Changes of Protein Composition in Membrane-Skeleton Complex of Erythrocytes Cryopreserved Under PEO-1500 Protection

Authors

  • Nina G. Zemlyanskikh Institute for Problems of Cryobiology and Cryomedicine of the National Academy of Sciences of Ukraine, Kharkiv, Ukraine
  • Pavlo M. Zubov Institute for Problems of Cryobiology and Cryomedicine of the National Academy of Sciences of Ukraine, Kharkiv, Ukraine
  • Lubov O. Babijchuk Institute for Problems of Cryobiology and Cryomedicine of the National Academy of Sciences of Ukraine, Kharkiv, Ukraine

Keywords:

cryopreservation, PEO-1500, membrane-cytoskeletal complex of erythrocytes

Abstract

When investigating the modification of protein composition of membrane-cytoskeleton complex (MCC) of the erythrocytes cryopreserved under PEO-1500 protection the change of relative content of band 3 protein, ankyrin, protein 4.2 and protein 4.9 in the solutions with high ionic strength and variation of the content of bivalent cations was found. It has been noted that MCC changes in the erythrocytes cryopreserved with PEO-1500 and frozen with no use of cryoprotectants are characterized with some common features. This may be stipulated by the absence inside cells of the substances stabilizing the protein structure at low temperatures. Alterations in MCC of erythrocytes cryopreserved with PEO-1500 protection may be partially reversible if the cells are transferred into physiological conditions.

References

Belous A.M., Bondarenko V.A., Bondarenko T.P. Structural changes of biochemical membranes during cooling.– Kiev: Naukova dumka, 1982.– 255 p.

Belous A.M., Babijchuk L.A., Zemlyanskikh N.G. Effect of dosed treatment with polyethylene oxide of 1500 m.m. on change of shape and permeability of erythrocyte plasma membrane // Doklady AN SSSR.– 1988.– N7.– P. 59-63.

Gulevsky A.K., Bondarenko V.A., Belous A.M. Barrier properties of biomembranes at low temperatures.– Kiev:Naukova dumka, 1988.– 208 p.

Cantor Ch., Schimmel P. Biophysical chemistry. P1. The conformation of biological macromolecules.– Moscow: Mir,1984.– 336 p.

Kozlov M.M., Markin V.S. Membrane skeleton of erythrocyte. Theoretical model // Biol. Membrany.– 1986.– Vol.3, N4.– P. 404-422.

Konev S.V. Structural lability of membranes and regulatory processes.– Minsk: Nauka i tekhnika, 1987.– 240 p.

Pushkar N.S., Shrago M.I., Belous A.M., Kalugin Yu.V. Cryoprotectants.– Kiev: Naukova dumka, 1978.– 204p.

Yakovenko E. E., Rozenberg Yu.M., Kolodey S.V. etc. Analysis of filtration ability of erythrocyte non-homogeneous suspensions // Biol. Membrany.– 2001.– Vol.18, N1.– P. 16-28.

An X.L., Takakuwa Y., Nunomura W., et. al. Modulation of band 3-ankyrin interaction by protein 4.1 // J. Biol. Chem.–1996.– Vol. 271, N52.– Р. 33187-33191.

Azim A.C., Knoll J.H.M., Beggs A.H. et al. Isoform cloning actin binding and chromosomal localization of human erythroid dematin, a member of the villin superfamily // J. Biol. Chem.–1995.– Vol. 270, N29.– P. 17407-17413.

Bruce L.J., Beckmann R., Ribeiro M. et al. A band 3-based maсrocomplex of integral and peripheral proteins in the RBC membrane // Blood.– 2003.– Vol. 101, N10.– P. 4180-4188.

Chasis J.A., Mohandas N., Shohet J.B. Erythrocyte membrane rigidity induced by glycophorin A - ligand interaction: evidence for a ligand-induced association between glycophorin A and skeletal proteins // J. Clin. Invest.– 1985. – Vol. 75, N6.– P. 1919-1926.

Eber S., Lux S.E. Hereditary spherocytosis – defects in proteins that connect the membrane skeleton to the lipid bilayer // Sem. Hematol. – 2004.– Vol. 41, N2.– P. 118-141.

Fairbanks G., Steek T.L., Wallach D.F.H. Electrolytic analysis of the major polypeptides of human erythrocyte membrane // Biochem.– 1971.– Vol. 10, N13.– P. 2606-2617.

Levitt J.A. Sulfhydryl-disulfide hypothesis of frost injury and resistance in plants // J. Theor. Biol.– 1962. – Vol. 3, N??.– P. 355-391.

Mauro-Chanteloup I., Delaunay J., Gane P. et al. Evidence that the red cell skeleton protein 4.2 interacts with the Rh membrane complex member CD47 // Blood.– 2003.– Vol. 101, N1.– P. 338-344.

Risinger M.A., Dolimast E.M., Cohen C.M. Human erythrocyte protein 4.2, a high copy number membrane protein, is N-myristylated // J. Biol. Chem.– 1992.– Vol.267, N8.– P. 5680-5685.

Rybicki A.C., Health R., Wolf G.L. et al. Deficiency of protein 4.2 in erythrocytes from a patient with a Coombs negative hemolytic anemia. Evidence for a role of protein 4.2 in stabilizing ankyrin on the membrane // J. Clin. Invest.– 1988.– Vol.81, N3. – P. 893-901.

Ursitti J.A., Fowler V.M. Immunolocalization of tropomodulin, tropomyosin and actin in spread human erythrocyte skeletons // J. Cell Sci.– 1994.– Vol. 107, Pt. 6.– P. 1633-1639.

Van Dort H.M., Knowles D.W., Chasis J.A. et al. Analysis of integral membrane protein contribution to the deformability and stability of the human erythrocyte membrane // J. Biol. Chem.– 2001.– Vol. 276, N50.– P. 46968-46974.

Vertessy B.G., Steck T.L. Elasticity of human red cell membrane skeleton. Effect of temperature and denaturants // Biophys. J.– 1989.– Vol. 55, N2.– P. 255-262.

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Published

2007-03-15

How to Cite

Zemlyanskikh, N., Zubov, P., & Babijchuk, L. (2007). Changes of Protein Composition in Membrane-Skeleton Complex of Erythrocytes Cryopreserved Under PEO-1500 Protection. Problems of Cryobiology and Cryomedicine, 17(1), 3–15. Retrieved from https://cryo.org.ua/journal/index.php/probl-cryobiol-cryomed/article/view/1955

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Section

Theoretical and Experimental Cryobiology