Biotechnologia Acta

...

  • Increase font size
  • Default font size
  • Decrease font size
Home Archive 2017 № 5 INHIBITION OF THE EXPRESSION OF PHYSIOLOGICAL PRIONS WITH ANTISENS-OLIGONUCLEOTIDES N. U. Susol, D. D.Ostapiv, V. V.Vlizlo
Print PDF

ISSN 2410-7751 (Print)
ISSN 2410-776X (Online)


"Biotechnologia Acta" V. 10, No 5, 2017
https://doi.org/10.15407/biotech10.05.043
Р. 43-50, Bibliography 13, English
Universal Decimal Classification: 577.113.6:602.643:54-126

INHIBITION OF THE EXPRESSION OF PHYSIOLOGICAL PRIONS
WITH ANTISENS-OLIGONUCLEOTIDES

N. U. Susol, D. D.Ostapiv, V. V.Vlizlo

Institute of Animal Biology of National Academy of Agrarian Sciences of  Ukraine,  Lviv

The aim of the research was to investigate the ability of new complexes as specific single-stranded oligonucleotides ‒ ODN ‒ with   dimethylaminomethylmethacrylate ‒ DMAEM ‒ based polymer carriers to inhibit the expression of the physiological prion. It has been established that the introduction of complexes of newly synthesized carriers based on dimethylaminomethyl methacrylate - PEG-DMAEM-MP-27 (magnetic particles) (MP-27), PEG- DMAEM-MP-2 (MP-2), PEG- DMAEM-MP-3 (MP-3)  with as ODH into the organism of rats leads to a decrease in the physiological prion content in the tissues of the spleen and small intestine. The influence of complexes of newly synthesized carriers  MP-27, MP-2 and MP-3 with as specific single-stranded oligonucleotides ODH on hematological and biochemical blood parameters of  Wistar rats was also studied.

Key words: prion infections, antisense-oligonucleotides, polymeric carriers.

© Palladin Institute of Biochemistry of National Academy of Sciences of Ukraine, 2017

  • References
    • 1. Whitechurch B. C., Welton J. M., Collins S. J., Lawson V. A. Prion Diseases. Adv. Neurobiol. 2017, V. 15, P.335–364. https://doi.org/10.1007/978-3-319-57193-5_13

      2. Malachin G., Reiten M. R., Salvesen O., Aanes H., Kamstra J. H., Skovgaard K., Heegaard P. H., Ersdal C., Espenes A., Tranulis M. A. Loss of prion protein induces a primed state of type I interferon-responsive genes. PLoS One. 2017 Jun 26;12(6):e0179881. https://doi.org/10.1371/journal.pone.0179881

      3. Friberg K.N. Hung G., Wancewicz Ed., Giles K., Freier S., Bennett F., Freyman Y., Ghaemmaghami S. Intracerebral Infusion of Antisense Oligonucleotides Into Prion-infected Mice. Mol. Ther. Nucleic Acids. Published online 7 February 2012. doi: 10.1038/mtna.2011.6.

      4. David R. Brown. Neurodegeneration and Prion Disease. Department of biology and biochemistry Universety of Bath, Bath BA2 7AY, UK. 2005.

      5. Diaz-Espinoza R., Morales R., Concha-Marambio L., Moreno-Gonzalez I., Moda F., Soto C. Treatment with a non-toxic, self-replicating anti-prion delays or prevents prion disease in vivo. Mol. Psychiatry. 2017 Jun 20. doi:10.1038/mp.2017.84 https://doi.org/10.1038/mp.2017.84

      6. European convention for the protection of vertebrate animals used for experimental and other scientific purposes. Strasburg: Council of Europe. 1986. 52 P.

      7. Lowry O. H., Rosebrough N. J., Farr A. L. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 1951, 193 (1), 265–275.

      8. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4 . Nature. 1970, V. 227, P. 680—685. doi:10.1038/227680a0

      9. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 1979, 76 (9), 4350–4354. https://doi.org/10.1073/pnas.76.9.4350

      10. Burnette W. N. Western blotting: electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radioiodinated protein A / W. B. Burnette / Anal. Biochem. 1981. V. 112, P. 195-203. https://doi.org/10.1016/0003-2697(81)90281-5

      11. Susol N. U., Martyn U. V., Kuzmina N. V., Vlizlo V. V. Effect of nanocarriers with antisense oligonucleotides on histological structure of organs where synthesizing prionprotein. Biol. Tvarin. 2016, 18 (3), 91–96. https://doi.org/10.15407/animbiol18.03.091

      12. Supattapone S., Wille H., Uyechi M. R. Branched polyamines cure prion-infected neuroblastoma cells. J. Virol. 2001, 75 (7), 3453–3461 P. doi: 10.1128/JVI.75.7.3453–3461.2001

      13. Fischer M., Appelhans D., Schwarz S. Influence of surface functionality of poly(propylene imine) dendrimers on protease resistance and propagation of the scrapie prion protein. Biomacromolecules. 2010, 11(5), 1314–1325. doi: 10.1021/bm100101s.


 

Additional menu

Site search

Site navigation

Home Archive 2017 № 5 INHIBITION OF THE EXPRESSION OF PHYSIOLOGICAL PRIONS WITH ANTISENS-OLIGONUCLEOTIDES N. U. Susol, D. D.Ostapiv, V. V.Vlizlo

Invitation to cooperation

Dear colleagues, we invite you to publish your articles in our journal.
© Palladin Institute of Biochemistry of the National Academy of Sciences of Ukraine, 2008.
All rights are reserved. Complete or partial reprint of the journal is possible only with the written permission of the publisher.
E-mail
for information: biotech@biochem.kiev.ua.