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WH Reinhart, LP Sung and S Chien
The ultimate cause of destruction of red blood cells (RBCs) after oxidative
damage with Heinz body formation is not well understood. We correlated the
changes in RBC morphology and membrane protein composition after oxidant
treatment with the alterations in deformability of whole cells and cell
membranes. The incubation of RBCs with phenylhydrazine concentrations of
0.3 to 100 mg/dL at 37 degrees C for one hour led to a dose-dependent
formation of Heinz bodies, ranging from isolated Heinz bodies at 1 mg/dL to
a confluent coating of the inner membrane surface at 100 mg/dL
phenylhydrazine. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis
revealed the presence of a large quantity of hemoglobin bound to the ghost
membrane of treated RBCs. Electrophoresis with and without dithiothreitol
indicated that disulfide bridges are abundant between hemoglobin molecules
and are also present among membrane proteins but are not the major bond
between hemoglobin and membrane. Changes of spectrin, ankyrin, band 3, and
band 6 and the appearance of a 260,000-dalton complex were also observed.
With phenylhydrazine concentrations below 30 mg/dL, even in the presence of
multiple Heinz bodies, the RBC deformability measured by filtration through
2.6-, 4.5-, and 6.8-microns pores and the membrane deformability determined
by a filter aspiration technique were not altered. With 100 mg/dL
phenylhydrazine, when the entire membrane was coated with Heinz bodies, RBC
filterability and membrane deformability were drastically reduced. These
results indicate that oxidative damage of RBCs with discrete Heinz body
formation causes focal membrane rigidification but does not affect the
global cellular deformability until the Heinz bodies nearly cover the
entire cell endoface.
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| Copyright © 1986 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||
