Bazı Antibiyotiklerin Koyun Dalak Glutatyon S-Transferaz Enzimi Üzerine İn Vitro Etkilerinin İncelenmesi

Year 2023, , 190 - 196, 28.06.2023

Ömer Faruk Çiftci , Songül Ünüvar , Yusuf Temel

https://doi.org/10.58605/bingolsaglik.1281161

Abstract

Glutatyon S-transferazlar (GST) hücre içi detoksifikasyon mekanizmasında görev alan multigen ailesine sahip izoenzimlerdir. GST'ler, faz II sistemi ile endojen ve eksojen kaynaklı kimyasalların toksik etkisini azaltır. GST izoenzimleri tarafından katalize edilen reaksiyonlarda, indirgenmiş glutatyonun (GSH) tiyol grubu sayesinde çeşitli elektrofillerle konjugasyon oluşturur. GST izoenzimleri hücrede sitozol ya da mikrozomlarda bulunabilir.
Bu çalışmada koyun dalak dokusundan sitozolik glutatyon S-transferaz enzimi, homojenat hazırlanması ve glutatyon agaroz afinite kromatografisi kullanılarak saflaştırıldı. İkinci aşamada saflaştırılan GST enzimi üzerine sefazolin sodyum, sefuroksim sodyum, sefaperazon sodyum, ampisillin, gentamisin, klindamisin ve tylosin antibiyotiklerin in vitro etkileri incelendi ve inhibisyon etkisi gösteren antibiyotikler için IC50 değerleri hesaplandı. Antibiyotiklerden sefaperazon sodyum, sefazolin sodyum, sefuroksim sodyum, klindamisin ve gentamisin, enzim aktivitesi üzerinde inhibisyon etkisi gösterirken ampisillinin aktivasyon etkisi gösterdiği tespit edildi. Tylosinin ise 0,545-5,45 mM aralığında enzim üzerinde herhangi etkiye sahip olmadığı belirlendi.

Keywords

Antibiyotik, Enzim, Glutatyon S-transferaz, İnhibisyon

References

• Aksoy, M., Ozaslan, M. S., & Kufrevioglu, O. I. (2016). Purification of glutathione S-transferase from Van Lake fish (Chalcalburnus tarichii Pallas) muscle and investigation of some metal ions effect on enzyme activity. Journal of Enzyme Inhibition and Medicinal Chemistry, 31(4), 546–550. https://doi.org/10.3109/14756366.2015.1046063
• Pljesa-Ercegovac, M., Savic-Radojevic, A., Matic, M., Coric, V., Djukic, T., Radic, T., & Simic, T. (2018). Glutathione transferases: Potential targets to overcome chemoresistance in solid tumors. International Journal of Molecular Sciences, 19(12). https://doi.org/10.3390/ijms19123785
• Temel, Y., & Taysi, M. Ş. (2018). The Effect of Mercury Chloride and Boric Acid on Rat Erythrocyte Enzymes. Biological Trace Element Research, 177–182. https://doi.org/10.1007/s12011-018-1601-x
• Temel, Y., Koçyigit, U. M., Taysi, M. S., Gökalp, F., Gürdere, M. B., Budak, Y., … Çiftci, M. (2018). Purification of glutathione S-transferase enzyme from quail liver tissue and inhibition effects of (3aR,4S,7R,7aS)-2-(4-((E)-3-(aryl)acryloyl)phenyl)-3a,4,7,7a-tetrahydro-1H-4,7-methanoisoindole-1,3(2H)-dione derivatives on the enzyme activity. Journal of Biochemical and Molecular Toxicology. https://doi.org/10.1002/jbt.22034
• Taysi, M. Ş., & Temel, Y. (2021). Glutathione S-transferase: Purification and Characterization from Quail (Coturnix coturnix japonica) Liver and the Impact of Some Metal Ions on Enzyme Activity. BioNanoScience, 11(1), 91–98. https://doi.org/10.1007/s12668-020-00811-4
• Aybek, H., Temel, Y., Ahmed, B. M., Ağca, C. A., & Çiftci, M. (2020). Deciphering of The Effect of Chemotherapeutic Agents on Human Glutathione S-Transferase Enzyme and MCF-7 Cell Line. Protein & Peptide Letters, 27(9), 888–894. https://doi.org/10.2174/0929866527666200413101017
• Özaslan, M. S., Demir, Y., Aslan, H. E., Beydemir, Ş., & Küfrevioğlu, Ö. İ. (2018). Evaluation of chalcones as inhibitors of glutathione S-transferase. Journal of Biochemical and Molecular Toxicology, 32(5), 1–6. https://doi.org/10.1002/jbt.22047
• Ballatori, N., Krance, S. M., Notenboom, S., Shi, S., Tieu, K., & Hammond, C. L. (2009). Glutathione dysregulation and the etiology and progression of human diseases. Biological Chemistry, 390(3), 191–214. https://doi.org/10.1515/BC.2009.033
• Singh, R. R., & Reindl, K. M. (2021). Glutathione S-Transferases in Cancer.
• Lebda, M., & Taha, N. (2012). Purification and Characterization of Glutathione-S-Transferase from Rat′s Liver: Effect of Carbon Tetrachloride and Camel′s Milk. Journal of Chromatography & Separation Techniques, 03(04). https://doi.org/10.4172/2157-7064.1000133
• Hutchings, M., Truman, A., & Wilkinson, B. (2019). Antibiotics: past, present and future. Current Opinion in Microbiology, 51(Figure 1), 72–80. https://doi.org/10.1016/j.mib.2019.10.008
• Martins Lopes, M. S., Machado, L. M., Ismael Amaral Silva, P. A., Tome Uchiyama, A. A., Yen, C. T., Ricardo, E. D., … Peixoto, R. D. (2020). Antibiotics, cancer risk and oncologic treatment efficacy: a practical review of the literature. Ecancermedicalscience, 14, 1106.
• Temel, Y., Ayna, A., Hamdi Shafeeq, I., & Ciftci, M. (2020). In vitro effects of some antibiotics on glucose-6-phosphate dehydrogenase from rat (Rattus norvegicus) erythrocyte. Drug and Chemical Toxicology, 43(2), 219–223. https://doi.org/10.1080/01480545.2018.1481083
• Ayna, A., Khosnaw, L., Temel, Y., & Ciftci, M. (2021). Antibiotics as Inhibitor of Glutathione S-transferase: Biological Evaluation and Molecular Structure Studies. Current Drug Metabolism, 22(4), 308–314. https://doi.org/10.2174/1389200222666210118102700
• Türkan, F., Huyut, Z., Taslimi, P., Huyut, M. T., & Gülçin, İ. (2020). Investigation of the effects of cephalosporin antibiotics on glutathione S-transferase activity in different tissues of rats in vivo conditions in order to drug development research. Drug and Chemical Toxicology, 43(4), 423–428. https://doi.org/10.1080/01480545.2018.1497644
• Larsson, D. G. J. (2014). Antibiotics in the environment. Upsala Journal of Medical Sciences, 119(2), 108–112. https://doi.org/10.3109/03009734.2014.896438
• Karaman, M., Temel, Y., & Bayindir, S. (2020). Inhibition effect of rhodanines containing benzene moieties on pentose phosphate pathway enzymes and molecular docking. Journal of Molecular Structure, 1220, 128700. https://doi.org/10.1016/j.molstruc.2020.128700
• Yüksel, F., & Temel, Y. (2022). Glutatyon S-transferaz: Koyun Dalak Dokusundan Saflaştırılması ve Karakterizasyonu. Journal of the Institute of Science and Technology, 12(4), 2352–2363. https://doi.org/10.21597/jist.1150868
• JAKOBY, H. P. (1974). the First the First. The Journal of Biological Chemistry, 240(november), 11.
• Balcı, N., Türkan, F., Şakiroğlu, H., Aygün, A., & Şen, F. (2019). Purification and characterization of glutathione S-transferase from blueberry fruits (Vaccinium arctostaphylos L.) and investigated of some pesticide inhibition effects on enzyme activity. Heliyon, 5(4). https://doi.org/10.1016/j.heliyon.2019.e01422
• Temel, Y., & Kocyigit, U. M. (2017). Purification of glucose-6-phosphate dehydrogenase from rat ( Rattus norvegicus ) erythrocytes and inhibition effects of some metal ions on enzyme activity, (March). https://doi.org/10.1002/jbt.21927
• Temel, Y., Bozkuş, T., Karagözoğlu, Y., & Çİftcİ, M. (2017). Glutatyon Redüktaz ( GR ) Enziminin Japon Bıldırcın ( Coturnix coturnix japanica ) Eritrositlerinden Saflaştırılması ve Karakterizasyonu Purification and Characterization of Glutathion Reductase Enzyme From Japanese Quail ( Coturnix coturnix japanica ) Er, 7(3), 143–150.
• Mirza Ahmed, B., Temel, Y., Çiftci, M. (2019). Purification and characterization glutathione S-transferase enzyme from quail (Coturnix, coturnix japonica) heart and investigation the effect of some metal ions on enzyme activity, Cumhuriyet Science Journal, 40, 802–812.
• Çomaklı, Veysel, Mehmet, Çiftçi, Ömer İrfan, K. (2011). Purification of Glutathione S-Transferase Enzyme from Rainbow Trout Erythrocytes and Examination of the Effects of Certain Antibiotics on Enzyme Activity Gökkuşağı Alabalık Eritrositlerinden Glutatyon. Hacettepe Journal of Biology and Chemistry, 39(4), 413–419.
• Bayindir, S., Temel, Y., Ayna, A., & Ciftci, M. (2018). The synthesis of N-benzoylindoles as inhibitors of rat erythrocyte glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase. Journal of Biochemical and Molecular Toxicology, 32(9), 1–9. https://doi.org/10.1002/jbt.22193