Ukr.Biochem.J. 2014; Volume 86, Issue 2, Mar-Apr, pp. 41-49

doi: http://dx.doi.org/10.15407/ubj86.02.041

Quantitative changes of main components of erythrocyte membranes which define architectonics of cells under pttg gene knockout

05.06.2015   Uncategorized   No comments

О. P. Kanyuka1, Ye. Z. Filyak1, O. R. Kulachkovskyy1, Y. L. Osyp2, N. O. Sybirna1

1Ivan Franko Lviv National University, Ukraine;
e-mail: kanokaol@yahoo.com;
2Lesya Ukrainka Eastern European National University, Lutsk, Ukraine

A pttg gene knockout affects the functional state of erythron in mice which could be associated with structural changes in the structure of erythrocyte membranes. The pttg gene knockout causes a significant modification of fatty acids composition of erythrocyte membrane lipids by reducing the content of palmitic acid and increasing of polyunsaturated fatty acids amount by 18%. Analyzing the erythrocyte surface architectonics of mice under pttg gene knockout, it was found that on the background of reduction of the functionally complete biconcave discs population one could observe an increase of the number of transformed cells at different degeneration stages. Researches have shown that in mice with a pttg gene knockout compared with a control group of animals cytoskeletal protein – β-spectrin was reduced by 17.03%. However, there is a reduction of membrane protein band 3 by 33.04%, simultaneously the content of anion transport protein band 4.5 increases by 35.2% and protein band 4.2 by 32.1%. The lectin blot analysis has helped to reveal changes in the structure of the carbohydrate determinants of ery­throcyte membrane glycoproteins under conditions of directed pttg gene inactivation, accompanied by changes in the type of communication, which joins the terminal residue in carbohydrate determinant of glycoproteins. Thus, a significant redistribution of protein and fatty acids contents in erythrocyte membranes that manifested in the increase of the deformed shape of red blood cells is observed under pttg gene knockout.

Keywords: , , , , , ,

References:

  1. Kanyuka OP, Filyak YeZ, Sybirna NA. Peculiarities of structural and functional organization of erythrocyte membranes in mice of wild-type and mice with pttg gene knockout. Studia Biologica. 2011; 5(1):97-101.
  2. Zhang X, Horwitz GA, Prezant TR, Valentini A, Nakashima M, Bronstein MD, Melmed S. Structure, expression, and function of human pituitary tumor-transforming gene (PTTG). Mol Endocrinol. 1999 Jan;13(1):156-66. PubMed, CrossRef
  3. Wang Z, Yu R, Melmed S. Mice lacking pituitary tumor transforming gene show testicular and splenic hypoplasia, thymic hyperplasia, thrombocytopenia, aberrant cell cycle progression, and premature centromere division. Mol Endocrinol. 2001 Nov;15(11):1870-9. PubMed, CrossRef
  4. Bacac M, Fusco C, Planche A, Santodomingo J, Demaurex N, Leemann-Zakaryan R, Provero P, Stamenkovic I. Securin and separase modulate membrane traffic by affecting endosomal acidification. Traffic. 2011 May;12(5):615-26. PubMed, CrossRef
  5. Kozinets GI, Shishkanova ZG, Novoderzhkina YuK,  Kozinets GI, Shishkanova ZG, Novoderzh­kina YuK. The configuration and the surface of blood cells in norm and pathology. Moscow: Triada-farm, 2004. 17 p.
  6. Novitsky VV, Ryazantseva  NV, Stepovaya EA. Fiziologiya i patofiziologiya eritrotsita [Erythrocyte physiology and patophysiology]. Tomsk: Uzd-vo Tomskogo un-ta, 2004. 200 p.
  7. Pogorelov VM, Kozinets GI. Diagnostic significance of the morphological features of erythrocytes in the peripheral blood smear. Hematol Transfusiol. 2005;50(5):13-17.
  8. Folch J, Lees M, Sloane Stanley GH. A simple method for the isolation and purification of total lipides from animal tissues. J Biol Chem. 1957 May;226(1):497-509. PubMed
  9. Sinyak KM, Orgel MYa, Krug VI.  Method of preparation of blood lipids for gas-chromatographic analysis. Lab Delo. 1976;(1):37-41. Russian. PubMed
  10. Dodge JT, Mitchell C, Hanahan DJ. The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. Arch Biochem Biophys. 1963 Jan;100(1):119-30. PubMed, CrossRef
  11. Gimsa J. A possible molecular mechanism governing human erythrocyte shape. Biophys J. 1998 Jul;75(1):568-9. PubMed, PubMedCentral, CrossRef
  12. Kolosova MV.  Common patterns and mechanisms of peripheral compartment of the erythron abnormalities under typical pathological processes during the  children’s diseases: Dis. … d-ra med. nauk.  Tomsk, 1999. 468 p.
  13. Chen JY, Huestis WH. Role of membrane lipid distribution in chlorpromazine-induced shape change of human erythrocytes. Biochim Biophys Acta. 1997 Jan 31;1323(2):299-309. PubMed, CrossRef
  14. Nakamura MT, Nara TY. Structure, function, and dietary regulation of delta6, delta5, and delta9 desaturases. Annu Rev Nutr. 2004;24(1):345-76. Review. PubMed, CrossRef
  15. Maretzki D, Mariani M, Lutz HU. Fatty acid acylation of membrane skeletal proteins in human erythrocytes. FEBS Lett. 1990 Jan 1;259(2):305-10. PubMed, CrossRef
  16. Gula NM, Margitych VM. Fatty acids and their derivatives thereof under pathological conditions.  K.: Naukova dumka, 2009. 335 p.
  17. Bodine DM 4th, Birkenmeier CS, Barker JE. Spectrin deficient inherited hemolytic anemias in the mouse: characterization by spectrin synthesis and mRNA activity in reticulocytes. Cell. 1984 Jul;37(3):721-9. PubMed,  CrossRef
  18. Low PS. Structure and function of the cytoplasmic domain of band 3: center of erythrocyte membrane-peripheral protein interactions. Biochim Biophys Acta. 1986 Sep 22;864(2):145-67. PubMed, CrossRef
  19. Konoplya AI. Correlation between structure and function of erythrocytes and immune homeostasis . Kursk: KSMU, 2008. 40 p.
  20. Antonyuk VO. Lectins and their stock sources. Lviv: Kvart, 2005. 550 p.
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