Abstract
The action of glucose as an osmolyte in relation to blood cells is not well-characterized in the literature. This study aimed to study the influence of glucose concentration on the stability of red blood cells. The stability of erythrocytes was evaluated by the half-transition point obtained from the curves of lysis induced by glucose in the absence of salt or by increase in medium hypotonicity in the absence and the presence of different concentrations of glucose. In the presence of 0.9 g/dl NaCl, there was no hemolysis with increasing concentration of glucose from 0 to 10 g/dl. In the absence of NaCl, the dependence of hemolysis with the 0–10 g/dl glucose was described by a decreasing sigmoid, with fully lysed and fully protected cells being encountered in the presence of 0–2 and 4–10 g/dl glucose, respectively. The possible origin of such stabilization effect is discussed with base of what is known about osmostabilization of biological complexes and about the influence of glucose on the rheological properties of erythrocytes.
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References
Borowitza, L. J., & Brown, A. D. (1974). The salt relations of marine and halophilic species of the intracellular green alga Dunaliella: The role of glycerol as a compatible solute. Archives of Microbiology, 96, 37–52.
Bowlus, R. D., & Somero, G. N. (1979). Solute compatibility with enzyme function and structure: Rationales for the selection of osmotic and end-products of anaerobic metabolism in marine invertebrates. Journal of Experimental Zoology, 208, 137–151.
Pollard, A., & Wyn-Jones, R. G. (1979). Enzyme activities in concentrated solution of glycinebetaine and other solutes. Planta, 144, 291–298.
Yancey, P. H. (1985). Organic osmotic effectors in cartilaginous fishes. In R. Gilles & M. Gilles-Ballien (Eds.), Transport processes, iono- and osmoregulation (pp. 424–436). Berlin: Springer-Verlag.
Santoro, M. M., Liu, Y., Khan, S. M. A., Hou, L. X., & Bolen, D. W. (1992). Increase thermal stability of proteins in the presence of naturally occurring osmolytes. Biochemistry, 31, 5278–5283.
Yancey, P. H. (2001). Water stress, osmolytes and proteins. American Zoologist, 41, 699–709.
Cunha, C. C., Arvelos, L. R., Costa, J. O., & Penha-Silva, N. (2007). Effects of glycerol on the thermal dependence of the stability of human erythrocytes. Journal of Bioenergetics and Biomembranes, 39, 341–347.
Penha-Silva, N., Arvelos, L. R., Cunha, C. C., Aversi-Ferreira, T. A., Gouvêa-Silva, L. F., Garrote-Filho, M. S., et al. (2008). Effects of glycerol and sorbitol on the thermal dependence of the lysis of human erythrocytes by ethanol. Bioelectrochemistry, 73, 23–29.
Gekko, K., & Timasheff, S. N. (1981). Mechanism of proteins stabilization by glycerol–preferential hydration in glycerol-water mixtures. Biochemistry, 20, 4667–4676.
Gekko, K., & Timasheff, S. N. (1981). Thermodynamic and kinetic examination of proteins stabilization by glycerol. Biochemistry, 20, 4677–4686.
Lee, J. C., & Timasheff, S. N. (1981). The stabilization of proteins by sucrose. Journal of Biological Chemistry, 256, 7193–7201.
Jaenicke, R., & Závodsky, P. (1990). Proteins under extreme physical conditions. Federation of European Biochemical Societies Letters, 268, 344–349.
Lien, Y. H. H., Pacelli, M. M., & Braun, E. J. (1993). Characterization of organic osmolytes in avian renal medulla—A nonurea osmotic gradient system. American Journal of Physiology, 264, R1045–R1049.
Timasheff, S. N. (1993). The control of proteins stability and association by weak-interactions with water–how do solvents affect these processes. Annual Review of Biophysics and Biomolecular Structure, 22, 67–97.
Liu, Y., & Bolen, D. W. (1995). The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes. Biochemistry, 34, 12884–12891.
Taylor, L. S., York, P., Williams, A. C., Edwards, H. G. M., Mehta, C., Jackson, G. S., et al. (1995). Sucrose reduces the efficiency of protein denaturation by chaotropic agent. Biochimica et Biophysica Acta, 1253, 39–46.
Wang, A., & Bolen, D. W. (1997). A naturally occurring protective system in urea-rich cells: Mechanism of osmolyte protection of proteins against urea denaturation. Biochemistry, 36, 9101–9108.
Timasheff, S. N. (1998). Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated. Advances in Protein Chemistry, 51, 355–432.
Timasheff, S. N. (2002). Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components. Proceedings of the National Academy of Sciences of the United States of America, 99, 9721–9726.
Boutron, P., & Arnaud, F. (1984). Comparison of the cryoprotection of red blood cells by 1,2-propanediol and glycerol. Cryobiology, 21, 348–358.
Pellerin-Mendes, C., Million, L., Marchand-Arvier, M., Labrude, P., & Vigneron, C. (1997). In vitro study of the effect of trehalose and dextran during freezing of human red blood cells in liquid nitrogen. Cryobiology, 35, 173–186.
Wagner, C. T., Martowicz, M. L., Livesey, S. A., & Connor, J. (2002). Biochemical stabilization enhances red blood cell recovery and stability following cryopreservation. Cryobiology, 45, 153–166.
Scott, K. L., Lecak, J., & Acker, J. P. (2005). Biopreservation of red blood cells: Past, present, and future. Transfusion Medicine Reviews, 19, 127–142.
de Freitas, M. V., Netto, R. C. M., Huss, J. C. C., de Souza, T. M. T., Costa, J. O., Firmino, C. B., et al. (2008). Influence of aqueous crude extracts of medicinal plants on the osmotic stability of human erythrocytes. Toxicology in Vitro, 22, 219–224.
Buttafava, A., Balduini, C., Minetti, G., & Paula, E. (2008). Resistance of human erythrocyte membranes to Triton X-100 and C12E8. Journal of Membrane Biology, 227, 39–48.
Domingues, C. C., Malheiros, S. V. P., & de Paula, E. (2008). Solubilization of human erythrocyte membranes by ASB detergents. Brazilian Journal of Medical and Biological Research, 41, 758–764.
Fonseca, L., Arvelos, L., Netto, R., Lins, A., Garrote-Filho, M., & Penha-Silva, N. (2010). Influence of the albumin concentration and temperature on the lysis of human erythrocytes by sodium dodecyl sulfate. Journal of Bioenergetics and Biomembranes, 42, 413–418.
Penha-Silva, N., Firmino, C. B., de Freitas Reis, F. G., Huss, J. C. C., de Souza, T. M. T., de Freitas, M. V., et al. (2007). Influence of age on the stability of human erythrocyte membranes. Mechanisms of Ageing and Development, 128, 444–449.
de Freitas, M. V., de Oliveira, M. R., dos Santos, D. F., de Cássia Mascarenhas Netto, R., Fenelon, S. B., & Penha-Silva, N. (2010). Influence of the use of statin on the stability of erythrocyte membranes in multiple sclerosis. Journal of Membrane Biology, 233, 127–134.
Mansur, P. H. G., Cury, L. K. P., Leite, J. O. B., Pereira, A. A., Penha-Silva, N., & Andrade, A. O. (2010). The approximate entropy of the electromyographic signals of tremor correlates with the osmotic fragility of human erythrocytes. BioMedical Engineering OnLine, 9, 29.
Riquelme, B., Foresto, P., D’Arrigo, M., Valverde, J., & Rasia, R. (2005). A dynamic and stationary rheological study of erythrocytes incubated in a glucose medium. Journal of Biochemical and Biophysical Methods, 62, 131–141.
Shin, S., Ku, Y.-H., Suh, J.-S., & Singh, M. (2008). Rheological characteristics of erythrocytes incubated in glucose media. Clinical Hemorheology and Microcirculation, 38, 153–161.
Fonseca, L. C., Correa, N. C. R., Garrote, M. D., Cunha, C. C., & Penha-Silva, N. (2006). Effects of the solvent composition on the stability of proteins in aqueous solutions. Química Nova, 29, 543–548.
Bolen, D. W., & Baskakov, I. V. (2001). The osmophobic effect: Natural selection of a thermodynamic force in protein folding. Journal of Molecular Biology, 310, 955–963.
Wang, A., Robertson, A. D., & Bolen, D. W. (1995). Effects of a naturally-occurring compatible osmolyte on the internal dynamics of ribonuclease-A. Biochemistry, 34, 15096–15104.
Saunders, A. J., Davis-Searles, P. R., Allen, D. L., Pielak, G. J., & Erie, D. A. (2000). Osmolyte-induced changes in protein conformation equilibria. Biopolymers, 53, 293–307.
Qu, Y., Bolen, C. L., & Bolen, D. W. (1998). Osmolyte-driven contraction of a random coil protein. Proceedings of the National Academy of Sciences of the United States of America, 95, 9268–9273.
Bakaltcheva, I. B., Odeyale, C. O., & Spargo, B. J. (1996). Effects of alkanols, alkanediols and glycerol on red blood cell shape and hemolysis. Biochimica et Biophysica Acta, 1280, 73–80.
De Loecker, R., Gossens, W., Van Duppen, V., Verwilghen, R., & De Loecker, W. (1993). Osmotic effects of dilution on erythrocytes after freezing and thawing in glycerol-containing buffer. Cryobiology, 30, 279–285.
Lang, F., Busch, G. L., Ritter, M., Völkl, H., Waldegger, S., Gulbins, E., et al. (1998). Functional significance of cell volume regulatory mechanisms. Physiological Reviews, 78, 247–306.
Bransky, A., Korin, N., Nemirovski, Y., & Dinnar, U. (2007). Correlation between erythrocytes deformability and size: A study using a microchannel based cell analyzer. Microvascular Research, 73, 7–13.
Fields, P. A. (2001). Protein function at thermal extremes: Balancing stability and flexibility. Comparative Biochemistry and Physiology Part A, 129, 417–431.
Waugh, R. E., & Sarelius, I. H. (1996). Effects of lost surface area on red blood cells and red blood cell survival in mice. American Journal of Physiology, 271, C1847–C1852.
Waugh, R. E., Narla, M., Jackson, C. W., Mueller, T. J., Suzuki, T., & Dale, G. L. (1992). Rheologic properties of senescent erythrocytes: Loss of surface area and volume with red blood cell age. Blood, 79, 1351–1358.
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Lemos, G.S.D., Márquez-Bernardes, L.F., Arvelos, L.R. et al. Influence of Glucose Concentration on the Membrane Stability of Human Erythrocytes. Cell Biochem Biophys 61, 531–537 (2011). https://doi.org/10.1007/s12013-011-9235-z
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DOI: https://doi.org/10.1007/s12013-011-9235-z