In vitro and in silico enzyme inhibition effects of some metal ions and compounds on glutathione S-transferase enzyme purified from Vaccinium arctostapylous L.

References

• Akkemik, E., Taser, P., Bayindir, A., Budak, H., & Ciftci, M. (2012). Purification and characterization of glutathione S-transferase from turkey liver and inhibition effects of some metal ions on enzyme activity. Environmental Toxicology and Pharmacology, 34(3), 888–894. https://doi.org/10.1016/j.etap.2012.08.010
   PubMed Web of Science ®Google Scholar
• Allocati, N., Masulli, M., Di Ilio, C., & Federici, L. (2018). Glutathione transferases: Substrates, inihibitors and pro-drugs in cancer and neurodegenerative diseases. Oncogenesis, 7(1), 8–15. https://doi.org/10.1038/s41389-017-0025-3
   PubMedGoogle Scholar
• Armstrong, R. N. (1997). Structure, catalytic mechanism, and evolution of the glutathione transferases. Chemical Research in Toxicology, 10(1), 2–18. https://doi.org/10.1021/tx960072x
   PubMed Web of Science ®Google Scholar
• 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), e01422. https://doi.org/10.1016/j.heliyon.2019.e01422
   PubMed Web of Science ®Google Scholar
• Basantani, M., & Srivastava, A. (2007). Plant glutathione transferases- a decade falls short. Canadian Journal of Botany, 85(5), 443–456. https://doi.org/10.1139/B07-033
   Google Scholar
• Buratti, F. M., Darney, K., Vichi, S., Turco, L., Di Consiglio, E., Lautz, L. S., Béchaux, C., Dorne, J.-L. C. M., & Testai, E. (2021). Human variability in glutathione-S-transferase activities, tissue distribution and major polymorphic variants: Meta-analysis and implication for chemical risk assessment. Toxicology Letters, 337, 78–90. https://doi.org/10.1016/j.toxlet.2020.11.007
   PubMed Web of Science ®Google Scholar
• Bursal, E., Turkan, F., Buldurun, K., Turan, N., Aras, A., Çolak, N., Murahari, M., & Yergeri, M. C. (2021). Transition metal complexes of a multidentate Schiff base ligand containing pyridine: Synthesis, characterization, enzyme inhibitions, antioxidant properties, and molecular docking studies. Biometals, 34(2), 393–406. https://doi.org/10.1007/s10534-021-00287-z
   PubMed Web of Science ®Google Scholar
• Cho, M. K., & Kim, S. G. (2000). Induction of class α glutathione S-transferases by 4-methylthiazole in the rat liver: Role of oxidative stress. Toxicology Letters, 115(2), 107–115. https://doi.org/10.1016/S0378-4274(00)00187-9
   PubMed Web of Science ®Google Scholar
• Comakli, V. M., Ciftci, M., & Kufrevioglu, O. I. (2013). Effects of some metal ions on rainbow trout erythrocytes glutathione S-transferase enzyme: An in vitro study. Journal of Enzyme Inhibition and Medicinal Chemistry, 28(6), 1261–1266. https://doi.org/10.3109/14756366.2012.729829
   PubMed Web of Science ®Google Scholar
• Connor, A. M., Luby, J. J., & Tong, C. B. S. (2002). Variation in antioxidant activity in blueberry and correlation among different antioxidant activity assays. Journal of the American Society for Horticultural Science, 127(2), 238–244. https://doi.org/10.21273/JASHS.127.2.238
   Web of Science ®Google Scholar
• Çelik, H. (2009). The performance of some northern highbush blueberry (Vaccinium corymbosum L.) varieties in North Eastern part of Anatolia. Anadolu Journal of Agricultural Sciences, 24(3), 141–146. https://dergipark.org.tr/en/pub/omuanajas/issue/20222/214406
   Google Scholar
• Ehlenfeldt, M. K., & Prior, R. L. (2001). Oxygen radical absorbance capacity (ORAC) and phenolic and anthocyanin concentrations in fruit and leaf tissues of highbush blueberry. Journal of Agricultural and Food Chemistry, 49(5), 2222–2227. https://doi.org/10.1021/jf0013656
   PubMed Web of Science ®Google Scholar
• Forman, H. J., Zhang, H., & Rinna, A. (2009). Glutathione: Overview of its protective roles, measurement, and biosynthesis. Molecular Aspects of Medicine, 30(1–2), 1–12. https://doi.org/10.1016/j.mam.2008.08.006
   PubMed Web of Science ®Google Scholar
• Gyamfi, M. A., Ohtani, I. I., Shinno, E., & Aniya, Y. (2004). Inhibition of glutathione S-transferases by thonningianin A, isolated from the African medicinal herb, Thonningia sanguinea, in vitro. Food and Chemical Toxicology, 42(9), 1401–1408. https://doi.org/10.1016/j.fct.2004.04.001
   PubMed Web of Science ®Google Scholar
• Gulçin, İ., Taslimi, P., Aygün, A., Sadeghian, N., Bastem, E., Kufrevioglu, O. I., Turkan, F., & Şen, F. (2018). Antidiabetic and antiparasitic potentials: Inhibition effects of some natural antioxidant compounds on α-glycosidase, α-amylase and human glutathione S-transferase enzymes. International Journal of Biological Macromolecules, 119, 741–746. https://doi.org/10.1016/j.ijbiomac.2018.08.001
   PubMed Web of Science ®Google Scholar
• Hayes, J. D., & Strange, R. C. (2000). Glutathione S-transferase polymorphisms and their biological consequences. Pharmacology, 61(3), 154–166. https://doi.org/10.1159/000028396
   PubMed Web of Science ®Google Scholar
• Hayeshi, R., Mutingwende, I., Mavengere, W., Masiyanise, V., & Mukanganyama, S. (2007). The inhibition of human glutathione S-transferases activity by plant polyphenolic compounds ellagic acid and curcumin. Food and Chemical Toxicology, 45(2), 286–295. https://doi.org/10.1016/j.fct.2006.07.027
   PubMed Web of Science ®Google Scholar
• Hellou, J., Ross, N. W., & Moon, T. W. (2012). Glutathione, glutathione S-transferase, and glutathione conjugates, complementary markers of oxidative stress in aquatic biota. Environmental Science and Pollution Research International, 19(6), 2007–2023. https://doi.org/10.1007/s11356-012-0909-x
   PubMed Web of Science ®Google Scholar
• Ioannıdes, C. (2002). Xenobiotic metabolism: An overview. In C. Ioannides (Ed.), Enzyme systems that metabolise drugs and other xenobiotics (pp. 1–32). John Wiley and Sons, Ltd. https://doi.org/10.1002/0470846305
   Google Scholar
• Jan, A., Azam, M., Siddiqui, K., Ali, A., Choi, I., & Haq, Q. (2015). Heavy Metals and Human Health: Mechanistic Insight into Toxicity and Counter Defense System of Antioxidants. International Journal of Molecular Sciences, 16(12), 29592–29630. https://doi.org/10.3390/ijms161226183
   PubMed Web of Science ®Google Scholar
• Kakkar, P., & Jaffery, F. N. (2005). Biological markers for metal toxicity. Environmental Toxicology and Pharmacology, 19(2), 335–349. https://doi.org/10.1016/j.etap.2004.09.003
   PubMed Web of Science ®Google Scholar
• Lin, C. Y., Fu, R. H., Chou, R. H., Chen, J. H., Wu, C. R., Chang, S. W., & Tsai, C. W. (2017). Inhibition of JNK by pi class of glutathione S-transferase through PKA/CREB pathway is associated with carnosic acid protection against 6-hydroxydopamine-induced apoptosis. Food and Chemical Toxicology, 103, 194–202. https://doi.org/10.1016/j.fct.2017.03.020
   PubMed Web of Science ®Google Scholar
• Liu, R. M., & Pravia, K. G. (2010). Oxidative stress and glutathione in TGF-beta-mediated fibrogenesis. Free Radical Biology & Medicine, 48(1), 1–15. https://doi.org/10.1016/j.freeradbiomed.2009.09.026
   PubMed Web of Science ®Google Scholar
• Lu, S. C. (2013). Glutathione synthesis. Biochimica et Biophysica Acta, 1830(5), 3143–3153. https://doi.org/10.1016/j.bbagen.2012.09.008
   PubMed Web of Science ®Google Scholar
• Mathew, N., Kalyanasundaram, M., & Balaraman, K. (2006). Glutathione S-transferase (GST) inhibitors. Expert Opinion on Therapeutic Patents, 16(4), 431–444. https://doi.org/10.1517/13543776.16.4.431
   Web of Science ®Google Scholar
• Pallardó, F. V., Markovic, J., García, J. L., & Viña, J. (2009). Role of nuclear glutathione as a key regulator of cell proliferation. Molecular Aspects of Medicine, 30 (1–2), 77–85. https://doi.org/10.1016/j.mam.2009.01.001
   PubMed Web of Science ®Google Scholar
• Park, S., Ahn, S., Shin, Y., Yang, Y., & Yeom, C. H. (2018). Vitamin C in Cancer: A Metabolomics Perspective. Frontiers in Physiology, 9, 762. https://doi.org/10.3389/fphys.2018.00762
   PubMed Web of Science ®Google Scholar
• Prior, R. L., Cao, G., Martin, A., Sofic, E., McEwen, J., O'Brien, C., Lischner, N., Ehlenfeldt, M., Kalt, W., Krewer, G., & Mainland, C. M. (1998). Antioxidant capacity as influenced by total phenolic and anthocyanin content, maturity and variety of Vaccinium species. Journal of Agricultural and Food Chemistry, 46(7), 2686–2693. https://doi.org/10.1021/jf980145d
   Web of Science ®Google Scholar
• Sheehan, D., Meade, G., Foley, V. M., & Dowd, C. A. (2001). Structure, function and evolution of glutathione transferases: Implications for classification of non-mammalian members of an ancient enzyme superfamily. The Biochemical Journal, 360(Pt 1), 1–16. https://doi.org/10.1042/bj3600001
   PubMed Web of Science ®Google Scholar
• Suthanthiran, M., Anderson, M. E., Sharma, V. K., & Meister, A. (1990). Glutathione regulates activation-dependent DNA synthesis in highly purified normal human T lymphocytes stimulated via the CD2 and CD3 antigens. Proceedings of the National Academy of Sciences of the United States of America, 87(9), 3343–3347. https://doi.org/10.1073/pnas.87.9.3343
   PubMed Web of Science ®Google Scholar
• Taslimi, P., Osmanova, S., Caglayan, C., Turkan, F., Sardarova, S., Farzaliyev, V., Sujayev, A., Sadeghian, N., & Gulçin, İ. (2018). Novel amides of 1,1-bis-(carboxymethylthio)-1-arylethanes: Synthesis, characterization, acetylcholinesterase, butyrylcholinesterase, and carbonic anhydrase inhibitory properties. Journal of Biochemical and Molecular Toxicology, 32(9), e22191. https://doi.org/10.1002/jbt.22191
   PubMed Web of Science ®Google Scholar
• Turkan, F., Balcı, N., & Sakiroglu, H. (2014). Purification and characterization of the glutaton S-transferase enzyme from the fruit fruit (Laurocerasus officinalis Roem.) and inhibition effects of enzyme activity. Journal of Science and Technology MSU, 2(2), 280–288. https://dergipark.org.tr/tr/pub/msufbd/issue/19659/370826
   Google Scholar
• van Bladeren, P. J. (2000). Glutathione conjugation as a bioactivation reaction. Chemico-Biological Interactions, 129(1–2), 61–76. https://doi.org/10.1016/S0009-2797(00)00214-3
   PubMed Web of Science ®Google Scholar
• Wang, S. Y., & Jiao, H. J. (2000). Scavenging capacity of berry crops on superoxide radicals, hydrogen peroxide, hydroxyl radicals, and singlet oxygen. Journal of Agricultural and Food Chemistry, 48(11), 5677–5684. https://doi.org/10.1021/jf000766i
   PubMed Web of Science ®Google Scholar
• Wu, G., Fang, Y. Z., Yang, S., Lupton, J. R., & Turner, N. D. (2004). Glutathione metabolism and its implications for health. The Journal of Nutrition, 134(3), 489–492. https://doi.org/10.1093/jn/134.3.489
   PubMed Web of Science ®Google Scholar