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 effect of growth and fermentation conditions on the production of catalase by T. aurantiacus WSH 03-01 was investigated in shaking flasks. Catalase activity reached 1594 u/mL when the culture was grown on a complex carbon source containing 20 g/L dextrin and 1% (V/V) ethanol, which was 23% higher than the sum produced on 20 g/L dextrin and 1% (V/V) ethanol, respectively. It was concluded that dextrin might act as a major carbon source in the complex, while ethanol was rather a stimulator than a carbon source. The stimulation effect of ethanol on catalase production was postulated to be two aspects; catalase-dependent alcohol metabolism is activated by acute alcohol, thus more catalase need to be synthesized for that use, named direct induction. As for indirect induction, which may result from little amount of H2O2 generation in process of NADH regeneration in respiratory chain. Peptone was shown to be a favorable nitrogen source for catalase production and its optimum concentration was found to be 10 g/L. Catalase production by T. aurantiacus WSH 03-01 was further improved by optimizing the initial pH, volume of medium in flasks as well as the concentration of external H2O2. Under the optimum culture conditions, the activity of catalase reached 2762 u/mL, which was nearly 6.8 times higher than that of the initiate conditions. Furthermore, the potential application of this novel catalase in the treatment of textile bleaching effluents was evaluated. Thermo-and alkaline stability of this catalase was compared with the commercial available catalases produced from bovine and Aspergillus niger. The crude enzyme from T. aurantiacus WSH 03-01 showed stronger stabilities at (70 degrees C, 80 degrees C, 90 degrees C) and (pH 9.0, pH 10.0, pH 11.0) than the other two types of catalases, indicating a great application potential in the clean production process of textile industry.
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PMID:[Thermo-alkali-stable catalase from Thermoascus aurantiacus and its potential use in textile bleaching process]. 1597 17

The present work studies the effect of parachlorophenylalanine (PCPA, 200 mg/kg intraperitoneally/48 hr for 7 days) on the oxidative stress and nephropathy induced by gentamicin (80 mg/kg intraperitoneally/daily for 7 days) in Wistar rats. The effect of PCPA on lipid peroxidation products and reduced glutathione content in renal and brain tissue, as well as on 5HT content in brain was assessed. Catalase and superoxide dismutase activities were determined in brain tissue. Blood urea nitrogen and creatinine in plasma and total protein content in urine were also measured. Gentamicin caused significant increases in proteinuria, non-protein nitrogen compounds and lipid peroxidation markers, together with decreases in both reduced glutathione content in renal and brain tissue and enzymatic activities in brain homogenates. PCPA harnessed the effect of gentamicin in the brain and the kidney, while PCPA alone induced brain oxidative stress. These results support the prooxidant action of PCPA in brain tissue and its capacity to exacerbate the oxidative stress and renal dysfunction induced by gentamicin, as well as the possible antioxidant property of serotonin.
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PMID:Parachlorophenylalanine exacerbates oxidative stress induced by gentamicin in rats. 1612 12

In this study, we aimed to investigate the possible protective effect of resveratrol on gentamicin induced nephrotoxicity. Experiments were carried out in male Wistar rats weighing 200-250 g. Gentamicin sulfate (80 mg/kg per day i.p.), resveratrol (10 mg/kg per day i.p.) and gentamicin together with resveratrol were administered for 6 d. The animals were sacrificed 24 h after the last injection. Urine, blood samples and tissue samples were collected from the animals on the seventh day of the treatment before they were sacrificed. Kidneys were collected for histopathological studies and fixed in 10% buffered formalin solution. Tissue samples were stored at -70 degrees C in liquid nitrogen for the determination of glutathione (GSH), glutathione-S-transferase (GST), malondialdehyde (MDA) and catalase (CAT). Glutathione assay was determined by the method of Beutler et al. GST amounts were measured by the method of Habig et al. Catalase activity was tested by Aebi's method and MDA was determined according to Thayer's method. Blood urea level was significantly increased in the gentamicin treated group. The study showed lowered levels of urea and creatinine levels in resveratrol administered groups when compared with gentamicin administered rats, and the difference was statistically significant. It has been determined that resveratrol caused statistically significant decrease in lipid peroxidation and reduced the level of catalase. Histopathological examination showed that resveratrol prevented partly gentamicin induced tubular damage. The results histopathologically demonstrated that resveratrol has a protective effect against gentamicin induced nephrotoxicity, lipid peroxidation and cellular damage in rats.
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PMID:Gentamicin-induced nephrotoxicity in rats ameliorated and healing effects of resveratrol. 1720 64

Catalase (CAT) is an enzyme capable of catalyzing the conversion of H(2)O(2) to O(2) and H(2)O. It has recently acquired interest due to its attractive potential application in the textile industries. In a previous study, a bacterium with slight halophilic and alkaliphilic characteristics, Bacillus sp. F26, was isolated and found to produce high-level alkaline CAT. In the present study, the effects of culture conditions on the CAT production were investigated. The results showed that the highest activity of CAT (13.9 U/mg protein) was obtained when glucose (15 g/L) was used as carbon source. The utilization of the mixture of corn steep liquid and beef extract stimulated both bacterial growth and CAT synthesis. The highest biomass (4.5 g/L) and activity of CAT (16.5 U/mg protein) were found synchronously when 10 g/L corn steep liquid and 10 g/L beef extract were used as nitrogen source. The addition of H(2)O(2) as an oxidative stress was used to enhance CAT production in the flasks. It was found that the activity of CAT was increased by 51.3-22.8 U/mg protein compared with the control when 2 mmol/L H(2)O(2) was added at later exponential phases (16 h), although the cell growth was significantly inhibited. Based on the above, an exponential H(2)O(2) feed strategy was developed, in which the feed rate of H(2)O(2) was controlled according to specific cell growth rate (mu). In this way, the maximum CAT production (29.9 U/mL) was obtained, which was 92.8 and 20.7% higher than that in batch and constant rate fed-batch fermentation, respectively.
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PMID:Study and improvement of the conditions for production of a novel alkali stable catalase. 1721 59

It is well known that eosinophils are involved in tyrosine nitration. In this study, we evaluated tyrosine nitration by rat eosinophils isolated from peritoneal fluid and constituent eosinophils in the stomach. Rat peritoneal eosinophils activated with 1 microM phorbol myristate acetate (PMA) and 50 microM NO2- showed immunostaining for nitrotyrosine only in smaller cells, despite the fact that eosinophils are capable of producing superoxide (O2*-) Free tyrosine nitrating capacity after incubation with PMA and NO2- was 4-fold higher in eosinophils than in neutrophils. Catalase and alpha- and gamma-tocopherol inhibited free tyrosine nitration by reactive nitrogen species from eosinophils but not that by peroxynitrite. Superoxide dismutase augmented free tyrosine nitration by activated eosinophils and peroxynitrite. The concentration of nitric oxide released from eosinophils was relatively low (0.32 microM/10(6) cells/h) and did not contribute to the formation of nitrotyrosine. On the other hand, most constituent eosinophils constituent in the rat stomach stimulated by PMA and NO2- showed tyrosine nitration capacity. These results suggest that intact cells other than apoptotic-like eosinophils eluted in the intraperitoneal cavity could not generate reactive species responsible for nitration by a peroxidase-dependent mechanism. In contrast, normal eosinophils in the stomach were capable of nitration, suggesting that the characteristics of eosinophils in gastric mucosa are different from those eluted in the peritoneal cavity.
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PMID:Biochemical characterization of reactive nitrogen species by eosinophil peroxidase in tyrosine nitration. 1733 38

IFNgamma is a potent immunomodulator which plays important roles in host defense. IFNgamma modulates transcription of growth-related genes [N-myc downstream regulator 1, growth arrest and DNA damage inducible gamma and inhibitor of DNA binding 2 (Id2)], which is followed by increased growth suppression in the mouse hepatoma cell line, H6. Further studies revealed modulation of genes involved in oxidative and nitrosative stress (iNos, gp91phox and Catalase) and increased generation of reactive oxygen species (ROS) and reactive nitrogen intermediates (RNIs) upon IFNgamma treatment. High amounts of ROS and RNI are responsible for IFNgamma-mediated reduction in cell growth as this process is blocked, using either diphenylene iodonium (DPI), an inhibitor of flavin-containing NADPH oxidases, or N-methyl L-arginine (LNMA), an inhibitor of nitric oxide synthase. Based on studies with LNMA and DPI, IFNgamma-modulated genes can be categorized into two distinct sets: oxidative and nitrosative stress independent (transporter associated with antigen processing 2, Cd80, Lmp10 and Icosl) and oxidative and nitrosative stress dependent (iNos, gp91phox, Catalase and Id2). In addition, DPI or LNMA blocked IFNgamma-induced activation of Ras, demonstrating the involvement of oxidative and nitrosative stress. Manumycin A, a farnesyl transferase inhibitor, blocked Ras activation and reduced NADPH oxidase activity and ROS amounts leading to increased cell growth in the presence of IFNgamma. Notably, the IFNgamma-induced MHC class I levels are not modulated in cells treated with DPI, LNMA or manumycin A. Together, these results delineate the role of high amounts of ROS, RNI and Ras activation in modulating expression of some genes and, thereby, function by IFNgamma. The implications of these results during modulation of immune responses by IFNgamma are discussed.
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PMID:Involvement of oxidative and nitrosative stress in modulation of gene expression and functional responses by IFNgamma. 1760 79

COPD is associated with an increased load on the diaphragm. Since chronic muscle loading results in changes in antioxidant capacity and formation of reactive oxygen and reactive nitrogen species, we hypothesized that COPD has a similar effect on the diaphragm, which is related to the severity of COPD. Catalase activity was determined spectrophotometrically. Levels of 4-hydroxy-2-nonenal (HNE)-protein adducts and 3-nitrotyrosine (NT) formation were measured using western blotting. Levels of malondialdehyde (MDA) were assessed by high-performance liquid chromatography. We found that catalase activity was approximately 89% higher in the diaphragm of severe COPD patients (FEV1 37+/-5% predicted) compared with non-COPD patients. MDA levels, a marker for lipid peroxidation, were significantly lower in the diaphragm of COPD patients compared with non-COPD patients, whereas the level of HNE-protein adducts was equal in both groups. NT formation was not different between groups. However, increasing hyperinflation and NT formation were inversely correlated. These results indicate that in COPD the diaphragm adapts to a higher work load by increasing catalase activity, resulting in a reduction in oxidative damage to lipids and tyrosine nitration of proteins.
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PMID:Oxidative and nitrosative stress in the diaphragm of patients with COPD. 1804 94

In the current work, regulation of the pap1(+) gene was investigated by the use of the pap1(+)-lacZ fusion gene and semi-quantitative reverse transcriptase-PCR. The synthesis of beta-galactosidase from the pap1(+)-lacZ fusion gene was significantly enhanced by nitric oxide (NO)-generating sodium nitroprusside (SNP) and nitrogen starvation. However, the induction by SNP and nitrogen starvation was observed to be much less in the Pap1p-negative cells harboring the fusion gene. Exogenous NO was more effectively scavenged in the Pap1p-positive cells than in the Pap1p-negative cells. Oxidative stress such as superoxide anion, hydrogen peroxide and cadmium could not give rise to an effect on the synthesis of beta-galactosidase from the fusion gene. The pap1(+) mRNA level was elevated in the wild-type cells by SNP and nitrogen starvation. Catalase activity, a major enzyme positively regulated by Pap1p, was significantly increased only in the Pap1p-positive cells by SNP. In brief, it is demonstrated that transcription of the Schizosaccharomyces pombe pap1(+) gene is positively regulated by nitrosative and nutritional stress in a Pap1p-dependent manner.
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PMID:The pap1(+) gene of fission yeast is transcriptionally regulated by nitrosative and nutritional stress. 1824 28

This paper studied the effects of nitrogen application rate on the soil enzyme activities in the rhizosphere of wheat cultivars Lankaoaizao 8, a large spike genotype, and Yumai 49-198, a small spike genotype, under high yield condition. The results showed that the enzyme activities in rhizosphere soil had similar changing trends with wheat growth. The protease, urease and dehydrogenase activities in rhizosphere soil increased with wheat growth, maximized at heading stage, jointing stage, and heading stage, respectively, and decreased thereafter. Catalase activity increased with wheat growth, and peaked at maturing stage. At the same growth stage, the protease, catalase and dehydrogenase activities in rhizosphere soil of the two cultivars increased with increasing nitrogen application rate and peaked at 180 kg N x hm(-2). Urease activity also increased with increasing nitrogen application rate, and the maximum activity was observed at 360 kg N x hm(-2).
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PMID:[Effects of nitrogen application rate on soil enzyme activities in wheat rhizosphere]. 1841 81

Acute cold stress caused lesions of gastric mucosa as a result of its attack by active oxygen and nitrogen compounds. The tissue regeneration is regulated by a cascade of tyrosine protein kinases. Gastric ulceration leads to a decrease in activity of tyrosine protein kinases and phosphatases, following by fall in phosphotyrosine content in proteins of plasma membranes of gastric mucosa cells. No changes in superoxide dismutase activity, slight increase in catalase activity, inhibition of glutathione peroxydase, significant increase in OH* content and decrease in zinc level were observed in the gastric mucosa cells of stressed rats. That increased oxidative damage can lead to inactivation of protein tyrosine phosphatases. Nitric oxide synthase activity was three times higher in gastric mucosa cells after the cold stress. That can promote nitrosylation of tyrosine residues. During following days nitric oxide synthase activity remains high. Superoxide dismutase is activated on the 4 and 5th day after the stress. Catalase activity normalizes after second day. Tyrosine protein kinase activity increases in membranes with maximum on the 4th day, and remains inhibited in cytosole. Tyrosine protein phosphatases keep inhibited as well. Gluthatione peroxydase activity and zinc level decreased on the 5th day. Obtained results can be the evidence of violations in signal transduction through protein tyrosine kinase cascades, due to the reduction in tyrosine phosphorylation, as a result of increase in the content of active oxygen and nitrogen species.
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PMID:[Functioning of tyrosine protein kinases and phosphatases in gastric mucosa cells under conditions of oxidative and nitrosative stress in gastric lesions]. 1924 21


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