Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.17.3.2 (xanthine oxidase)
8,383 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects of dehydroepiandrosterone sulfate (DHEAS) on mimetic aging action of cultured neurons were studied in two models: the cultured cerebral cortex neurons were exposed to the xanthine oxidase-hypoxanthine(XO-HPX) system; serum free culture of cerebral cortex neurons. The results indicated that when cultured neurons were incubated for 6 h with XO-HPX system or 24 h serum free cultures, LDH release and MDA content increased while the number of surviving neurons decreased. The activities of superoxide dismutase (SOD) and glutathione peroxidase (GSH-Px) decreased and morphological injury developed. DHEAS (25, 50, 100 micrograms.L-1) concentration-dependently increased the number of surviving neurons and the activities of SOD and GSH-Px. It also inhibited the elevation of LDH and MDA induced by free radical and serum free cultures. The results suggest that DHEAS prevent the toxicity of free radical and serum free culture insults by suppressing the generation of lipid peroxide and increasing the activities of antioxidant enzymes.
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PMID:[Effects of dehydroepiandrosterone sulfate on mimetic aging actions of cerebral cortex of fetal rats in vitro]. 1201 9

The protective action of zinc compounds in Crohn's disease-like inflammatory bowel disease in animals has been shown. A similar action of zinc sulfate on ulcerative colitis has not been defined. The present study aimed to delineate the protective action of zinc sulfate and the pathogenic mechanisms of 2,4-dinitrobenzene sulfonic acid (DNBS)-induced ulcerative colitis in rats. Zinc sulfate at different concentrations was given either orally (p.o.) or rectally (p.r.) to rats at 42, 48, 66 and 72 h following the induction of colonic inflammation by DNBS. Rats were killed 96 h after instillation of DNBS rectally to assess the severity of colonic damage, myeloperoxidase and xanthine oxidase activities. The involvement of mast cell degranulation and histamine release in the pathogenesis of DNBS-induced colitis was determined by using a mast cell stabilizer (ketotifen) and histamine receptor blockers (terfenadine and ranitidine). DNBS given rectally produced inflammation and ulceration in rats with a pathology resembling ulcerative colitis. Myeloperoxidase activity but not xanthine oxidase activity was sharply increased by this agent. Intrarectal administration of zinc solution and parenteral injection of histamine blockers significantly reduced tissue damage and myeloperoxidase but not xanthine oxidase activity. Ketotifen, a mast cell stabilizer, also significantly decreased mucosal injury and myeloperoxidase activity in the colon. In conclusion, mast cell degranulation followed by histamine release plays an important role in the pathogenesis of DNBS-induced ulcerative colitis. Zinc given rectally has a therapeutic effect against this colitis model, perhaps through the reduction of inflammation and inhibition of the above pathogenic mechanisms.
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PMID:Delineation of the protective action of zinc sulfate on ulcerative colitis in rats. 1204 10

The iron chelator deferoxamine has been reported to inhibit both xanthine oxidase (XO) and xanthine dehydrogenase activity, but the relationship of this effect to the availability of iron in the cellular and tissue environment remains unexplored. XO and total xanthine oxidoreductase activity in cultured V79 cells was increased with exposure to ferric ammonium sulfate and inhibited by deferoxamine. Lung XO and total xanthine oxidoreductase activities were reduced in rats fed an iron-depleted diet and increased in rats supplemented with iron, without change in the ratio of XO to total oxidoreductase. Intratracheal injection of an iron salt or silica-iron, but not aluminum salts or silica-zinc, significantly increased rat lung XO and total xanthine oxidoreductase activities, immunoreactive xanthine oxidoreductase, and the concentration of urate in bronchoalveolar fluid. These results suggest the possibility that the production of uric acid, a major chelator of iron in extracellular fluid, is directly influenced by iron-mediated regulation of the expression and/or activity of its enzymatic source, xanthine oxidase.
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PMID:Iron regulates xanthine oxidase activity in the lung. 1216 76

An active glycoprotein fraction containing 58 % protein was isolated from Aloe vera gel by precipitation with 55 % ammonium sulfate followed by gel permeation using DEAE-Sephacel A-25, Sepharose 6B and Sephadex G-50 columns in a yield of 3 x 10 -3 %. The glycoprotein fraction showed a single band corresponding to a subunit of verectin at the same position when stained with both Coomassie brilliant blue and periodic acid-Schiff reagents on 18 % SDS-PAGE. The molecular weight (14 kDa) was confirmed by Sephadex G-50 column chromatography. The glycoprotein fraction showed a radical scavenging activity against superoxide anion generated by the xanthine-xanthine oxidase system as well as inhibition of cyclooxygenase-2 and reduction of thromboxane A 2 synthase level in vitro.
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PMID:Radical scavenging glycoprotein inhibiting cyclooxygenase-2 and thromboxane A2 synthase from aloe vera gel. 1267 34

Previous studies demonstrated that the polyanion dextran sulfate (DS) protects rat coronary and porcine aortic endothelium (PAE) from oxygen-derived free radical (OFR) injury due to hydrogen peroxide (H2O2) or xanthine/xanthine oxidase (X/XO). To determine if DS has a similar protective effect in bovine aortic endothelium (BAE) and bovine brain microvascular endothelium (BBME), H2O2 or X/XO was added to confluent cultures. Cell injury was assessed 1 d later by measuring the percentage of viable cells (by trypan blue exclusion) and the release of lactate dehydrogenase (LDH) into the medium. After H2O2 doses of 6.0 mM for BAE and BBME and 0.8 mM for PAE, and after X doses of 10 microM and XO doses of 0.3 U/mL for all cell types, approximately 50% of cells were viable. Cultures were pretreated with DS (0.001 to 500 microg/mL) 24 to 26 h prior to H2O2 or X/XO exposure. Pretreatment at concentrations of 0.5, 5, and 50 microg/mL significantly increased the percentage of viable cells and reduced LDH release in cultures of PAE, but not BAE or BBME, treated with H2O2. Similarly, pretreatment with DS concentrations of 5 and 50 microg/mL significantly increased the percentage of viable cells and reduced LDH release in cultures of PAE, but not BAE or BBME, treated with X/XO. Thus, DS protected porcine but not bovine endothelium. Catalase (10 U/mL) increased the percentage of viable cells and reduced LDH release in H2O2-treated BAE and BBME, suggesting that DS likely acts by a different mechanism and does not neutralize H2O2. These results suggest that the protective effect of DS on OFR-injured endothelium is species-dependent.
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PMID:Dextran sulfate protects porcine but not bovine cultured endothelial cells from free radical injury. 1276 Apr 71

The objective of this study was to examine the influence of reactive oxygen species (ROS) on equine sperm capacitation. Motile equine spermatozoa were separated on a discontinuous Percoll gradient, resuspended at 10 x 10(6)ml in Tyrode's medium supplemented with BSA (0.5%) and polyvinyl alcohol (0.5%) and incubated at 39 degrees C for 2h with or without the xanthine (X; 0.1mM)-xanthine oxidase (XO; 0.01 U/ml) system or NADPH (0.25 mM). The importance of hydrogen peroxide or superoxide for capacitation was determined by the addition of catalase (CAT; 150 U/ml) or superoxide dismutase (SOD; 150 U/ml), respectively. Following incubation, acrosomal exocytosis was induced by a 5 min incubation at 39 degrees C with progesterone (3.18 microM), and sperm viability and acrosomal integrity were then determined by staining with Hoechst 33258 and fluoroisothiocyanate-conjugated Pisum sativum agglutin. To examine tyrosine phosphorylation, treatments were subjected to sodium dodecyl sulfate-polyacrylaminde gel electrophoresis (SDS-PAGE) followed by Western blot analysis with the anti-phosphotyrosine antibody (alpha-PY; clone 4G10). Capacitation with the X-XO system or NADPH led to a significant (P<0.0001) increase in live acrosome-reacted spermatozoa compared to controls. The addition of CAT or SOD prevented the increase in live acrosome-reacted spermatozoa associated with X-XO treatment. Incubation with the X-XO system was also associated with a significant (P<0.005) increase in tyrosine phosphorylation when compared to controls, which could be prevented by the addition of CAT but not SOD. This study indicates that ROS can promote equine sperm capacitation and tyrosine phosphorylation, suggesting a physiological role for ROS generation by equine spermatozoa.
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PMID:Reactive oxygen species promote tyrosine phosphorylation and capacitation in equine spermatozoa. 1451 78

We report the characterization of the molecular properties and EPR studies of a new formate dehydrogenase (FDH) from the sulfate-reducing organism Desulfovibrio alaskensis NCIMB 13491. FDHs are enzymes that catalyze the two-electron oxidation of formate to carbon dioxide in several aerobic and anaerobic organisms. D. alaskensis FDH is a heterodimeric protein with a molecular weight of 126+/-2 kDa composed of two subunits, alpha=93+/-3 kDa and beta=32+/-2 kDa, which contains 6+/-1 Fe/molecule, 0.4+/-0.1 Mo/molecule, 0.3+/-0.1 W/molecule, and 1.3+/-0.1 guanine monophosphate nucleotides. The UV-vis absorption spectrum of D. alaskensis FDH is typical of an iron-sulfur protein with a broad band around 400 nm. Variable-temperature EPR studies performed on reduced samples of D. alaskensis FDH showed the presence of signals associated with the different paramagnetic centers of D. alaskensis FDH. Three rhombic signals having g-values and relaxation behavior characteristic of [4Fe-4S] clusters were observed in the 5-40 K temperature range. Two EPR signals with all the g-values less than two, which accounted for less than 0.1 spin/protein, typical of mononuclear Mo(V) and W(V), respectively, were observed. The signal associated with the W(V) ion has a larger deviation from the free electron g-value, as expected for tungsten in a d(1) configuration, albeit with an unusual relaxation behavior. The EPR parameters of the Mo(V) signal are within the range of values typically found for the slow-type signal observed in several Mo-containing proteins belonging to the xanthine oxidase family of enzymes. Mo(V) resonances are split at temperatures below 50 K by magnetic coupling with one of the Fe/S clusters. The analysis of the inter-center magnetic interaction allowed us to assign the EPR-distinguishable iron-sulfur clusters with those seen in the crystal structure of a homologous enzyme.
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PMID:Incorporation of either molybdenum or tungsten into formate dehydrogenase from Desulfovibrio alaskensis NCIMB 13491; EPR assignment of the proximal iron-sulfur cluster to the pterin cofactor in formate dehydrogenases from sulfate-reducing bacteria. 1466 76

Bovine pulmonary artery smooth muscle possesses the tissue inhibitor of matrix metalloproteinase-2 (TIMP-2) as revealed by Western immunoblot study of its cytosol fraction with bovine polyclonal TIMP-2 antibody. This potent polypeptide inhibitor of matrix metalloproteinases (MMPs) was purified to homogeneity from cytosol fraction of bovine pulmonary artery smooth muscle. This inhibitor was purified by ammonium sulfate precipitation followed by gelatin sepharose and lentil lectin sepharose affinity chromatography and continuous elution electrophoresis by Prep Cell Model 491 (Bio-Rad, USA). SDS-PAGE revealed that the inhibitor has an apparent molecular mass of 21 kDa and was confirmed as TIMP-2 by (i) Western immunoblot assay using bovine polyclonal TIMP-2 antibody; and also by (ii) amino terminal amino acid sequence analysis of the purified inhibitor is found to be identical with TIMP-2 obtained from other sources. The purified 21 kDa inhibitor was found to be active against matrix metalloproteinase-2 (MMP-2, 72 kDa gelatinase) and matrix metalloproteinase-9 (MMP-9, 92 kDa gelatinase), the ambient MMPs in the pulmonary artery smooth muscle. The inhibitor was also found to be sensitive to the activated 72 kDa gelatinase-TIMP-2 complex and also active human interstitial collagenase. By contrast, it was found to be insensitive to the serine proteases: trypsin and plasmin. The inhibitor was heat and acid resistant and it had the sensitivity to trypsin degradation and reduction-alkylation. Treatment of the inhibitor with hydrogen peroxide, superoxide generating system (hypoxanthine plus xanthine oxidase) and peroxynitrite inactivated the inhibitor.
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PMID:Identification, purification and partial characterization of tissue inhibitor of matrix metalloproteinase-2 in bovine pulmonary artery smooth muscle. 1467 7

Nine kinds of hetero-chitooligosaccharides (hetero-COSs) with relatively higher molecular weights (90, 75 and 50-HMWCOS), medium molecular weights (90, 75 and 50-MMWCOS), and lower molecular weights (90, 75 and 50-LMWCOS) were prepared from partially deacetylated hetero-chitosans (90, 75 and 50% deacetylated chitosan), and their scavenging activities were investigated against 1,1-diphenyl-2-picrylhydrazyl (DPPH), hydroxyl, superoxide and carbon-centered radicals using electron spin resonance (ESR) spin-trapping technique. Superoxide, hydroxyl and carbon-centered radicals were generated from hypoxanthine-xanthine oxidase reaction, hydrogen peroxide-ferrous sulfate (Fenton reaction) and azo compound 2,2-azobis-(2-amidinopropane)-hydrochloride (AAPH), respectively. The ESR results revealed that 90-MMWCOS, which is having relatively medium molecular weights prepared from 90% deacetylated chitosan, showed the highest scavenging activity on all tested radicals. In addition, the radical scavenging activity of hetero-COSs increased with a dose-dependent manner, and it was dependent on their degree of deacetylation values and molecular weights.
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PMID:Free radical scavenging properties of hetero-chitooligosaccharides using an ESR spectroscopy. 1487 80

The association of beta-lactoglobulin (beta-LG) and alpha-lactalbumin (alpha-LA) with milk fat globule membrane (MFGM), when whole milk was treated by high pressure in the range 100 to 800 MPa, was investigated using sodium dodecyl sulfate (SDS)-PAGE under reducing and nonreducing conditions. In SDS-PAGE under reducing conditions, beta-LG was observed in the MFGM material isolated from milk treated at 100 to 800 MPa for 30 min, and small amounts of alpha-LA and kappa-casein were also observed at pressures >600 MPa for 30 min. However, these proteins were not observed in SDS-PAGE under nonreducing conditions. These results indicate that beta-LG and alpha-LA associated with MFGM proteins via disulfide bonds during the high-pressure treatment of whole milk. The amount of beta-LG associated with the MFGM increased with an increase in pressure up to 800 MPa and with increasing time of pressure treatment. The maximum value for beta-LG association with the MFGM was approximately 0.75 mg/g of fat. Of the major original MFGM proteins, no change in butyrophilin was observed during the high-pressure treatment of whole milk, whereas xanthine oxidase was reduced to some extent beyond 400 MPa. In contrast to the behavior during heat treatment, PAS 6 and PAS 7 were stable during high-pressure treatment, and they remained associated with the MFGM.
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PMID:High-pressure-induced interactions between milk fat globule membrane proteins and skim milk proteins in whole milk. 1554 61


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