    Grant amount:\4940000 ( Direct expense: \3800000 、 Indirect expense:\1140000 )

    Three types of glycopolymers bearing multivalent N-glycans (plant complex type, high-mannose type, or animal complex type) were synthesized. Their suppressive functions on Th2 cellular immune response induced by Japanese cedar pollen allergen, Cry j1, were analyzed by using dendritic cells. And then, structural features of newly identified Japanese cypress pollen allergen, Cha o3, were analyzed. The glycoform of Cha o 3 is similar to those of major glycoallergens in cedar or cypress pollens (Cry j1 and Jun a1).

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  • Preparation of functional glyco-polymers and analysis of their cellular immune activities to develop anti-pollinosis drugs(Fostering Joint International Research)

    Grant number:15KK0282  2015 - 2017

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research Fund for the Promotion of Joint International Research (Fostering Joint International Research)  Fund for the Promotion of Joint International Research (Fostering Joint International Research)

    MAEDA Megumi, VAN DAMME Els J.M., Rahman Ziaur

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    Grant amount:\14040000 ( Direct expense: \10800000 、 Indirect expense:\3240000 )

    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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Class subject in charge

  • Laboratory in Agrochemical Bioscience 2 (2024academic year) Second semester  - 月5~8,火5~8,木5~8,金5~8

  • Current Topics of Applied Cellular Biochemistry (2024academic year) Late  - その他

  • Biochemistry and Bioengineering of Useful Enzymes (2024academic year) Prophase  - 火3~4

  • Advanced Study (2024academic year) Other  - その他

  • Introduction for Biochemistry 1 (2024academic year) 1st and 2nd semester  - 木1,木2

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