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Altered band 3 structure and function in glycophorin A- and B-deficient
(MkMk) red blood cells
LJ Bruce, JD Groves, Y Okubo, B Thilaganathan and MJ Tanner
Department of Biochemistry, School of Medical Sciences, University of
Bristol, UK.
The anion transport activity of the human erythrocyte anion transporter
(band 3; AE1) has been examined in both normal and glycophorin A (GPA)-
deficient (MkMk) human red blood cells (RBCs). The sulfate transport
activity of MkMk cells (from two ethnically diverse sources) was
approximately 60% that of normal erythrocytes under the transport assay
conditions used. However, MkMk and normal RBCs contained similar amounts of
band 3. The reduction in sulfate transport activity was shown to be caused
by an increase in the apparent Km for sulfate in MkMk RBCs, suggesting the
band 3 in the MkMk RBCs has a lowered binding affinity for sulfate anions.
The size of the N-glycan chain on band 3 of the MkMk cells was larger than
that on band 3 from normal RBCs. In contrast, the size of the N-glycan
chain on the glucose transporter (GLUT1) from MkMk cells was smaller than
that on GLUT1 from normal cells. The possible role of GPA in the
biosynthesis and anion transport activity of band 3 in normal RBCs is
discussed.
Volume 84,
Issue 3,
pp. 916-922,
08/01/1994
Copyright © 1994 by The American Society of Hematology
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