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Membrane glycoprotein modifications of G6PD deficient red blood cells
Author(s) -
HORN S.,
BASHAN N.,
PELEG N.,
GOPAS J.
Publication year - 1995
Publication title -
european journal of clinical investigation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.164
H-Index - 107
eISSN - 1365-2362
pISSN - 0014-2972
DOI - 10.1111/j.1365-2362.1995.tb01522.x
Subject(s) - glycoprotein , membrane glycoproteins , red blood cell , erythrocyte membrane , membrane , microbiology and biotechnology , chemistry , biochemistry , medicine , biology
. 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 macrophages, without pre‐exposure to oxidants in vivo . Phagocytosis was partially (60%) inhibited by incubating macrophages with either galactose or mannose, or by incubating RBCs with β‐galactosidase, indicating the involvement of lectin‐like receptors in the recognition of G6PD deficient RBCs. Membrane glycoproteins on G6PD deficient cells were detected by binding of Con A to both intact RBCs and to purified membrane proteins. The results demonstrated modifications in the glycoprotein pattern of G6PD deficient RBCs compared to untreated controls. These included reduction in the amounts of several high molecular weight glycoproteins and appearance of lower molecular weight bands. These results suggest that G6PD deficient RBCs undergo glycoprotein modifications, which may lead to premature removal from circulation, even in non‐acute hemolysis.