Expression cloning of a human Fc receptor for IgA
| Autor: | Li Shen, Charles R. Maliszewski, M. A. Schoenborn, C. J. March, S D Gimpel |
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| Jazyk: | angličtina |
| Rok vydání: | 1990 |
| Předmět: |
IgA binding
Glycosylation Rosette Formation T-Lymphocytes Immunology Molecular Sequence Data Palatine Tonsil Restriction Mapping Fc receptor Gene Expression Receptors Fc Biology Immunoglobulin G Cell Line Sequence Homology Nucleic Acid Immunology and Allergy Humans Amino Acid Sequence Cloning Molecular Receptors Immunologic Receptor Opsonin Gene Library Base Sequence Articles DNA Flow Cytometry Fragment crystallizable region Molecular biology Raji cell Immunoglobulin A biology.protein Antibody |
| Zdroj: | The Journal of Experimental Medicine |
| ISSN: | 1540-9538 0022-1007 |
| Popis: | 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). |
| Databáze: | OpenAIRE |
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