Study of the cytotoxic effect of secretory phospholipase A2 of Vipera nikolskii venom on the model of HeLа and ECV340 cell lines
https://doi.org/10.24884/1607-4181-2024-31-3-89-94
Abstract
Snake venoms have long been the subject of research in order to obtain new antitumor compounds. Snake secretory phospholipase A2 has cytotoxic properties that are realized through different mechanisms depending on the enzyme structure and cell type. HeLa and ECV340 cells were used as a model to evaluate the toxic effect of sPLA2 in the venom of V. nikolskii with and without sPLA2 inhibition. Varespladib was used as an inhibitor of sPLA2. In order to understand the mechanism of the toxic effect of sPLA2, the enzyme was activated by adding an emulsion of phospholipids, bovine serum albumin, and Ca2+ to the samples. The results indicate that the cytotoxic effect of sPLA2 on ECV 340 cells is associated with the catalytic activity of the enzyme; the weak cytotoxic effect of the venom on HeLa cells was preserved upon enzyme activation.
Thus, we have proposed a methodological approach that allows to evaluate the toxic effect of sPLA2, which has enzymatic activity, in the whole venom of V. nikolskii in relation to various cell lines.
About the Authors
M. A. Solovyeva
Pavlov University
Russian Federation
Competing Interests:
Russian Federation
Solovyeva Marina A., Assistant of the Department of Biological Chemistry
6-8, L’va Tolstogo str., Saint Petersburg, 197022
Competing Interests:
Authors declare no conflict of interest
L. V. Galebskaya
Pavlov University
Russian Federation
Competing Interests:
Russian Federation
Galebskaya Lyudviga V., Dr. of Sci. (Med.), Professor of the Department of Biological Chemistry
6-8, L’va Tolstogo str., Saint Petersburg, 197022
Competing Interests:
Authors declare no conflict of interest
M. A. Galkin
Pavlov University
Russian Federation
Competing Interests:
Russian Federation
Galkin Mikhail A., Cand. of Sci. (Biol.), Associate Professor of the Department of Biological Chemistry
6-8, L’va Tolstogo str., Saint Petersburg, 197022
Competing Interests:
Authors declare no conflict of interest
O. S. Shemchuk
Pavlov University
Russian Federation
Competing Interests:
Russian Federation
Shemchuk Olga S., Postgraduate Student of the Department of General and Bioorganic Chemistry
6-8, L’va Tolstogo str., Saint Petersburg, 197022
Competing Interests:
Authors declare no conflict of interest
V. V. Sharoyko
Pavlov University
Russian Federation
Competing Interests:
Russian Federation
Sharoyko Vladimir V., Dr. of Sci. (Biol.), Professor of the Department of General and Bioorganic Chemistry
6-8, L’va Tolstogo str., Saint Petersburg, 197022
Competing Interests:
Authors declare no conflict of interest
L. V. Vasina
Pavlov University
Russian Federation
Competing Interests:
Russian Federation
Vasina Lyubov V., Dr. of Sci. (Med.), Head of the Department of Biological Chemistry
6-8, L’va Tolstogo str., Saint Petersburg, 197022
Competing Interests:
Authors declare no conflict of interest
References
1. Tasoulis T., Isbister G. K. A review and database of snake venom proteomes // Toxins (Basel). 2017;9(9):290. https://doi.org/10.3390/toxins9090290.
2. Snake venom phospholipase A2 enzymes // Handbook of Venoms and Toxins of Reptiles. CRC Press. 2020:189–222.
3. Lomonte B., Angulo Y., Moreno E. Synthetic peptides derived from the C Terminal region of Lys49 Phospholipase A2 Homologues from Viperidae Snake Venoms: Biomimetic activities and potential applications // Curr. Pharm. Des. Bentham Science Publishers Ltd. 2010;16(28):3224–3230. https://doi.org/10.2174/138161210793292456.
4. Benati R. B., Costa T. R., Cacemiro M. D. C. et al. Cytotoxic and pro-apoptotic action of MjTX-I, a phospholipase A2 isolated from Bothrops moojeni snake venom, towards leukemic cells // J. Venom. Anim. Toxins Incl. TroP. Dis. BioMed Central Ltd. 2018;24(1). https://doi.org/10.1186/S40409-018-0180-9.
5. Nikolaou A., Kokotou M. G., Vasilakaki S., Kokotos G. Small-molecule inhibitors as potential therapeutics and as tools to understand the role of phospholipases A2 // Biochim. Biophys. Acta Mol. Cell. Biol. Lipids. 2019;1864(6):941– 956. https://doi.org/10.1016/j.bbalip.2018.08.009.
6. Kovalchuk S. I., Ziganshin R. H., Starkov V. G. et al. Quantitative proteomic analysis of venoms from russian vipers of pelias group: phospholipases A2 are the main venom components // Toxins (Basel). 2016;8(4):105. https://doi.org/10.3390/toxins8040105.
7. Ramazanova A. S., Zavada L. L., Starkov V. G. et al. Heterodimeric neurotoxic phospholipases h j – the first proteins from venom of recently established species Vipera nikolskii: Implication of venom composition in viper systematics // Toxicon. 2008;51:524‒537. https://doi.org/10.1016/j.toxicon.2007.11.001.
8. Ayvazyan N., Ghukasyan G., Ghulikyan L. et al. The contribution of phospholipase A2 and metalloproteinases to the synergistic action of viper venom on the bioenergetic profile of vero cells // Toxins. 2022;14:724. https://doi.org/doi.org/10.3390/toxins14110724.
9. Hiu J. J., Yap M. K. K. Cytotoxicity of snake venom enzymatic toxins: phospholipase A2 and L-amino acid oxidase // Biochemical Society Transactions. 2020;48:719–731. https://doi.org/10.1042/BST20200110.
10. Cheremnykh E. G., Osipov A. V., Starkov V. G. et al. Comparative study of the effect of snake venoms on the growth of ciliates TETRAHYMENA PYRIFORMIS: identification of venoms with high antiprotozoal activity // Reports of the Russian Academy of Sciences. Life Sciences. 2022;503:197–202. https://doi.org/10.31857/S2686738922020068.
Supplementary files
Review
For citations:
Solovyeva M.A., Galebskaya L.V., Galkin M.A., Shemchuk O.S., Sharoyko V.V., Vasina L.V. Study of the cytotoxic effect of secretory phospholipase A2 of Vipera nikolskii venom on the model of HeLа and ECV340 cell lines. The Scientific Notes of the Pavlov University. 2024;31(3):89-94. (In Russ.) https://doi.org/10.24884/1607-4181-2024-31-3-89-94
Views:
159
Email this article 