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)

High levels of ceruloplasmin mRNA were measured in the uterus of both pregnant and non-pregnant rats. No mRNA for alpha 2-macroglobulin and alpha 1-acid glycoprotein could be detected in the uterus in contrast to the high levels of those two mRNAs found in the decidua in the mid-gestation period. Synthesis of plasma proteins with a protective function in the decidua or uterus may be important in maintaining homeostasis at different stages of reproduction. In addition, ceruloplasmin synthesis by the uterus may be part of a system transporting copper to the fetus.
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PMID:The expression of genes coding for positive acute-phase proteins in the reproductive tract of the female rat. High levels of ceruloplasmin mRNA in the uterus. 246 86

Several investigators have suggested that gastrointestinal inflammation has a role in the pathogenesis of ankylosing spondylitis. To test this hypothesis markers of gastrointestinal immunostimulation, as manifested by serum IgA concentrations, were compared with serum markers of inflammation, as manifested by acute phase proteins. Serum samples from 45 unrelated Caucasian patients with ankylosing spondylitis (AS) were tested for correlation of serum IgA and six acute phase proteins: C reactive protein (CRP), alpha 1-antitrypsin, alpha 1-antichymotrypsin, caeruloplasmin, alpha 1-acid glycoprotein (AGP), and haptoglobin. Serum IgA was shown to be significantly positively correlated with four of these six acute phase proteins: CRP (r = 0.58, p less than 0.001), alpha 1-antitrypsin (r = 0.29, p less than 0.05), AGP (r = 0.61, p less than 0.01), and haptoglobin (r = 0.58, p less than 0.001), suggesting that gastrointestinal immunostimulation does have a role in the pathogenesis of inflammation in AS. In addition, the microheterogeneity of the pattern of glycosylation of AGP, expressed as reactivity coefficients, was examined. The AGP reactivity coefficient has been shown to increase in infection, remain the same in systemic lupus erythematosus, and decrease in rheumatoid arthritis. It was found that the AGP reactivity coefficient was significantly decreased in patients with AS as compared with healthy controls (p less than 0.006). As recent studies have indicated that patterns of glycosylation reflect intrahepatocellular biosynthetic processes induced by cytokines our data suggest that cytokine-hepatocellular mechanisms in AS may be similar to those occurring in rheumatoid arthritis, but different from those in systemic lupus erythematosus or infection.
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PMID:Serum IgA, acute phase proteins, and glycosylation of alpha 1-acid glycoprotein in ankylosing spondylitis. 246 28

Serum viscosity's increase in diabetes has been linked to the presence of microvascular sequelae and to changes in serum protein composition. The major change is a decline in albumin and an increase in the levels of acute-phase proteins. In this study, albumin and five acute phase proteins--alpha-1 acid glycoprotein, alpha-1 antitrypsin, haptoglobin, ceruloplasmin, and C-reactive protein--were measured. Levels in adult diabetes (principally type II) were compared with those in both subjects with glucose intolerance and control subjects (healthy subjects and nondiabetic ambulatory patients). Haptoglobin, alpha-1 acid glycoprotein, and C-reactive protein increased markedly in both diabetes and glucose intolerance; ceruloplasmin and alpha-1 antitrypsin increased more marginally. Serum albumin level decreased more strikingly as hyperglycemia advanced. Acute-phase proteins also increased in advanced glucose intolerance as in established diabetes. The acute-phase protein elevation did not differ with degree of control or duration of diabetes. When diabetics were divided into those with and without clinically detectable evidence of microvascular sequelae, elevation of haptoglobin, C-reactive protein and alpha-1 acid glycoprotein, and depression of albumin were found to progress with number of sequelae. The levels of these proteins, particularly haptoglobin, were also highly correlated with serum viscosity expressed as viscosity number. Mild serum albumin depression and a more striking acute-phase protein elevation are greater in diabetes with microangiopathy, develop in glucose intolerance, and contribute substantially to elevated plasma viscosity in diabetes.
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PMID:Increased levels of acute-phase serum proteins in diabetes. 247 61

In comparison with healthy persons, chronic uremic patients on regular hemodialysis treatment had significantly higher blood serum concentrations of alpha 1-acid glycoprotein, ceruloplasmin and C4 complement component, while levels of haptoglobin, C3 and transferrin were lower. Serum alpha 2-macroglobulin and alpha 1-antitrypsin levels were similar in both groups. Hemodialysis with cuprophan membrane induced only slight changes in some of these glycoproteins during a 48-hour follow-up period. Seven hours after termination of hemodialysis slight, but significant, decreases in blood serum transferrin and alpha 1-antitrypsin concentrations were observed. Hemodialysis thus does not seem to induce a conspicuous acute-phase reaction.
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PMID:Hemodialysis and the acute-phase response in chronic uremic patients. 248 60

The synthesis of all the major acute phase plasma proteins is stimulated in rat hepatoma and primary cultures of hepatocytes by three, structurally and functionally distinct groups of hormones: 1) hepatocyte-stimulating factors (HSF) and interleukin-6 (IL-6); 2) interleukin-1 (IL-1) and tumor necrosis factor (TNF); and 3) glucocorticoids. Each plasma protein gene requires a specific combination of these 3 hormone types for maximal expression. One set of acute phase proteins, including alpha 2-macroglobulin, alpha 1-antichymotrypsin ( = contrapsin), cysteine protease inhibitor ( = thiostatin), alpha 1-antitrypsin, ceruloplasmin and fibrinogens are predominantly regulated by the keratinocyte-derived HSF-III/-II or IL-6, while a second set of proteins, including alpha 1-acid glycoprotein (AGP), haptoglobin and complement C3 are predominantly regulated by keratinocyte-derived HSF-I, IL-1 or TNF. In conjunction with the above peptide hormones, glucocorticoids synergistically enhance the stimulated expression of most, but not all, acute phase proteins. An exceptionally strong synergy between HSF (or IL-6), IL-1 and glucocorticoids is noted for the activation of the AGP gene. To elucidate the molecular mechanisms of regulation, we have identified the cis-acting genetic elements through which all these hormones control the transcriptional activity of the AGP gene. It appears that acute phase activates a specific nuclear binding protein in the rat liver that interacts with the peptide hormone responsive element located 5 kb upstream of the transcriptional start site.
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PMID:Regulation of acute phase protein genes by hepatocyte-stimulating factors, monokines and glucocorticoids. 248 67

In a group of 76 clinically healthy human volunteers, we found a high correlation (r = 0.997, p less than 0.001) between the ceruloplasmin oxidase activities in serum (mean 127.2 U/l) and plasma (mean 124.0 U/l). Similarly high correlation was observed for immunoreactive ceruloplasmin, which was assayed in 65 samples (r = 0.993, p less than 0.001), with means of 306.1 mg/l in serum and 296.4 mg/l in plasma. Although the difference between the means measured in serum and plasma is in both cases statistically significant, it is clinically irrelevant according to the criteria of the College of American Pathologists. Finally, a high correlation between serum and plasma concentrations (r = 0.970, p less than 0.001, N = 32) was also found for acid alpha 1-glycoprotein, whose sialic acid content is greater than that of ceruloplasmin; in this case there was no statistically significant difference between the means. These results suggest that in humans, ceruloplasmin does not bind to erythrocyte and/or platelet membranes via sialyl groups during clotting, which disagrees with the hypothesis of Paynter (Aust. J. Biol. Sci. (1982) 35, 353--361) in cows and sheep.
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PMID:Serum and plasma ceruloplasmin in humans. 250 29

Previous studies in our laboratory have shown that specific glycan structures are required for the normal secretion of some glycoproteins. Bromoconduritol is known to inhibit the removal of the innermost glucose moiety from the Glc3Man9(GlcNAc)2 precursor of N-linked glycoproteins. We have used this inhibitor to investigate the possible role of glycan structure in the intracellular transport of secretory glycoproteins of Hep G2 cultures. Cells were pretreated with 1mM bromoconduritol for 1h, pulsed with [35S]-methionine for 10min and chased for varying intervals. Specific glycoproteins and albumin were immunoprecipitated from the cell lysate and medium. We found that bromoconduritol-treatment inhibited the secretion of alpha 1-protease inhibitor, ceruloplasmin, alpha 2-macroglobulin, transferrin, and alpha-fetoprotein. Apparently, the glucosylated high-mannose intermediate is not secreted, since glycoproteins in the medium are of complex form. We conclude that the removal of the innermost glucose residue from secretory glycoprotein represents an important regulatory step in the intracellular transport pathway.
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PMID:Bromoconduritol treatment delays intracellular transport of secretory glycoproteins in human hepatoma cell cultures. 254 90

Through a process resembling receptor-mediated endocytosis, liver endothelium binds and internalizes the plasma glycoprotein ceruloplasmin (CP) on the luminal side. The protein is then transported via a vesicular system to the albuminal side where it is externalized to the space of Disse. In its path, the glycoprotein is fully desialylated. To determine if the endosomal compartment is involved in this transport, we used endosomal inhibitors NH4Cl, ethylamine as well as monensin to quantitatively measure the magnitude of radiolabeled CP transport across purified liver endothelial cells. All three reagents inhibited the transport of CP and its discharge by endothelium. The magnitude of inhibition was dose-related for all three reagents. We conclude that the endosomal compartment is involved in the transendothelial transport of CP across the liver endothelium.
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PMID:The role of endosomal traffic in the transendothelial transport of ceruloplasmin in the liver. 256 66

We are interested in determining whether carbohydrates are important regulatory determinants in the intracellular transport and secretion of glycoproteins. In the present study, we have used swainsonine, an indolizidine alkaloid, to modify the structure of N-glycosidically linked complex oligosaccharides. By inhibiting Golgi mannosidase II, swainsonine prevents the trimming of GlcNAc(Man)5(GlcNAc)2 to GlcNAc-(Man)3(GlcNAc)2, resulting in the formation of hybrid-type oligosaccharides. We find, from pulse-chase experiments using [35S]methionine and immunoprecipitation of individual proteins from culture media, that swainsonine treatment (1 microgram/ml) accelerated the secretion of glycoproteins (transferrin, ceruloplasmin, alpha 2-macroglobulin, and alpha 1-antitrypsin) by decreasing the lag period by 10-15 min relative to untreated cultures. The enhanced secretion was specific for glycoproteins since the secretion of albumin, a nonglycoprotein, was unaffected. When alpha 1-antitrypsin was immunoprecipitated from the cell lysates, sodium dodecyl sulfate-polyacrylamide gel electrophoresis fluorographic analysis demonstrated that the conversion of the high-mannose precursor to the hybrid form in swainsonine-treated cells occurred more rapidly (by about 10 min) than the conversion to the complex form in control cells. Since both the hybrid and complex forms of alpha 1-antitrypsin are terminally sialylated by sialyltransferase in the trans-Golgi, these results suggest that swainsonine-modified glycoproteins traverse the Golgi more rapidly than their normal counterparts. Therefore, accelerated transport within this organelle may account for the decreased lag period of glycoprotein secretion in the swainsonine-treated cultures.
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PMID:Swainsonine treatment accelerates intracellular transport and secretion of glycoproteins in human hepatoma cells. 257 69

Liver endothelium can remove and transport the glycoprotein transferrin (TF). During this process the molecules are desialylated; however, in contrast with other such glycoproteins, for example caeruloplasmin, only half of transported TF is desialylated. To explore which component of TF is desialylated, we double-labelled fully sialylated TF with [3H]sialic acid residues and a 125I-protein moiety. This was then 'chased' through purified liver endothelium in pulse-chase experiments. Endothelium-conditioned TF was fractionated on an RCA120 affinity column into sialylated and desialylated components. Each component was then re-fractionated on a concanavalin A affinity column, which separates the glycoprotein according to the branching pattern of its glycan chain. The desialylated fraction was eluted only as a triantennary component, whereas the non-desialylated fraction consisted only of bi- and tetra-antennary chains. The significance of this selective desialylation of triantennary chain of TF in the subsequent metabolism of its iron content and its possible role in the pathogenesis of alcohol-induced hepatic siderosis are discussed.
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PMID:Desialylation of transferrin by liver endothelium is selective for its triantennary chain. 259 20


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