Affiliations: [a] Department of Physiology, Nippon Medical School, Sendagi 1-1-5, Bunkyo-ku, Tokyo 113, Japan | [b] Division of Biochemistry, Institute of Medical Science, The Jikei University School of Medicine, Tokyo, Japan | [c] Department of Neurology, Faculty of Medicine, Kyoto University, Kyoto, Japan | [d] Laboratory of Chemical Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA
Note: [] Accepted by: Editor N. Ohshima
Abstract: The effect of superoxide anions (O2−) on red blood cells (RBC) deformability and membrane proteins was investigated using hypoxanthine-xanthine oxidase system. Exposure of RBC to O2− caused a marked decrease in RBC deformability with a concomitant increase in cell volume and shape changes. The RBC exposed to O2− also displayed pronounced degradation of membrane proteins such as band 3 protein and spectrin; new bands of low molecular weight products appeared as the original membrane proteins tended to diminish, without the appearance of high molecular weight products. Since the membrane proteins are involved in processes regulating membrane properties such as permeability and viscoelasticity, the decreased deform ability induced by O2− may be attributable to changes in membrane proteins. Interestingly, resealed ghosts exposed to O2− did not show any significant change in membrane proteins, which suggests the existence of further generation of O2− and subsequent production of other active oxygen species mediated by O2−-initiated autoxidation of hemoglobin in intact RBC. Furthermore, electrophoretic analysis suggested that active oxygens increased the endogenous proteolytic susceptibility of RBC. In conclusion, a close linkage was suggested between RBC deformability and the membrane proteins.
Keywords: red blood cells (RBC), superoxide anion, deformability, membrane protein, band 3 protein
DOI: 10.3233/BIR-1992-292-303
Journal: Biorheology, vol. 29, no. 2-3, pp. 217-229, 1992
