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)

To investigate the involvement of oxygen free radicals and their scavenger systems in the defenses of compromised hosts against pulmonary infections, we determined superoxide anion (SOA) and superoxide dismutase (SOD; EC 1.15.1.1) concentrations in the blood of compromised hosts and noncompromised hosts, with or without pneumonia. In the compromised hosts without pneumonia (compromised controls), SOD concentrations were lower than in noncompromised hosts (healthy controls). However SOA values in compromised controls did not differ statistically from that in healthy controls. Similar changes were observed in noncompromised hosts with pneumonia. In compromised hosts with pneumonia, SOD concentrations were further decreased by pulmonary infections. By contrast, SOA values were increased in pneumonia. There were, however, no differences in the values for ceruloplasmin among all the groups. The values for alpha 2-macroglobulin and alpha1-antitrypsin were within normal limits in compromised controls but were greater in compromised hosts with pneumonia. These results suggest that a decreased activity concentration of SOD in compromised controls may be partly responsible for the depression of the host's immune defenses.
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PMID:Concentrations of superoxide dismutase and superoxide anion in blood of patients with respiratory infections and compromised immune systems. 244 6

Inflammation increases plasma levels of ceruloplasmin, a copper protein with possible antioxidant function. This paper describes modulation of these increases by copper intake, and describes combined effects of inflammation and copper intake on Cu-Zn and extracellular (EC) superoxide dismutase (SOD) activities. Turpentine injections in rats fed 1 of 4 copper levels increased ceruloplasmin activities, but values were sensitively limited by copper intake. Cu-Zn SOD activities in the liver, but not in erythrocytes or lungs, were reduced by inflammation in each dietary copper group. Inflammation in rats fed a standard mixed feed diet reduced plasma EC superoxide dismutase activities measured by inhibition of pyrogallol autoxidation. Different results were obtained with 3 xanthine oxidase based SOD assays which were each subject to assay interference. Studies in humans found a group of rheumatoid arthritis patients to possess relatively low erythrocyte SOD and relatively high ceruloplasmin activities. Activity levels of SOD, but not of ceruloplasmin, increased after 4 weeks of copper supplementation (2 mg/day). The fate of cellular Cu-Zn SOD activity contents in inflamed tissues is largely uninvestigated. However, interleukin-1, a hormone released at inflammation sites, elevated Cu-Zn SOD activities in cultured fibroblasts.
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PMID:Effects of inflammation on copper antioxidant enzyme levels. 256 Jun 8

The present study was designed to investigate the effects of nickel chloride on dietary iron deficiency in rats. The degree of iron deficiency was relatively moderate, but a more generalized anemia occurred in iron deficiency, in absence of nickel chloride. Moderate iron deficiency anemia induced increased lactate-dehydrogenase activity of serum and bone marrow, perhaps related to the decreased production of energy by oxidative means. Nickel chloride, perhaps for its ability to change iron absorption, for the maintenance of bone marrow metabolism and for to increase ceruloplasmin activity, inhibited the alteration on hemoglobin synthesis. Furthermore, nickel chloride possibly for its action on copper content and Cu-Zn superoxide-dismutase activity, inhibits the shortening of the red cell life span, caused by superoxide radicals.
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PMID:Influence of nickel chloride on iron-deficiency in rats. 263 91

Copper uptake from human ceruloplasmin (Cp) into cells of a human erythroleukemic cell line, K562, was investigated. The interaction between ascorbic acid and the copper atoms in ceruloplasmin was a focal point of the study. Nondenatured 67Cu-labeled ceruloplasmin (67Cu-Cp) was prepared by an ascorbate-catalyzed exchange of Cp with 67CuCl2 in vitro. The complex was stable, even in the presence of 1.0 mM ascorbate. Adding K562 cells and incubating at 37 degrees C resulted in an immediate transfer of 67Cu from ceruloplasmin to the cells. At 37 degrees C the copper accumulated by the K562 cells resisted dissociation by mild acid washing. The rate of transfer of 67Cu was proportional to the Cp concentration in the medium. Ascorbate (100 microM) enhanced the uptake of 67Cu at least fourfold. D-Isoascorbate worked as well as L-ascorbate, suggesting that the reducing potential of the vitamin (or its isomer) was important in the uptake of copper. Approximately 20% of the 67Cu absorbed into the cytosol was precipitable with antibodies to Cu-Zn superoxide dismutase (Cu-Zn SOD). Ascorbate, however, did not enhance the incorporation of radioactivity into Cu-Zn SOD, suggesting that copper may not be the only rate-limiting factor in the synthesis of this enzyme in K562 cells. The possible relevance of these observations to vitamin C deficiency is discussed.
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PMID:Ascorbate enhances copper transport from ceruloplasmin into human K562 cells. 272 26

The evolutionary relationships of blue copper proteins are reviewed. Five homologous families of small blue proteins are recognized. Despite differences in length their peptide chains can all be accommodated into the eight-stranded fold of plastocyanin with some adjustments at three of the loops and the two termini. The C-termini of the blue oxidases ceruloplasmin and Neurospora laccase also fit into this fold and they are suggested to be homologous to the small blue proteins. The alignment of their amino acid sequences suggest some of the histidines to be binding active site copper. A superposition of the structures of poplar plastocyanin and bovine Cu-Zn superoxide dismutase (SOD) showed that 68 out of 99 alpha-carbons in plastocyanin overlapped with corresponding atoms in SOD with a rms distance of 2.99 A. In addition three of the histidine residues that were proposed to be copper-binding in laccase and ceruloplasmin aligned with ligands to the Cu-Zn pair in a SOD. Thus also SOD might be related to the blue proteins.
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PMID:Evolution of blue copper proteins. 304 63

Serum superoxide dismutase (SOD) activity concentrations, though small compared to tissue levels, could contribute to extracellular superoxide radical detoxification and act as indicators of copper status. The present study identified the response of rat serum SOD activity contents to marginal and deficient copper intakes and to inflammation. Rats fed copper-deficient diet (less than 0.2 mg/kg Cu) for 5 wk displayed serum SOD activity contents that were only about 20% of those found in rats fed copper-supplemented diet (6.0 mg/kg Cu). Activities in rats fed a marginal diet (1.5 mg/kg Cu) were about 55% of those in the adequate rats. Turpentine-induced inflammation lowered serum SOD in rats within each dietary group. However, the change in the marginal group was not statistically significant. Based on chromatographic characterizations and inhibitor studies, rat serum SOD activity seemed to result primarily from a copper protein other than ceruloplasmin, Cu-Zn SOD or the recently discovered tissue extracellular SOD. In conclusion, low copper intake and inflammation may compromise extracellular defenses against superoxide. In addition, serum SOD activities could provide a non-ceruloplasmin-related means of assessing copper status, but nondietary variables can also affect these SOD values.
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PMID:Influence of copper intake and inflammation on rat serum superoxide dismutase activity levels. 335 62

As part of a study to determine the effect of 150 mg zinc/day on plasma lipoproteins, healthy young female (n = 26; mean age 27 years) and male (n = 21; mean age 28 years) volunteers took part in a double-blind cross-over trial lasting 12 weeks. During 6 weeks of supplementation, plasma Zn rose significantly in both groups, indicating compliance. Plasma total cholesterol remained unchanged in both males and females. However, mean LDL-cholesterol decreased from 2.38 to 2.17 mmol/l in females and there was a trend for total HDL-cholesterol to be redistributed in that HDL2 rose and HDL3 fell slightly. In parallel with these changes in females, Zn supplements reduced the ferroxidase activity of serum caeruloplasmin (from 13.0 to 11.3 U/ml) and the antioxidant activity of erythrocyte superoxide dismutase (E-SOD) (from 4557 to 3638 U/g Hb) and CuZn E-SOD (from 2184 to 1672 U/g Hb). Plasma Cu and haematocrit were unaffected. No such changes were seen in males in either lipoproteins or these indicators of Cu status. Since the females were lighter than the males but received the same dose, a dose-response effect rather than a sex difference cannot be ruled out. Overall, Zn supplements significantly decrease a major risk factor for CHD in females but reduced their Cu status.
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PMID:The effect of zinc supplements on lipoproteins and copper status. 336 92

Caeruloplasmin and albumin were compared as potential donors of copper to Cu2Zn2-superoxide dismutase (CuZn-SOD) in culture. Aortas from 15-day copper-deficient chicks were suspended in oxygenated, serum-free, Waymouth medium (752/1) for 24 h. SOD activity was restored when the medium was supplemented with CuCl2, a copper-albumin complex or caeruloplasmin, all present at a level equivalent to 5 microM-copper. Activation did not occur at 4 degrees C or with Cu-EDTA as the supplement. Mn2+ and Zn2+, alone or in combination, did not activate nor enhance the activation achieved by CuCl2. The activation with CuCl2 was not inhibited by cycloheximide or cordycepin. [67Cu]Caeruloplasmin and albumin when added to the medium transferred radioactive copper to at least three cytosolic protein fractions, one of which was determined by immunoprecipitation to be CuZn-SOD. The transfer of 67Cu from caeruloplasmin was inhibited by increasing amounts of unlabelled caeruloplasmin; disodium EDTA (1.0 mM) had no effect on the transfer of copper from caeruloplasmin. These data show that aortic SOD activity, suppressed in copper deficiency, can be restored by incubating the aortas in culture medium supplemented with copper salts. In this system, caeruloplasmin and Cu-albumin appear equally capable of activating aortic CuZn-SOD. Moreover, the transfer of copper into the enzyme structure appears to be the primary event restoring catalytic activity to the enzyme.
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PMID:Regulation of aortic CuZn-superoxide dismutase with copper. Caeruloplasmin and albumin re-activate and transfer copper to the enzyme in culture. 343 77

Experiments were conducted in copper deficient male and female rats fed diets containing fructose or starch in order to determine whether the same type of interaction between copper status and dietary carbohydrate found in male rats also occurs in the female rat. Mortality occurred only in the male rats fed the fructose diet deficient in copper with 40% of the animals dying during the 8 week study. Only anemia, hypercholesterolemia, increased BUN, heart hypertrophy and reduced body weight were observed in these animals which could be related to their mortality. Despite the increased mortality, plasma ceruloplasmin, erythrocyte SOD and hepatic copper concentrations were reduced to a similar extent in all rats regardless of the sex of the animals or of the type of dietary carbohydrate fed. The results of the present study indicate that although direct measurements of copper status of female rats fed fructose diet deficient in copper are similar to their male counterpart, they are apparently protected from the lethal consequences of the deficiency.
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PMID:Female rats are protected against the fructose induced mortality of copper deficiency. 374 32

The administration of very low doses of bacterial endotoxin protects rats during exposure to hyperoxia and is associated with the induction of lung antioxidant enzyme activities. Copper-deficient rats have increased susceptibility to O2 toxicity, which may be related to their decreased lung superoxide dismutase activity (SOD) or decreased plasma ceruloplasmin concentrations. To determine whether endotoxin can protect against hyperoxia in this susceptible model, we exposed copper-deficient and control rats to a fractional inspiratory concentration of O2 greater than 0.95 for 96 h after pretreatment with 500 micrograms/kg of bacterial endotoxin or phosphate-buffered saline (PBS). Mortality in the copper-deficient and control rats given PBS and exposed to O2 for 96 h was 100%. Copper-deficient rats died significantly earlier during the exposure than controls. No mortality occurred in either group treated with endotoxin and hyperoxia despite the decreased activity of copper-dependent enzymes in the copper-deficient rats. Copper-deficient rats treated with endotoxin and exposed to hyperoxia did increase lung Cu-Zn-SOD activity, but activity remained below levels found in air-exposed controls. Mn-SOD activity was found to be induced above air-exposed controls in the copper-deficient rats treated with endotoxin and exposed to hyperoxia. Hyperoxic exposure resulted in a marked increase in plasma ceruloplasmin concentrations in the control rats, but no increases in ceruloplasmin occurred in the copper-deficient animals. Endotoxin protects copper-deficient rats from hyperoxia despite their decreased lung Cu-Zn-SOD activity, and decreased plasma ceruloplasmin.
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PMID:Effects of bacterial endotoxin on protecting copper-deficient rats from hyperoxia. 375 84


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