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)

Arthritis induced by 6-sulphanilamidoindazole in older rats is not inhibited by a one-week treatment with superoxide dismutase, peroxidase or desferrioxamine. It is concluded that oxygen radicals hardly play a special part in the pathogenesis of 6-SAI arthritis. C-reactive protein and caeruloplasmin are demonstrated to be acute-phase reactants also in 6-SAI arthritis, although on the whole the acute-phase reaction is relatively weak. The steroid dexamethasone and the nonsteroid benoxaprofen caused strong antiinflammatory activity at low doses. The data presented complete the picture of 6-SAI arthritis as a special inflammatory reaction in rats.
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PMID:6-Sulphanilamidoindazole-induced arthritis in rats: substance effects and acute-phase reaction. 243 28

The leakage of different serum proteins, including immunoglobulins, into human cerebral gliomas was studied by use of the unlabeled peroxidase-antiperoxidase (PAP) method on cryostat and paraffin sections. Our series of 50 tumour biopsies included 21 isomorphic astrocytomas and oligodendrogliomas (grade II), 19 anaplastic astrocytomas and oligodendrogliomas (grade III), and 10 glioblastomas (grade IV). The immunohistochemical staining of the serum proteins was similar on paraffin and cryostat sections and graded with respect to occurrence, distribution, and intensity. Serum proteins of a small hydrodynamic radius with a low serum concentration (prealbumin) or with a high serum concentration (albumin) were diffusely present in the interstitial spaces of all glioma types. Serum proteins with a medium molecular size and variable serum concentrations, i.e. IgG, IgA, and ceruloplasmin, were detected preferentially in anaplastic gliomas and in glioblastomas (grade III and IV) displaying comparable distribution patterns but different intensities. Alpha-2-macroglobulin a serum protein with a large hydrodynamic radius was also demonstrated in grade III and IV gliomas, whereas IgM and beta-lipoprotein being the largest serum proteins tested were almost restricted to blood vessels and tumour necroses. In addition, most serum proteins occurred with high intensities in those areas of isomorphic grade II gliomas that showed a macro- or microcystic or mucinous tissue degeneration. The varying immunohistochemical staining results for the serum proteins studied indicate that the blood-brain barrier within isomorphic and anaplastic gliomas is not completely disturbed. It appears that the vascular permeability is preferentially increased for small-sized serum proteins, whereas the leakage of larger serum proteins into the glioma interstitium seems to depend on the tumour type and on increasing malignancy.
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PMID:Immunohistochemical demonstration of serum proteins in human cerebral gliomas. 244 Feb 23

The levels of superoxide dismutase (SOD) and myeloperoxidase (MPO) in polymorphonuclear leukocytes (PMN), and serum ceruloplasmin activity and copper content, were measured in 60 patients with psoriasis and 33 healthy controls. There were no significant differences in the activity of MPO between the patients and the controls. However, SOD activity in PMN was significantly lower in the patients than in the controls. Serum ceruloplasmin activity and copper levels were significantly higher in the psoriatics than in the controls.
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PMID:Superoxide dismutase and myeloperoxidase activity in polymorphonuclear leukocytes, and serum ceruloplasmin and copper levels, in psoriasis. 253 38

Influence of main serum proteins (albumin, immunoglobulin G) and proteins-antioxidants (ceruloplasmin, transferrin, superoxide dismutase) on the oxidative damage of erythrocytes by myeloperoxidase and hypochlorite was investigated. The proteins were determined to act as protectors and decrease the degree of hemoglobin oxidation, ceruloplasmin and albumin possessing the highest antioxidant activity.
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PMID:[Erythrocyte oxidative damage by myeloperoxidase. The protective action of serum proteins]. 254 30

It was observed that during the storage of human extracellular fluids at -20 degrees C the azide-inhibitable ferroxidase activity of caeruloplasmin declined, whilst a new azide-resistant ferroxidase activity (ARFA) developed. The literature suggested that storage-induced ARFA might be due to either a poorly defined enzymatic activity of a low density lipoprotein (LDL) or to lipid peroxides formed within the different lipoprotein fractions. To study this further, the major lipoprotein classes were separated from human serum by density gradient centrifugation. After storage of the lipoprotein fractions, it was found that the LDL fraction had the highest specific activity of ARFA and the highest content of lipid peroxidation products, as assessed by diene conjugates. The ARFA of LDL correlated with its content of diene conjugates and TBA reactive material, which initially suggested that the Fe(II) oxidising activity of peroxidase LDL arose from the reduction of peroxides by Fe(II) in the classical reaction between the metal ion and free radical reduction of lipid peroxides. However, steady state kinetic analysis indicated an enzymic role of LDL in Fe(II) oxidation, with lipid peroxides acting as a substrate for the enzyme. These results indicate that LDL may contain a peroxidase activity, catalysing the oxidation of Fe(II) by lipid peroxides, as well as a ferrous oxidase activity where O2 is the oxidising substrate.
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PMID:Lipoprotein oxidation and induction of ferroxidase activity in stored human extracellular fluids. 270 24

The dimeric Vinca alkaloid vinblastine (VLB) undergoes metabolic transformation to three products in a reaction catalyzed by the human serum copper oxidase ceruloplasmin. The enzyme reaction requires chlorpromazine as a shuttle oxidant, and the course of the oxidation reaction appears to be subject to the nature of the shuttle oxidant used. Preparative-scale incubations have resulted in the isolation of three products, which were characterized by chemical and spectral analyses. The metabolites were identified as the ring fission product catharinine, obtained by oxidation of the Iboga ring system; an enamine/ether derivative obtained by oxidation of the Aspidosperma portion of VLB; and a metabolite embodying the same structural changes in both parts of the vinblastine dimeric structure. Catharinine is identical with the product of VLB oxidation obtained by peroxidase oxidation. The other two products are new metabolites and are derivatives of VLB. All of the metabolites are less active than VLB when tested in vitro vs the human T-cell leukemic cell line (CRFF-CEM).
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PMID:In vitro metabolic transformations of vinblastine: oxidations catalyzed by human ceruloplasmin. 276 88

In athletes of high skills, a 5-percent decline of the body weight over 5 days by means of restricting water, fats and carbohydrates consumption was followed by reduced activity of ceruloplasmin and lysozyme of blood serum. After sauna attendance with a purpose of lessening the body weight, there was, along with a certain rise of the immunologic responsiveness of the body, a decrease in peroxidase activity, in the content of iron and copper in blood cells in the presence of appreciable losses of trace elements with sweat. Enrichment of the athletes' diets with trace elements combined with vitamins and bendasole hydrochloride in the course of sauna-induced body weight lessening not only prevented the negative alterations but also exerted a beneficial action on the function of certain body systems.
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PMID:[The effect of a rapid decrease in body weight and enriching rations with microelements on various functions of the athlete's body]. 281 9

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

Tyrosinase usually catalyzes the conversion of monophenols to o-diphenols and oxidation of diphenols to the corresponding quinones. However, when 3,4-dihydroxymandelic acid was provided as the substrate, it catalyzed an unusual oxidative decarboxylation reaction generating 3,4-dihydroxybenzaldehyde as the sole product. The identity of the product was confirmed by high-performance liquid chromatography (HPLC) as well as ultraviolet and infrared spectral studies. None of the following enzymes tested catalyzed the new reaction: galactose oxidase, ceruloplasmin, superoxide dismutase, ascorbate oxidase, dopamine beta-hydroxylase, and peroxidase. Phenol oxidase inhibitors such as phenylthiourea, potassium cyanide, and sodium azide inhibited the reaction drastically, suggesting the participation of the active site copper of the enzyme in the catalysis. Mimosine, a well-known competitive inhibitor of tyrosinase, competitively inhibited the new reaction also. 4-Hydroxymandelic acid and 3-methoxy-4-hydroxymandelic acid neither served as substrates nor inhibited the reaction. Putative intermediates such as 3,4-dihydroxybenzyl alcohol and (3,4-dihydroxybenzoyl)formic acid did not accumulate during the reaction. Oxidation to a quinone methide derivative rather than conventional quinone accounts for this unusual oxidative decarboxylation reaction. Earlier from this laboratory, we reported the conversion of 4-alkylcatechols to quinone methides catalyzed by a cuticular phenol oxidase [Sugumaran, M., & Lipke, H. (1983) FEBS Lett. 155, 65-68]. Present studies demonstrate that mushroom tyrosinase will also catalyze quinone methide production with the same active site copper if a suitable substrate such as 3,4-dihydroxymandelic acid is provided.
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PMID:Tyrosinase catalyzes an unusual oxidative decarboxylation of 3,4-dihydroxymandelate. 309 74

We have examined whether the toxic effects of homocysteine on cultured endothelial cells could result from the formation and action of hydrogen peroxide. In initial experiments with a cell-free system, micromolar amounts of copper were found to catalyze an oxygen-dependent oxidation of homocysteine. The molar ratio of homocysteine oxidized to oxygen consumed was approximately 4.0, which suggests that oxygen was reduced to water. The addition of catalase, however, decreased oxygen consumption by nearly one-half, which suggests that H2O2 was formed during the reaction. Confirming this hypothesis, H2O2 formation was detected using the horseradish peroxidase-dependent oxidation of fluorescent scopoletin. Ceruloplasmin was also found to catalyze oxidation of homocysteine and generation of H2O2 in molar amounts equivalent to copper sulfate. Finally, homocysteine oxidation was catalyzed by normal human serum in a concentration-dependent manner. Using cultured human and bovine endothelial cells, we found that homocysteine plus copper could lyse the cells in a dose-dependent manner, an effect that was completely prevented by catalase. Homocystine plus copper was not toxic to the cells. Specific injury to endothelial cells was seen only after 4 h of incubation with homocysteine plus copper. Confirming the biochemical studies, ceruloplasmin was also found to be equivalent to Cu++ in its ability to cause injury to endothelial cells in the presence of homocysteine. Since elevated levels of homocysteine have been implicated in premature development of atherosclerosis, these findings may be relevant to the mechanism of some types of chronic vascular injury.
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PMID:Endothelial cell injury due to copper-catalyzed hydrogen peroxide generation from homocysteine. 351 79


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