Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P04040 (Catalase)
 3,577 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The ability of aurothioglucose and D(-)-penicillamine hydrochloride to inhibit selenium-dependent glutathione peroxidase (SeGSH-Px) in vitro and to increase exudative diathesis in vitamin E-deficient chickens was studied. Aurothioglucose and penicillamine competitively inhibited SeGSH-Px in inverse proportion to the concentration of hydrogen peroxide and reduced glutathione, respectively, in chick liver postmitochondrial supernatant assay preparations. Neither drug inhibited glutathione reductase or superoxide dismutase at the concentrations tested; however, both inhibited catalase in a semilogarithmic fashion. This was true for both the purified bovine enzyme and chick liver homogenate. Aurothioglucose and penicillamine injected subcutaneously at the back of the neck increased exudative diathesis in vitamin E-deficient chickens fed 0.1 ppm Se, and effectively overcame the protective effect of selenium 72 h after injection in chicks fed vitamin E-free, low selenium diets supplemented with 0.0-0.1 ppm Se. Assays of plasma and of liver, lung and kidney postmitochondrial supernatants indicated that all observed reductions in SeGSH-Px activity preceded increases in exudative diathesis. Plasma and liver SeGSH-Px activities were lower at early times (6-24 h) after treatment with high doses of either drug. Lung SeGSH-Px activities were only lower in chicks receiving 240 mg penicillamine/kg 6 h after treatment; kidney SeGSH-Px activities were only lower in chicks treated with the highest dose of aurothioglucose 48 h after treatment. Brain SeGSH-Px activities were unaffected by drug treatment and the heart had higher SeGSH-Px activities only at 6 h after treatment with the highest dose of either drug compared to saline controls. Catalase activities in liver homogenates were only significantly altered by penicillamine; the highest dose caused the activity to be higher than that in saline-treated chicks. The cause of the lower SeGSH-Px activities could be either lower enzyme concentrations in tissues of the drug-treated groups and/or direct inhibition. Whatever the mechanism, it is concluded that exudative diathesis can be used to determine which drugs reduce SeGSH-Px activity in the chick.
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PMID:Drug-induced changes in selenium-dependent glutathione peroxidase activity in the chick. 393 15

The ability to grow a clone of the cell line, MLA144, which is a constitutive producer of interleukin 2 (IL-2), in serum-free medium permitted the study of the direct effect of various agents on cell growth and IL-2 production in a homogeneous population. Bovine serum albumin (BSA) at 4 mg/ml was optimal for cell growth and IL-2 production. Selenium at 10 ng/ml enhanced IL-2 production nearly twofold and lithium at 42 ng/ml also enhanced IL-2 production by nearly twofold. Neither compound at these levels altered cellular proliferation. Two other compounds, iron and zinc, known to be associated with cellular proliferation and/or immunoregulation did not alter IL-2 production. Catalase or horseradish peroxidase was able to substitute for BSA and maintain the long-term growth of the MLA144 clone with only a 30% decrease in the rate of cellular proliferation and a 50% decrease in IL-2 production compared to cells maintained in the serum-free formulation with BSA. Addition of 0.5 mg of BSA to the catalase serum-free formulation increased the production of IL-2 to 70% of that of cells cultured in the BSA-containing serum-free formulation. The catalase-containing serum-free formulation has the advantage of consisting of only three proteins, catalase, insulin, and transferrin, at a very low protein content. The catalase-containing serum-free medium also supported the long-term growth of a human T-cell line, HSB-2.
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PMID:Modulation of interleukin 2 release from a primate lymphoid cell line in serum-free and serum-containing media. 393 31

The trace element selenium is known to be a part of the enzyme glutathione peroxidase (glutathione-hydrogen peroxide oxidoreductase, E.C.1.11.1.9). Studies have shown that selenium in the enzyme exists in at least two forms or oxidation states. It is probable that selenium has been incorporated into the enzyme as the selenocysteine amino acid. In the present study, the Raman spectra of selenocystine and selenomethionine have been obtained, structural assignments have been verified, and the behavior of the two selenoamino acids have been monitored under varying conditions of oxidative stress. The assignments will assist in the interpretation of the spectrum of the actual enzyme.
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PMID:The Raman spectra of selenomethionine and selenocystine. 645 62

Our previous studies have demonstrated a decreased glutathione feroxidase (GSH-Px) activity of erythrocytes and leucocytes from multiple sclerosis (MS) patients. In the present communication these activities were compared with the activities of associated enzymes (glutathione reductase (GSSG-RD), glucose-6-phosphate dehydrogenase (G-6-PD) and catalase). All enzymic activities were compared between MS patients, other neurologic patients (ON patients) and normal control individuals. Compared to data of ON patients and normal controls, in MS the ratio of GSHPx/GSSGRD in lympho- and granulocytes was significantly decreased (2 alpha less than or equal to 0.05) by 35% and 51%, respectively. The significant correlation between GSSG-RD and the GSH-Px activity (2 alpha less than or equal to 0.05, r = 0.501) found in control lymphocytes was not present in MS lymphocytes. However, the lymphocyte GSH-Px activities of controls as well as of MS correlated with the corresponding serum selenium levels (2 alpha less than or equal to 0.05, r = 0.594 and 2 alpha less than or equal to 0.01, r = 0.967, respectively). The G-6-PD activity was insignificantly increased by 41% in MS lymphocytes compared to normal control. Catalase activity was unchanged in lymphocytes but decreased 50% in MS granulocytes compared to normal control. No significant differences were found between MS and the ON group. The catalase activity of MS erythrocytes was increased by 63% (2 alpha less than or equal to 0.05) in comparison with both the normal control and ON data.
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PMID:Glutathione peroxidase and reductase, glucose-6-phosphate dehydrogenase and catalase activities in multiple sclerosis. 669 53

The effects of dietary vitamin E and selenium on the oxidant defense system (glutathione peroxidase, catalase, glutathione reductase, reduced glutathione, and superoxide dismutase) were investigated in the chick. Two-week-old chicks were reared using a vitamin E-free, low-selenium, semipurified basal diet alone or supplemental with vitamin E (100 IU/kg) and/or selenium (.10 ppm). Whereas vitamin E sustained chick growth, survival, and protection from exudative diathesis (ED), it did not significantly affect the enzymatic components of the oxidant defense system. Dietary selenium promoted chick growth and protection against ED in the absence of vitamin E and sustained glutathione peroxidase activity in several tissues. The latter effect was associated with decreases in reduced glutathione concentrations observed in liver and blood. Catalase and superoxide dismutase activities were increased in liver and brain in selenium deficiency. Glutathione reductase activities in liver, kidney, lung, and brain were not affected by diet.
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PMID:Influences of dietary vitamin E and selenium on the oxidant defense system of the chick. 732 95

Murine L1210 and human HL-60 leukemia cells grown for 5-7 days in medium containing 1% serum without selenium supplementation [Se(-) cells] were severely depressed in selenoperoxidase (SePX) activity relative to selenium-supplemented controls [Se(+) cells]. Catalase (CAT) activity in Se(-) cells was unaffected up to this point, but thereafter began to increase. Two manifestations of this increase have been differentiated for both cell lines: (a) short-term induction of CAT (up to approx. twofold) after 2-3 weeks, followed by (b) long-term selection for cells that irreversibly express much higher levels of CAT, e.g., > 100 times (L1210) and > 10 times (HL-60) the levels observed in Se(+) controls after approximately 20 weeks. Although superoxide dismutase, glutathione S-transferase, and glucose-6-P dehydrogenase activities were unchanged in Se(-) cells, GSH levels were elevated by 50-100%; like short-term CAT elevation, this could be reversed by supplying Se. Short-term Se(-) cells were more sensitive to H2O2-induced killing than Se(+) cells, evidently because SePX activity was important for peroxide detoxification. However, long-term Se(-) cells were markedly more resistant to H2O2 than Se(+) counterparts, consistent with the much higher levels of CAT in the former. Southern blot analysis revealed that the copy number of CAT DNA in a clone of long-term Se(-) L1210 cells was four- to fivefold greater than that in an Se(+) clone. Northern blot analysis of RNA from the same Se(-) clone showed a CAT mRNA level that was at least 40 times higher than that of the Se(+) control. Similar trends were observed for HL-60 cells. These results suggest that elevated CAT during long-term Se deprivation is a reflection of amplification and greater transcription of the CAT gene.
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PMID:Amplification and hyperexpression of the catalase gene in selenoperoxidase-deficient leukemia cells. 787 6

We have characterized the effect of angiotensin converting enzyme (ACE) inhibitors on the activity of CuZn-superoxide dismutase (CuZn-SOD), Mn-superoxide dismutase (Mn-SOD), catalase, and selenium-dependent glutathione peroxidase (Se-GPx). CF1 mice (4-month-old females) were administered water containing enalapril (20 mg/l) or captopril (50 mg/l), during 4 to 11 weeks. After 11 weeks, enalapril treatment caused an increase in the activity of CuZn-SOD, Mn-SOD and Se-GPx, from 19 +/- 4 to 46 +/- 7, 2.1 +/- 0.2 to 3.8 +/- 0.2 units/mg protein and 27 +/- 3 to 54 +/- 3 milliunits/mg protein, respectively. After 11 weeks, captopril treatment increased the activities (P < 0.05) of CuZn-SOD, MnSOD and Se-GPx to 35 +/- 4, 2.9 +/- 0.2 units/mg protein, and 38 +/- 2 milliunits/mg protein, respectively. Catalase activity was not affected by the treatments. These results suggest that ACE inhibitors may protect cell components from oxidative damage by increasing the enzymatic antioxidant defenses.
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PMID:Superoxide dismutase and glutathione peroxidase activities are increased by enalapril and captopril in mouse liver. 789 34

It is well known that reperfusion damage of ischemic myocardium may be attributed to alterations in the antioxidant defense system against free radical aggression. In addition, the degree of myocardial damage may depend on the duration and severity of ischemia that precedes reperfusion. We carried out serial ischemic experiments (10, 30, 60 and 120 min) in ex-vivo rat hearts followed by 30 min reperfusion and we assayed the glutathione-dependent enzymatic activities (selenium-dependent glutathione-peroxidase: GSH-Px; selenium-independent glutathione peroxidase: GST-Px; glutathione-transferase: GST and glutathione-reductase: GS-SG-Red), Catalase activity (CAT) and non-proteic thiol compounds (NP-SH) at the end of reperfusion. We found a significant reduction of NP-SH, GSH-Px and CAT in ischemic/reperfused hearts from 30 min on, while GST activity was increased. In addition, we observed the appearance of a selenium-independent glutathione peroxidase activity (GST-Px) belonging to the GST system. In conclusion, we found the longer the duration of ischemia the greater the inbalance between the myocardial antioxidant system especially the GST activation, suggesting in particular for GST-Px, a role in the control of the damage against oxygen toxicity during ischemia/reperfusion.
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PMID:Myocardial antioxidant defense mechanisms: time related changes after reperfusion of the ischemic rat heart. 801 40

The role of oxidative stress in mercuric chloride (HgCl2)-induced nephrotoxicity is uncertain and controversial. We demonstrate that I.L.C-PK1 cells, exposed to HgCl2, generate massive amounts of hydrogen peroxide, the latter completely quenched by the hydrogen peroxide scavenger, pyruvate. HgCl2 exerts a dose-dependent cytotoxicity which is attenuated by pyruvate and catalase. Cellular generation of hydrogen peroxide arises, at least in part, from mitochondria since mitochondrial rates of generation of hydrogen peroxide increase in response to HgCl2; HgCl2 also provokes a shift in absorbance spectra in rhodamine 123 loaded-mitochondria and stimulates mitochondrial state 4 respiration. HgCl2, applied for one hour, impairs cellular vitality as demonstrated by the MTT assay, an assay dependent in part on mitochondrial function. HgCl2 impairs function in other organelles such as lysosomes that maintain a transmembrane proton gradient; these latter effects are partially attenuated by pyruvate. We complement these in vitro findings with in vivo evidence demonstrating that HgCl2 stimulates renal generation of hydrogen peroxide. The functional significance of such generation of hydrogen peroxide was evaluated in rats deficient in selenium and vitamin E, a nutrient deficiency that impairs the scavenging of hydrogen peroxide and promotes the toxicity of this oxidant. In these rats serum creatinine values were significantly higher on sequential days following the administration of HgCl2. To probe the renal response to oxidative stress induced by HgCl2, we examined hydrogen peroxide-scavenging enzymes and redox-sensitive genes. Catalase activity was unaltered whereas glutathione peroxidase activity was decreased, effects that may contribute to the net renal generation of hydrogen peroxide. The redox sensitive enzyme, heme oxygenase, was markedly up-regulated in the kidney in response to HgCl2. HgCl2 also induced members of the bcl family, bcl2 and bclx, genes that protect against apoptosis and oxidant injury. In another model of oxidant-induced renal injury, the glycerol model, bcl2 mRNA was not induced at 6 and 24 hours after the administration of glycerol. In summary, we demonstrate that HgCl2 potently stimulates renal generation of hydrogen peroxide in vitro and in vivo and such generation of peroxide contributes to renal dysfunction in vitro and in vivo. We also demonstrate that in response to HgCl2, redox sensitive genes are expressed including heme oxygenase and members of the bcl family.
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PMID:Renal oxidant injury and oxidant response induced by mercury. 887 81

Free radical metabolism can be altered by several interventions, including dietary restriction (DR) and exercise. Most of the previous work has focused on the liver and skeletal muscle. The following experiments were performed to determine whether long-term DR and chronic exercise affect free radical metabolism and change the status of the antioxidant defenses of the heart. Rats were subjected to DR and/or endurance exercise for 18.5 months and were sacrificed along with their ad lib fed and sedentary controls. Both DR and exercise decreased the malondialdehyde content of cardiac mitochondria, indicating a decrease in lipid peroxidation damage. The antioxidant enzymes in the cytosol, superoxide dismutase, selenium dependent glutathione peroxidase, and glutathione S-transferase were all increased by DR. Catalase activity was unaffected by DR but was increased by exercise. The following results demonstrate that long-term DR and exercise modulate the extent of free radical damage in the heart and enhance the antioxidant defense system.
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PMID:Exercise and diet modulate cardiac lipid peroxidation and antioxidant defenses. 890 82


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