Disease relevance of GSR

• Both low (33 mg/kg) and very high (13,200 mg/kg) levels of vitamin C decreased body weight, glutathione reductase, and unsaturation of fatty acids in membrane lipids [1].
• Isolated ventricular premature beats and runs of slow ventricular rhythm with H(2)O(2) more frequently occurred in HF compared to SHAM despite an increased antioxidant capacity including Cu/Zn and Mn superoxide dismutase, catalase, glutathione reductase, and glutathione peroxidase [2].
• It is concluded that the newborn piglet is less susceptible to oxygen-induced lung injury compared to adults of other species, and the increase in the lung complement of SOD, GR, GP and GSH may contribute to the apparent resistance to oxygen toxicity [3].
• A reduced activity of glutathione reductase, indicating a riboflavin deficiency, was observed only when the low protein diet was additionally deprived of a vitamin-mineral premix containing a fodder B2 preparation [4].

High impact information on GSR

• The polypeptide chain folding near the FAD binding site is different from those observed in other flavoproteins, such as glutathione reductase and glycolate oxidase [5].
• These Fe(III) complexes were enzymatically reduced also by other flavoenzymes, namely glutathione reductase (EC 1.6.4.2), cytochrome c reductase (EC 1.6.99.3), and cytochrome P450 reductase (EC 1.6.2.4) with somewhat lower efficacy [6].
• Further supplementation with 13,200 mg vitamin C/kg also reduced protein and lipid peroxidation, but decreased hepatic glutathione reductase and uric acid and resulted in a lower body weight of the animals [1].
• Erythrocyte GPx, GST, GRd activities and GSH levels significantly reduced in experimental OME guinea pigs when compared with the control and melatonin-treated animals [7].
• Trivalent arsenic compounds increased intracellular oxidized glutathione (GSSG) and total glutathione (GSH) and cellular glutathione peroxidase (cGPX) and glutathione S-transferase (GST) activity, but not glutathione reductase activity [8].

Chemical compound and disease context of GSR

• Activities of glutathione peroxidase (GPX) and glutathione reductase (GR) were enhanced in co-administered group. gamma-Glutamyl transpeptidase (GGT), a marker enzyme of alcohol induced toxicity, was also reduced, as was the glutathione content [9].

Biological context of GSR

• The concurrent development of glucose-6-phosphate dehydrogenase, glutathione reductase, and glutathione peroxidase during 45-60 days of gestation indicates an increased ability of the fetal brain to detoxify lipid peroxidation products by reinforcing the glutathione system [10].

Anatomical context of GSR

• These results are consistent with the view that the activity of the enzyme glutathione reductase, though not primarily related to pigmentation, plays an important role in the regulation and control of the biosynthetic activity of melanocytes leading to various types of melanin pigments [11].
• NAD(P)H oxidation rates in intact mitochondria did not correlate consistently with glutathione reductase and peroxidase activities in sonicated mitochondria suggesting in situ regulation by other endogenous factors [12].
• Compared to whole testicular homogenates, Leydig cells contained significantly (P < 0.01) less G-6-PDH, total SOD, glutathione reductase and total glutathione, but significantly (P < 0.001) more glutathione peroxidase [13].
• Whereas glutathione reductase activity declined in the cerebral cortex and hypothalamus [14].
• Glutathione reductase (GRd) activity declined in cerebral cortex and hypothalamus in the cytosolic fractions and only in cerebellum in the mitochondrial fraction [15].

Associations of GSR with chemical compounds

• Evidence for the postulated role of glutathione reductase in melanin pigmentation has been obtained by determinations of the glutathione concentrations in Tortoiseshell guinea pig skin of different colors (black, yellow, red, and white) [11].
• The sign reversal is also present in a closely related disulfide enzyme, glutathione reductase, but absent in glucose oxidase [16].
• In addition, non-protein thiols and glutathione reductase (GRD; E.C.1.6.4.2) were examined in the same manner [17].
• The assayed nitrofuran compounds did not inhibit LADH lipoamide reductase activity, at variance with their action on glutathione reductase (Grinblat et al., Biochem Pharmacol 38: 767-772, 1989) [18].
• The positions of bands II, IX, and X are nearly identical to those in the flavoprotein glutathione reductase; x-ray structural investigations on this enzyme indicate that there is extensive hydrogen bonding between FAD and protein in this molecule [19].

Other interactions of GSR

• The concentrations of glutathione and alpha-tocopherol and the activities of glutathione reductase and catalase were elevated in the urinary bladders of the animals exposed to the fern [20].
• Aortic cholesterol concentration and glutathione reductase activity were important factors in the advancement of severe plaque formation [21].
• The antioxidative enzymes, superoxide dismutase, catalase, glutathione peroxidase and glutathione reductase, increased during the first 10 days of neonatal growth and then levelled off [22].
• In the system containing MV or FAD, other one-electron reducing flavoenzymes such as nicotinamide adenine dinucleotide (reduced form) (NADH) dehydrogenase, lipoamide dehydrogenase and glutathione reductase with an appropriate electron donor, could replace XO [23].

Analytical, diagnostic and therapeutic context of GSR

• Circular dichroism studies of glutathione reductase [24].
• The MALDI spectra indicate the presence of 5'-nucleotidase, phosphatase, kinase, glutathione reductase, and renin activities in the kidney protein extract [25].
• Purification of glutathione reductase from porcine erythrocytes by the use of affinity chromatography on 2', 5'-ADP-Sepharose 4B and crystallization of the enzyme [26].
• The results of our studies indicated the stimulation of a number of antioxidative enzymes, including Mn-superoxide dismutase (Mn-SOD), catalase, glutathione peroxidase, and glutathione reductase, after repeated stunning and reperfusion [27].

References