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 equilibrium binding of ([125I]ceruloplasmin) ([125I]CP) to a specific receptor of human erythrocytes was investigated. It was shown that reaching the binding equilibrium is a slow process. A strong dependence of binding on Ca2+ concentration (from 0.1 to 1 mM) was revealed; the optimal values were achieved at millimolar concentrations of Ca2+.Mg2+ do not affect the binding of [125I]CP. Under conditions of optimal binding (0.01 M Tris-HCl buffer pH 7.4 containing 158 mM NaCl and 1 mM Ca2+, 4 degrees C), the values of constants for [125I]CP binding to intact erythrocytes (Kd = 1.0 nm) and to membrane fragments (Kd = 0.8 nM) as well as the number of binding sites (16.3 X 10(-15) mol per 40,000,000 erythrocytes) were determined. No ceruloplasmin transport across the erythrocyte membrane was observed. This finding and the similarity of Kd values for ceruloplasmin binding to membrane fragments and to intact erythrocytes indicate that the effect of ceruloplasmin on human erythrocytes is due to the protein molecule interaction with membrane receptors.
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PMID:[Characteristics of ceruloplasmin interaction with a specific receptor of human erythrocytes]. 283 96

Distribution of the transcriptionally active sequences in rat liver chromatin DNA fragments released from chromatin sites with different sensitivity to endogenous Ca2+, Mg2+-DNases was studied by the dot hybridization method with cloned DNA-probes. The internal fragment of the rat chromosomal ceruloplasmin gene containing coding sequences and the promoter region of the metallothionein-I gene were specific probes for the transcriptionally active liver chromatin. cDNA of beta-globin gene was the control for the transcriptionally inert DNA sequences. Mononucleosomal length, DNA (175-215 bp) formed in the course of mile nuclease digestion (less than 1% mononucleosomes and acid-soluble material) was 3-6-fold enriched in transcribed sequences of the ceruloplasmin gene as compared to oligonucleosomal DNA fragments produced in the same digestion conditions (fractions containing fragments 750-850 and greater than 2000 bp). The relative amount of the ceruloplasmin gene in mononucleosomal length DNA formed during the mild digestion was 12-25-fold greater than in total rat liver DNA and 25-50-fold greater than in the mononucleosomal DNA (150-175 bp) produced in the course of extensive digestion (80-85% mononucleosomes and 15-20% acid-soluble material) by endogenous Ca2+, Mg2+-DNases. The promoter metallothionein-I gene sequences exhibited the same distribution among chromatin fragments as the coding ceruloplasmin gene sequence. Distribution of the nontranscribed beta-globin sequences in liver chromatin DNA fragments produced at different stages of nuclease digestion was not related to chromatin sensitivity to endogenous DNases. These sequences were distributed similarly in different DNA size classes and total DNA.
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PMID:[Distribution of transcription-active DNA sequences in rat liver chromatin during fragmentation with endogenous DNAses]. 357 99

This study describes the carioprotective effect of ceruloplasmin (CAS 9031-37-2) against oxygen free radical injury, as indicated by several biochemical indicators and some cardiodynamic variables. Isolated rat hearts (n = 4-8, p < 0.05, for each experimental point) in Langendorff preparation were exposed to oxygen free radicals generated by electrolysis (10 mA) in the absence and the presence of 0.25 mumol/l purified ceruloplasmin and denaturated ceruloplasmin, in Krebs-Henseleit perfusion solutions. Biochemical indicators (noradrenaline, malondialdehyde, creatine-kinase, lactate dehydrogenase, aspartate aminotransferase, Ca2+ and Mg2+) as well as the electrocardiogram and the left ventricular pressure (LVP), were altered by oxygen free radicals formation, denoting major cellular and tissular damages in the nontreated hearts. Ceruloplasmin exhibited a cardioprotective effect and prevented the oxygen free radical-induced release of noradrenaline, indicating that it can also protect the sympathetic nerve endings from oxygen free-radical injury. Purified ceruloplasmin, a circulating extracellular antioxidant and oxygen free radical scavenger, seems to be an effective heart protective agent against myocardial and neuronal injuries generated by oxygen free radicals.
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PMID:Protection of myocardial tissue against deleterious effects of oxygen free radicals by ceruloplasmin. 777 45

The copper-glutathione complex (Cu(I)-GSH) efficiently acted in vitro as the source of Cu(I) in the reconstitution of apoceruloplasmin. Copper was found to reinstate in the various sites in a multistep process, with metal entry into the protein in a first phase, and a second step involving conformational changes of the protein leading to the recovery of the native structural and functional properties. This latter phase was found to be strongly facilitated by Mg2+ or Ca2+ and by ATP. Both Mg2+ and ATP had to be present for optimal reconstitution. These results may shed some light on the mechanisms governing the biosynthesis of ceruloplasmin in vivo. Cu(I)-GSH was the only complex able to reconstitute ceruloplasmin at neutral pH. Glutathione may thus function to shuttle the metal from the membrane copper pump, as the Wilson disease ATPase, and ceruloplasmin in the secretory compartments of the cell. The finding that ceruloplasmin acquires the native conformation after metal entry through a complex pathway triggered by Mg2+ and ATP suggests that they may act as physiological modulators of this process in vivo.
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PMID:Reconstitution of ceruloplasmin by the Cu(I)-glutathione complex. Evidence for a role of Mg2+ and ATP. 856 46

Binding of calcium to human and sheep ceruloplasmin was investigated by metal substitution with manganese and competitive displacement of bound manganese by calcium monitored by electron paramagnetic resonance spectroscopy. The Kd for calcium was found to be 1.4 mM. Magnesium also bound to ceruloplasmin, with Kd = 0.3 and 0.7 mM for the human and sheep protein, respectively. The thermal stability of ceruloplasmin, as studied by differential scanning calorimetry, was affected by calcium but not by magnesium. A considerable increase of the Tm value, from 73.8 to 83.1 degrees C, was observed for sheep ceruloplasmin in the presence of calcium. The Tm value of the human protein was only slightly altered by calcium (from 85.1 to 87 degrees C). The interaction of ceruloplasmin with the chromatographic material used for its isolation, Sepharose 4B derivatized with chloroethylamine, was weakened by calcium. This allowed us to set up a novel purification scheme that made it possible to efficiently isolate ceruloplasmin and prothrombin from plasma with the same single-step chromatography.
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PMID:Divalent cation binding to ceruloplasmin. 857 94

We previously found an inverse correlation between platelet ionized magnesium concentration ((Mg2+)i) and serum total cholesterol concentration in normal male but not female subjects. In the present study, we determined the platelet (Mg2+)i by using a fluorescent ionized magnesium (Mg2+) indicator, FURAPTRA, and measured the serum concentrations of the following: total cholesterol; very-low-density lipoprotein cholesterol (VLDL-C); low-density lipoprotein cholesterol (LDL-C); high-density lipoprotein cholesterol (HDL-C); antioxidized low-density lipoprotein (LDL) autoantibodies; lipoprotein(a); apolipoproteins A-I (apo A-I) and B (apo B); triglycerides; estradiol-17 (E2); ceruloplasmin (Cp); and selected electrolytes, including total and ionized magnesium and calcium and total protein and albumin. In men, but not in women, platelet (Mg2+)i significantly inversely correlated with serum total cholesterol (r = -0.52, p < 0.02), LDL-C (r = -0.54, p < 0.009 by a "direct" method; r = -0.40, p < 0.05 by an electrophoretic method), and apo B (r = -0.42, p < 0.04). We found no significant correlations between platelet (Mg2+)i and any other variables, including serum total and ionized magnesium, antioxidized LDL autoantibodies, Cp, and E2. We speculate that decreased platelet (Mg2+)i is a possible marker for platelet membrane alterations that may affect platelet involvement in thrombosis and atherogenesis.
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PMID:Gender-specific correlation of platelet ionized magnesium and serum low-density-lipoprotein cholesterol concentrations in apparently healthy subjects. 901 95

In an attempt to identify components of a ferric citrate uptake system in Pseudomonas aeruginosa, a mutant library of a siderophore-deficient strain (IA614) was constructed and screened for defects in citrate-promoted growth in an Fe-restricted medium. A mutant disrupted in gene PA3901, encoding a homologue of the outer-membrane ferric citrate receptor, FecA, of Escherichia coli (FecA(E.c.)), was recovered and shown to be deficient in citrate-promoted growth and citrate-mediated Fe uptake. A mutant disrupted in gene PA4825, encoding a homologue of the MgtA/MgtB Mg2+ transporters in Salmonella enterica, was similarly deficient in citrate-promoted growth, though this was due to a citrate sensitivity of the mutant apparently resulting from citrate-promoted acquisition of Fe2+ and resultant oxidative stress. Consistent with citrate delivering Fe to cells as Fe2+, a P. aeruginosa mutant lacking the FeoB Fe2+ transporter homologue, PA4358, was compromised for citrate-promoted growth in Fe-restricted medium and showed markedly reduced citrate-mediated Fe uptake. Subsequent elimination of two Fe3+ transporter homologues, PA5216 and PA4687, in the feoB mutant failed to further compromise citrate-promoted growth or Fe uptake, though the additional loss of pcoA, encoding a periplasmic ferroxidase implicated in Fe2+ acquisition, completely abrogated citrate-mediated Fe uptake. Fe acquisition mediated by other siderophores (e.g. pyoverdine) was, however, unaffected in the quadruple knockout strain. These data indicate that Fe delivered to P. aeruginosa by citrate is released as Fe2+, probably in the periplasm, prior to its transport into cells via Fe transport components.
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PMID:Citrate-mediated iron uptake in Pseudomonas aeruginosa: involvement of the citrate-inducible FecA receptor and the FeoB ferrous iron transporter. 1911 71

Oxidative stress is one of the common causes in etiopathogenesis of attention deficit hyperactivity disorder (ADHD). Hence, the salivary levels of protein thiols, ceruloplasmin, magnesium and pseudocholinesterase were estimated in children with ADHD. The symptoms of ADHD were identified using Conner's rating and DSM IV criteria. Saliva was collected and assessed for the levels of protein thiols, ceruloplasmin, magnesium and pseudocholinesterase, spectrophotometrically. It was also checked for pH and the flow rate was noted down. There was a significant increase (P < 0.001) in the salivary protein thiols and pseudocholinesterase levels in ADHD children when compared to controls. Ceruloplasmin levels did not show any significant change. Magnesium levels were significantly decreased (P < 0.001) in cases when compared to controls. Further, a receiver operating characteristic curve for validity of the biochemical parameters in saliva of ADHD children indicated a sensitivity and specificity above 90% for protein thiols and magnesium values. Our study shows that protein thiols, magnesium, and pseudocholinesterase might have a role in the pathogenesis of ADHD and saliva can be effectively used as a non-invasive tool for evaluation of such children.
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PMID:Altered biochemical parameters in saliva of pediatric attention deficit hyperactivity disorder. 2196 65