glutathione reductase

Glutathione reductase (EC 1.6.4.2) is an enzyme that maintains the supply of reduced glutathione [1].

Nitrofurazone (Nitrofural; Furacilin) is an orally active nitroaromatic broad-spectrum antibiotic with activity against both Gram-positive and Gram-negative bacteria. It is commonly used for establishing breast cancer models.

L-Glutathione reduced (Glutathione) is a naturally occurring tripeptide found in cells as an endogenous antioxidant that scavenges oxygen free radicals. L-Glutathione reduced is a cofactor for certain enzymes and is involved in the rearrangement of protein disulfide bonds and the reduction of peroxides.

Glutathione oxidized (L(-) -glutathione) is the oxidized form of Glutathione, which is a major antioxidant and antidote in cells. Glutathione oxidized can be used to study sickle cells and red blood cells.

LCS3 is a reversible and non-competitive synergistic inhibitor of glutathione disulfide reductase (GSR) and thioredoxin reductase 1 (TXNRD1) with IC50s of 3.3 μM and 3.8 μM, respectively. LCS3 has antitumour activity, induces apoptosis and can be used in the study of lung adenocarcinoma (LUAD).

Dantrolene is a postsynaptic muscle relaxant by inhibiting Ca2+ ions release from sarcoplasmic reticulum stores by antagonizing ryanodine receptors.

Antitrypanosomal agent 1 is a potent and selective trypanothione reductase (TR) inhibitor (IC50: 3.3 μM) that also inhibits glutathione reductase (IC50: 64.8 μM) and T. brucei (EC50: 1 μM).

Glutathione Reductase, Wheat germ (EC 1.6.4.2), is a crucial flavoprotein in the antioxidant defense system. In this process, reduced glutathione (GSH) detoxifies hydrogen peroxide via glutathione peroxidase, becoming oxidized to form oxidized glutathione (GSSG). Glutathione Reductase (GR) then reduces GSSG back to GSH using NADPH, which is converted to NADP+. The regenerated GSH is available for further hydrogen peroxide detoxification. Glutathione Reductase utilizes FAD as a cofactor.

Glutathione Reductase, Wheat germ (EC 1.6.4.2), is an essential flavoprotein in the antioxidant defense system. The reduced glutathione (GSH) is used by glutathione peroxidase to detoxify hydrogen peroxide, during which it is oxidized to form oxidized glutathione (GSSG). The GSSG is then reduced back to GSH by glutathione reductase (GR) using NADPH, which is converted to NADP+ in the process. The regenerated GSH can continue detoxifying hydrogen peroxide. Glutathione Reductase utilizes FAD as a cofactor.

Dantrolene-13C3 is the 13C3-labeled form of Dantrolene. Dantrolene (T8452) (F368) serves as a muscle relaxant and non-competitively inhibits human erythrocyte glutathione reductase (glutathione reductase), exhibiting Ki and IC50 values of 111.6 μM and 52.3 μM, respectively. Additionally, Dantrolene (T8452) acts as a ryanodine receptor antagonist and a stabilizer of Ca2+ signals. It is utilized in the treatment of muscle spasms and malignant hyperthermia.

N6022(IC50 of 8 nM) is an effective, reversible, and selective S-Nitrosoglutathione reductase(GSNOR) inhibitor.

3-Amino-1,2,4-triazole (Trapidil impurity B) is an inhibitor of catalase, capable of inducing the compensatory mechanism for hydrogen peroxide detoxification. This mechanism involves increasing the activities of glutathione peroxidase and glutathione reductase.

Trypanothione synthetase-IN-5 (compound 9) is an inhibitor of trypanothione reductase (TR), showing an IC50 of 20.5 μM against Leishmania infantum TR. It also exhibits inhibitory activity against human glutathione reductase (hGR), with an IC50 of 62.4 μM.

CS47 is a reversible inhibitor of thioredoxin reductase 1 (TrxR1). It activates stress-responsive glutathione (GSH) and iron regulatory pathways, leading to GSH depletion. This results in reactive oxygen species (ROS) accumulation, promoting HO-1 overexpression and causing intracellular iron overload, which ultimately induces ferroptosis in lung cancer not dependent on the KRAS gene. CS47 exhibits anticancer activity with low cytotoxicity to normal lung fibroblasts.

Ophthalmic acid is a ubiquitous metabolite and glutathione modulator with a Ki value of 0.95 mM for glyoxalase I. Ophthalmic acid competitively inhibits glyoxalase I, glutathione S-transferase, glutaredoxin, glutamate-cysteine ligase, protein disulfide reductase (glutathione), and non-selective cation channels. Ophthalmic acid is applicable to diabetes-related investigations and is particularly valuable for studies involving oxidative stress, glutathione metabolism, redox regulation, and metabolic dysfunction.

Glutathione can occur in reduced (GSH), oxidized (GSSG), or in mixed disulfide forms and is ubiquitous in multiple biological systems serving as the major thiol-disulfide redox buffer of the cell. GSSG is the oxidized form of GSH . It can be reduced back to GSH through the NADPH-dependent enzyme glutathione reductase. GSSG functions as a hydrogen acceptor in the enzymatic determination of NADP+ and NADPH and can be a proximal donor in S-glutathionylation post translational modifications. The ratio of reduced glutathione to oxidized glutathione within cells is often used as an indicator of oxidative stress, with higher concentrations of GSSG predicting increased oxidative stress.

(E)-Ajoene is a disulfide that has been found inA. sativumand has diverse biological activities.1,2,3,4It is active against Gram-positive and Gram-negative bacteria (MICs = 10-250 and 150->500 μg/ml, respectively) and fungi (MICs = 15-50 μg/ml).1(E)-Ajoene inhibits proliferation of a variety of cancer cells, including MDA-MB-231 breast, HeLa cervical, and WHCO1 esophageal cancer cells (IC50s = 18.6, 61, and 39.2 μM, respectively).2It also inhibits human glutathione reductase andT. cruzitrypanothione reductase when used at a concentration of 200 μM.3(E)-Ajoene (25 mg/kg) is neuroprotective in a gerbil model of ischemia-reperfusion injury, reducing reactive astrocytosis and microgliosis in the hippocampal CA1 region.4 1.Yoshida, H., Iwata, N., Katsuzaki, H., et al.Antimicrobial activity of a compound isolated from an oil-macerated garlic extractBiosci. Biotechnol. Biochem.62(5)1014-1017(1998) 2.Kaschula, C.H., Hunter, R., Hassan, H.T., et al.Anti-proliferation activity of synthetic ajoene analogues on cancer cell-linesAnticancer Agents Med. Chem.11(3)260-266(2011) 3.Gallwitz, H., Bonse, S., Martinez-Cruz, A., et al.Ajoene is an inhibitor and subversive substrate of human glutathione reductase and Trypanosoma cruzi trypanothione reductase: Crystallographic, kinetic, and spectroscopic studiesJ. Med. Chem.42(3)364-372(1999) 4.Yoo, D.Y., Kim, W., Nam, S.M., et al.Neuroprotective effects of Z-ajoene, an organosulfur compound derived from oil-macerated garlic, in the gerbil hippocampal CA1 region after transient forebrain ischemiaFood Chem. Toxicol.721-7(2014)

L-SelenoMethionine (L-(+)-Selenomethionine) is a naturally occurring amino acid. It promotes cell cycle progression and elevates the expression of the antioxidant enzymes thioredoxin reductase, glutathione reductase.

TRi-1 is irreversible inhibitor of cytosolic thioredoxin reductase 1 (TXNRD1), with an IC50 of 12 nM. TRi-1 has little mitochondrial toxicity for anticancer therapy

Hemustine is an inhibitor of human glutathione reductase and widely used as an anti-tumor agent.

Thioredoxin reductase peptide, corresponding to residues 53-67 in thioredoxin reductase (TrxR), is used in thioredoxin reductase research. Mammalian thioredoxin reductase (TR) catalyzes the reduction of the redox-active disulfide bond of thioredoxin (Trx) and is structurally and mechanistically similar to glutathione reductase, except for a C-terminal 16-amino acid extension containing a rare vicinal selenylsulfide bond.

Thioredoxin reductase peptide acetate corresponds to residues 53–67 in thioredoxin reductase (TrxR), used in thioredoxin reductase research.Mammalian thioredoxin reductase (TR) catalyzes the reduction of the redox-active disulfide bond of thioredoxin (Trx