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Globin-chain specificity of oxidation-induced changes in red blood cell
membrane properties
SL Schrier and N Mohandas
Division of Hematology, Stanford University School of Medicine, CA
94305-5112.
We have previously shown that excess unpaired alpha- and beta-globin chains
in severe alpha- and beta-thalassemia interacting with the membrane
skeleton induce different changes in membrane properties of red blood cells
(RBCs) in these two phenotypes. We suggest that these differences in
membrane material behavior may reflect the specificity of the membrane
damage induced by alpha- and beta-globin chains. To further explore this
hypothesis, we sought in vitro models that induce similar membrane
alterations in normal RBCs. We found that treatment of normal RBCs with
phenylhydrazine produced rigid and mechanically unstable membranes in
conjunction with selective association of oxidized alpha-globin chains with
the membrane skeleton, features characteristic of RBCs in severe
beta-thalassemia. Methylhydrazine, in contrast, induced selective
association of oxidized beta-globin chains with the membrane skeleton and
produced rigid but hyperstable membranes, features that mimicked those of
RBCs in severe alpha- thalassemia. These findings suggest that consequences
of oxidation induced by globin chains are quite specific in that those
agents that cause alpha-globin chain accumulation at the membrane produce
rigid but mechanically unstable membranes, whereas membrane accumulation of
beta- globin chains results in rigid but mechanically stable membranes.
These in vitro experiments lend further support to the hypothesis that
membrane-associated alpha- and beta-chains induce oxidative damage to
highly specific different skeletal components and that the specificity of
this skeletal damage accounts for the differences in material membrane
properties of these oxidatively attacked RBCs and perhaps of alpha- and
beta-thalassemic RBCs as well.
Volume 79,
Issue 6,
pp. 1586-1592,
03/15/1992
Copyright © 1992 by The American Society of Hematology
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