Purification of Glutathione Reductase from Human Erythrocytes: Inhibition Profile of Some Anti-Epileptic Drugs

Demir, Yeliz

doi:10.21597/jist.525154

Cited by 7 publications

(7 citation statements)

References 31 publications

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“…Other authors investigated the in vitro primary effects of some active pharmaceutical ingredients on GST and GR enzymes, which are closely related to drug response in treating many diseases [42–44] . In some research, it was documented that antifungal, antibacterial, and antibiotic agents and calcium channel blockers showed high inhibition potency on hGSTpi [45–47] .…”

Section: Resultsmentioning

confidence: 99%

Structure‐Activity Relationship of Methyl 4‐Aminobenzoate Derivatives as Being Drug Candidate Targeting Glutathione Related Enzymes: in Vitro and in Silico Approaches

Korkmaz¹,

Güller²,

Kalın³

et al. 2023

Chemistry & Biodiversity

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A thiol compound, glutathione, is essential for healthy cell defence against xenobiotics and oxidative stress. Glutathione reductase (GR) and glutathione S‐transferase (GST) are two glutathione‐related enzymes that function in the antioxidant and the detoxification systems. In this study, potential inhibitory effects of methyl 4‐aminobenzoate derivatives on GR and GST were examined in vitro. GR and GST were isolated from human erythrocytes with 7.63 EU/mg protein and 5.66 EU/mg protein specific activity, respectively. It was found that compound 1 (methyl 4‐amino‐3‐bromo‐5‐fluorobenzoate with Ki value of 0.325±0.012 μM) and compound 5 (methyl 4‐amino‐2‐nitrobenzoate with Ki value of 92.41±22.26 μM) inhibited GR and GST stronger than other derivatives. Furthermore, a computer‐aided method was used to predict the binding affinities of derivatives, ADME characteristics, and toxicities. Derivatives 4 (methyl 4‐amino‐2‐bromobenzoate) and 6 (methyl 4‐amino‐2‐chlorobenzoate) were estimated to have the lowest binding energies into GR and GST receptors, respectively according to results of in silico studies.

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Section: Resultsmentioning

confidence: 99%

Structure‐Activity Relationship of Methyl 4‐Aminobenzoate Derivatives as Being Drug Candidate Targeting Glutathione Related Enzymes: in Vitro and in Silico Approaches

Korkmaz¹,

Güller²,

Kalın³

et al. 2023

Chemistry & Biodiversity

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“…Some epilepsy drugs have been reported to inhibit the GR enzyme. It was found the order of drugs that affect as inhibitor follows: phenytoin (K I : 0.15 ± 0.03 mM) > gabapentin (K I : 0.19 ± 0.05 mM) > primidone (K I : 5.74 ± 1.14 mM) [9]. Senturk et al [82] investigated the inhibitory effect of some antibiotics on GR.…”

Section: Two-dimensional Schematic Views Of Brimonidine and Proparaca...mentioning

confidence: 99%

“…It plays a role in the pathogenesis of eye diseases, including glaucoma, keratoconjunctivitis, pinguecula, pterygium, cataract, macular degeneration, diabetic retinopathy, and dry eye [4][5][6][7]. DOI: 10.1002/bab.2107 Published online 28 January 2021 in Wiley Online Library (wileyonlinelibrary.com) Oxidative stress has various harmful impacts and can give rise to aging, neurological disease, tumorigenesis, and cell death [8][9][10][11][12]. Reactive oxygen species (ROS) can promote signal proliferation and possess normal physiological roles [13][14][15].…”

Section: Introductionmentioning

confidence: 99%

The effect of brimonidine and proparacaine on metabolic enzymes: Glucose‐6‐phosphate dehydrogenase, 6‐phosphogluconate dehydrogenase, and glutathione reductase

Çalışkan

Kesebir

Demir

et al. 2021

Biotech and App Biochem

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Oxidative stress is to upregulate the pentose phosphate pathway (PPP). The PPP consists of two functional branches, glucose-6-phosphate dehydrogenase (G6PD) and 6-phosphogluconaste dehydrogenase (6PGD). Glutathione reductase (GR) has a significant role in catalyzing an oxidized glutathione form into a reduced form. The purpose of this study is to investigate the effects of brimonidine and proparacaine on the activity of 6PGD, G6PD, and GR enzymes purified from human erythrocytes. Brimonidine displayed considerable inhibition profile against G6PD with IC 50 value and K I constant of 29.93 ± 3.56 and 48.46 ± 0.66 μM, respectively. On the other hand, proparacaine had no inhibitory effect against G6PD. K I values were found to be 66.06 ± 0.78 and 811.50 ± 11.13 μM for brimonidine and proparacaine, respectively, for 6PGD. K I values were found to be 144.10 ± 2.01 and 1,654.00 ± 26.29 μM for brimonidine and proparacaine, respectively, for GR. Herein, also in silico molecular docking studies were performed between drugs and enzymes.

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“…Fundamentally, GR plays a crucial role in preserving the redox balance inside the cell and supporting defensive systems that protect cells from oxidative stress brought on by free radicals. 6 GR catalyzes an enzyme activity that results in reduced glutathione, which is essential for neutralizing hydrogen peroxide inside of cells. This is accomplished by reduced glutathione by the catalytic action of glutathione peroxidase, which transforms hydrogen peroxide into water.…”

Section: Introductionmentioning

confidence: 99%

Investigation of the effect of isoxazole derivatives on glutathione-dependent enzymes associated with cancer

Esra Duran

2024

MOJABB

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Globally, cancer is currently the second-most common cause of death. As such, it is a crucial problem that affects society's well-being all around the world. Chemotherapy is the most commonly used treatment for cancer. It is a technique that uses drugs to kill cancerous cells or the cancerous organism itself. Chemotherapy has been used to treat metastatic cancer for the past 50 years, with varying degrees of effectiveness. One of the main problems with many chemotherapeutic drugs is that they might damage healthy cells and organs. These drugs frequently have a low therapeutic index, a restricted ability to selectively target cancerous cells, and a high propensity to develop drug resistance after extended use. Furthermore, a rise in the expression of glutathione reductase (GR; EC 1.8.1.7) and glutathione S-transferase (GST; EC 2.5.1.18) can be seen with time. Extensive study on proteins and their functions in the development of cancer cells has been conducted in recent years. Glutathione-S-transferases (GSTs) are a superfamily of enzymes that play a critical role in the detoxification of cells by protecting them against reactive electrophiles such as chemotherapeutic drugs and reactive oxygen species. Glutathione reductase (GR), on the other hand, is an essential antioxidant enzyme that supports cellular protection against oxidative stress. In addition to its antioxidant role, GR has become a target for the synthesis of antimalarial and anticancer medications. In the current investigation, affinity chromatography was used to purificate the GST and GR enzymes from human erythrocytes. Through the calculation of IC50 and KI values for these derivatives, the effects of isoxazole derivatives on these purified enzymes were examined, with an emphasis on identifying the forms of inhibition.

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Purification of Glutathione Reductase from Human Erythrocytes: Inhibition Profile of Some Anti-Epileptic Drugs

Cited by 7 publications

References 31 publications

Structure‐Activity Relationship of Methyl 4‐Aminobenzoate Derivatives as Being Drug Candidate Targeting Glutathione Related Enzymes: in Vitro and in Silico Approaches

Structure‐Activity Relationship of Methyl 4‐Aminobenzoate Derivatives as Being Drug Candidate Targeting Glutathione Related Enzymes: in Vitro and in Silico Approaches

The effect of brimonidine and proparacaine on metabolic enzymes: Glucose‐6‐phosphate dehydrogenase, 6‐phosphogluconate dehydrogenase, and glutathione reductase

Investigation of the effect of isoxazole derivatives on glutathione-dependent enzymes associated with cancer

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