Abstract
Membrane protein modification can change cell surface properties which canbe correlated with altered macrophage-erythrocyte interactions. Mouseerythrocytes were incubated in phosphate buffer for different times toinduce protein modification. Mouse erythrocyte membrane changes wereanalyzed by infrared analyses and gel electrophoresis. Proteolyticdigestion of membrane proteins was observed. After 22 hours preliminaryincubation, the number of erythrocytes adhering to a monolayer ofmacrophages reached a maximum, the majority of which had not beenphagocytosed. Most of the erythrocytes incubated for 40 hours underwentphagocytosis after adhesion to the macrophages.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
REFERENCES
Brovelli, A. et al. (1991) Red Blood Cell Aging (Magnani, M. and De Flora, A., eds.). Plenum Press, New York, pp. 59–63.
Bartosz, G. (1991) Erythrocyte aging: physical and chemical membrane changes. Gerontology 37:33–67.
Kay, M. M. B., Wyant, T. and Goodman, J. (1994) Autoantibodies to band 3 during aging and disease and aging interventions. Ann. N.Y. Acad. Sci. USA 719:419–447.
Schluter, K., and Drenckhanhn, D. (1986). Co-clustering of denatured hemoglobin with band 3: Its role in binding of autoantibodies against band 3 to abnormal and aged erythrocytes. Proc. Natl. Acad. Sci. USA 83:6137–6141.
Lutz, H. U. (1992) Naturally occurring anti-band 3 antibodies. Transfusion Medicine Reviews 6:201–211.
Beppu, M., Ochiai, H., and Kikugawa, K. (1989) Macrophage recognition of periodate-treated erythrocytes: Involvement of disulfide formation of the erythrocyte membrane proteins. Biochim. Biophys. Acta. 979:35–45.
Beppu, M., Takahashi, T., Kashiwada, M., Masukawa, S., and Kikugawa, K. (1994) Macrophage recognition of saccharide chains on the erythrocytes damaged by iron-catalyzed oxidation. Arch. Biochem. Biophys. 312:189–197.
Stocchi, V. et al. (1994) Inactivation of rabbit red blood cell hexoquinase activity promoted in vitro by an oxygen-radical generation system. Arch. Biochem. Biophys. 311:160–167.
Turrini, F., Manu, F., Cappadoro, M., Ulliers, D., Giribaldi, G., and Arese, P. (1994) Binding of naturally occurring antibodies to oxidatively and nonoxidatively modified erythrocyte band 3. Biochim. Biophys. Acta 1190:297–303.
Ferrali, M., Signorini, C., Ciccoli, L., and Comporti, M. (1992) Iron released from an erythrocyte lysate by oxidative stress is diffusible and in redox active form. Biochem. J. 285:295–301.
Ferrali, M., Signorini, C., Ciccoli, L. and Comporti, M. (1993) Iron release and membrane damage in erythrocytes exposed to oxidizing agents: phenylhydrazine, divicine and isouramil. FEBS Letters 319:40–44.
Signorini, C., Ferrali, M., Ciccoli, L., Sugherini, L., Magnani, A., and Comporti, M. (1995) Iron release, membrane protein oxidation and erythrocyte ageing. FEBS Letters 362:165–170.
Alvarez, F. J., Jordán, J. A., Herr\'aez, A., Díez, J. C., and Tejedor, M. C. (1998) Hypotonically loaded rat erythrocytes deliver encapsulated substances into peritoneal macrophages. J. Biochem. 123:233–239.
Alvarez et al. (1998) Cross-linking treatment of loaded erythrocytes increases delivery of encapsulated substance to macrophages. Biotechnol. Appl. Biochem. 27:139–143.
Jordán, J. A. et al. (1998) Differential induction of macrophage recognition of carrier erythrocytes by treatment with band 3 cross-linkers. Biotechnol. Appl. Biochem. 27:133–137.
Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685.
Jordán, J. A., DeLoach, J. R., Luque, J., and Díez, J. C. (1996) Targeting of mouse erythrocytes by band 3 crosslinkers. Biochim. Biophys. Acta. 1291:27–34.
Morrison, M., Michaels, A. W., Phillips, D. R. and Choi, S. (1974) Life span of erythrocyte membrane protein. Nature 248:763–789.
Vaysse, J., Gattegno, L., Bladier, D., and Aminoff, D. (1986) Adhesion and erythrophagocytosis of human senescent erythrocytes by autologous monocytes and their inhibition by beta-galactosyl derivatives. Proc. Natl. Acad. Sci. USA 83:1339–1343.
Davies, K. J. A., and Goldberg, A. L. (1987) Oxygen radicals stimulate intracellular proteolysis and lipid peroxidation by independent mechanism in erythrocytes. J. Biol. Chem. 263:8220–8226.
Kay, M. M. B. (1983) Appearance of a terminal differentiation antigen on senescent and damaged cells and its implications for physiologic autoantibodies. Biomembrane 11:119–159.
Beppu, M., Iosue, M., Ishikawa, T., and Kikugawa, K. (1994) Presence of membrane bound proteinases that preferentially degrade oxidatively damaged erythrocyte proteins as secondary antioxidant defense. Biochim. Biophys. Acta 1196:81–87.
Beppu, M., Takahashi, T., Hayshi, T., and Kikugawa, K. (1994) Mechanism of macrophage recognition of SH-oxidized erythrocytes: recognition of glycophorin A on erythrocytes by a macrophage receptor for sialosaccharides. Biochim. Biophys. Acta 1223:55–56.
Lutz, H. U. et al. (1987) Naturally occurring anti-band 3 antibodies and complement together mediate phagocytosis of oxidatively stressed human erythocytes. Proc. Natl. Acad. Sci. USA 84:7368–7372.
Sambrano, G. R., Parthasarathy, S., and Steinberg, D. (1994) Recognition of oxidatively damaged erythrocytes by a macrophage receptor with specificity for oxidized low density lipoprotein. Proc. Natl. Acad. Sci. USA 91:3265–3269.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Olmos, G., Lotero, L.A., Herráez, A. et al. Influence of Aerobic Oxidation of Mouse Erythrocytes on their Recognition by Macrophages. Biosci Rep 20, 157–166 (2000). https://doi.org/10.1023/A:1005511402046
Issue Date:
DOI: https://doi.org/10.1023/A:1005511402046