759
Views
20
CrossRef citations to date
0
Altmetric
Research Articles

A study on the effects of inhibition mechanism of curcumin, quercetin, and resveratrol on human glutathione reductase through in vitro and in silico approaches

, , , &
Pages 1744-1753 | Received 06 Feb 2020, Accepted 28 Feb 2020, Published online: 16 Mar 2020

References

  • Acan, N. L., & Tezcan, E. F. (1991). Kinetic-Properties of sheep brain Glutathione-Reductase. Enzyme, 45(3), 121–124. doi:10.1159/000468877
  • Adem, S., Aslan, A., Ahmed, I., Krohn, K., Guler, C., Comakli, V., Demirdag, R., & Kuzu, M. (2016). Inhibitory and activating effects of some flavonoid derivatives on human pyruvate kinase Isoenzyme M2. Archiv Der Pharmazie, 349(2), 132–136. doi:10.1002/ardp.201500357
  • Adem, S., & Ciftci, M. (2016). Purification and biochemical characterization of Glucose 6-Phosphate Dehydrogenase, 6-Phosphogluconate dehydrogenase and glutathione reductase from rat lung and inhibition effects of some antibiotics. Journal of Enzyme Inhibition and Medicinal Chemistry, 31(6), 1342–1348. doi:10.3109/14756366.2015.1132711
  • Adem, S., Comakli, V., Kuzu, M., & Demirdag, R. (2014). Investigation of the effects of some phenolic compounds on the activities of Glucose-6-phosphate Dehydrogenase and 6-Phosphogluconate Dehydrogenase from human erythrocytes. Journal of Biochemical and Molecular Toxicology, 28(11), 510–514. doi:10.1002/jbt.21592
  • Akkemik, E., Senturk, M., Ozgeris, F. B., Taser, P., & Ciftci, M. (2011). In vitro effects of some drugs on human erythrocyte glutathione reductase. Turkish Journal of Medical Sciences, 41(2), 235–241. doi:10.3906/sag-1002-4.
  • Awasthi, Y. C., Chaudhary, P., Vatsyayan, R., Sharma, A., Awasthi, S., & Sharma, R. (2009). Physiological and Pharmacological significance of glutathione-conjugate transport. Journal of Toxicology and Environmental Health-Part B-Critical Reviews, 12(7), 540–551. doi:10.1080/10937400903358975
  • Ballatori, N., Krance, S. M., Notenboom, S., Shi, S. J., Tieu, K., & Hammond, C. L. (2009). Glutathione dysregulation and the etiology and progression of human diseases. Biological Chemistry, 390(3), 191–214. doi:10.1515/BC.2009.033
  • Bankapalli, K., Saladi, S., Awadia, S. S., Goswami, A. V., Samaddar, M., & D'Silva, P. (2015). Robust Glyoxalase activity of Hsp31, a ThiJ/DJ-1/PfpI family member protein, is critical for oxidative stress resistance in saccharomyces cerevisiae. Journal of Biological Chemistry, 290(44), 26491–26507. doi:10.1074/jbc.M115.673624
  • Bayrak, C., Taslimi, P., Karaman, H. S., Gulcin, I., & Menzek, A. (2019). The first synthesis, carbonic anhydrase inhibition and anticholinergic activities of some bromophenol derivatives with S including natural products. Bioorganic Chemistry, 85, 128–139. doi:10.1016/j.bioorg.2018.12.012
  • Berkholz, D. S., Faber, H. R., Savvides, S. N., & Karplus, P. A. (2008). Catcalytic cycle of human glutathione reductase near 1 angstrom resolution. Journal of Molecular Biology, 382(2), 371–384. doi:10.1016/j.jmb.2008.06.083
  • Beutler, E. (1984). Red cell metabolism: A manual of biochemical methods. Grune and Starton.
  • Bhuyan, D. J., Amrita, B. (2018). Phenolic compounds: Potential health benefits and toxicity. In Q. V. Vuong. (Eds.), Utilisation of bioactive compounds from agricultural and food waste (Vol. 1, pp. 27–59). CRC Press.
  • Bradford, M. M. (1976). Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding. Analytical Biochemistry, 72(1-2), 248–254. doi:10.1016/0003-2697(76)90527-3
  • Cakmak, R., Durdagi, S., Ekinci, D., Senturk, M., & Topal, G. (2011). Design, synthesis and biological evaluation of novel nitroaromatic compounds as potent glutathione reductase inhibitors. Bioorganic & Medicinal Chemistry Letters, 21(18), 5398–5402. doi:10.1016/j.bmcl.2011.07.002
  • Carlberg, I., & Mannervik, B. (1975). Purification and characterization of the flavoenzyme glutathione reductase from rat liver. The Journal of Biological Chemistry, 250(14), 5475–5480.
  • Ceylan, H., Demir, Y., & Beydemir, S. (2019). Inhibitory Effects of Usnic and Carnosic Acid on Some Metabolic Enzymes: An in vitro Study. Protein & Peptide Letters, 26(5), 364–370. doi:10.2174/0929866526666190301115122
  • Dalmizrak, O., Terali, K., Asuquo, E. B., Ogus, I. H., & Ozer, N. (2019). The Relevance of Glutathione Reductase Inhibition by Fluoxetine to Human Health and disease: Insights derived from a combined kinetic and docking study. The Protein Journal, 38(5), 515–524. doi:10.1007/s10930-019-09834-7
  • Davioud-Charvet, E., Delarue, S., Biot, C., Schwobel, B., Boehme, C. C., Mussigbrodt, A., Maes, L., Sergheraert, C., Grellier, P., Schirmer, R. H., & Becker, K. (2001). A prodrug form of a Plasmodium falciparum glutathione reductase inhibitor conjugated with a 4-anilinoquinoline. Journal of Medicinal Chemistry, 44(24), 4268–4276. doi:10.1021/jm010268g
  • Demir, Y. (2019). Purification of glutathione reductase from human erythrocytes: Inhibition profile of some anti-epileptic drugs. Journal of the Institute of Science and Technology, 9(4), 2140– 2147. doi:10.21597/jist.525154.
  • Deneke, S. M., & Fanburg, B. L. (1989). Regulation of cellular glutathione. American Journal of Physiology-Lung Cellular and Molecular Physiology, 257(4), L163–L173. doi:10.1152/ajplung.1989.257.4.L163
  • Elliott, A. J., Scheiber, S. A., Thomas, C., & Pardini, R. S. (1992). Inhibition of Glutathione-Reductase by Flavonoids - a structure activity study. Biochemical Pharmacology, 44(8), 1603–1608. doi:10.1016/0006-2952(92)90478-2
  • Erden, I. M., Akgün, A., & Kahraman, A. (2003). The effects of exogenous glutathione on reduced glutathione level, glutathione peroxidase and glutathione reductase activities of rats with different ages and gender after whole-body Γ-irradiation. AGE, 26(3-4), 55–58. doi:10.1007/s11357-003-0005-8
  • Gonul Baltaci, N., Guler, C., Ceylan, H., Kalin, S. N., Adem, S., Kocpinar, E. F., Erdogan, O., & Budak, H. (2018). In vitro and in vivo effects of iron on the expression and activity of glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and glutathione reductase in rat spleen. Journal of Biochemical and Molecular Toxicology, 33(1), e22229. doi:10.1002/jbt.22229
  • Iio, M., Kawaguchi, H., Sakota, Y., Otonari, J., & Nitahara, H. (1993). Effects of polyphenols, including flavonoids, on Glutathione-S-Transferase and Glutathione-Reductase. Bioscience Biotechnology and Biochemistry, 57(10), 1678–1680. doi:10.1271/bbb.57.1678
  • Jankun, J., Wyganowska-Świątkowska, M., Dettlaff, K., Jelińska, A., Surdacka, A., Wątróbska-Świetlikowska, D., & Skrzypczak-Jankun, E. W. A. (2016). Determining whether curcumin degradation/condensation is actually bioactivation (Review). International Journal of Molecular Medicine, 37(5), 1151–1158. doi:10.3892/ijmm.2016.2524
  • Jenner, P., & Olanow, C. W. (1998). Understanding cell death in Parkinson’s disease. Annals of Neurology, 44(3), S72–S84. doi:10.1002/ana.410440712
  • Jozefczak, M., Remans, T., Vangronsveld, J., & Cuypers, A. (2012). Glutathione Is a Key Player in Metal-Induced Oxidative Stress Defenses. International Journal of Molecular Sciences, 13(3), 3145–3175. doi:10.3390/ijms13033145
  • Kang, K. W., Ryu, J. H., & Kim, S. G. (2000). The essential role of phosphatidylinositol 3-kinase and of p38 mitogen-activated protein kinase activation in the antioxidant response element-mediated rGSTA2 induction by decreased glutathione in H4IIE hepatoma cells. Molecular Pharmacology, 58(5), 1017–1025. doi:10.1124/mol.58.5.1017
  • Karaman, M., Akkemik, E., Budak, H., & Ciftci, M. (2012). In vitro effects of some drugs on human erythrocyte glutathione reductase. Journal of Enzyme Inhibition and Medicinal Chemistry, 27(1), 18–23. doi:10.3109/14756366.2011.572879
  • Kavishe, R. A., Koenderink, J. B., & Alifrangis, M. (2017). Oxidative stress in malaria and artemisinin combination therapy: Pros and Cons. The Febs Journal, 284(16), 2579–2591. doi:10.1111/febs.14097
  • Kerlund, B., Tynell, E., Bratt, G., Bielenstein, M., & Lidman, C. (1997). N-acetylcysteine treatment and the risk of toxic reactions to trimethoprim-sulphamethoxazole in primary Pneumocystis carinii prophylaxis in HIV-infected patients. Journal of Infection, 35(2), 143–147. doi:10.1016/S0163-4453(97)91578-4
  • Kocaoglu, E., Talaz, O., Cavdar, H., Senturk, M., Supuran, C. T., & Ekinci, D. (2019). Determination of the inhibitory effects of N-methylpyrrole derivatives on glutathione reductase enzyme. Journal of Enzyme Inhibition and Medicinal Chemistry, 34(1), 51–54. doi:10.1080/14756366.2018.1520228
  • Kondo, T., Dale, G. L., & Beutler, E. (1980). Glutathione Transport by inside-out Vesicles from Human-Erythrocytes. Proceedings of the National Academy of Sciences of Sciences, 77(11), 6359–6362. doi:10.1073/pnas.77.11.6359
  • Kowaltowski, A. J., & Fiskum, G. (2005). Redox mechanisms of cytoprotection by Bcl-2. Antioxidants & Redox Signaling, 7(3-4), 508–514. doi:10.1089/ars.2005.7.508
  • Kuzu, M., Aslan, A., Ahmed, I., Comakli, V., Demirdag, R., & Uzun, N. (2016). Purification of glucose-6-phosphate dehydrogenase and glutathione reductase enzymes from the gill tissue of Lake Van fish and analyzing the effects of some chalcone derivatives on enzyme activities. Fish Physiology and Biochemistry, 42(2), 483–491. doi:10.1007/s10695-015-0153-7
  • Lew, V. L., Tiffert, T., & Ginsburg, H. (2003). Excess hemoglobin digestion and the osmotic stability of Plasmodium falciparum-infected red blood cells. Blood, 101(10), 4189–4194. doi:10.1182/blood-2002-08-2654
  • Lineweaver, H., & Burk, D. (1934). The determination of enzyme dissocation constants. Journal of the American Chemical Society, 57, 685. doi:10.1021/ja01318a036
  • Lipinski, C. A., Lombardo, F., Dominy, B. W., & Feeney, P. J. (2001). Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Advanced Drug Delivery Reviews, 46(1-3), 3–26. doi:10.1016/S0169-409X(00)00129-0
  • Liu, X. D., & Sturla, S. J. (2009). Profiling patterns of glutathione reductase inhibition by the natural product illudin S and its acylfulvene analogues. Molecular Biosystems, 5(9), 1013–1039. doi:10.1039/b904720d
  • Meierjohann, S., Walter, R. D., & Muller, S. (2002). Regulation of intracellular glutathione levels in erythrocytes infected with chloroquine-sensitive and chloroquine-resistant Plasmodium falciparum. Biochemical Journal, 368(3), 761–768. doi:10.1042/bj20020962
  • Narayanankutty, A., Job, J. T., & Narayanankutty, V. (2019). Giutathione, an Antioxidant Tripeptide: Dual Roles in Carcinogenesis and Chemoprevention. Current Protein & Peptide Science, 20(9), 907–917. doi:10.2174/1389203720666190206130003
  • Ozaslan, M. S., Demir, Y., Aksoy, M., Kufrevioglu, O. I., & Beydemir, S. (2018). Inhibition effects of pesticides on glutathione-S-transferase enzyme activity of Van Lake fish liver. Journal of Biochemical and Molecular Toxicology, 32(9), e22196. ARTN e2219610. doi:10.1002/jbt.22196
  • Postma, N. S., Mommers, E. C., Eling, W. M. C., & Zuidema, J. (1996). Oxidative stress in malaria; Implications for prevention and therapy. Pharmacy World and Science, 18(4), 121–129. doi:10.1007/BF00717727
  • Schirmer, R. H., Müller, J. G., & Krauth-Siegel, R. L. (1995). Disulfide-Reductase inhibitors as chemotherapeutic-agents - the design of drugs for Trypanosomiasis and Malaria. Angewandte Chemie International Edition in English, 34(2), 141–154. doi:10.1002/anie.199501411
  • Schrödinger, L. (2009a). SiteMap, version2.3. New York, NY: SiteMap, Schrödinger, LLC, 2020.
  • Schrödinger, L. (2009b). Induced fit docking protocol; Glide version 5.5; Prime version 2.1.
  • Schrödinger, L. (2015). QikProp, version 4.4. New York, NY: QikProp, Schrödinger, LLC, 2020.
  • Schrödinger, L. (2017). Drug discovery suite. New York, NY: Maestro, Schrödinger, LLC, 2020.
  • Seefeldt, T., Dwivedi, C., Peitz, G., Herman, J., Carlson, L., Zhang, Z. L., & Guan, X. M. (2005). 2-acetylamino-3-[4-(2-acetylamino-2-carboxyethylsulfanylcarbonylamino)-phenylcarbamoylsulfanyl]propionic acid and its derivatives as a novel class of glutathione reductase inhibitors. Journal of Medicinal Chemistry, 48(16), 5224–5231. doi:10.1021/jm050030i
  • Tandogan, B., Kuruuzum-Uz, A., Sengezer, C., Guvenalp, Z., Demirezer, L. O., & Ulusu, N. N. (2011a). In vitro effects of rosmarinic acid on glutathione reductase and glucose 6-phosphate dehydrogenase. Pharmaceutical Biology, 49(6), 587–594. doi:10.3109/13880209.2010.533187
  • Tandogan, B., Güvenç, A., Çalış, İ., & Ulusu, N. N. (2011b). In vitro effects of compounds isolated from Sideritis brevibracteata on bovine kidney cortex glutathione reductase. Acta Biochimica Polonica, 58(4), 471–475. doi:10.18388/abp.2011_2213
  • Taser, P., & Ciftci, M. (2012). Purification and characterization of glutathione reductase from turkey liver. Turkish Journal of Veterinary & Animal Sciences, 36(5), 546–553. doi:10.3906/vet-1103-5.
  • Tekman, B., Ozdemir, H., Senturk, M., & Ciftci, M. (2008). Purification and characterization of glutathione reductase from rainbow trout (Oncorhynchus mykiss) liver and inhibition effects of metal ions on enzyme activity. Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology, 148(2), 117–121. doi:10.1016/j.cbpc.2008.04.005
  • Townsend, D. M., Tew, K. D., & Tapiero, H. (2003). The importance of glutathione in human disease. Biomedicine & Pharmacotherapy, 57(3-4), 145–155. doi:10.1016/S0753-3322(03)00043-X
  • Turkan, F., Huyut, Z., Demir, Y., Ertas, F., & Beydemir, S. (2019). The effects of some cephalosporins on acetylcholinesterase and glutathione S-transferase: An in vivo and in vitro study. Archives of Physiology and Biochemistry, 125(3), 235–243. doi:10.1080/13813455.2018.1452037
  • Ulusu, N. N., & Tandoğan, B. (2007). Purification and kinetic properties of glutathione reductase from bovine liver. Molecular and Cellular Biochemistry, 303(1-2), 45–51. doi:10.1007/s11010-007-9454-1
  • Vijayalingam, S., Parthiban, A., Shanmugasundaram, K. R., & Mohan, V. (1996). Abnormal antioxidant status in impaired glucose tolerance and non-insulin-dependent diabetes mellitus. Diabetic Medicine, 13(8), 715–719. doi:10.1002/(SICI)1096-9136(199608)13:8<715::AID-DIA172>3.0.CO;2-Z
  • Wongtrakul, J., Sukittikul, S., Saisawang, C., & Ketterman, A. J. (2012). Mitogen-activated protein kinase p38b interaction with delta class glutathione transferases from the fruit fly, Drosophila melanogaster. Journal of Insect Science, 12(107), 1–12. doi:10.1673/031.012.10701
  • Yiğit, B., Kaya, R., Taslimi, P., Işık, Y., Karaman, M., Yiğit, M., Özdemir, İ., & Gulçin, İ. (2019). Imidazolinium chloride salts bearing wingtip groups: Synthesis, molecular docking and metabolic enzymes inhibition. Journal of Molecular Structure, 1179, 709–718. doi:10.1016/j.molstruc.2018.11.038
  • Zimmermann, A. K., Loucks, F. A., Schroeder, E. K., Bouchard, R. J., Tyler, K. L., & Linseman, D. A. (2007). Glutathione binding to the Bcl-2 homology-3 domain groove - A molecular basis for Bcl-2 antioxidant function at mitochondria. Journal of Biological Chemistry, 282(40), 29296–29304. doi:10.1074/jbc.M702853200
  • Zuzak, E., Horecka, A., Kiełczykowska, M., Dudek, A., Musik, I., Kurzepa, J., & Kurzepa, J. (2017). Glutathione level and glutathione reductase activity in serum of coronary heart disease patients. Journal of Pre-Clinical and Clinical Research, 11(2), 103–105. doi:10.26444/jpccr/81277

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.