Antitumor RNase (binase) induces the alteration of cellular permeability

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Abstract

Some RNases including ones of microbial origin possess
antitumor activity, which mechanisms remains unclear. Here
we investigated the first step of RNase action towards
eukaryotic cells which is connected with increase of cell
permeability for ions and macromolecules.
Using radiological analysis of 45Са2+uptake by Candida
yeast and fluorescence imaging of human embryo kidney
cells HEK stained by Ca2+-specific Fura-2/АМ day the level
of intracellular Ca2+ under treatment with the RNase of
Bacillus intermedius (binase) was studied. Viability of lung
carcinoma epithelial cells A549 treated by binase was
measured by WST proliferation kit, stability of erythrocytes
was tested by lysis assay.
We have shown that binase induces the permeability
increase of lower and higher eukaryotic cells for Ca2+as
well as the increase of protein permeability of A549 cells.
Binase treatment protects erythrocytes from osmotic
shock.
The protective or cytotoxic binase effect followed by
increase of cellular permeability is realized depending on the
dell type, where the expression of КСa channels and of certain
oncogens, particularly of ras family, is crucial. The obtained
data supports the significance of the cell permeability increase
as a primary step in the mechanisms of binase-induced
biological effects.

About the authors

H A Cabrera-Fuentes

Kazan (Volga-Region) Federal University, Kazan

Kazan (Volga-Region) Federal University, Kazan

P V Zelenikhin,

Kazan (Volga-Region) Federal University, Kazan

Kazan (Volga-Region) Federal University, Kazan

A I Kolpakov,

Kazan (Volga-Region) Federal University, Kazan

Kazan (Volga-Region) Federal University, Kazan

O N Ilinskaya

Kazan (Volga-Region) Federal University, Kazan

Kazan (Volga-Region) Federal University, Kazan

References

  1. Spalletti-Cernia D., Sorrentino R., Di Gaetano S. et al. Antineoplastic ribonucleases selectively kill thyroid carcinoma cells via caspase-mediated induction of apoptosis. J. Clin. Endocrinol. Metab. 2003; 88(6): 2900-7.
  2. Makarov A.A., Kolchinsky A., Ilinskaya O.N. Binase and other microbial RNases as potential anticancer agents. BioEssays 2008; 30: 781-90.
  3. Lee J.E., Raines R.T. Ribonucleases as novel chemotherapeutics: the ranpirnase example. BioDrugs 2008; 22(1): 53-8.
  4. Ardelt W., Shogen K., Darzynkiewicz Z. Onconase and amphinase, the antitumor ribonucleases from Rana pipiens oocytes. Curr. Pharm. Biotechnol. 2008; 9(3): 215-25.
  5. Sevcik J., Urbanikova L., Leland P.A. et al. X-ray structure of two crystalline forms of a streptomycete ribonuclease with cytotoxic activity. J. Biol. Chem. 2002; 277(49): 47325-30.
  6. Ilinskaya O.N. Dreyer F., Mitkevich V.A. et al. Changing the net charge from negative to positive makes ribonuclease Sa cytotoxic. Protein Sci. 2002; 11(10): 2522-25.
  7. Makarov A.A., Ilinskaya O.N. Cytotoxic ribonucleases: molecular weapons and their targets. FEBS Lett. 2003; 540(1-3): 15-20.
  8. Ilinskaya O., Decker K., Koschinski A. et al. Bacillus intermedius ribonuclease as inhibitor of cell proliferation and membrane current. Toxicology 2001; 156(2-3): 101-7.
  9. Mitkevich V.A., Petrushanko I.Y., Kretova O.V. et al. Oncogenic c-kit transcript is a target for binase. Cell Cycle 2010; 9(13): 2674-8.
  10. 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.
  11. Ilinskaya O.N., Koschinski A., Repp H. et al. RNase induced apoptosis: fate of calcium-activated potassium channels. Biochemie 2008; 90(5): 717-25.
  12. Zhao H., Ardelt B., Ardelt W. et al. The cytotoxic ribonuclease onconase targets RNA interference (siRNA). Cell Cycle 2008; 7(20): 3258-61.
  13. Bracale A., Spalletti-Cernia D., Mastronicola M. et al. Essential stations in the intracellular pathway of cytotoxic bovine seminal ribonuclease. Biochem. 2002; 362(Pt 3): 553-60.
  14. Navarro S., Aleu J., Jiménez M. et al. The cytotoxicity of eosinophil cationic protein/ribonuclease 3 on eukaryotic cell lines takes place through its aggregation on the cell membrane. Cell Mol. Life Sci. 2008; 65(2): 324-37.
  15. Кабрера-Фуентес Э.А., Калачева Н.В., Мухаметшина Р.Т. и др. Проникновение биназы в клетки альвеолярного эпителия не индуцирует их гибель. Биомед. Хим. 2012; 58(3): 272-80.
  16. Schulga A., Kurbanov F., Kirpichnikov M. et al. Comparative study of binase and barnase: experience in chimeric ribonucleases. Protein Eng. 1998; 11(9): 773-80.
  17. Yakovlev G.I., Moiseyev G.P., Struminskaya N.K. et al. Mutational analysis of the active site of RNase of Bacillus intermedius (BINASE). FEBS Lett. 1994; 354 (3): 305-6.
  18. Ilinskaya O.N., Ivanchenko O.B., Karamova N.S. et al. SOSinducing ability of native and mutant microbial ribonucleases. Mut. Res. 1996; 354(2): 203-9.
  19. Noll T., Wozniak G., McCarson K. et al. Effect of factor XIII on endothelial barrier function. J. Exp. Med. 1999; 189(3): 1373-82.
  20. Kolpakov A.I., Kupriianova F.G. Effect of exogenous ribonucleases on the propagation of Candida tropicalis yeast. Mikrobiologiia 1992; 61(6): 969-74.
  21. Porta C., Paglino C., Mutti L. Ranpirnase and its potential for the treatment of unresectable malignant mesothelioma. Biologics 2008; 2(4): 601-9.
  22. Ilinskaya O.N., Koschinski A., Mitkevich V.A. et al. Cytotoxicity of RNases is increased by cationization and counteracted by Kca channels. BBRC 2004; 314: 550-54.
  23. Hollenhorst M.I., Richter K., Fronius M. Ion transport by pulmonary epithelia. J. Biomed. Biotechnol. 2011. Epub. 2011 Oct 27.
  24. Rodenhuis S., van de Wetering M.L, Mooi W.J. et al. Mutational activation of the K-ras oncogene: a possible pathogenetic factor in adenocarcinoma of the lung. N. Engl. J. Med. 1987; 317(15): 929-35.
  25. Xiao G.C., Otani S., Yan L. et al. Inhibition of Farnesyl Protein Transferase, H-ras Oncogene Expression and P21ras Membrane Association by Natural Products in Human Solid Tumor Cell Lines. J. Asian Nat. Prod. Res. 1998; 1: 29-51.
  26. Lang F., Birka C., Myssina S. et al. Erythrocyte ion channels in regulation of apoptosis. Adv. Exp. Med. Biol. 2004; 559: 211-7.

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