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Molecular basis of altered red blood cell membrane properties in Southeast
Asian ovalocytosis: role of the mutant band 3 protein in band 3
oligomerization and retention by the membrane skeleton
SC Liu, J Palek, SJ Yi, PE Nichols, LH Derick, SS Chiou, D Amato, JD Corbett, MR Cho and DE Golan
Department of Biomedical Research, St Elizabeth's Medical Center of Boston,
Tufts University Medical School, MA 02135, USA.
Southeast Asian ovalocytosis (SAO) is an asymptomatic trait characterized
by rigid, poorly deformable red cells that resist invasion by several
strains of malaria parasites. The underlying molecular genetic defect
involves simple heterozygous state for a mutant band 3 protein, which
contains a deletion of amino acids 400 through 408, linked with a Lys
56-to-Glu substitution (band 3-Memphis polymorphism). To elucidate the
contribution of the mutant SAO band 3 protein to increased SAO red blood
cell (RBC) rigidity, we examined the participation of the mutant SAO band 3
protein in increased band 3 attachment to the skeleton and band 3
oligomerization. We found first that SAO RBC skeletons retained more band 3
than normal cells and that this increased retention preferentially involved
the mutant SAO band 3 protein. Second, SAO RBCs contained a higher
percentage of band 3 oligomer-ankyrin complexes than normal cells, and
these oligomers were preferentially enriched by the mutant SAO protein. At
the ultrastructural level, the increased oligomer formation of SAO RBCs was
reflected by stacking of band 3-containing intramembrane particles (IMP)
into longitudinal strands. The IMP stacking was not reversed by treating
SAO RBCs in alkaline pH (pH 11), which is known to weaken ankyrin-band 3
interactions, or by removing the cytoplasmic domain of band 3 from SAO
membranes with trypsin. Finally, we found that band 3 protein in intact SAO
RBCs exhibited a markedly decreased rotational mobility, presumably
reflecting the increased oligomerization and the membrane skeletal
association of the SAO band 3 protein. We propose that the mutant SAO band
3 has an increased propensity to form oligomers, which appear as
longitudinal strands of IMP and exhibit increased association with membrane
skeleton. This band 3 oligomerization underlies the increase in membrane
rigidity by precluding membrane skeletal extension, which is necessary for
membrane deformation.
Volume 86,
Issue 1,
pp. 349-358,
07/01/1995
Copyright © 1995 by The American Society of Hematology
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