The Receptor with High Affinity for IgE

  1. Derek J. Chadwick Organizer,
  2. David Evered Organizer and
  3. Julie Whelan
  1. Henry Metzger Chairman1,2,
  2. Jean-Pierre Kinet1,
  3. Ulrich Blank1,
  4. Larry Miller1 and
  5. Chise Ra1

Published Online: 28 SEP 2007

DOI: 10.1002/9780470513866.ch7

Ciba Foundation Symposium 147 - IgE, Mast Cells and the Allergic Response

Ciba Foundation Symposium 147 - IgE, Mast Cells and the Allergic Response

How to Cite

Metzger, H., Kinet, J.-P., Blank, U., Miller, L. and Ra, C. (2007) The Receptor with High Affinity for IgE, in Ciba Foundation Symposium 147 - IgE, Mast Cells and the Allergic Response (eds D. J. Chadwick, D. Evered and J. Whelan), John Wiley & Sons, Ltd., Chichester, UK. doi: 10.1002/9780470513866.ch7

Author Information

  1. 1

    Section on Chemical Immunology, Arthritis and Rheumatism Branch, National Instiute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA

  2. 2

    Department of Health & Human Sciences, Building 10 Room 9N228, National Institutes of Health, Bethesda, MD 20892, USA

Publication History

  1. Published Online: 28 SEP 2007

ISBN Information

Print ISBN: 9780471923091

Online ISBN: 9780470513866

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Keywords:

  • cDNAs;
  • IgE;
  • T lymphocytes;
  • β chain;
  • transfection experiments

Summary

The cDNAs for each of the three types of polypeptide that form the high affinity IgE receptor have been cloned and sequenced. Analysis of the predicted amino acid sequence and other data suggests that the four-chained structure (αβγ2) contains seven transmembrane segments. The α chain resembles the immunoglobulin-binding chain found in other Fc receptors, but the β and γ chain sequences do not resemble other known proteins. (The one exception: the transmembrane segment of the γ chains, which is homologous to the corresponding segment of the ζ chain of the CD3 complex found on T lymphocytes.) Efficient expression of IgE binding by the rat receptor in COS cells was observed only when the coding sequences for each of the three chains were co-transfected. So far, only the cDNA for the human α chain has been successfully cloned. We attempted to express this chain by co-transfecting its cDNA with those for the rat β and γ chains. Surprisingly, co-transfection with the cDNA for the γ chain was sufficient, although when the β and γ chains were both co-transfected, expression of αβγ oligomers was evident. Approaches being used to define by genetic manipulation the functional role of various parts of the receptor are discussed.