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Oxidant damage to erythrocyte membrane in glucose-6-phosphate dehydrogenase
deficiency: correlation with in vivo reduced glutathione concentration and
membrane protein oxidation
RM Johnson, Y Ravindranath, M el-Alfy and G Goyette
Department of Pediatrics Wayne State University School of Medicine,
Detroit, MI.
Chronic nonspherocytic hemolytic anemia has been observed in a recently
described glucose-6-phosphate dehydrogenase (G6PD) variant, G6PDWayne. The
mechanical properties of these erythrocytes and other G6PD variants were
examined. The deformability of G6PD-deficient erythrocytes was normal, as
determined by osmotic scan ektacytometry, and was not significantly
affected by hemolytic crisis. In the common varieties of G6PD deficiency,
the mechanical stability of the red blood cell (RBC) membrane was greater
than normal, but G6PDWayne membranes were abnormally susceptible to
shear-induced fragmentation. There was no evidence for a concurrent genetic
defect in spectrin, because self- association constants and tryptic digests
were normal. The fragility of G6PDWayne membranes appeared to be a
consequence of oxidative damage to membrane thiol groups associated with a
low glutathione (GSH) level in these RBCs. Associations among GSH level,
thiol oxidation, and membrane instability were also found when a larger
group of G6PD-deficient RBCs were examined. In normal erythrocytes,
1-chloro-2,4-dinitrobenzene was used to reduce GSH levels by 50%. Membrane
thiol oxidation and membrane fragility both increased when these cells were
kept at 4 degrees C for 3 to 5 days. Our findings suggest that chronic
depletion of GSH leads to the destabilization of membrane skeleton through
oxidation of membrane protein thiols.
Volume 83,
Issue 4,
pp. 1117-1123,
02/15/1994
Copyright © 1994 by The American Society of Hematology
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