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)

NADH oxidation by pig liver plasma membranes is stimulated by ceruloplasmin (CUP) reaching a maximal value at 50 U/ml of CUP. NADH oxidation activated by CUP is proportional to the amount of protein. Concanavalin A (Con A) which recognizes the glucidic residues of the CUP required for binding to the receptor inhibits the NADH oxidation in a dose-responsive manner. Both adriamycin and bathophenantroline disulfonate (BPS), previously reported as transplasma membrane electron transport inhibitors, also inhibit the CUP-stimulated NADH oxidation of pig liver plasma membranes. Our results show a clear interaction between CUP and the NADH oxidase of plasma membrane, which supports an oxidative role for CUP in its growth effect.
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PMID:Ceruloplasmin stimulates NADH oxidation of pig liver plasma membrane. 149 78

Luminol chemiluminescence was observed by addition of menadione to yeast cell suspension and was amplified 1000-fold by further addition of Fe-complex. Catalase, superoxide dismutase and ceruloplasmin had inhibitory effects on luminol chemiluminescence, indicating the extracellular generation of active oxygens (H2O2 and O2-) and reduction of Fe-complex. The generation of H2O2 and reduction of Fe-complex were mainly dependent on the activity of NADH: menadione oxidoreductase in the plasma membrane and cytosol fractions. Both luminol chemiluminescence and H2O2 production were sensitive to the inhibitory effects of proton conductor, ionophorous antibiotics and ATPase inhibitor rather than the inhibitors of the mitochondria electron transport system. The incubation of glucose with yeast cells caused a parallel increase in luminol chemiluminescence, H2O2 production and intracellular NADH concentration. These facts suggest that menadione-catalyzed H2O2 production and chemiluminescence are used as the indicators of cell activity to keep the NADH concentration and NADH: menadione oxidoreductase activity which may be sensitive to the change in pH and ion concentrations.
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PMID:Extracellular generation of active oxygen species catalyzed by exogenous menadione in yeast cell suspension. 187

1. Neocuproine binding to ceruloplasmin markedly increases the chlorpromazine-ceruloplasmin-catalyzed oxidation of NADH. 2. 1,10-Phenanthroline and 2,2'-dipyridyl inhibit neocuproine activation in a competitive manner. 3. The order of enzyme chelator complex stability was: phenanthroline greater than dipyridyl greater than neocuproine.
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PMID:Interaction of neocuproine, 1,10-phenanthroline and 2,2'-dipyridyl with human ceruloplasmin. 334 23

Content of lipid peroxidation products in liver mitochondria, enzymatic system of the peroxidation initiation (NADPH.H+- and NADH.H+-dependent oxydoreductases) at the early and final steps of liver microsomal redoxchain as well as the activity of protective enzymes superoxide dismutase, ceruloplasmin, catalase and glutathione reductase, preventing the excessive accumulation of lipid peroxidation products in liver mitochondria and erythrocytes were studied in rats with hypokinesia within 1 and 2 months. An increase in content of diene conjugates and malonic dialdehyde as well as in activity of NADPH.H+- and NADH.H+-nitroblue tetrazolium-oxydoreductases in liver microsomes, a decrease in activity of catalase and superoxide dismutase in liver mitochondria were observed in the animals within two months of their mobility restriction. These alterations were among the essential mechanisms responsible for an increase in content of lipid peroxidation products under conditions of hypokinesia.
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PMID:[Enzyme system of initiation and protection against lipid peroxidation in the liver and blood of rats with hypokinesia]. 336 22

Promazine is enzymically oxidized by ceruloplasmin without reduction of the 610 nm absorption band of the enzyme. Fluoride inhibited the reaction in a non-competitive manner. The ceruloplasmin oxidase activity is markedly enhanced when promazine is added in the presence of NADH; possibly through a change in enzyme conformation.
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PMID:Interaction of promazine with human ceruloplasmin. 362 97

Experimental rats were subjected to an extreme action: 3-hour immobilization with simultaneous electrostimulation. A complete healing of erosion-ulcerous defects of the gastroduodenal mucosa was recorded in rats given diets with an increased (by 4 g) protein content (group I), on day 5. The mucosal affections in the rats receiving a standard ration still persisted. The content of creatine-phosphate in the gastric wall tissue, decreased under the extreme action, was rapidly recovered in group I rats, no changes in the proper fluorescence level of reduced NADH and flavoproteins were noted. In group II rats both parameters returned to normal only on day 5. Blood serum ceruloplasmin (CP) activity increased during first 3 days with a similar rate in both animal groups. However, in the following 2 days CP activity in group I rats became completely normal, while that in group II animals was still rising. The results of the study have shown that the diet with increased protein content stimulates epithelization of the gastroduodenal mucosa due to the improvement of the bioenergy processes in the gastroduodenal area, and to intensified adaptation potentialities of the body.
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PMID:[Effect of a diet with an increased protein content on reparative processes in experimental ulcerous lesions of the gastric and duodenal mucosa]. 379 50

The plasma membrane of eukaryotic cells contains an NADH oxidase which can transfer electrons across the membrane. This oxidase is controlled by hormones, growth factors and other ligands which bind to receptors in the plasma membrane. Oncogenes also affect activity of the oxidase. Natural serum components such as diferric transferrin and ceruloplasmin which stimulate proliferation also stimulate membrane oxidase activity. Additional growth factors can be required to complement the proliferative effect. Electron transport across the plasma membrane can be measured by the reduction of impermeable electron acceptors, such as ferricyanide, which also stimulate cell growth. The oxidants activate growth-related signals such as cytosolic alkalinization and calcium mobilization. Antiproliferative agents such as adriamycin and retinoic acid inhibit the plasma membrane electron transport. Flavin, Coenzyme Q and an iron chelate on the cell surface are apparent electron carriers for the transmembrane electron transport. Coenzyme Q10 stimulates cell growth, and Coenzyme Q analogs such as capsaicin and chloroquine reversibly inhibit both growth and transmembrane electron transport. Addition of iron salts to the depleted cells restores activity and growth. The ligand-activated oxidase in the plasma membrane introduces a new basis for control of signal transduction in cells. The redox state of the quinone in the oxidase is proposed to control tyrosine kinase either by generation of H2O2 or redox-induced conformational change.
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PMID:Coenzyme Q10, plasma membrane oxidase and growth control. 775 19

Adult and young camel ceruloplasmin (Cp) were isolated and purified using the single-step chromatography on amino ethyl-activated sepharose. There are no differences between the adult and the young camel protein. The molecular mass of the protein, as estimated by SDS-PAGE (denaturant conditions), was approximately 130000 Da. The electrophoretic mobility of camel Cp is slightly higher as compared to human and sheep protein suggesting that the camel Cp is homogeneous, compact and more acid. The copper content was estimated to be 5.8+/-0.3 atoms per molecule. The spectroscopic feature includes an absorption maximum at 610 nm, which could be attributed to type 1 copper. The EPR spectrum was completely devoid of any typical signal of the type 2 copper. The kinetic parameters of the adult camel Cp for the specific activity as p-phenylendiamine oxidase were determined as K(m)=0.42 mM and V(max)=0.93 microM NADH/mn/mg Cp. The optimum pH for the activity was 5.7.
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PMID:Purification and partial characterization of camel (Camelus Dromedarius) ceruloplasmin. 1195 33

It is thought that changes in gene expression in the brain mediate chronic ethanol-induced complex behaviors such as tolerance, dependence, and sensitization, and also relate to ethanol-induced brain toxicity. Using high-density filter-based cDNA microarrays (GeneFilters), we analyzed the expression of over 5000 genes in the dorsal hippocampus of rats treated with 12% ethanol or tap water for 15 months. Ethanol-induced changes in gene expression were particularly prominent in two groups of genes. One group consisted of oxidoreductases, including ceruloplasmin, uricase, branched-chain alpha-keto acid dehydrogenase, NADH ubiquinone oxidoreductase, P450, NAD+-isocitrate dehydrogenase, and cytochrome c oxidase, which may be related to ethanol-induced oxidative stress. The other group of genes included ADP-ribosylation factor, RAS related protein rab10, phosphatidylinositol 4-kinase, dynein-associated polypeptides, and dynamin-1, which seem to be involved in membrane trafficking. The results may reveal some of the pathways involved in ethanol-induced pathophysiological changes.
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PMID:Microarray analysis of gene expression in rat hippocampus after chronic ethanol treatment. 1246 20

Tranquillizing drugs of the phenothiazine class form charge-transfer complexes with a ceruloplasmin-Cu(II) ion [De Mol NJ. 1985 Biochim Pharmacol 34, 2605-2609], the interaction resulting in a stimulatory effect on the ceruloplasmin catalyzed oxidation of catecholamines and NADH; the latter used as substrate in the present study. A good correlation between stability of the enzyme-drug complex and electron donor ability of the phenothiazine molecule was obtained for drugs with an aliphatic propyl side chain in 10-position (promazine > chlorpromazine > triflupromazine). The hydrofobic methyl group in the side chain of levomepromazine appeared to reduce the stability. A simple correlation between specific efficiency of the enzyme-drug complex and electron donor ability was not obtained (chlorpromazine > promazine = levomepromazine > triflupromazine). The Km-values, characterizing the reaction between NADH and the different enzyme-drug complexes, were estimated. The data suggest that the enzyme-chlorpromazine complex has the best affinity for NADH. The stimulatory effect of levomepromazine closely followed that of promazine.
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PMID:A kinetic study on the phenothiazine dependent oxidation of NADH by bovine ceruloplasmin. 1650 25


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