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)

Ceruloplasmin as a modulator was used for the first time in the clinical practice in 30 patients with gastric cancer in the course of postoperative intraabdominal adjuvant chemotherapy. It was established that ceruloplasmin was well tolerated by the patients and its use during polychemotherapy is accompanied by normalization of the levels of natural ceruloplasmin and iron in the blood serum that are usually reduced in patients with gastric cancer, reduces activation of lipid peroxidation and improves the course of postoperative period. Ceruloplasmin possesses a week immunomodulating action in polychemotherapy which is expressed in the increase of the percentage content of T-lymphocytes. Use of ceruloplasmin tended to improve the functional state of the cardiovascular system.
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PMID:[The use of ceruloplasmin in combination with adjuvant polychemotherapy in stomach cancer]. 204 39

Coagulation factors V and VIII are substrates for activated protein C. Binding sites for the protease have been localized to homologous sequences within the terminal A domains of these proteins. Since ceruloplasmin contains significant sequence homology to these domains, a study was undertaken to determine whether ceruloplasmin was an activated protein C-binding protein. Ceruloplasmin was observed to inhibit the activated protein C-catalyzed inactivation of both factor Va and factor VIII. Searches of the ceruloplasmin sequence revealed a decapeptide sequence, HAGMETTYTV (residues 1028-1037) that shares 60 and 40% sequence identity with the activated protein C binding sequence in factors VIII and V, respectively. This peptide also inhibited factor Va inactivation and in addition was observed to enhance the amidolytic activity of activated protein C. The ferrous oxidase activity of ceruloplasmin was stimulated 5-fold by activated protein C, and this effect was negated by the peptide HAGMETTYTV. These results indicate that these conserved sequences of ceruloplasmin and factors V and VIII interact with activated protein C and suggest that this region may be important in the regulation of this anticoagulant protein.
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PMID:Characterization of an interaction between protein C and ceruloplasmin. 210 10

Ceruloplasmin oxidation by hypochlorite results in the bleaching of the protein solution; the oxidase activity remains, however, unchanged. Hypochlorite exerts a complex effect on the protein activity. After a short-term (5 min) incubation with hypochlorite the enzyme activity increases with a further progressive decrease. It is supposed that the oxidase activity of ceruloplasmin is not coupled with copper ions of the first type responsible for the blue staining of the protein solution. The low susceptibility of functional properties of ceruloplasmin to hypochlorite raises its potency as an antioxidative agent.
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PMID:[Oxidation of ceruloplasmin by hypochlorite. The loss of blue color and preservation of oxidase activity]. 216 6

The hybridoma technology was used to produce monoclonal antibodies to human ceruloplasmin. The antibodies were found to be related to Ig G1. Using these monoclonal antibodies for PAP-ELISA of ceruloplasmin, it was possible to determine 10(-11) M of the protein. Monoclonal antibodies coupled to CNBr-Sepharose were used for the rapid one-stage purification of ceruloplasmin from human placental serum. Ceruloplasmin obtained by this method contained no type 2 copper normally detected in protein preparations by conventional methods.
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PMID:[Monoclonal antibodies to ceruloplasmin and their use for immunoenzyme assay of this protein]. 218 38

Stress such as inflammation produces an acute phase response that includes elevated levels of ceruloplasmin, the main copper component of plasma. Inflammatory effects on cellular copper enzyme activity levels are largely unknown. Cu-Zn superoxide dismutase (SOD) activities in liver, the main site of ceruloplasmin secretion, decreased with turpentine-induced inflammation (0.1 mL, intramuscular, leg) in rats fed any of three copper levels (adequate = 6 mg/kg, marginal = 2.5 mg/kg and deficient less than 0.5 mg/kg). Ceruloplasmin activities rose significantly with inflammation in the adequate and marginal groups but not in the deficient animals. Hepatic Cu-Zn SOD immunoreactive protein levels were unaffected by copper status or inflammatory state. Erythrocyte Cu-Zn SOD activities were influenced by dietary copper but not inflammation. An additional group of rats fed 15 mg copper/kg did not show a turpentine-induced decrease in liver Cu-Zn activity levels. Inflammatory effects on other copper enzyme activities did occur as evidenced by increases in ceruloplasmin and decreases in serum extracellular SOD. In conclusion, an acute phase response in rats increased the amount of dietary copper required to maintain hepatic Cu-Zn SOD activity at levels equal to those of nonstressed, copper-adequate rats. Rat erythrocyte Cu-Zn SOD activities provided a blood measurement reflective of copper intake with or without stress, but these values did not reflect decreases in liver Cu-Zn SOD activities after 3 d of inflammation.
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PMID:Effects of inflammation and copper intake on rat liver and erythrocyte Cu-Zn superoxide dismutase activity levels. 221 50

Cigarette smokers have a biochemical defect in the ferroxidase activity of their serum ceruloplasmin. Ceruloplasmin is one of the main serum antioxidants, and this defect in ferroxidase activity most likely accounts for the previously observed decrease in smoker serum antioxidant activity. This defect may be related to oxidation of ceruloplasmin in the lung. We hypothesized that vitamin E might be able to reverse the decrease in smoker ferroxidase activity and thus restore serum antioxidant activity. To test this hypothesis, we administered high-dose vitamin E to a group of young asymptomatic cigarette smokers (n = 8). Although serum levels of vitamin E significantly increased (8.7 +/- 0.8 to 20.6 +/- 3.1 micrograms/ml, p = 0.01), the ferroxidase activity of smoker serum (0.139 +/- 0.02 (0.139 +/- 0.02 to 0.144 +/- 0.03 U/ml, p = 0.824), and the antioxidant activity of serum (45.8 +/- 7.2 to 51.6 +/- 8.4%, p = 0.587) remained unchanged. Thus, at the current dose and duration of supplementation, vitamin E was unable to reverse the defect in smoker serum ferroxidase activity and thus unable to augment the antioxidant capacity of the serum.
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PMID:Failure of high-dose vitamin E to correct ceruloplasmin ferroxidase deficiency in cigarette smokers. 224 Aug 29

The influence of ceruloplasmin on cell proliferation in regeneration liver of the rat has been studied. Ceruloplasmin stimulates cell proliferation in regeneration liver increasing functional activity of the mononuclear phagocytes.
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PMID:[The effect of ceruloplasmin on hepatocyte proliferation in the regenerating rat liver]. 228 30

Lipid peroxidation products were measured in the plasma of 24 kidney transplant patients and 12 healthy volunteers (controls) by: (1) 2-thiobarbituric acid assay and (2) the intensity of fluorescence products of malonaldehyde cross-linked proteins. Plasma levels of creatinine, ceruloplasmin, transferrin, prealbumin, albumin and total protein were also measured. Elevated lipid peroxidation products and lowered transferrin levels were observed in transplant patients compared to controls. Ceruloplasmin levels were slightly but significantly elevated in recent transplant recipients (less than 6 months, n = 12, Group A) while no difference was observed between older transplant recipients (greater than 6 months, n = 12, Group B) and controls. Serum, creatinine levels were also slightly but significantly elevated in both groups of patients compared to controls. Serum prealbumin, albumin and total protein levels in both groups of transplant recipients were not different from controls or reference range values.
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PMID:Elevated lipid peroxidation products and depleted transferrin levels in the plasma of kidney transplant recipients. 229 70

cDNA clones corresponding to rat ceruloplasmin were isolated from newborn rat lung and liver cDNA libraries and the nucleotide sequence was obtained. The derived amino acid sequence of rat ceruloplasmin is 93% homologous to the corresponding human sequence and contains a 19-amino acid leader peptide plus 1040 amino acids of mature protein. Southern blot analysis indicates that the ceruloplasmin gene exists as a single copy in the rat haploid genome. Using these cDNA clones in RNA blot analysis, a single 3.7-kilobase ceruloplasmin-specific transcript is detected in fetal rat liver and lung by day 15 of gestation. During fetal development the abundance of this transcript increases selectively in these two tissues and at birth is 60% of that found in the adult liver. Postnatally the temporal pattern of ceruloplasmin gene expression in lung and liver differs. Within the first 3 weeks postpartum ceruloplasmin mRNA content decreases in lung to undetectable levels, while that in the liver reaches adult levels. Primer extension reveals a single identical start site of ceruloplasmin gene transcription in lung and liver and biosynthetic studies indicate that each tissue synthesizes a ceruloplasmin protein which is qualitatively similar to that synthesized by adult liver. Ceruloplasmin mRNA is also detected in human fetal lung explant and a human lung adenocarcinoma cell line suggesting that a similar pattern of expression occurs in the developing human lung. These data indicate that lung is the predominant extrahepatic site of ceruloplasmin gene expression during fetal development and suggest that this protein may play a previously unappreciated role in lung development or pulmonary antioxidant defense.
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PMID:Primary structure of rat ceruloplasmin and analysis of tissue-specific gene expression during development. 233 46

Ceruloplasmin from the turtle Caretta caretta was isolated to purity by using the single-step procedure recently developed by us to purify sheep and chicken ceruloplasmin. It has a Mr of ca. 145,000 and a total copper content of 5.1 +/- 0.2 atoms of copper per molecule, 50% of which are detectable by EPR. The spectroscopic features include an absorption maximum at 603 nm in the electronic spectrum and the total absence of any resonance attributable to Type 2 copper in the EPR spectrum. Turtle ceruloplasmin was found to be unusually resistant to aging and proteolysis, when compared to ceruloplasmins isolated from other species. p-Phenyl-endiamine oxidase activity measurements revealed an unusually low catalytic efficiency, while the kinetic parameters of Fe(II) oxidation were consistent with those reported for other species of ceruloplasmin.
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PMID:Unusual stability properties of a reptilian ceruloplasmin. 233 57


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