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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. 2014; 60(5): 14-22


Glycoprotein sialylation and NEU1 and ST6GAL1 expressions in erythremia

Maslak HS1, Kostiuk OV1, Minchenko DO2,3, Brazaluk OZ1, Shevtsova AI1, Minchenko OH2

  1. Dnipropetrovsk Nat. Med. Academy of Ministry of Health of Ukraine, Ukraine
  2. O.V. Palladin Institute of biochemistry NAS of Ukraine, Kyiv, Ukraine
  3. O.O. Bohomolets Nat.Med.University, Kiyv, Ukraine
DOI: https://doi.org/10.15407/fz60.05.014

Abstract

In stress, it was showed the organ and tissue changes associated with damage by lipid peroxides, and the disrupted barrier function. As a consequence, it was to lead to a syndrome of “stress-induced lung” and violation of oxygen delivery to the tissues and hypoxia. Purpose of the study was to investigate the dynamics of changes in gas exchange, blood glucose, body temperature, oxidant and antioxidant system activity, as well as mitochondrial respiration by Chance under the influence of chronic stress (6-hour immobilization daily for 3 weeks). It was identified 4 phase changes of energy metabolism in the dynamics of chronic stress. In the first phase, hypomethabolic, instability oxidative metabolism, decreased oxidation of NADdependent substrates, significant elevation of FAD-dependent substrates oxidation and low MRU were found. The activity of superoxide dismutase (MnSOD) was increased; it was occurred on a background low activity of glutathione peroxidase, and of misbalanced antioxidant system. After seven immobilizations, second phase - shift in energy metabolism, was observed, and then the third phase (hypermetabolic) started. It was characterized by gradual increase in oxidative metabolism, the restoration of oxidation of NAD-dependent substrates, MRU, as well as optimizing balance of oxidant and antioxidant systems. The fourth phase was started after 15 immobilizations, and characterized by the development of adaptive reactions expressed in increased tolerance of energy metabolism to the impact of immobilization. The results are correlated with changes in the dynamics of blood corticosterone. Thus, it was found the phase character of the energy metabolism rebuilding during the chronic stress.

Keywords: Аcute stress, сhronic stress, energy metabolism,lipid peroxidation, mitochondrial respiration, corticosterone

References

  1. Schwarzkopf M, Knobeloch KP, Rohde E, Hinderlich S, Wiechens N, Lucka L, Horak I, Reutter W, Horstkorte R. Sialylation is essential for early development in mice. Proc Natl Acad Sci USA 2002 Apr 16; 99(8): 5267-5270. CrossRef PubMed PubMedCentral
  2.  
  3. Wang PH, Lee WL, Juang CM, Yang YH, Lo WH, Lai CR, Hsieh SL, Yuan CC. Altered mRNA expressions of sialyltransferases in ovarian cancers. Gynecol Oncol 2005 Dec; 99(3): 631-9. CrossRef PubMed
  4.  
  5. Ceciliani F, Pocacqua V. The acute phase protein alpha1- acid glycoprotein: a model for altered glycosylation during diseases. Curr Protein Pept Sci 2007 Feb; 8(1): 91-108. CrossRef PubMed
  6.  
  7. Orczyk-Pawilowicz M, Hirnle L, Katnik-Prastowska I. Alterations of N-glycan branching and expression of sialic acid on amniotic fluid alpha-1-acid glycoprotein derived from second and third trimesters of normal and prolonged pregnancies. Clin Chim Acta 2006 May; 367(1-2): 86–92. CrossRef PubMed
  8.  
  9. Gunnarsson P, Fornander L, Påhlsson P, Grenegård M. Sialic acid residues play a pivotal role in alpha(1)-acid glycoprotein (AGP)-induced generation of reactive oxygen species in chemotactic peptide pre-activated neutrophil granulocytes. Inflamm Res 2010 Feb; 59(2): 89-95. CrossRef PubMed
  10.  
  11. Han S, Ritzenthaler JD, Wingerd B, Rivera HN, Roman J. Extracellular matrix fibronectin increases prostaglandin E2 receptor subtype EP4 in lung carcinoma cells through multiple signaling pathways : the role of AP-2 . J Biol Chem 2007; 282(11): 7961-72. CrossRef PubMed
  12.  
  13. Pankov R, Yamada KM. Fibronectin at a glance. J Cell Sci 2002 Oct 15; 115(Pt 20): 3861-3. CrossRef PubMed
  14.  
  15. Pan D, Song Y. Role of altered sialylation of the I-like domain of ß1 integrin in the binding of fibronectin to ß1 integrin: thermodynamics and conformational analyses.  Biophys J 2010 Jul 7; 99(1): 208-17. CrossRef PubMed PubMedCentral
  16.  
  17. Patel RY, Balaji PV. Identification of linkage-specific sequence motifs in sialyltransferases. Glycobiology 2006 Feb; 16(2): 108-16. CrossRef PubMed
  18.  
  19. Miyagi T. Aberrant expression of sialidase and cancer progression. Proc Jpn Acad Ser B Phys Biol Sci 2008; 84(10): 407-18. CrossRef PubMed PubMedCentral
  20.  
  21. Raval GN, Parekh LJ, Patel DD, Jha FP, Sainger RN, Patel PS. Clinics usefulness of alterations in sialic acid, sialyltransferase and sialoproteins in breast cancer. Indian J Clin Biochem 2004 Jul; 19(2): 60-71. CrossRef PubMed PubMedCentral
  22.  
  23. Katoh S, Maeda S, Fukuoka H, Wada T, Moriya S, Mori A, Yamaguchi K, Senda S, Miyagi T. A crucial role of sialidase Neu1 in hyaluronan receptor function of CD44 in T helper type 2-mediated airway inflammation of murine acute asthmatic model. Clin Exp Immunol 2010 Aug; 161(2): 233–41. CrossRef  
  24. Cross AS, Hyun SW, Miranda-Ribera A, Feng C, Liu A, Nguyen C, Zhang L, Luzina IG, Atamas SP, Twaddell WS, Guang W, Lillehoj EP, Puche AC, Huang W, Wang L-X, Passaniti A, Goldblum SE. NEU1 and NEU3 sialidase activity expressed in human lung microvascular endothelia: NEU1 restrains endothelial cell migration, whereas NEU3 does not. J Biol Chem 2012 May 4; 287(19): 15966–80. CrossRef PubMed PubMedCentral
  25.  
  26. Nakano V, Fontes Piazza RM, Avila-Campos MJ. A rapid assay of the sialidase activity in species of the bacteroides fragilis group by using peanut lectin gemagglutination. Anaerobe 2006 Oct-Dec; 12(5-6): 238–41. CrossRef PubMed
  27.  
  28. Minchenko OH, Ochiai A, Opentanova IL, Ogura T, Minchenko DO, Caro J, Komisarenko SV, Esumi H. Overexpression of 6-phosphofructo-2-kinase/fructose-2,6- bisphosphatase-4 in the human breast and colon malignant tumors. Biochimie 2005 Nov; 87(11): 1005-10. CrossRef PubMed
  29.  
  30. Sata T, Roth J, Zuber C, Stamm B, Heitz PU. Expression of alpha 2,6-linked sialic acid residues in neoplastic but not in normal human colonic mucosa. A lectin-gold cytochemical study with Sambucus nigra and Maackia amurensis lectins. Am J Pathol 1991 Dec; 139(6): 1435-48. PubMed PubMedCentral
  31.  
  32. Tajiri M, Yoshida S, Wada Y. Differential analysis of sitespecific glycans on plasma and cellular fibronectins: application of a hydrophilic affinity method for glycopeptide enrichment.Glycobiology. 2005 Dec; 15(12): 1332-40. CrossRef PubMed
  33.  
  34. Higai K, Aoki Y, Azuma Y, Matsumoto K. Glycosylation of site-specific glycans of a1-acid glycoprotein and alterations in acute and chronic inflammation. Biochim Biophys Acta 2005 Aug 30;1725(1):128-35. CrossRef PubMed
  35.  
  36. Nakano M, Kakehi K, Tsai M, Lee YC. Detailed structural features of glycan chains derived from alpha1-acid glycoproteins of several different animals: the presence of hypersialylated, O-acetylated sialic acids but not disialyl residues. Glycobiol 2003 May; 14(5): 431-441. CrossRef PubMed
  37.  
  38. Videira PA, Amado IF, Crespo HJ, Algueró MC, Dall'Olio F, Cabral MG, Trindade H. Surface alpha 2-3- and alpha 2-6-sialylation of human monocytes and derived dendritic cells and its influence on endocytosis. Glycoconj J. 2008 Apr; 25(3): 259-68. CrossRef PubMed
  39.  
  40. Katnik-Prastowska I, Kratz EM, Faundez R, ChelmonskaSoyta A. Lower expression of the alpha2,3-sialylated fibronectin glycoform and appearance of the asialo-fibronectin glycoform are associated with high concentrations of fibronectin in human seminal plasma with abnormal semen parameters. Clin Chem Labor Med 2006; 44(9): 1119–25. CrossRef PubMed
  41.  
  42. Erat MC, Schwarz-Linek U, Pickford AR. Implications for collagen binding from the crystallographic structure of fibronectin 6FnI1-2FnII7FnI. J Biol Chem 2010 Oct 29; 285(44): 33764 -70. CrossRef PubMed PubMedCentral
  43.  
  44. Crostek L, Cylwik B, Krawiec A, Korcz W, Szmitkowski M. Relationship between serum sialic acid and sialylation glycoproteins in alcoholics. Alcohol Alcoholism 2007 Nov-Dec; 42(6): 588-92. CrossRef PubMed
  45.  
  46. Uemura T, Shiozaki K, Yamaguchi K, Miyazaki S, Satomi S, Kato K, Sakuraba H, Miyagi T. Contribution of sialidase NEU1 to suppression of metastasis of human colon cancer cells through desialylation of integrin beta4. Oncogene. 2009 Mar 5; 28(9): 1218-29. CrossRef PubMed
  47.  
  48. Nanetti L, Vignini A, Raffaelli F, Taffi R, Silvestrini M, Provinciali L, Mazzanti L. Sialic acid and sialidase activity in acute stroke. Dis Markers 2008; 25(3): 167-73. CrossRef PubMed PubMedCentral
  49.  
  50. Sönmez H, Süer S, Güngör Z, Baloglu H, Kökoglu E. Tissue and serum sialidase levels in breast cancer. Cancer Lett 1999 Feb 8; 136(1): 75-8. CrossRef  
  51. Miyagi T, Wada T, Yamaguchi K, Hata K. Sialidase and malignancy: a minireview. Glycoconj J 2004; 20(3): 189-98. CrossRef PubMed
  52.  
  53. Miyagi T, Wada T, Yamaguchi K, Shiozaki K, Sato I, Kakugawa Y, Yamanami H, Fujiya T. Human sialidase as a cancer marker. Proteomics 2008 Aug; 8(16): 3303-11. CrossRef PubMed
  54.  
  55. Hedlund M, Hg E, Varki A, Varki NM. Alpha 2-6-Linked sialic acids on N-glycans modulate carcinoma differentiation in vivo. Cancer Res 2008 Jun 15; 68(2): 388-94. CrossRef PubMed
  56.  
  57. Vakonakis I, Staunton D, Ellis IR, Sarkies P, Flanagan A, Schor AM, Schor SL, Campbell ID. Motogenic sites in human fibronectin are masked by long range interactions. J Biol Chem. 2009 Jun 5; 284(23): 15668-75. CrossRef PubMed PubMedCentral
  58.  

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