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 effects of transition metals on nonenzymatic and ceruloplasmin catalyzed epinephrine oxidation were investigated by studying rates of epinephrine oxidation in purified buffers and in the presence of metal chelating agents. We found that epinephrine does not "autoxidize" in sodium chloride solutions prepared with deionized water that was further purified by chromatography over Chelex 100 resin prior to use. Epinephrine was oxidized rapidly in sodium chloride prepared with tap water (1.20 +/- 0.12 nmoles/min) or in deionized water (0.40 +/- 0.80 nmoles/min), but this oxidation was prevented by the addition of Desferal, a potent metal chelating agent. Epinephrine oxidation was enhanced upon the addition of ceruloplasmin, and this oxidation rate could be slowed, but not eliminated, by the addition of Desferal. If epinephrine solutions were preincubated for 72 hours with Desferal prior to ceruloplasmin addition, however, no oxidation was observed. Epinephrine was shown to form colored complexes with both iron and copper at pH 7.0. The Fe(III)-epinephrine complex was much more stable than was the Cu(II)-epinephrine complex. Oxygen consumption studies of ceruloplasmin catalyzed epinephrine oxidation showed that copper was a better promoter of epinephrine oxidation than was iron, suggesting that ceruloplasmin-catalyzed epinephrine oxidation results from adventitious copper bound to the purified enzyme. In light of these results, the physiological relevance of ceruloplasmin catalyzed oxidation of biogenic amines may be minor.
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PMID:The role of metals in the enzymatic and nonenzymatic oxidation of epinephrine. 849 1

Purified diets deficient in copper and based on either sucrose, egg white, and corn oil or sucrose, casein, corn starch, and safflower oil were fed to young rats. Graded amounts of copper were supplied in drinking solutions with the former diet and by addition to the latter diet; anatomical, chemical, and physiologic responses were compared. Three micrograms Cu/ml and 5 micrograms Cu/g were sufficient to maximize the direct assessments of copper nutriture (copper in blood plasma, heart, and liver). Nutritional adequacy by indirect criteria (heart iron, plasma ceruloplasmin, heart weight divided by body weight, plasma cholesterol, and body weight) generally was found with 3 micrograms/ml and 4 micrograms/g. Anemia was an insensitive characteristic of deficiency. Liver iron was minimized by 4 micrograms Cu/ml and 5 micrograms Cu/g. Most of the differences in response to copper added to water in comparison to copper added to diet probably were explained by the lower amount of copper in the casein diet. Responses to the two dietary regimens were similar when variables were plotted against liver copper. Correlation coefficients with liver copper ranged from 0.52 for liver zinc to 0.96 for heart iron. Liver copper probably is the best index of copper nutriture.
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PMID:Comparative responses of rats to different copper intakes and modes of supplementation. 850 63

NMR evaluation of skin rat inflammation, 24 h after UVB exposition and 48 h after vesicatory (croton oil) application, shows significant variations of relaxation times. Cutaneous T1 and T2 are enhanced in both cases, and plasmatic T2 is increased in croton oil inflammation. At the same time, these two inflammations induce in plasma: a significant increase in ceruloplasmin (respectively 70 and 42%); a decrease in iron transferrin (48 and 53%) and iron saturation (%) of transferrin (53 and 68%); an increase in the protein level of 45% for croton oil treated animals. In skin, for each inflammation, T1 is significantly correlated with cutaneous water content (r = 0.6 and r = 0.35). T1 appears to be more representative than T2 of hydration and molecular dynamic modifications, induce by oedema formation. In plasma, T2 is significantly correlated with ceruloplasmin (4 = 0.67) and protein level (r = 0.45), and reflects more specially than T1 the modifications of the medium composition. The decrease in T2 may be the expression of the diminution of the medium water molecules' mobility, in connection with the increase in protein concentration.
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PMID:[Proton magnetic resonance of plasma in the evaluation of systemic effects of cutaneous inflammation in rats]. 859 11

1. Male albino rats of 21 days age were exposed to 10 p.p.m. cadmium (CdCl2 salt) in drinking water, ad libitum, for 90 days. It increased the brain cadmium levels by 76% (P < 0.05) and 165% (P < 0.001) respectively at 30 and 90 days of exposure compared to controls. 2. Cadmium increased blood-brain barrier permeability of fluoroscein dye (24%, P < 0.02) and the levels of brain microvessel malondialdehyde (31%, P < 0.01) at 90 days of exposure. However, these parameters did not alter significantly at 30 days of exposure. 3. Increased activities of microvessel superoxide dismutase (18%, P < 0.02), glutathione peroxidase (20%, P < 0.01) and catalase (28%, P < 0.01) were observed at 30 days of exposure. 4. The continuation of the Cd treatment for 90 days decreased the levels of superoxide dismutase (30%, P < 0.001), glutathione peroxidase (23%, P < 0.005), catalase (25%, P < 0.005), glutathione reductase (18%, P < 0.02), vitamin E (20%, P < 0.01), glutathione (26%, P < 0.01), ascorbic acid (18%, P < 0.05) and ceruloplasmin (13%, P < 0.05) in the microvessal preparation compared to controls. 5. It appears that Cd-induced blood-brain barrier dysfunction may be related to the depletion of microvessel antioxidant substances along with increase in lipid peroxidation at 90 days of exposure.
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PMID:Cadmium-induced alterations in blood-brain barrier permeability and its possible correlation with decreased microvessel antioxidant potential in rat. 873 64

The effect of curcumin on the biochemical changes induced by isoproterenol (ISO) administration in rats was examined. ISO (300 mg Kg-1 administered subcutaneously twice at an interval of 24 h) caused a decrease in body weight and an increase in heart weight, water content as well as in the levels of serum marker enzymes viz creatine kinase (CK), lactate dehydrogenase (LDH) and LDH1 isozyme. It also produced electrocardiographic changes such as increased heart rate, reduced R amplitude and ST elevation. Curcumin at a concentration of 200 mg.Kg-1, when administered orally, showed a decrease in serum enzyme levels and the electrocardiographic changes got restored towards normalcy. Myocardial infarction was accompanied by the disintegration of membrane polyunsaturated fatty acids expressed by increase of thiobarbituric acid reactive substance (TBARS), a measure of lipid peroxides and by the impairment of natural scavenging, characterized by the decrease in the levels of superoxide dismutase, catalase, glutathione peroxidase, ceruloplasmin, alpha tocopherol, reduced glutathione (GSH) and ascorbic acid. The oral pretreatment with curcumin two days before and during ISO administration decreased the effect of lipid peroxidation. It was shown to have a membrane stabilizing action by inhibiting the release of beta-glucuronidase from nuclei, mitochondria, lysosome and microsome. Curcumin pre- and co-treatment decreased the severity of pathological changes and thus, could have a protective effect against the damage caused by myocardial infarction (MI).
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PMID:Protective role of curcumin against isoproterenol induced myocardial infarction in rats. 885 58

The aim of this study was to investigate whether or not the human immune system can be activated by a noninfectious stimulus, thereby improving the physiological status of the individual. The effect of a single cold water immersion (14 degrees C for 1 h) on the immune system of athletic young men, monitored immediately after immersion, was minimal. With the continuation of the cold water immersions (three times a week for a duration of 6 weeks) a small, but significant, increase in the proportions of monocytes, lymphocytes with expressed IL2 receptors (CD25) and in plasma tumour necrosis factor alpha content was induced. An increase in the plasma concentrations of some acute phase proteins, such as haptoglobin and haemopexin, was also observed. After 6 weeks of repeated immersions a trend towards an increase in the plasma concentrations of IL6 and the amount of total T lymphocytes (CD3), T helper cells (CD4), T suppressor cells (CD8), activated T and B lymphocytes (HLA-DR) and a decrease in the plasma concentration of alpha 1-antitrypsin was observed. Concentrations of IL1 beta, neopterin, C-reactive protein, orosomucoid, ceruloplasmin, macroglobulin, immunoglobulins (IgG, IgM, IgA) and C3, C4 components of the complement, as well as the total number of erythrocytes, leucocytes, granulocytes and neutrophils showed no significant changes after the repeated cold water immersions. It was concluded that the stress-inducing noninfectious stimuli, such as repeated cold water immersions, which increased metabolic rate due to shivering the elevated blood concentrations of catecholamines, activated the immune system to a slight extent. The biological significance of the changes observed remains to be elucidated.
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PMID:Immune system of cold-exposed and cold-adapted humans. 892 15

The effect of moderately high dietary zinc (Zn) on the activities of plasma (PL) ceruloplasmin (CP), and PL and erythrocyte (RBC) copper (Cu), Zn superoxide dismutase (SOD) was determined in weanling rats fed Cu-deficient (DEF; < 1 mg Cu/kg), marginal (MAR; 2 mg Cu/kg), or control (CON; 5 mg Cu/kg) copper diets containing normal or high Zn (HZn; 60 mg/kg) for 4 wk and supplemented with oral Cu (CuS; 5 mg/L) in drinking water for 0, 1, 3, or 7 d. PL Cu decreased (67% compared to CON; p < or = 0.05) in the DEF and increased to control level after 3 d of CuS; increased in the MAR group after 1 d of CuS. HZn reduced overall PL Cu by 27% in all groups, but did not alter the linear increase in PL Cu between 0 and 3 d of Cu S. PL CP activity altered concomitantly with PL Cu levels: The time course of increase in CP activity after 0-3 d of CuS was not influenced by HZn in the diet and CP declined in the DEF group by 92%. There was no correlation between dietary Cu level and PL CP. PL SOD activity decreased by 46% (p < or = .05) in the DEF group, increased to control activity after 1 d of CuS and declined slightly after 7 d; MAR diet did not alter PL SOD. HZn diet increased PL SOD activity in all groups by 150%, reduced activity in the DEF and MAR groups by 65 and 37% and delayed the recovery of PL SOD after CuS. RBC SOD declined in the DEF and MAR groups by 56 and 33% (p < or = 0.05) and did not respond to CuS; HZn diet did not influence RBC SOD activity. These data indicate that moderately high Zn in the diet reduces PL Cu, but not PL CP activity or the recovery of PL Cu or CP activity after oral CuS of Cu-deficient rats, modifies the response of PL SOD to dietary Cu, but does not influence RBC SOD activity.
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PMID:Effect of high dietary zinc on plasma ceruloplasmin and erythrocyte superoxide dismutase activities in copper-depleted and repleted rats. 897 59

Cadmium administered to rats per os is accumulated in the duodenal mucosa in the form of metallothionein (MT). Therefore, this toxic metal can influence the efficiency of essential metal absorption, especially their concentration in the maternal organism, which plays an essential role during fetal development. The aim of this study is to elucidate the mechanism of the origin of Zn, Cu, and Fe deficiency in fetal rat livers after maternal exposure to cadmium in drinking water and to investigate the roles of MT and ceruloplasmin (Cp) in this phenomenon. Cadmium was given to pregnant dams exposed for 0-20 days of gestation in drinking water at concentrations of 6. 25-100 microg Cd/ml. After cessation of exposure, at the lowest dose, a decrease in Cu and Fe concentrations in the duodenal mucosa was found. Simultaneously, diminution in concentration of two cited metals and Cp activity in serum of dam blood was noted. The lowest dose of cadmium developed a drop tendency in microsomal fetal liver iron. Significant correlations were observed between fetal liver Cu contents and Cp activity in serum of dams and Cu concentrations in serum of dams. Diminished Cp activity in serum of dams is related to reduced availability of Cu and Fe in fetuses. In conclusion, it is suggested that the mechanism of Cu and Fe deficit content in fetuses is based on the diminution of absorption of these metals by dam intestines exposed to cadmium on the reduction of metal concentrations in blood serum and, in consequence, their decreasing availability in fetuses.
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PMID:Cadmium interaction with essential metals (Zn, Cu, Fe), metabolism metallothionein, and ceruloplasmin in pregnant rats and fetuses. 900 5

1,1'-dimethylferricinium (DMFe+), a stable and pH-insensitive blue dye, was prepared via enzymatic oxidation of a 1,1'dimethyl-ferrocene (DMFe):2-hydroxypropyl-beta-cyclodextrin (HPCD) water-soluble inclusion complex, using bilirubin oxidase immobilized onto porous aminopropyl glass beads via glutaraldehyde activation. In the presence of glucose, DMFe+ was reduced to DMFe by reacting with the reduced glucose oxidase (FADH2), and the absorbance decrease was followed at 650 nm. In acetate pH 5.2 buffer, the response to glucose in blood serum was nonlinear, especially in the low concentration range, because of a competition for the reduced glucose oxidase between the DMFe+ dye and oxygen. At this pH, endogenous ceruloplasmin was also observed to oxidize residual DMFe (16%) in the dye preparation, causing an increase in absorbance at 650 nm. An assay protocol was then developed using maleate buffer, pH 6.5, to overcome these interferences as well as mutarotation of alpha-D-glucose. The results obtained for glucose in the blood serum samples agreed well with those of the reference hexokinase/glucose-6-phosphate dehydrogenase method.
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PMID:An improved enzymatic assay for glucose determination in blood serum using a 1,1'-dimethylferricinium dye. 910 Mar 58

Mammalian ferritins are 24-mers assembled from two types of polypeptide chain which provide the molecule with different functions. H(eavy) chains catalyse the first step in iron storage, the oxidation of iron(II). L(ight) chains promote the nucleation of the mineral ferrihydrite enabling storage of iron(III) inside the protein shell. We report here the comparison of the three-dimensional structures of recombinant human H chain (HuHF) and horse L chain (HoLF) ferritin homopolymers, which have been refined at 1.9 A resolution. There is 53% sequence identity between these molecules, and the two structures are very similar, the H and L subunit alpha-carbons superposing to within 0.5 A rms deviation with 41 water molecules in common. Nevertheless, there are significant important differences which can be related to differences in function. In particular, the centres of the four-helix bundles contain distinctive groups of hydrophilic residues which have been associated with ferroxidase activity in H chains and enhanced stability in L chains. L chains contain a group of glutamates associated with mineralisation within the iron storage cavity of the protein.
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PMID:Comparison of the three-dimensional structures of recombinant human H and horse L ferritins at high resolution. 915 81


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