Transformed lung epithelial cells produce microbial RNAse (binase)
- Authors: Dudkina E.V1, Singh I.2, Ulyanova V.V1, Shah Mahmud R.1, Barreto G.2, Ilinskaya O.N1
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Affiliations:
- Kazan (Volga region) Federal University
- Max-Planck Institute for Heart and Lung Research
- Issue: Vol 9, No 3 (2014)
- Pages: 63-67
- Section: Articles
- URL: https://genescells.ru/2313-1829/article/view/120307
- DOI: https://doi.org/10.23868/gc120307
- ID: 120307
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Abstract
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About the authors
E. V Dudkina
Kazan (Volga region) Federal University
I. Singh
Max-Planck Institute for Heart and Lung Research
V. V Ulyanova
Kazan (Volga region) Federal University
R. Shah Mahmud
Kazan (Volga region) Federal University
G. Barreto
Max-Planck Institute for Heart and Lung Research
O. N Ilinskaya
Kazan (Volga region) Federal University
References
- Ferlay J., Shin H.R., Bray F. et al. Estimates of worldwide burden of cancer in 2008: GLOBOCAN 2008. Int. J. Cancer 2010; 127: 2893-917.
- Чиссов В.И., Александрова Л.М., Бутенко А.В. Научные основы и перспективы развития клинической онкологии. Вестник Росздравнадзора 2010; 4: 68-71.
- orchilin V.P. Recent approaches to intracellular delivery of drugs and DNA and organelle targeting. Annu. Rev. Biomed. Eng. 2006; 8: 343-75.
- Rawat A., Vaidya B., Khatri K. et al. Targeted intracellular delivery of therapeutics: an overview. Pharmazie 2007; 62(9): 643-58.
- Seth P. Vector-mediated cancer gene therapy. Cancer Biol. Ther. 2005; 4(5): 512-7.
- Vogelstein B., Kinzler K.W. Cancer genes and the pathways they control. Nat. Med. 2004; 10: 789-99.
- Chirino A.J., Ary M.L., Marshall S.A. Minimizing the immunogenicity of protein therapeutics. Drug Discovery Today 2004; 9(2): 82-90.
- Saxena S.K., Shogen K., Ardelt W. Onconase and its therapeutic potential. Lab. Med. 2003; 34: 380-7.
- Porta C., Paglino C., Mutti L. Ranpirnase and its potential for the treatment of unresectable malignant mesothelioma. Biologics 2008; 2(4): 601-9.
- Makarov A.A., Ilinskaya O.N. Cytotoxic ribonucleases: molecular weapons and their targets. FEBS Lett. 2003; 540: 15-20.
- Makarov A.A., Kolchinsky A., Ilinskaya O.N. Binase and other microbial RNases as potential anticancer agents. Bioessays. 2008; 30(8): 781-90.
- Mitkevich V.A., Petrushanko I.Y., Spirin P.V. et al. Sensitivity of acute myeloid leukemia Kasumi-1 cells to binase toxic action depends on the expression of KIT and АML1-ETO oncogenes. Cell Cycle 2011; 10(23): 4090-97.
- Зеленихин П.В., Черепнев Г.В., Керн Ф. и соавт. Биназа не индуцирует поликлональный Т-клеточный ответ. Доклады академии наук 2006; 407(3): 1-3.
- Cabrera Fuentes H.A., Kalacheva N.V., Mukhametshina R.T. et al. Binase penetration into alveolar epithelial cells does not induce cell death. Biomed. Khim. 2012; 58: 272-80.
- Znamenskaya L.V., Vershinina O.A., Vershinina V.I. et al. Expression of the genes for guanyl-specific ribonucleases from Bacillus intermedius and Bacillus pumilus is regulated by the two component signal transduction system PhoP-PhoR in B. subtilis. FEMS Microbiology Letters 1999; 173: 217-22.
- Sagar A.J., Pandit M.W. Denaturation studies on bovine pancreatic ribonuclease/ Effect of trichloroacetic acid. Biochim. Biophys. Acta 1983; 743: 303-9.
- Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-85.
- Polyakov K.M., Lebedev A.A., Okorokov A.L. et al. The structure of substrate-free microbial ribonuclease binase and of its complexes with 3'-GMP and sulfate ions. Acta Cryst. D Biol. Crystallogr. 2002; 58: 744-50.
- Mitkevich V.A., Schulga A.A., Trofimov A.A. et al. Structure and functional studies of the ribonuclease binase Glu43Ala/Phe81Ala mutant. Acta Cryst. D Biol. Crystallogr. 2013; 69: 991-96.
- Poliakov K.M., Goncharuk D.A., Trofimov A.A. et al. X-ray diffraction and biochemical studies of W34F mutant ribonuclease binase. Mol. Biol. (Russia) 2010; 44: 922-28.
- Schulga A.A., Nurkiyanova K.M., Zakharyev V.M., et al. Cloning of the gene encoding RNase binase from Bacillus intermedius 7P. Nucleic Acids Res. 1992; 20: 2375.
- Arnold U., Leich F., Neumann P. et al. Crystal structure of RNase A tandem enzymes and their interaction with the cytosolic ribonuclease inhibitor. FEBS J. 2011; 278: 331-40.
- Gotte G., Mahmoud Helmy A., Ercole C. et al. Double domain swapping in bovine seminal RNase: formation of distinct N-and C-swapped tetramers and multimers with increasing biological activities. PloS One 2012; 7: e46804.
- Garvie C.W., Vasanthavada K., Xiang Q. Mechanistic insights into RNase L through use of an MDMX-derived multi-functional protein domain. Biochim. Biophys. Acta 2013; 1834: 1562-71.
- Flotte T.R. Gene therapy progress and prospects: recombinant adeno-assotiated virus (rAAV) vectors. Gene Ther. 2004; 11(10): 805-10.