LOCALIZATION OF THE PHYSIOLOGICAL PRION AND Na+–K+ ATPase ACTIVITY IN TISSUES OF RATS PRION-REPLICATING SYSTEM
DOI: http://dx.doi.org/10.30970/sbi.0503.167
Abstract
Immunohistochemical studies of prion-replicating tissues, in six months rats, showed presence of the physiological prion in small intestine, particularly in cells of the jejunum villi own plate – lymphocytes and monocytes. In spleen, physiological prion localization was found in red pulp lymphocytes, located near the capsule and trabecules. In cells of white pulp the physiological prion was not found. Instead, most of it was located in microgluecytes of medulla oblongata. The Na+–K+ ATPase activity and the concentration of sodium and potassium ions in rat prion-replicating organs were determined. Enzyme activity was highest in the medulla oblongata, and the concentration of ions – in spleen. A direct positive correlation between the amount of physiological prion and the activity of Na+–K+ ATPase was established.
Keywords
Full Text:
PDF (Українська)References
1. Болдырев А.А. Na+-K+ АТФ-аза как олигомерный ансамбль. Биохимия, 2001; 66(8): 1013-1025. | |
| |
2. Вербицький П.І. Губчастоподібна енцефалопатія великої рогатої худоби та інші пріонні інфекції. К.: Ветінформ, 2005. 240 с. | |
| |
3. Григорьев В.Б. Прионные болезни человека и животных. Вирусология, 2004; 49(5): 4-12. | |
| |
4. Лакин Г.Ф. Биометрия. М.: Высш. школа, 1990. 352 с. | |
| |
5. Лапач С.И., Губенко А.В., Бабич П.П. Статистические методы в медико-биологических исследованиях с использованием Excel. Киев: Морион, 2000. 319 с. | |
| |
6. Лопина О. Д. Взаимодействие каталитической субъединицы Na/K-АТФ-азы с клеточными белками и другими эндогенными регуляторами. Биохимия, 2001; 66(10): 1389-1400. | |
| |
7. Новак В.П., Мельниченко А.П. Цитологія, гістологія, ембріологія: навч. посібник. Біла Церква, 2005. 256 с. | |
| |
8. Остапченко Л.І., Михайлик І.В. Біологічні мембрани: методи дослідження структури та функцій. К.: ВПЦ Київський університет, 2006. 215 с. | |
| |
9. Тица Н. Энциклопедия клин. лаб. тестов. Москва: Лабинформ, 1997. С. 225-226. | |
| |
10. Шкундина И.С., Тер-Аванесян М.Д. Прионы. Успехи биол. химии, 2006; 46: 3-423. | |
| |
11. Alper T., Haig D.A., Clarke M.C. The exceptionally small size of the scrapie agent. Biochem. Biophys. Res. Commun, 1966; 22(3): 278-284. | |
| |
12. Caetano F.A., Lopes M.H. Endocytosis of Prion Protein Is Required for ERK1/2 Signaling Induced by Stress-Inducible Protein 1. Journ. of Neuroscience, 2008; 28(26): 6691-6702. | |
| |
13. Jorgensen P. L. Purification of Na+-K+ АТPase: enzyme sources, preparative problems, and preparation from mammalian kidney. Methods in Еnzymology, 1988; 156: 29-43. | |
| |
14. Hope J., Reekie L., Hunter N. et al. Fibrils from brains of cows with new cattle disease contam scrapieassociated protein. Nature, 1988; 336: 390-392. | |
| |
15. Kingsbury D.T., Smeltzer D.A., Gibbs C.J., Gajdusek D.C. Evidence for normal cell-mediated immunity in scrapie-infected mice. Infect. Immun, 1981; 32: 1176-1180. | |
| |
16. Kovacs G., Budka H. Prion Diseases: From Protein to Cell Pathology. Am. Journ. of Pathology, 2008; 172(3): 555-565. | |
| |
17. Krammer C., Vorberg I., Schatzl H.M., Gilch S. Therapy in Prion Diseases: From Molecular and Cellular Biology to Therapeutic Targets. Infections Disorders - Drug Targets, 2009; 9: 3-14. | |
| |
18. Kuehnel W. Color Atlas of Cytology, Histology and Microscopic Anatomy. New York: Thieme Stuttgart, 2003. 534 p. | |
| |
19. Lowry O.N., Rosenbrough N.I., Forr A.R. et al. Protein measurement with the Folin phenol reagent. J. Biol. Chem, 1951; 193(1): 265-275. | |
| |
20. Linden R, Martins V.R., Prado M.A. Physiology of the Prion Protein. Physiol Rev, 2008; 88: 673-728. | |
| |
21. Prusiner S.B. Genetic and infectious prion diseases. Arch. Neurol, 1993; 50: 1129-1153. | |
| |
22. Tessier P., Lindquist S. Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI+]. Nature Structural & Molecular Biology, 2009; 16(6): 598-605. | |
| |
23. Westergard L., Christensen H., Harris D. The cellular prion protein (PrPC): its physiological function and role in disease. Biochim. Biophys. Acta, 2007; 1772: 629-644. | |
| |
24. Weissmann C. The state of the prion. Nat. Rev. Microbiol, 2004; 2: 861-871. | |
| |
25. Will R.G. The spongioform encephalopathies. J. Neurol. Neurosurg. Psychiat, 1991; 54: 761-763. | |
| |
26. Winklhofer K.F., Heske J., Heller U. et al. Determinants of the in vivo folding of the prion protein. A bipartite function of helix 1 in folding and aggregation. J. Biol. Chem, 2003; 278(17): 14961-14970. | |
| |
27. Yuan J., Xiao X., McGeehan J. et al. Insoluble aggregates and protease‐resistant conformers of prion protein in uninfected human brains. J. Biol. Chem, 2006; 281: 34848-34858. | |
| |
28. Yuan J., Kinter M., McGeehan J. et al. Concealment of epitope by reduction and alkylation in prion protein. Biochem. Biophys. Res. Commun, 2005;326: 652-659. | |
| |
29. Zanata S.M., Lopes M.H., Mercadante A.F. et al. Stress-inducible protein 1 is a cell surface ligand for cellular prion that triggers neuroprotection. EMBO J, 2002; 21: 3307-3316. | |
| |
30. Zou W.Q., Langeveld J., Xiao X. et al. PrP conformational transitions alter species preference of a PrP‐specific antibody. J. Biol. Chem, 2010; 285: 13874-13884. | |
| |
31. Zou W.Q., Puoti G., Xiao X. et al. Variably protease‐sensitive prionopathy: a new sporadic disease of the prion protein. Ann. Neurol, 2010; 68: 162-172. | |
| |
32. Zou W.Q., Zhou X., Yuan J., Xiao X. Insoluble cellular prion protein and its association with prion and Alzheimer diseases. Prion J, 2011; 5: 172-178. | |
| |
33. www.videotest.ru | |
Refbacks
- There are currently no refbacks.
Copyright (c) 2011 Studia biologica
This work is licensed under a Creative Commons Attribution 4.0 International License.