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著作: Ohgomori Tomohiro/Nanao Tomohisa/[森田 明典]/Ikekita Masahiko/Asn54-linked glycan is critical for functional folding of intercellular adhesion molecule-5./[Glycoconjugate Journal]

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EID
265047
EOID
696183
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0
LastModified
2013年7月24日(水) 19:05:01
Operator
森田 明典
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Owner
森田 明典
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種別 必須 学術論文(審査論文)
言語 必須 英語
招待 推奨
審査 推奨 Peer Review
カテゴリ 推奨 研究
共著種別 推奨
学究種別 推奨
組織 推奨
著者 必須
  1. (英) Ohgomori Tomohiro
    役割 任意
    貢献度 任意
    学籍番号 推奨
  2. (英) Nanao Tomohisa
    役割 任意
    貢献度 任意
    学籍番号 推奨
  3. 森田 明典([徳島大学.大学院医歯薬学研究部.保健学域.保健科学部門.放射線科学系.医用理工学])
    役割 任意
    貢献度 任意
    学籍番号 推奨
  4. (英) Ikekita Masahiko
    役割 任意
    貢献度 任意
    学籍番号 推奨
題名 必須

(英) Asn54-linked glycan is critical for functional folding of intercellular adhesion molecule-5.

副題 任意
要約 任意

(英) Intercellular adhesion molecule-5 (ICAM-5, telencephalin) is a dendritically polarized type I membrane glycoprotein, and promotes dendritic filopodia formation. Although we have determined the N-glycan structures of ICAM-5 in a previous report, their function is unknown. Here, we produced fifteen ICAM-5 gene constructs, in which each potential N-glycosylation site was mutated, to elucidate the function of the N-glycans of ICAM-5, and observed the effects of transfection of them on a neuronal cell line, Neuro-2a (N2a). Only the N54Q mutant, which is the mutant for the most N-terminal glycosylation site, failed to induce filopodia-like protrusions in N2a cells. Immunofluorescence staining and cell surface biotinylation revealed that N54Q ICAM-5 was confined to the ER and also could not be expressed on the cell surface. This is further supported by the biochemical evidence that almost all N-glycans of N54Q ICAM-5 were digested by Endo glycosidase H and peptide:N-glycanase, indicating that almost all of them retain high-mannose-type structures in ER. In additon, it also failed to form disulfide bonds or functional protein complexes. The stable transformants of N54Q ICAM-5 showed retarded cell growth, but it was interesting that there was no apparent ER stress, because the mutant was sequentially degraded via ER associated degradation pathway by comparing the susceptibilities of the responses to various inhibitors of this pathway in wild-type and N54Q ICAM-5 transfectants. Taken together, the Asn(54)-linked glycan is necessary for normal trafficking and function of ICAM-5, but is unassociated with ER-associated degradation of it.

キーワード 推奨
  1. (英) Animals
  2. (英) Asparagine
  3. (英) Cell Adhesion Molecules
  4. (英) Cell Line, Tumor
  5. 小胞体(endoplasmic reticulum)
  6. (英) Glycoside Hydrolases
  7. (英) Glycosylation
  8. (英) Humans
  9. 免疫組織化学(immunohistochemistry)
  10. (英) Mannose
  11. (英) Mice
  12. (英) Microscopy, Fluorescence
  13. (英) Mutagenesis, Site-Directed
  14. (英) Nerve Tissue Proteins
  15. (英) Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
  16. (英) Polysaccharides
  17. (英) Protein Folding
  18. (英) Protein Processing, Post-Translational
  19. (英) Protein Transport
  20. (英) Pseudopodia
  21. (英) Rats
  22. (英) Transfection
発行所 推奨
誌名 必須 Glycoconjugate Journal(International Glycoconjugate Organization)
(pISSN: 0282-0080, eISSN: 1573-4986)
ISSN 任意 1573-4986
ISSN: 0282-0080 (pISSN: 0282-0080, eISSN: 1573-4986)
Title: Glycoconjugate journal
Title(ISO): Glycoconj J
Supplier: Kluwer Online
Publisher: Springer
 (NLM Catalog  (Scopus  (CrossRef (Scopus information is found. [need login])
必須 29
必須 1
必須 47 55
都市 任意
年月日 必須 2011年 12月 21日
URL 任意
DOI 任意 10.1007/s10719-011-9363-0    (→Scopusで検索)
PMID 任意 22187327    (→Scopusで検索)
NAID 任意
WOS 任意
Scopus 任意
評価値 任意
被引用数 任意
指導教員 推奨
備考 任意
  1. (英) Affiliation: Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, Yamazaki, Noda, Chiba, Japan. ohgomori@med.nagoya-u.ac.jp

  2. (英) PublicationType: Journal Article