| ID | JOS-j.carres.2011.05.012 |
| 著者：名前 | 武内, 智春/ 西山, 和沙/ Yamada, Atsushi/ 田村, 真由美/ 高橋, 秀依/ 夏苅, 英昭/ 相川, 順一/ 相川（小島）, 京子/ 荒田, 洋一郎/ Kasai, Ken-ichi |
| 著者：別形式 | Takeuchi, Tomoharu / Nishiyama, Kazusa / Yamada, Atsushi / Tamura, Mayumi / Takahashi, Hideyo / Natsugari, Hideaki / Aikawa, Jun-ichi / Kojima-Aikawa, Kyoko / Arata, Yoichiro / Kasai, Ken-ichi |
| 著者：カナ | タケウチ, トモハル/ ニシヤマ, カズサ/ ヤマダ, アツシ/ タムラ, マユミ/ タカハシ, ヒデヨ/ ナツガリ, ヒデアキ/ アイカワ, ジュンイチ/ アイカワ(コジマ), キョウコ/ アラタ, ヨウイチロウ/ カサイ, ケンイチ |
| 著者：所属 | 城西大学薬学部 / 帝京大学薬学部 / 帝京大学薬学部 / 城西大学薬学部 / 帝京大学薬学部 / 帝京大学薬学部 / 理化学研究所基幹研究所 / お茶の水女子大学大学院人間文化創成科学研究科, / 城西大学薬学部 / 帝京大学薬学部 |
| 著者：所属(別形式） | Josai University, Pharmaceutical Sciences, Laboratory of Molecular Immunology / Teikyo University, School of Pharmaceutical Sciences, Laboratory of Synthetic Organic and Medicinal Chemistry / Teikyo University, School of Pharmaceutical Sciences, Laboratory of Synthetic Organic and Medicinal Chemistry / Josai University, Pharmaceutical Sciences, Laboratory of Molecular Immunology / Teikyo University, School of Pharmaceutical Sciences, Laboratory of Synthetic Organic and Medicinal Chemistry / Teikyo University, School of Pharmaceutical Sciences, Laboratory of Synthetic Organic and Medicinal Chemistry / RIKEN Advanced Science Institute / Ochanomizu University, Graduate School of Humanities and Sciences / Josai University, Pharmaceutical Sciences, Laboratory of Molecular Immunology / Teikyo University, School of Pharmaceutical Sciences, Department of Biological Chemistry |
| 著者版フラグ | author |
| 出版者 | Elsevier |
| NCID | AA00598932 |
| 冊子ISSN | 00086215 |
| 電子ISSN | 00086215 |
| 掲載誌名 | |
| 巻 | 346 |
| 号 | 13 |
| 刊行年月 | 2011-09 |
| 開始ページ | 1837 |
| 終了ページ | 1841 |
| コンテンツ作成日 | 2011-03-29 |
| コンテンツ修正日 | 2011-05-09 |
| コンテンツ登録日 | 2011-05-12 |
| 識別番号：DOI | info:doi/10.1016/j.carres.2011.05.012 |
| 識別番号：DOI（リンク） | |
| 抄録 | Galβ1-4Fuc is a key structural motif in Caenorhabditis elegans glycans and is responsible for interaction with C. elegans galectins. In animals of the clade Protostomia, this unit seems to have important roles in glycan?protein interactions and corresponds to the Galβ1-4GlcNAc unit in vertebrates. Therefore, we prepared an affinity adsorbent having immobilized Galβ1-4Fuc in order to capture carbohydrate-binding proteins of C. elegans, which interact with this disaccharide unit. Adsorbed C. elegans proteins were eluted with ethylenediaminetetraacetic acid (EDTA) and followed by lactose (Galβ1-4Glc), digested with trypsin, and were then subjected to proteomic analysis using LC-MS/MS. Three annexins, namely NEX-1, -2, and -3, were assigned in the EDTA-eluted fraction. Whereas, galectins, namely LEC-1, -2, -4, -6, -9, -10, and DC2.3a, were assigned in the lactose-eluted fraction. The affinity of annexins for Galβ1-4Fuc was further confirmed by adsorption of recombinant NEX-1, -2, and -3 proteins to the Galβ1-4Fuc column in the presence of Ca2+. Furthermore, frontal affinity chromatography analysis using an immobilized NEX-1 column showed that NEX-1 has an affinity for Galβ1-4Fuc, but no affinity towards Galβ1-3Fuc and Galβ1-4GlcNAc. We would hypothesize that the recognition of the Galβ1-4Fuc disaccharide unit is involved in some biological processes in C. elegans and other species of the Protostomia clade. |
| キーワード | |
| 言語 | eng |
| 資源タイプ | text |
| ジャンル | |
| フォーマット | application/pdf |
| このアイテムを表示する：本文(pdf) |  ( 1.7MB) ダウンロード回数： 回 |
| このアイテムを表示する：URI | |
