The Journal of Experimental Medicine
Avanti Polar Lipids, Inc.
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Journal of Experimental Medicine, Vol 172, 1665-1672, Copyright © 1990 by Rockefeller University Press


ARTICLES

Expression cloning of a human Fc receptor for IgA

CR Maliszewski, CJ March, MA Schoenborn, S Gimpel and L Shen
Immunex Corporation, Seattle, Washington 98101.

IgA, the predominant isotype in secretions, mediates the neutralization and removal of environmental antigens from mucosal sites. Although cell surface receptors for the Fc region of IgA (Fc alpha R) have been implicated in a variety of immune effector mechanisms, the molecular features of Fc alpha R remain only marginally characterized. In this report, we describe the isolation of a clone from a myeloid cell line cDNA library that directs the expression of a cell surface molecule with IgA binding specificity. The cDNA encodes a peptide of Mr 30,000 including a putative transmembrane region with features atypical of conventional membrane-anchored proteins. Databank searches indicate that the human myeloid cell Fc alpha R sequence is unique, is a member of the immunoglobulin gene superfamily, and is related to Fc receptors for IgG (Fc gamma RI, II, and III) and IgE (Fc epsilon RI).
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