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:1.16.3.1 (ceruloplasmin)
5,074 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The studies made showed that repeated combined action of chemical factors (pesticides of different chemical groups, Cd and Pb salts, nitrates) in the doses studied resulted in an increase of the lipid peroxidation (LPO) in tissues, accumulation of its end products in biosubstrates, and activation of catalase and peroxidase oxidoreductases in blood of test animals. Combined action of chemical factors and gamma radiation was found out to make for increasing in lipid peroxidation and involving of ceruloplasmin in the LPO inhibition. Depletion of the antioxidant system in repeated irradiations against the background of chemical loading was accompanied by accumulation of the LPO products. We conclude that in the pathogenesis of the revealed changes in associated effects of ionizing radiation, pesticides, nitrates, Plumbum and Cadmium salts, the LPO activation in the presence of the antioxidant system depletion is most important, in view of which fact the specific criteria for the studied factors combined effects on the organism appear to be the activity of the oxidation-reduction enzymes and the level of the-active products, with the chief preventive measures being directed towards increasing of radioresistance of the organism through correction of the antioxidant deficiency.
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PMID:[An experimental study of the mechanism of the combined action on the body of ionizing radiation, pesticides, nitrates and lead and cadmium salts]. 863 Aug 18

All organisms are protected from harmful reactive oxygen which is produced also under physiological conditions by a complex antioxidative system. Our work was aimed at the ascertainment of the level of reduced and oxidated glutathione in erythrocytes of healthy people, the concentrations of ceruloplasmin (GSH) and transferrin (GSSG) in the serum, as well as the investigation of the relationship to antioxidative enzymes ---Cu, Zn-superoxide dismutase (SOD), catalase (CAT) and Se-glutathione-peroxidase (GPx) in erythrocytes. We discovered a mutual direct linear correlation between the levels of GSH, GSSG, CPL and TRF, indirect linear relation between the concentrations of TRF, GSH, GSSG and activities of SOD and GPx, between the concentrations of CPL and GPx activities, and a direct linear relation between concentrations of GSH and TRF with CAT activity. The results indicate to a mutual dependence of investigated nonenzymatic antioxidative factors and antioxidative enzymes. (Tab2, Fig. 4, Ref.13.).
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PMID:[Levels of erythrocyte glutathione and ceruloplasmin and transferrin in the serum and their role in antioxidant protection]. 868 24

Glutathione is activated to a mutagen by gamma-glutamyl transpeptidase. Other thiols, such as cysteine, penicillamine, cysteine ethylester, and cysteinylglycine, are direct mutagens in the Ames Salmonella mutagenicity test. Thiol mutagenesis is oxidative in nature and involves H2O2 and possibly hydroxyl radicals. Transition metals are crucial for thiol autoxidation. The role of copper and ceruloplasmin (CP) in thiol-dependent mutagenesis was studied in Salmonella typhimurium strain TA102. Cu and CP at low concentrations enhanced thiol-dependent mutagenesis in the presence, but not in the absence, of added Fe. The degree of enhancement depended on the type of thiol. At high Cu or CP concentrations, thiol mutagenesis was inhibited. Cu also decreased the mutagenicity of H2O2. Cu- and CP-enhanced mutagenesis were inhibited by radical scavengers, catalase, and peroxidase but not by superoxide dismutase. The effects of Cu and CP on thiol-dependent mutagenesis were similar to their effects on thiol-driven lipid peroxidation. The results indicate that the role of Cu and CP in the enhancement of thiol mutagenesis is the facilitation of the transfer of electrons from a thiol to iron, rather than in catalysis of the Fenton reaction.
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PMID:Role of copper and ceruloplasmin in oxidative mutagenesis induced by the glutathione-gamma-glutamyl transpeptidase system and by other thiols. 902 Mar 9

Oxidative damage (lipid peroxidation, LPO) induced in a completely defined system containing glutathione (GSH), purified gamma-glutamyl transpeptidase (GGT), and EDTA- and ADP-chelated ferric iron was enhanced by catalytic amounts of cupric ions and by ceruloplasmin (CP). The enhancement depended on GSH concentration, GGT activity, the presence of iron, and the chelation of copper by o-phenanthroline. High concentrations of CP inhibited LPO. Cu- and CP-enhanced, GSH-GGT-driven LPO was inhibited by the chain-breaking radical scavengers butylated hydroxyanisol, alpha-tocopherol, and Trolox C (a synthetic analog of alpha-tocopherol) but not by the hydroxyl scavenger mannitol. Ascorbic acid increased LPO in the presence of Cu or CP. Cu-enhanced LPO was partially sensitive to superoxide dismutase but not to catalase or horseradish peroxidase. The results indicate that Cu and CP enhance thiol-driven LPO and promote thiol-dependent mutagenesis by a very similar, if not the same, mechanism and are in agreement with the idea that this enhancement is due to redox reactions of chelated Cu and Fe, rather than to the reactivity of Cu in the Fenton reaction.
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PMID:Promotion of glutathione-gamma-glutamyl transpeptidase-dependent lipid peroxidation by copper and ceruloplasmin: the requirement for iron and the effects of antioxidants and antioxidant enzymes. 902 Mar 10

Interactions between plasma proteins and MPO were studied. The protein fraction of normal plasma and serum was shown to exhibit an inhibitory effect on the peroxidase activity of MPO. Most of the inhibitory effect could be retained on an MPO-coupled affinity chromatography column. In particular, a protein with apparent mol. wt of 130 kD showed affinity for MPO. The protein was identified as ceruloplasmin by N-terminal amino acid sequencing and immunochemistry. During separation procedures the peroxidase inhibitory effect was limited to ceruloplasmin-containing fractions of plasma. Purified ceruloplasmin inhibited the peroxidase activity of MPO in a concentration-dependent manner, and exhibited selective binding to MPO-coated microtitre plates. This binding could be inhibited by MPO dissolved in buffer. Correspondingly the binding of MPO to ceruloplasmin-coated plates could be blocked by ceruloplasmin in solution, showing a physical interaction to occur between the two proteins under physiological conditions. We also found affinity to exist between MPO and C3 (and its C3d-containing fragments). However, C3 and C3 fragments did not inhibit the peroxidase reaction in vitro. We propose that ceruloplasmin takes part in the clearance and inactivation of MPO, in vivo. We also speculate that impaired inactivation of MPO may have a pathophysiological role in inflammatory diseases characterized by autoantibodies to MPO, such as rapidly progressive glomerulonephritis with P-ANCA (perinuclear anti-neutrophil cytoplasmic antibodies).
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PMID:Binding and inhibition of myeloperoxidase (MPO): a major function of ceruloplasmin? 909 26

The spontaneous autoxidation of the neurotoxin 6-hydroxydopamine proceeds by a free radical chain reaction involving the superoxide anion radical and produces the corresponding chromogen 6-hydroxydopamine quinone and hydrogen peroxide. The rate of this reaction is increased in the presence of ceruloplasmin and peroxidase, and reduced by superoxide dismutase, catalase, and DT-diaphorase. We report some explanations of why these proteins may increase or reduce the rate of autoxidation of 6-hydroxydopamine.
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PMID:Modulation of 6-hydroxydopamine oxidation by various proteins. 917 10

The dimeric Catharanthus alkaloid vincristine (1) is oxidized to the same ring fission product in incubations with either horseradish peroxidase or the human serum copper oxidase ceruloplasmin. Horseradish peroxidase-catalyzed oxidation of vincristine requires hydrogen peroxide, whereas ceruloplasmin-catalyzed oxidation of vincristine requires chlorpromazine as a "shuttle oxidant". Preparative-scale incubations allowed for the production, isolation, structural characterization, and biological evaluation of the metabolite. The metabolite was identified as the heterocyclic ring cleavage product N-formylcatharinine (5). N-Formylcatharinine was 118 times less active than vincristine in an in vitro test against a human T-cell leukemic cell line. Therefore, these enzyme-catalyzed reactions lead to bioinactivation of vincristine.
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PMID:Oxidations of vincristine catalyzed by peroxidase and ceruloplasmin. 939 81

Human ceruloplasmin exhibited different antioxidant effects according to the electron donors in a metal-catalyzed oxidation system. Purified ceruloplasmin did not play a significant role in the protection of DNA strand breaks in the ascorbate/Fe3+/O2 system. However, when ascorbates were replaced with a thiol-reducing equivalent such as dithiothreitol, DNA strand breaks were significantly prevented by the same amount of ceruloplasmin. Ceruloplasmin did not catalyze the decomposition of H2O2 in the absence of reduced glutathione. On the contrary, ceruloplasmin showed a potent peroxidase ability to destroy H2O2 in the presence of reduced glutathione. In conclusion, the removal of H2O2 by human ceruloplasmin is not simply stoichiometric but thiol-dependent.
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PMID:Thiol-linked peroxidase activity of human ceruloplasmin. 971 67

Structural integrity may be needed for the glutathione-linked peroxidase activity of human ceruloplasmin. Intact human ceruloplasmin has a potent peroxidase property to decompose H2O2 in the presence of reduced glutathione. However, the fragment of approximately 116000 Da produced by proteolytic degradation had less than one-third of the glutathione-linked peroxidase activity of intact ceruloplasmin. When further proteolysis occurred, glutathione-linked peroxidase activity of human ceruloplasmin disappeared. In contrast, ceruloplasmin (116000 Da and <96000 Da) fragmented by proteolysis significantly removed H2O2 irrespective of the presence of reduced glutathione. Although proteolytic fragmentation of ceruloplasmin occurs, the antioxidant activity of ceruloplasmin that prevents DNA strand breaks in a metal-catalyzed reaction system was significantly maintained.
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PMID:Requirement of intact human ceruloplasmin for the glutathione-linked peroxidase activity. 982 10

The activities of lipid peroxidation processes and enzymes of antioxidant system in the blood of patient with renal failure have been studied. The results demonstrated stimulation of lipid peroxidation processes in blood serum, cellular membranes of erythrocytes and in urine. The study of the antioxidant system discovered the inhibition of various enzymes: superoxide dismutase and peroxidase, inhibiting production of active oxygen forms; transferring and ceruloplasmin as regulators of Fe2+/Fe3+ ratio, glutathione reductase and glutathione peroxidase influencing the ratio of oxidated and reduced glutathione forms and the level of SH-groups. So, determination of lipid peroxidation processes and antioxidant enzymes in blood is the sensitive inform test in diagnostics of chronic renal failure.
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PMID:[Antioxidants of blood enzymes in kidney function disorders in man]. 984 45


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