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Blood, 15 April 2001, Vol. 97, No. 8, pp. 2496-2505
RED CELLS
Coexpression of band 3 mutants and Rh polypeptides: differential
effects of band 3 on the expression of the Rh complex containing D
polypeptide and the Rh complex containing CcEe polypeptide
Roland Beckmann,
Jonathan
S. Smythe,
David J. Anstee, and
Michael J. A. Tanner
From the Department of Biochemistry, University of
Bristol, and the Bristol Institute for Transfusion Sciences, United
Kingdom.
K562 cells were stably transfected with cDNAs encoding the band 3 found in Southeast Asian ovalocytosis (B3SAO, deletion of residues
400-408), band 3 with a transport-inactivating E681Q point mutation
(B3EQ), or normal band 3 (B3). Flow cytometric analysis and
quantitative immunoblotting revealed that B3SAO expressed alone was
translocated to the plasma membrane, at levels similar to B3 or B3EQ.
Nine monoclonal antibodies that reacted with extracellular loops of B3
also reacted with B3SAO, although the affinity of most antibodies for
the mutant protein was reduced. Both known Wrb epitopes
were expressed on K562/B3SAO cells, demonstrating that B3SAO interacts
with glycophorin A. The growth rates of K562 clones expressing
equivalent amounts of B3 and B3EQ were the same, suggesting that the
potentially toxic transport function of band 3 may be regulated in K562
cells. The band 3-mediated enhancement of Rh antigen reactivity and
the depression of Rh epitopes on SAO erythrocytes were investigated by
comparing the coexpression of B3, B3SAO, or B3EQ in K562 clones
expressing exogenous RhcE or RhD polypeptides. The results are
consistent with an interaction between band 3 and the Rh
polypeptide-Rh glycoprotein (RhAG) complex, which may enhance
translocation of the complex or affect its conformation in the plasma
membrane. The data suggest that the interaction between band 3 and the
RhD-RhAG complex is weaker than it is between band 3 and the
RhCcEe-RhAG complex.
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