MEMBRANE GLYCOPROTEIN MODIFICATIONS OF G6PD DEFICIENT RED-BLOOD-CELLS

In this study, the composition and the role of membrane glycoproteins in phagocytosis were determined in G6PD deficient RBCs. G6PD deficient RBCs were recognized and significantly phagocytosed by murine macroph ages, without pre-exposure to oxidants in vivo. Phagocytosis was parti ally (60%) inhibited by incubating macrophages with either galactose o r mannose, or by incubating RBCs with beta-galactosidase, indicating t he involvement of lectin-like receptors in the recognition of G6PD def icient RBCs. Membrane glycoproteins on G6PD deficient cells were detec ted by binding of Con A to both intact RBCs and to purified membrane p roteins. The results demonstrated modifications in the glycoprotein pa ttern of G6PD deficient RBCs compared to untreated controls. These inc luded reduction in the amounts of several high molecular weight glycop roteins and appearance of lower molecular weight bands. These results suggest that G6PD deficient RBCs undergo glycoprotein modifications, w hich may lead to premature removal from circulation, even in non-acute hemolysis.