Українська English

ISSN 2522-9028 (Print)
ISSN 2522-9036 (Online)
DOI: https://doi.org/10.15407/fz

Fiziologichnyi Zhurnal

is a scientific journal issued by the

Bogomoletz Institute of Physiology
National Academy of Sciences of Ukraine

Editor-in-chief: V.F. Sagach

The journal was founded in 1955 as
1955 – 1977 "Fiziolohichnyi zhurnal" (ISSN 0015 – 3311)
1978 – 1993 "Fiziologicheskii zhurnal" (ISSN 0201 – 8489)
1994 – 2016 "Fiziolohichnyi zhurnal" (ISSN 0201 – 8489)
2017 – "Fiziolohichnyi zhurnal" (ISSN 2522-9028)

Fiziol. Zh. 2007; 53(4): 54-59


Changes in protein composition of membranecytoskeletalcomplex in mammalian erythrocytes under cryopreservation

O. Denysova, N. Zemlyanskikh, G. Zhegunov.

    Kharkiv, zooveterinary academy



Abstract

Protein composition of mammalian erythrocyte membrane- cytoskeletal complex under the influence of cryoprotectants and freezing-thawing process was studied by the methods of electrophoresis. No quantitative and qualitative differences in the research objects on basic structural proteins in all experi- mental variants were revealed. Slight changes in cryopre- servation process were noted in bovine erythrocytes, where there was a reduction of protein band 6. This may be related to either cryostability of protein or insufficient sensitivity of the method.

References

  1. Бабійчук Л.О., Землянських Н.Г., Кузьміна Л.М. Новий метод кріоконсервування еритроцитів для клінічної практики // Трансплантологія. – 2000. – 1, № 1. – С. 296–298.
  2. Бейли Н. Статистические методы в биологии. – М.: Мир, 1963. – 71 с.
  3. Белоус А.М., Бондаренко В.А. Структурные изменения биологических мембран при охлаждении. – К.: Наук. думка, 1982. – 255 с.
  4. Гулевский А.К. Барьерно-транспортные свойства плазматических мембран в процессе криокон- сервирования: Автореф. дис. ... д-ра биол. наук. – Харьков, 1986. – 42 с.
  5. Жегунов Г.Ф., Денисова О.Н., Землянских Н.Г. Криоконсервирование и сохранность эритроцитов животных // Проблемы криобиологии. – 2005. – 3, №3. – С. 566–569.
  6. Кудрявцев А.А., Кудрявцева Л.А. Клиническая гематология животных. – М.: Колос, 1974. – 398 с.
  7. Мокеев И. Н. Инфузионно-трансфузионная терапия: Справочник. – М., 1998. – 232 с.
  8. Остерман Л.А. Методы исследования белков и нуклеиновых кислот: Электрофорез и ультра- центрифугирование (практическое пособие). – М.: Наука, 1981. – 288 с.
  9. 9. Пушкарь Н.С., Шраго М.И., Белоус А.М., Калугин Ю.В. Криопротекторы. – К.: Наук. думка, 1978. – 204 с.
  10. 10. Семенова Н.В., Федорова Л.И., Виноградов В.Л. и др. Сравнительное изучение криоконсервиро- ванных эритроконцентратов при различных спосо- бах их отмывания// Гематология и трансфузиол. – 1986. – № 10.– С. 42–52.
  11. Черницкий Е.А., Воробей А.Б. Структура и функ- ция эритроцитарных мембран.- Минск: Наука и техника, 1981. – 213 с.
  12. An X., Lecomte M.C., Chasis J.A. et al. Shear-response of the spectrin dimmer-tetramer equilibrium in the red blood cell membrane // J.Biol.Chem. – 2002. – 277, № 35. – P. 31796–31800
  13. Ballas S.K. Red cell membrane protein in change caused by freezing and mechanism of cryoprotection by glyc- erol // Transfusion. – 1981. – 21, № 2. – P. 203–210.
  14. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utiliz- ing the principle of protein-dye binding // Anal. Biochem. – 1976. – 72. – P. 248–254.
  15. Bruce L.J., Becrmann R., Ribeiro M.L. et al. A band 3- based macrocomplex of integral and peripheral pro- teins in the RBC membrane // Blood. – 2003. – 101, №10. – P. 4180–4188.
  16. Fairbanks G., Steсk T. L., Wallach D. F. H. Electro- lytic analysis of the major polypeptides of the human erythrocyte membrane// Biochemistry. – 1971. – 10. – Р. 2606–2617.
  17. Guerra-Shinohara E.M., Barretto O.C. The erythrocyte cytoskeleton protein 4.2 is not demonstrable in sev- eral mammalian species // Braz. J. Med. Biol. Res. – 1999. – 32, №6. – Р. 683–687.
  18. Matei H., Frentescu L., Benga Gh. Comparative stud- ies of the protein composition of red blood cell membranes from eight mammalian species //J. Cell. Mol. Med. – 2000. – 4, № 4. – Р. 270–276.
  19. 19. Muldrew K., Mcgann L.E., The osmotic rupture hy- pothesis of intracellular freezing // Cryobiology. – 1993. – 30. – P. 620.
  20. 20. Nicola V., Le Van Kim C., Gane P. et al. Rh-RhAG/ ankirin-R, a new interaction site between the membrane bilayer and the red cell skeleton, is impaired by Rh null - associated mutation // J.Biol.Chem. – 2003. – 278, – №28.– P. 25526–25533.
  21. Peters L.L., Jindel Y.K., Gwynn B. et al. Mild spherocy-tosis and altered red cell ion transport in protein 4. 2-null mice // J. Clin. Invest. – 1999 – 11. – P. 1527–1537.
  22. Scott K.L., Lecal J., Acker J.P. Biopreservation of red blood cells: past, present and future // Trans. Med. Reviews. – 2005. – 19, №2. – Р. 127–142.
  23. Shohet S.B. Possible roles for the membrane cytoskel- eton in regulation red cell stability and deformability // Scand. J. Clin. Lab. Invest. Suppl. – 1981. – 156. – P. 123–130.
  24. Wagner C.T., Martowicz M.L., Livesey S.A. et al. Bio- chemical stabilization enhances red blood cell recovery and stability following cryopreservation // Cryobio- logy. – 2002. – 45. – P. 153–166.
  25. Walson P.F., Kunze E., Cramer P., Hammerstedt R.H. A comparison of critical osmolarity and hydraulic conductivity and its activation energy in fowl and bull spermatozoa // J.Androl. – 1992. – 13. – P. 131–138.

© National Academy of Sciences of Ukraine, Bogomoletz Institute of Physiology, 2014-2024.