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Alteration of the erythrocyte membrane skeletal ultrastructure in
hereditary spherocytosis, hereditary elliptocytosis, and pyropoikilocytosis
SC Liu, LH Derick, P Agre and J Palek
Department of Biomedical Research, St Elizabeth's Hospital, Boston, MA
02135.
The membrane skeleton of normal erythrocytes is largely organized into a
hexagonal lattice of junctional complexes (JC) crosslinked by spectrin
tetramers, and occasional double tetramers and hexamers. To explore
possible skeletal alterations in hereditary spherocytosis (HS),
elliptocytosis (HE), and pyropoikilocytosis (HPP), we have studied the
ultrastructure of the spread membrane skeletons from a subpopulation of HS
patients with a partial spectrin deficiency ranging from 43% to 86% of
normal levels, and in patients with HPP who, in addition to a mild spectrin
deficiency, also carried a mutant spectrin that was dysfunctional, thus
reducing the ability of spectrin dimers to assemble into tetramers.
Membrane skeletons derived from Triton-treated erythrocyte ghosts were
examined by negative staining electron microscopy. HS membrane skeletons
contained structural elements, consisting of JC and spectrin filaments
similar to the normal skeleton. However, less spectrin filaments
interconnected the JC, and the decrease of spectrin filaments attached to
JC appeared to correlate with the severity of spectrin deficiency. Only in
severe HS associated with severe spectrin deficiency was the loss of
spectrin sufficient enough to disrupt the overall skeletal architecture. In
contrast, membrane skeletons prepared from red blood cells (RBCs) of
subjects with HPP were strikingly different from HS RBCs with a comparable
degree of spectrin deficiency. Although HPP RBCs were only mildly deficient
in spectrin, their skeletal lattice was grossly disrupted, in contrast to
only mild ultrastructural abnormalities of HS membrane skeletons with a
nearly identical degree of spectrin deficiency. Skeletons from patients
with common mild HE or asymptomatic carriers, carrying the mutant spectrin
but having normal spectrin content, exhibited a moderate disruption of the
skeletal lattice. We propose that the above differences in skeletal
ultrastructure may underlie differences in the biomechanical properties and
morphology of HS, HE, and HPP RBCs.
Volume 76,
Issue 1,
pp. 198-205,
07/01/1990
Copyright © 1990 by The American Society of Hematology
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