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2013 Fiscal Year Final Research Report

Preparation of sialylated IgG and elucidation of the mechanism for its anti-inflammatory properties

Research Project

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Project/Area Number 23590578
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeMulti-year Fund
Section一般
Research Field Immunology
Research InstitutionNational Hospital Organization,Yamaguchi - Ube Medical Center

Principal Investigator

MIMURA YUSUKE  独立行政法人国立病院機構山口宇部医療センター(臨床研究部), その他部局等, 研究員 (00219718)

Project Period (FY) 2011 – 2013
KeywordsIgG / glycosylation / sialylation / DC-SIGN
Research Abstract

The attachment of oligosaccharide, at Asn297, of the IgG-Fc heavy chain is essential for optimal activation of Fc effector functions. It has recently been shown that IgG with oligosaccharides bearing terminal sialic acid residues mediates anti-inflammatory therapeutic effects. We expressed an IgG1 Phe243Ala (F243A) mutant in both human and rodent cell lines, and sialylation was found to be markedly increased. The mechanism by which the sialic acid residues in the IgG-Fc oligosaccharides exert an anti-inflammatory effect has been investigated by using dendritic cells that express DC-SIGN.

  • Research Products

    (2 results)

All 2013

All Presentation (2 results)

  • [Presentation] Enhanced sialylation of a mouse-human chimeric IgG1 antibody produced in human embryonic kidney 293 (HEK293) cells2013

    • Author(s)
      Mimura, Y, et al.
    • Organizer
      第42回日本免疫学会学術集会
    • Place of Presentation
      千葉
    • Year and Date
      20131211-13
  • [Presentation] Increased sialylation of a recombinant IgG mutant produced in human embryonic kidney 293 (HEK293) cells2013

    • Author(s)
      Mimura, Y, et al.
    • Organizer
      15th International Congress of Immunology
    • Place of Presentation
      Milan
    • Year and Date
      20130822-27

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Published: 2015-07-16  

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