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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. 2006; 52(1): 3-7

Proteasomal degradation of RNA of differentNO-synthase isoforms

V.E. Dosenko, V.Yu. Zagoriy, A.A. Moibenko

    О.О. Bogomolets Institute of Physiology, National Academyof Sciences of Ukraine, Kyiv



Abstract

Using a developed method of determination of the RNase activity of the proteasome in vitro with the application of reverse transcription followed by subsequent polymerase chain reaction it was shown that 26S proteasome from the proteasomal fraction II effectively cleaves RNA, encoding ac- tin, myosin and all isoforms of NO synthase. The intensity of RNA degradation by proteasome and specific RNases is simi- lar. It was also shown that clasto-lactacystin ?-lactone, a spe- cific proteasome inhibitor significantly depresses RNase ac- tivity of the proteasome. Thus, proteasome is capable to de- grade certain eukariotic RNA in vitro and the proposed method can be used in order to discover specific substances such as inhibitors of RNase activity of the proteasome.

Full text: (PDF, in Ukrainian)

References

  1. Досенко В.Є., Загорій В.Ю., Мойбенко О.О., Пархоменко О.М. Патофізіологічні аспекти генетичного поліморфізму ендотеліальної NO-синтази // Фізіол. журн. – 2002. – 48, №6. – С. 86–10
  2. Евтеева И.Н., Куличкова В.А., Обухова А.Д. и др.EGF регулирует специфическую эндорибонуклеазную активность 26S протеасом из клеток A431:потенциальная роль протеасом в контроле стабильности мРНК // Цитология. –2003. – 45, №5. –С. 488–492.
  3. Куличкова В.А., Миттенберг А.Г., Евтеева И.Н. и др. Селективный эффект эпидермального фактора роста на эндорибонуклеазную активность различных субпопуляций протеасом из клеток линии A431// Там же. –2004. – 46, №6. – С. 525–530.
  4. Токтарова М.В., Куличкова В.А., Миттенберг А.Г. и др. Селективный эффект индукторов апоптоза на эндорибонуклеазную активность 26S протеасом и альфа-RNP субъединиц в клетках K562: возможное вовлечение 26S протеасом и альфа-RNP в регуляцию стабильности РНК // Там же. – №3. – С. 283–290.
  5. Ballut L., Petit F., Mouzeyar S. et al. Biochemical identification of proteasome-associated endonuclease activity in sunflower // Biochim. and Biophys. Acta. –2003. –1645, № 1. – P. 30–39.
  6. Chase B.I., Zhou Y., Xiang Y. et al. Proteasome-mediated degradation of RNase L in response to phorbol12-myristate-13-acetate (PMA) treatment of mouse L929 cells // J. Interferon Cytokine Res. – 2003. – 23,№10. – P. 565–573.
  7. Chu Y., Heistad D.D., Knudtson K.L. et al. Quantification of mRNA for endothelial NO synthase in mous blood vessels by real-time polymerase chain reaction //Arterioscler. Thromb. Vasc. Biol. – 2002. – 22, №4. –P.611–616.
  8. Gautier-Bert K., Murol B., Jarrousse A.S. et al. Substrate affinity and substrate specificity of proteasomeswith RNase activity // Mol. Biol. Rep. – 2003. – 30,№1. –P. 1–7.
  9. 9. Giulivi C., Davies K.J.A. Dityrosine and tyrosine oxi-dation products are endogenous markers for the selec-tive proteolysis of oxidatively modified red blood cellhemoglobin by (the 19 S) proteasome // J. Biol. Chem. –1993. – 268. – P. 8752–4753.
  10. 10. Goldberg AL. Protein degradation and protectionagainst misfolded or damaged proteins // Nature. – 2003. –426. – P.895–899.
  11. Horikoshi T., Page J., Lei G. et al. Proteasomal RNaseactivity in human epidermis // In Vivo. – 1998. – 12,№2. – P. 155–158.
  12. Jarrousse A.S., Petit F., Kreutzer-Schmid C. et al. Pos-sible involvement of proteasomes (prosomes) inAUUUA-mediated mRNA decay // J. Biol. Chem. –1999. – 274, №9. – P. 5925–5930.
  13. Jorgensen L., Hendil K.B. Proteasome subunit zeta, aputative ribonuclease, is also found as a free monomer// Mol. Biol. Rep. – 1999. – 26, №1–2. – P. 119–23.
  14. Lasch P., Petras T., Ullrich O. et al. Hydrogen perox-ide-induced structural alterations of RNAse A // J. Biol.Chem. – 2001. – 276, №12. – P.9492–9502.
  15. Laufs U., Liao J.K. Post-transcriptional regulation ofendothelial nitric oxide synthase mRNA stability byRho GTPase //Ibid. – 1998. – 273, №37. –P. 24266–24271.
  16. Matsushita H., Chang E., Glassford A.J. et al. eNOSactivity is reduced in senescent human endothelial cells:preservation by hTERT immortalization // Circulat.Res. – 2001. – 89, №9. – P. 793–798.
  17. Park C.O., Yi H.G. Apoptotic change and NOS activ-ity in the experimental animal diffuse axonal injurymodel // Yonsei Med. J. – 2001. – 42, №5. – P. 518–526.
  18. Petit F., Jarrousse A.S., Boissonnet G. et al.Proteasome (prosome) associated endonuclease acti-vity // Mol. Biol. Rep. – 1997. – 24, №1–2. – P. 113–117.
  19. 19. Petit F., Jarrousse A.S., Dahlmann B. et al. Involvementof proteasomal subunits zeta and iota in RNA degrada-tion // Biochem. J. – 997. – 26, Pt 1. – Р. 93–98.
  20. 20. Pouch M.N., Petit F., Buri J. et al. Identification andinitial characterization of a specific proteasome(prosome) associated RNase activity // J. Biol. Chem. –1995. –270, №37. – P. 22023–22028.
  21. Rudnicki M.A., Jackowski G., Saggin L., McBurneyActin and myosin expression during develop-ment of cardiac muscle from cultured embryonalcarcinoma cells // Dev. Biol. –1990. – 138, №2. –Р. 348–358.
  22. Searles C.D., Miwa Y., Harrison D., Ramasamy S.,regulation of endothelial nitric oxidesynthase guring cell growth // Circulat. Res. – 1999. –85. – P. 588–595.
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