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Cloning and characterization of Fc alpha Rb, a novel Fc alpha receptor
(CD89) isoform expressed in eosinophils and neutrophils
TB van Dijk, M Bracke, E Caldenhoven, JA Raaijmakers, JW Lammers, L Koenderman and RP de Groot
Department of Pulmonary Diseases, University Hospital Utrecht, The
Netherlands.
The Fc receptor for IgA (Fc alpha R, CD89) is a transmembrane glycoprotein
found on monocytes, macrophages, neutrophils, and eosinophils. Here we
describe the characterization of a novel isoform of the Fc alpha R cloned
from a human eosinophil cDNA library. This clone, Fc alpha Rb, lacks the
exon encoding the transmembrane/intracellular region of wild type Fc alpha
R, which is replaced by 23 new amino acids. Expression of Fc alpha Rb mRNA
could be detected in eosinophils and neutrophils. IIA1.6 murine pro-B cells
transfected with Fc alpha Rb cDNA secrete high levels of the protein, but
also a substantial amount of Fc alpha Rb is expressed at the cell membrane.
Membrane-bound Fc alpha Rb binds IgA-coated beads equally well as wild type
Fc alpha R. Surface expression is not affected by phosphatidyl inositol
phospholipase C, indicating that glycosyl phosphatidyl inositol-linkage of
Fc alpha Rb is not likely. In IIA1.6 cells expressing Fc alpha Rb and FcR
gamma, which is necessary for signal transduction by wild type Fc alpha R,
no tyrosine phosphorylation or Ca(2+)-mobilization could be observed after
receptor cross-linking. These results indicate that Fc alpha Rb is likely
to have a different function than wild-type Fc alpha R receptor.
Volume 88,
Issue 11,
pp. 4229-4238,
12/01/1996
Copyright © 1996 by The American Society of Hematology
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