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Relationship of the human erythrocyte Wrb antigen to an interaction between
glycophorin A and band 3
MJ Telen and JA Chasis
Department of Medicine, Duke University Medical Center, Durham, NC 27710.
The Wrb antigen is a high-frequency human erythrocyte antigen invariably
absent from En (a-) erythrocytes, which lack glycophorin A. However,
glycophorin A from En (a+) Wr (a+b-) red cells has an amino acid sequence
identical to that of glycophorin A from Wr (b+) erythrocytes. Evidence has
suggested that the Wrb antigen may require the interaction of glycophorin A
with either a lipid moiety or with another erythrocyte-integral membrane
protein, band 3. We have investigated the role of band 3 in Wrb expression
using murine monoclonal antibodies (MoAbs) with Wrb specificity. These
antibodies reacted by radioimmunoassay (RIA) only with cells expressing
both glycophorin A and band 3. In immunoprecipitation studies, Wrb
antibodies immunoprecipitated both band 3 and glycophorin A, while
antibodies specific for band 3 or glycophorin precipitated only the protein
with which they were reactive. These data strongly suggest that band 3 is
the other membrane component necessary for expression of Wrb and that band
3 and glycophorin A are closely associated in the erythrocyte membrane.
Volume 76,
Issue 4,
pp. 842-848,
08/15/1990
Copyright © 1990 by The American Society of Hematology
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