Modification of glycophorin A during oxidation of erythrocyte membrane

Beppu, Masatoshi; Takanashi, Masaya; Murakami, Koji; Kato, Tetsuta; Kikugawa, Kiyomi

doi:10.1016/0005-2736(90)90134-a

Cited by 3 publications

(2 citation statements)

References 30 publications

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“…1, 2, 2.1, and 4.1 [13], and in band Nos. 1, 2, 3, 4.1, 4.2, 5, and 6 oxidized during lipid oxidation [2]. The erythrocyte membrane skeleton has previously been identified with inner surface fibrillar material, and stabilizes the cell shape and maintains the membrane structure [11].…”

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confidence: 99%

Increase in Oxidized Proteins in Theileria sergenti-Infected Erythrocyte Membrane.

Yagi

Thongnoon²,

Shiono

et al. 2002

The Journal of Veterinary Medical Science

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ABSTRACT. As a part of the elucidation of the pathogenesis of anemia in Theileria sergenti infection, oxidized-erythrocyte membrane proteins (OEMPs) collected from T. sergenti-infected calves were examined. The amount of OEMPs were seen to increase with the progress of the anemia and showed a maximum value around the crisis period of the infection. The increase of OEMPs coincided with band N os. 1, 2, 2.1, 3, 4.1, 5, 6, and 7. The majority of them was located at the Triton X-100 un-extractive phase, and was confirmed as cytoskeletal proteins. This evidence indicates the enhancement of erythrocytic oxidation, and suggests that it might be one of the aggravati ng factors of anemia in T. sergenti infection.

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confidence: 99%

Increase in Oxidized Proteins in Theileria sergenti-Infected Erythrocyte Membrane.

Yagi

Thongnoon²,

Shiono

et al. 2002

The Journal of Veterinary Medical Science

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“…Modifications of cells membrane glycoproteins (mainly band 3 and glycophorine A) due to scenescence or oxidation have been previously described [24,25]. Those glycoproteins are known to be modified during blood preservation, oxidation and in various hemolytic anaemias [21,22,38,45,46]. In G6PD deficient RBCs, in contrast to scenescence or oxidation of RBCs in vitro, we could not demonstrate any significant change in the amount of sugars recognized by Con A in band 3.…”

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confidence: 99%

Membrane glycoprotein modifications of G6PD deficient red blood cells

Horn

Bashan

Peleg

et al. 1995

Eur J Clin Investigation

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Abstract. 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 ,f3-galactosidase, indicating the involvement of lectinlike 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.

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The inverted hexagonal phase is more sensitive to hydroperoxidation than the multilamellar phase in phosphatidylcholine and phosphatidylethanolamine aqueous dispersions

et al. 1992

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The effect of phase behaviour (hexagonal II phase and lamellar phase) on the peroxidation of membrane phospholipids has been investigated in dilinoleoyl phosphatidylcholine (DLPC)/dilinoleoyl phosphatidylethanolamine (DLPE) aqueous dispersions. Peroxidation was initiated with a water-soluble radical inducer 2,2'-azobis (2-amidino-propane) dihydrochloride (AAPN). The phospholipid morphology was monitored by 31P-nuclear magnetic resonance (NMR). Phospholipid hydroperoxides (PCOOH and PEOOH) were determined by chemiluminescence high-performance liquid chromatography (CL-HPLC). In pH-induced phase transition systems, DLPE in the bilayer state was much less oxidized than in the hexagonal II state. In composition-induced phase transition systems, the formation of total hydroperoxides and the consumption of alpha-tocopherol in the hexagonal II phase were greater than in the bilayer phase. These data suggest that the hexagonal II phase is more sensitive to hydroperoxidation than the bilayer phase in phospholipid aqueous dispersions.

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Modification of glycophorin A during oxidation of erythrocyte membrane

Cited by 3 publications

References 30 publications

Increase in Oxidized Proteins in Theileria sergenti-Infected Erythrocyte Membrane.

Increase in Oxidized Proteins in Theileria sergenti-Infected Erythrocyte Membrane.

Membrane glycoprotein modifications of G6PD deficient red blood cells

The inverted hexagonal phase is more sensitive to hydroperoxidation than the multilamellar phase in phosphatidylcholine and phosphatidylethanolamine aqueous dispersions

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