Signal Transduction via Fc Receptors; Involvement of Tyrosine Kinase and Redox Regulation by ADF

  • Satoshi Iwata
  • Mitsuhiro Matsuda
  • Katsuji Sugie
  • Yasuhiro Maeda
  • Takumi Kawabe
  • Hajime Nakamura
  • Hiroshi Masutani
  • Toshiyuki Hori
  • Junji Yodoi
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 371)

Abstract

Low affinity Fc receptors for IgE (FcɛRII) were initially described on the surface of peripheral blood B lymphocytes1,2 and turned out to be identical to CD23, one of the B cell activation antigens. Cloning of FcɛRII cDNA revealed a unique primary structure compared to other Fc receptors such as FcγRI-III or FcɛRI, consisting of a cytoplasmic N-terminal domain of 23 amino acids, a transmembrane domain of 21 amino acids, extracellular C- terminal domain of 321 amino acids and no signal sequence.1 FcɛRII belongs to the c-type animal lectin superfamily, whereas FcɛRI and FcγRI-III belong to the immunoglobulin superfamily.

Keywords

Hydrolysis Lymphoma Tyrosine Leukemia Oligomer 

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Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • Satoshi Iwata
    • 1
  • Mitsuhiro Matsuda
    • 1
  • Katsuji Sugie
    • 2
  • Yasuhiro Maeda
    • 1
  • Takumi Kawabe
    • 1
  • Hajime Nakamura
    • 1
  • Hiroshi Masutani
    • 1
  • Toshiyuki Hori
    • 1
  • Junji Yodoi
    • 1
  1. 1.Department of Biological ResponsesInstitute for Virus ResearchJapan
  2. 2.Department of Late Effect Studies, Radiation Biology CenterKyoto UniversitySakyo-ku, KyotoJapan

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