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)

1. Male rats were maintained from wearing to between 4 and 16 weeks of age on a semisynthetic diet which was deficient in copper. 2. Methyl esters of fatty acids from adipose tissue of the rats were analysed by gas-liquid chromatography and the desaturase activity of liver microsomes, with [1-14C]=stearic acid as the substrate, was determined. Liver and plasma Cu concentration, cytohrome c oxidas (EC 1.9.3.I) activity and caeruloplasmin activity were determined as indices of Cu status. 3. Cu deficiency was associated with decreased mono-unsaturated:saturated ratios for C16 and C18 fatty acids from subcutaneous adipose tissue and decreased desaturase activity for liver microsomes. When Cu-deficient rats were given free access to the Cu-adequate diet or were injected intraperitoneally with an aqueous solution of CuSO4, that is, when the animals were related with Cu, the indices of Cu status, and desaturase activity for liver microsomes returned to values found in control animals. 4. When Cu or a Cu-chelator (Neocuproine) was added to microsomes, there was no effect on the activity of the desaturase enzyme system; the stability of the desaturase was not affected by Cu. 5. These results are indicative of an involvement of Cu in the desaturase reaction. It is suggested that the site of this involvement could be the terminal component of the microsomal electron transport chain.
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PMID:Effect of dietary copper deficiency. in the rat on fatty acid composition of adipose tissue and desaturase activity of liver microsomes. 16

Inflammation, induced by turpentine (0.1 ml i.m.), protected against carbon tetrachloride (CCl4)-induced hepatotoxicity based on serum activities of sorbitol dehydrogenase. Inflammation was confirmed by elevated serum ceruloplasmin activities, and was associated with high hepatic levels of metallothionein, a zinc protein proposed to protect against CCl4-induced injury. Inflammation suppressed cytochrome P-450 activities, but this was not associated with protection against CCl4-promoted liver microsomal injury as assessed by glucose-6-phosphatase activity loss. Thus, protection against plasma membrane injury did not result primarily from depressed microsomal activation of CCl4. Each effect of inflammation reported here resembled effects of zinc injections. This similarity strengthens the hypothesis that metallothionein protects against CCl4-induced hepatic plasma membrane injury.
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PMID:Inflammation, an inducer of metallothionein, inhibits carbon-tetrachloride-induced hepatotoxicity in rats. 131 82

In a previous study (Minotti, G., and Ikeda-Saito, M. (1991) J. Biol. Chem. 266, 20011-20017) we demonstrated the existence of a M(r) 66,000 microsomal iron protein (MIP) which stimulates NADPH oxidation by shunting electrons from NADPH-cytochrome P-450 reducase to its bound Fe(III). In the present study, purified MIP was depleted of iron and the apoMIP was examined for its ability to incorporate Fe(III) upon an incubation with Fe(II). It was found that apoMIP had an oxygen-dependent ferroxidase activity coupled with the incorporation of Fe(III). The reconstituted MIP exhibited a Fe(III) content and an NADPH oxidation activity similar to those of native MIP. However, the reconstitution of MIP from apoMIP and Fe(II) had to be performed in the presence of detergents to prevent the formation of protein aggregates and the oxidative incorporation of an iron which could not react with NADPH-cytochrome P-450 reductase. This redox inactive iron was probably bound nonspecifically to artifactual sites formed by the protein aggregates.
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PMID:Fe(II) oxidation and Fe(III) incorporation by the M(r) 66,000 microsomal iron protein that stimulates NADPH oxidation. 155 97

An experiment was conducted with growing rats to investigate the effects of feeding excessive specific L-amino acids for 8 days on serum and tissue cholesterol, alpha-tocopherol, ascorbic acid, and copper, and on liver microsomal cytochrome P-450. To a 10% casein diet were added 4% L-methionine, 5% L-cystine, 5% L-histidine, 5% L-threonine, 5% L-tryptophan, 5% L-phenylalanine, 5% L-tyrosine, 6% L-valine, 7% L-isoleucine, 7% L-lysine, or 8% L-leucine. Excessive cystine and histidine increased serum cholesterol and alpha-tocopherol. Excessive cystine and methionine increased liver and kidney alpha-tocopherol and ascorbic acid. Excessive tyrosine and phenylalanine caused a marked increase in serum copper and ceruloplasmin activity, whereas excessive cystine, methionine, and histidine caused a decrease in the ceruloplasmin activity. Excessive histidine increased liver cytochrome P-450, whereas excessive tyrosine markedly decreased liver cytochrome P-450.
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PMID:Effects of dietary excess amino acids on the concentrations of cholesterol, alpha-tocopherol, ascorbic acid, and copper in serum and tissues of rats. 209 20

This article reports correlations among gamma-glutamyltransferase (GGT), fetal haemoglobin (fH), alpha-fetoprotein, 5'-nucleotidase, ceruloplasmin, and direct, indirect, and total bilirubin in the serum of blood taken from the umbilical cords of 128 newborns delivered after 37-42 weeks of gestation. GGT was significantly correlated with alpha-fetoprotein, but not with direct bilirubin, indirect bilirubin, total bilirubin, fH, or %fH. Neither fH nor %fH were correlated with alpha-fetoprotein, but there was highly significant negative correlation between both fH and %fH on the one hand, and gestational age and weight at birth on the other. The %fH was also correlated negatively with ceruloplasmin, which in turn exhibited negative correlation with alpha-fetoprotein. The predominant forms of GGT in umbilical cord and adult sera were, respectively, those with alpha 1 and alpha 2 mobility. In cord sera, delipidation with n-butanol brought about loss of GGT activity and a shift from an alpha 1 to an alpha 2 position, whereas no significant effect of this kind was observed in adult sera. Affinity chromatography through Concanavalin A-Sepharose showed cord sera to contain a proportion of bound-GGT (68.5 +/- 5.5%) that was significantly greater (p less than 0.001) than that found in adult sera (59.8 +/- 10.2%). It is concluded that the high GGT activity of cord sera is probably due to hepatic immaturity rather than maternal sources, enzymatic induction or microsomal lesions; that the predominant form of GGT in cord serum may be a complex with HDL and less sialized than the adult enzyme; and that, of the factors examined, the best indicator of neonatal maturity is fetal haemoglobin.
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PMID:Cord serum gamma glutamyltransferase in newborns. 244 3

Previous studies in this laboratory (1) have shown that tunicamycin-treatment inhibits the secretion of three secretory glycoproteins--alpha 2-macroglobulin, ceruloplasmin, and alpha 1-protease inhibitor in human hepatoma (Hep G2) cell cultures. In the present study, we have investigated (i) their site of accumulation within the endoplasmic reticulum/Golgi pathway, and (ii) the solubility characteristics of these unglycosylated proteins. Using percoll density gradient centrifugation, we found that tunicamycin-treatment markedly inhibited the transport of alpha 2-macroglobulin, ceruloplasmin and alpha 1-protease inhibitor from the rough endoplasmic reticulum. However, there was no detectable changes in their solubility properties as both the glycosylated and unglycosylated species were associated with the 100,000 xg supernatant fraction following disruption of the microsomal fraction (i) with 0.2% Triton X-100 and (ii) by repeated freeze-thaw cycles. Also no evidence of protein aggregation was detected by liquid chromatography of the unglycosylated proteins on Bio-Gel A-1.5 column.
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PMID:Accumulation of unglycosylated liver secretory glycoproteins in the rough endoplasmic reticulum. 247 24

The status and transfer of metals across the rat placenta were studied by subcellular and molecular fractionations of this organ at 2 and 24 h after iv injection of radiolabeled metals. The soluble and nuclear fractions showed higher contents of copper and zinc, whereas most of the nickel was associated with the soluble fraction. Cadmium was almost evenly distributed between the microsomal and nuclear fractions. Gel filtration of the soluble fractions showed nickel associated with an unknown low molecular weight form; zinc with high molecular weight proteins; copper with metallothionein, ceruloplasmin, and high molecular weight proteins; and cadmium with high molecular weight proteins and metallothionein.
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PMID:The metabolism of metals in rat placenta. 248 64

Content of lipid peroxidation products in liver mitochondria, enzymatic system of the peroxidation initiation (NADPH.H+- and NADH.H+-dependent oxydoreductases) at the early and final steps of liver microsomal redoxchain as well as the activity of protective enzymes superoxide dismutase, ceruloplasmin, catalase and glutathione reductase, preventing the excessive accumulation of lipid peroxidation products in liver mitochondria and erythrocytes were studied in rats with hypokinesia within 1 and 2 months. An increase in content of diene conjugates and malonic dialdehyde as well as in activity of NADPH.H+- and NADH.H+-nitroblue tetrazolium-oxydoreductases in liver microsomes, a decrease in activity of catalase and superoxide dismutase in liver mitochondria were observed in the animals within two months of their mobility restriction. These alterations were among the essential mechanisms responsible for an increase in content of lipid peroxidation products under conditions of hypokinesia.
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PMID:[Enzyme system of initiation and protection against lipid peroxidation in the liver and blood of rats with hypokinesia]. 336 22

Cadmium chloride was administered in drinking water at a concentration of 50 ppm cadmium to female rats for 20 days of gestation. The foetuses were then removed from the uteri of the dams. Gestational exposure to oral cadmium resulted in decreased zinc, copper, iron, metallothionein, and thionein-bound zinc content in foetal liver as well as in reduced copper content in placenta and foetal intestine, brain and kidney. Subcellular fractionation of the foetal liver revealed decreased nuclear and cytoplasmic zinc content as well as decreased microsomal iron content. Pregnant rats exposed to oral cadmium revealed decreased serum zinc and iron concentration as well as reduced ceruloplasmin activity. The decreased zinc, copper, and iron content in foetal organs is suggested to be causally connected with the diminished availability of these metals in the maternal circulation.
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PMID:Effect of oral cadmium administration to female rats during pregnancy on zinc, copper, and iron content in placenta, foetal liver, kidney, intestine, and brain. 399 9

The subcellular localization in rat liver cells of retinol-binding protein (RBP), prealbumin, ceruloplasmin, albumin, and class I transplantation antigen chains was investigated by radioimmunoassay determinations. The concentration of RBP was high in the rough and smooth endoplasmic reticulum (SER). The relative concentrations of prealbumin, ceruloplasmin and albumin were similar in the endoplasmic reticulum fractions and in the Golgi fraction. Neither of the proteins were found in significant amounts in the post-microsomal supernatant nor in the plasma membrane. The concentrations of the class I transplantation antigen chains were higher in the Golgi fraction than in the endoplasmic reticulum fractions. In the rough endoplasmic reticulum (RER) fraction ceruloplasmin and the class I antigens partially interact with high-molecular weight (MW) components, presumably membrane-bound glycosyltransferases. RBP, prealbumin and albumin seemed to be present in free form within the microsomal lumen. In vitamin A deficiency the RBP and to a lesser extent the prealbumin concentrations in the endoplasmic reticulum fractions were significantly increased, as compared to fractions from normal livers. This suggests that the presence of vitamin A is a prerequisite for the transport of RBP from the endoplasmic reticulum to the Golgi complex. The intracellular concentrations of albumin and ceruloplasmin were not significantly altered by vitamin A deficiency. In contrast, the amounts of the class I antigen heavy chains were found to be increased.
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PMID:Subcellular localization in normal and vitamin A-deficient rat liver of vitamin A serum transport proteins, albumin, ceruloplasmin and class I major histocompatibility antigens. 633 57


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