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)

A large colony of fawn-hooded (FH) rats, comprising five original families and six generations of their progeny, was developed for genetic and comparative studies of their bleeding tendency. The characteristics of the bleeding diathesis in these rats are similar to those originally reported in related rats by Tschopp and Zucker. FH rats have normal clot retraction, ADP-induced platelet aggregation and platelet ADP; variable aggregation with collagen; minimal aggregation with adrenaline and cobra venom factor; and reduced platelet ATP, ATP/ADP ratio, serotonin content and -14C-serotonin release. In comparison to age- and sex-matched Wistar rats, FH rats have significantly prolonged partial thromboplastin time, shortened Russell's viper venom time and increased factor X and XI levels. Other coagulation screening tests and specific assays for fibrinogen, plasminogen and factors VII, VIII and IX were normal. Some age- and sex-related differences in coagulation and other parameters were observed within each rat strain. Plasma proteins, glycoproteins and ceruloplasmin (copper oxidase activity) showed no abnormalities, nor did initial studies of immunoglobulins and complement. However, FH rats have significantly lower glucose and higher cholesterol levels than comparable Wistar rats.
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PMID:Characterization of the fawn-hooded rat as a model for hemostatic studies. 116 25

The introduction deals with of the history, etiology and, briefly, clinical manifestations of endemic nephropathy. The authors state that a large number of investigations have been done until today, but without producing a diagnostic test for early diagnosis of the disease. This led the authors to pursue certain laboratory investigations. The control group consisted of 30 healthy individuals while patients diagnosed as Endemic Nephropathy were grouped according to stages of the disease: initial, developed, terminal stages. Nucleotides in erythrocytes (5' UMP, 5' IMP, 5' GMP, 5,CMP, 5' AMP, 5' ADP, 5' ATP) were determined on the Acidic Aminoanalyzer, with use of a special UV detector. Catecholamines in the urine were determined by using ratiofluorometery. Creatinine phosphocinase, hydroxybutirat--dehydrogenase and 2,3 DPG were determined on the "Carlbiochem" enzymometer. LDH, its isoenzymes as well as its profile were determined by electrophoresis on starch gel. Specific proteins such as haptoglobin, alpha 2 macroglobulin, alpha 1 antitrypsin, alpha 1 acid glycoprotein, properdin factor B, ceruloplasmin were determined on the Immunochemistry Analyzer. Total cholesterol and cholesterol in lipoproteins fractions VLDL, LDL and HDL were determined on the Cholesterol Analyzer. All results were evaluated statistically. Our conclusion is that they are interesting and contribute to the diagnosis of endemic nephropathy.
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PMID:[Levels of immunoglobulins in various media from healthy pregnant women and women with diabetes mellitus and EPH gestosis]. 191 49

The oxidation of 2-keto-4-thiomethyl butyric acid (KTBA) and methionine to ethylene has been used to evaluate generation of ferryl species or hydroxyl radicals by H2O2-activated haemproteins or free ferric ions. Hydrogen peroxide was generated by a glucose oxidase-glucose system at a rate of 1 microM/min. Free ferric in the presence of H2O2 oxidizes KTBA, and this was highly inhibited by hydroxyl radical scavengers, caeruloplasmin, superoxide dismutase (SOD) and EDTA. However, when metmyoglobin, methaemoglobin (MtHb) or horseradish peroxidase (HRP) were tested in the same model system, hydroxyl radical scavengers suppressed partially KTBA oxidation and caeruloplasmin, SOD and EDTA failed to inhibit the reaction. Cytochrome-c was found to be a weak promoter of KTBA oxidation in the presence of H2O2. Methionine was oxidized to ethylene by an active system which generates hydroxyl radicals, but not by H2O2-activated metmyoglobin. Ferric ions chelated to membranes or ADP in the presence of H2O2 generated enzymatically, initiated membranal lipid peroxidation only in the presence of ascorbic acid, and this was inhibited by EDTA. In contrast, metmyoglobin and methaemoglobin activated by H2O2 generated by the same system, initiated membranal lipid peroxidation and this was not inhibited by EDTA. It is concluded that ferryl and not HO. is the main oxidant in systems containing myoglobin and haemoglobin activated by low concentrations of H2O2.
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PMID:The generation of ferryl or hydroxyl radicals during interaction of haemproteins with hydrogen peroxide. 285 14

The lipid peroxidation process is enhanced in both hyperoxygenated or underoxygenated tissues though its mechanism of production is different. Because in thyroid functional diseases there are severe disorders in tissue oxygenation we studied the lipid peroxidation process by using the serum level of malondialdehyde (MDA) as indicator. We also determined the serum ceruloplasmin (CP), an enzymatic protein belonging to the circulating system of antioxidative protection and also playing a role in the cell-mediated immunity. We also followed serum level of uric acid (UA). The determinations were performed on serum samples collected from three groups: 1, adult control subjects: 2. adult untreated hyperthyroid patients, and 3. adult hypothyroid thyroidectomized patients to whom replacement therapy was discontinued for at least 15 days. The mean MDA level was significantly higher in both hyperthyroid and hypothyroid patients by comparison to the control group. CP mean level was significantly lower than in controls. It was concluded that in post thyroidectomy hypothyroidism an enhancement of lipid peroxidation does exist and that its consequences are probably aggravated by the low serum CP level. The enhancement of the process occurs by other mechanisms than for hyperthyroid group. At hypothyroid patients there is an ADP excess which is degenerated to xanthine, the substrate of xanthine oxidase resulting in toxic anion superoxide and UA. In contrast with hyperthyroid group, in hypothyroid patients we observed significant higher values of UA in comparison to the controls. The excess of MDA found in hyperthyroid patients is statistically significant, but its consequences are probably less severe because the serum CP is higher than normal, a rather expected finding for an autoimmune disease.
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PMID:Significance of high levels of serum malonyl dialdehyde (MDA) and ceruloplasmin (CP) in hyper- and hypothyroidism. 338 87

Superoxide (.O-2) is demonstrated to participate at the prostaglandin phase swelling (2-4 h) of carrageenan paw edema. Superoxide production is inhibited in vitro by typical anti-inflammatory drugs, but these drugs did not scavenge superoxide which was produced by xanthine oxidase. Phosphate, pyrophosphate, ATP, ADP and sulfate were essential for superoxide production by macrophages. These anions can induce paw swelling and are reported to increase in rheumatic patients. A mixture of macrophages and lymphocytes from BCG sensitized guinea-pigs was cultured for 2 days with SOD or D-mannitol. Nitroblue tetrazolium reduction (formazan formation) was inhibited by these agents, suggesting that the hydroxyl radical (.OH) is necessary for metabolic activation of macrophage. Lympholine-like factor of which production or release is enhanced by hydroxyl radical, activates macrophage. Production of oxygen radicals may increase rapidly by this chain cycle reaction. Possible relations of oxygen radicals to prostaglandin(s) biosyntheses, chemotaxis, lysosomal enzyme release protease participation, were discussed. Endogenous SOD, epinephrine, ceruloplasmin, blood plasma proteins, inflammatory fluid, may modulate the amount of superoxide by their superoxide scavenging capacities.
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PMID:Inflammation and superoxide production by macrophages. 626 69

Microsomal lipid peroxidation induced by NADPH, but not by ascorbate, was found to be inhibited by liver cytosol. This inhibition was not dependent on glutathione and was enhanced by ADP in presence of Fe2+ at a concentration of 50 microM or higher. ATP was also effective, but not AMP or cyclic AMP. The cytosolic factor appeared to be a protein as it was heat-labile (greater than 70 degrees C), was non-dialyzable and was precipitated by ammonium sulfate and acetone. It was stable for several months in frozen state and also when heated at 50 degrees C for 10 min. The inhibition by the cytosolic protein was obtained by producing a lag in the activity of lipid peroxidation and was reversed by ceruloplasmin but not by catalase, cytochrome c, hemoglobin or superoxide dismutase. This inhibitory effect by cytosol was limited to formation of lipid peroxides whereas oxygen uptake and NADPH oxidation remained unaffected. Regulation of lipid peroxidation by nucleotide-Fe complexes and cytosolic proteins is indicated by these studies.
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PMID:Inhibition of microsomal lipid peroxidation by cytosolic protein in presence of ADP and high concentration of Fe2+. 650 75

Self-reduction of an Fe3+-ADP-adriamycin complex under anaerobic conditions and reduction of ferricytochrome c by the complex under aerobic conditions were strongly inhibited by ceruloplasmin, but not by superoxide dismutase or albumin at the same protein concentration. Ceruloplasmin, a protein with ferroxidase activity, is able to catalyse oxidation of Fe2+ to the ferric state. The inhibitory activity of ceruloplasmin towards reactions stimulated by the complex suggests that Fe2+ is formed during the self-reduction process. As expected, the Fe3+-ADP-adriamycin complex stimulated lipid peroxidation in which the Fe2+ moiety was implicated. This stimulation was again effectively prevented by ceruloplasmin but not by superoxide dismutase.
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PMID:Inhibition by the protein ceruloplasmin of lipid peroxidation stimulated by an Fe3+-ADP-adriamycin complex. 669 26

Microsomal NADPH-dependent lipid peroxidation catalyzed by ADP-Fe3+ was inhibited by the addition of caeruloplasmin. The antioxidant effect of caeruloplasmin was independent of the superoxide anion (O-2) scavenging activity. Since caeruloplasmin enhanced the function of ADP-Fe3+ acting as electron acceptor for microsomal electron transport system, the antioxidant effect of caeruloplasmin is considered to depend on the ferroxidase activity.
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PMID:Antioxidant effect of caeruloplasmin on microsomal lipid peroxidation. 682 43

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

This study evaluated the effects of ceruloplasmin, the copper-containing blue oxidase of vertebrate plasma, on the relaxation of rabbit aortic rings after endothelial release of nitric oxide (NO). Ceruloplasmin at physiological, i.e., micromolar, concentrations inhibited relaxation of rabbit aorta induced by endothelium-dependent agonists like acetylcholine or ADP, whereas it was ineffective toward vasodilation due to direct stimulation of smooth muscle cells by nitroglycerin. The effect was reversible and specific for native, fully metalated ceruloplasmin, since relaxation was not impaired by the heat-treated or metal-depleted derivatives. A trapping mechanism, involving a direct interaction of NO or other NO-containing species (like nitrosothiols and iron-dinitrosyls) with the copper sites and/or with the free thiol of ceruloplasmin, could be safely excluded on the basis of spectroscopic and chemical analyses of the protein exposed to authentic NO, nitrosothiols, or iron-dinitrosyls. The data presented in this paper constitute the first evidence of impairment of the endothelium-dependent vasodilatation by a plasma protein and may shed some light on the still uncertain physiological role of ceruloplasmin.
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PMID:Ceruloplasmin impairs endothelium-dependent relaxation of rabbit aorta. 943 22


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