Disease relevance of GPX1

• Based on theoretical evidence, it has been proposed that HIV-1 may encode several selenoprotein modules, one of which (overlapping the env gp41-coding region) has highly significant sequence similarity to the mammalian selenoprotein glutathione peroxidase (GPx; EC ) [1].
• RESULTS--In group B, a 15-minute cardiac arrest induced an increase in MDA, a significant reduction of GSH, and no change in SOD and GSH-PX activities compared with group A. In group C, there were further increases in MDA and reductions in GSH content and GSH-PX activity compared with group A; SOD activity remained substantially unchanged [2].
• Ebselen, a seleno-organic compound which inhibits arachidonic acid lipoxygenase activity and exerts glutathione peroxidase-like activity, ameliorated delayed cerebral vasospasm in a canine two-hemorrhage model [3].
• After a single low dose (2-3 mg/kg body weight), GR and GSH Px activities were reduced [4].
• The activities of G-6-PDH, GR and GSH Px correlated with the total paraquat dose and with the extent of pulmonary fibrosis measured with an electronic image analyzer [4].

High impact information on GPX1

• No differences were present in total glutathione, thiobarbituric acid reactivity, or superoxide dismutase and glutathione peroxidase activity in the ischemic zones of the two groups [5].
• Biopsies were taken from the ischemic and nonischemic zones to determine levels of total glutathione, superoxide dismutase and glutathione peroxidase activity, and reactivity to thiobarbituric acid, an index of lipid peroxidation [5].
• The agents studied were diamide (which nonenzymatically oxidizes GSH to GSSG), tert-butyl hydroperoxide (an organic peroxide specifically reduced by glutathione peroxidase, thereby generating GSSG for GSH), and 1,3-bis(2-chloroethyl)-1-nitrosourea (an inhibitor of NADPH:GSSG reductase, which presumably allows the accumulation of GSSG) [6].
• After radiation, however, the activity of xanthine oxidase, superoxide dismutase, and glutathione peroxidase were significantly (p < 0.002) higher in the intestine of dogs fed elemental diet without the added glutamine [7].
• The sample was assayed for tissue malondialdehyde (MDA), the content of reduced glutathione (GSH), and the activities of superoxide dismutase (SOD) and glutathione peroxidase (GSH-PX) [2].

Chemical compound and disease context of GPX1

• AIMS: To determine the effects of L-arginine on the central organ injury due to severe hemorrhagic shock and reinfusion and the relationship among endogenous antioxidants, superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GSH-Px) in dogs [8].

Biological context of GPX1

• Oxidative stress was measured by determining GSH/GSSG ratios and gene-expression (SOD1, CAT, GSHS, GPX1, CCS, p27KIP, Bcl-2) [9].
• Daunorubicin (15 mg/kg) or placebo (normal saline) was administered by iv bolus to New Zealand white rabbits and 3 to 4 days later, hearts were removed to measure contractility (dF/dt), concentrations of daunorubicin and daunorubicinol, and evidence of oxidative stress on glutathione and glutathione peroxidase [10].
• The Di29 nucleotide and deduced amino acid sequences were very similar to those described for lymphatic filariae and predicted a secreted form of glutathione peroxidase with a cysteine residue substituted for selenocysteine in the active site [11].
• A cDNA clone, Di29, encoding a homolog of glutathione peroxidase, was isolated from a Dirofilaria immitis adult female cDNA expression library by a combination of polymerase chain reaction amplification with primers designed from the Brugia pahangi glutathione peroxidase gene sequence and hybridization screening of D. immitis cDNA libraries [11].

Anatomical context of GPX1

• No significant changes were detected in activities of catalase, superoxide dismutase or glutathione peroxidase in erythrocytes or myocardial tissue from control and adriamycin-treated animals [12].
• Among the three species considered, sheep presented the lowest plasmatic GSH and the highest lymphocyte GSHPx activity [13].
• Expression of GSH-PO was recognized in the foamy cytoplasm of macrophages and smooth muscle cells in the early and advanced atherosclerotic lesions [14].
• Tissue samples from liver, kidney and small intestines were taken for histological studies and liver samples were also taken for the mesurement of SOD, CAT, GSH-Px tissue levels [8].
• Activities of glutathione peroxidase and reductase were significantly higher and lower, respectively, in the ischemic myocardium than those of the nonischemic myocardium immediately after repetitive brief ischemia, but no differences between these regions were seen in activities after 3 or 24 h [15].

Associations of GPX1 with chemical compounds

• In the arterial wall, there was a slight decrease in the activity of SOD, a significant decrease in the activity of GSH-px (p less than 0.01), and also a significant decrease in the concentration of glutathione (p less than 0.01) up to the eighth day following SAH [16].
• Prevention of volume overload-induced decrease in myocardial contractility by vitamin E was associated with a decrease in cardiac MDA and an increase in cardiac antioxidant reserve and glutathione peroxidase activity towards control levels [17].
• Litter effects were observed for VE, Cu, UA, and Gpx [18].
• Aging was associated with decreased RP, VA, VE, Se, and Cu and with increased RT, Cp, and Gpx [18].
• Activities of the detoxifying enzymes catalase and glutathione peroxidase I in prostate were increased by estradiol-17 beta treatment, whereas in kidney or liver they were not affected or changed to a lesser degree than observed in prostate [19].

Other interactions of GPX1

• Activities of superoxide dismutase, catalase, and glutathione peroxidase was not decreased in HF [20].
• The enzymes include the glutathione biosynthesis system consisting of gamma-glutamylcysteine synthetase and glutathione synthetase, as well as glutathione peroxidase, glutathione reductase and glutathione-S-transferase [21].

Analytical, diagnostic and therapeutic context of GPX1

• Dirofilaria immitis: molecular cloning and expression of a cDNA encoding a selenium-independent secreted glutathione peroxidase [11].
• We used immunohistochemistry to localize canine Apolipoprotein B-100 (CApoB-100) and glutathione peroxidase (GSH-PO) in canine atherosclerotic lesions [14].
• Blood samples were taken for the measurement of blood urea nitrogen (BUN), creatinine, aspartate aminotransferase (AST), alanine aminotransferase (ALT), lactate dehydrogenase (LDH), intraerythrocytic SOD, CAT, GSH-Px, and serum nitrite and nitrate levels [8].

References