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 authors present a system for the appraisal of the nutritional and inflammatory condition in patients suffering from cystic fibrosis (CF) in the phase of apparent inactivity of pulmonary infection, using a system of indices based on the quantification of some plasmatic proteins. The plasmatic appraisals of 4 visceral proteins (albumin, thyroxine-binding prealbumin, retinol-binding protein and transferrin) and, as well, of 5 proteins of the acute phase (alpha-1-acid glycoprotein, alpha-1-antitrypsin, alpha-2-macroglobulin, haptoglobin and ceruloplasmin) were obtained in a control group of 16 healthy children and in another of 14 children affected by CF. With the proteic plasmatic appraisals of the control group, the knowledge of their biological value and after a statistical-mathematical analysis, the most sensitive, specific and independent proteins were determined for evaluating the nutritional and inflammatory condition, obtaining two simple formulas which were denominated Nutritional-Inflammatory Prognostic Indices (NIPI) A and B (NIPI A = alpha-1-acid glycoprotein + haptoglobin/albumin + prealbumin; NIPI B = haptoglobin/albumin). From the analysis of the results, it can be deduced that the children with CF are affected by an inflammatory process, very probably infectious.
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PMID:[Evaluation of the inflammatory and nutritional status in children with cystic fibrosis]. 267 74

A new human hepatocellular carcinoma (HCC) cell line, KYN-2, has been established from a surgical specimen obtained from a 52-year-old Japanese male HCC patient. The originally resected HCC was classified as pleomorphic HCC corresponding to Edmondson-Steiner's grade III with a thick trabecular to solid arrangement. The cell line has been maintained for 17 months through 35 passages. Morphologically, the KYN-2 cells have retained the characteristics of the original HCC, being pleomorphic and composed of various types such as cells with relatively small, polygonal, eosinophilic cytoplasm and oval-shaped nuclei with a marked tendency to pile up, flat cells with abundant clear cytoplasm and oval-shaped nuclei, and many multinucleated giant cells, proliferating in a pavement-like cell arrangement. Some junctional complexes and a number of microvilli are evident between the cells by electron microscopy. Functionally, these cells were found to secrete albumin, alpha 1-acid glycoprotein, alpha 1-antitrypsin, ceruloplasmin, transferrin, complement C, fibrinogen, fibronectin, prothrombin, retinol-binding protein (serum type), alpha-fetoprotein (AFP), carcinoembryonic antigen (CEA), ferritin and beta 2-microglobulin in chemically defined medium (CDM). The secretion of AFP and CEA is apparently dependent upon culture medium and passage. The doubling time of cells growing in serum-containing medium at the 14th passage was 84 h, and those of cells in serum-containing medium, HB101 (serum-free medium) and CDM at late passage were 28, 68, and 42 h, respectively. Chromosome analysis revealed that the chromosome number ranged from 56 to 69 without a mode, and the presence of marker chromosomes. HB virus DNA sequence was not detected by hybridization analysis. The tumorigenicity of KYN-2 cells was identified by development of tumors in nude mice after subcutaneous injection of the cells; the tumors showed an appearance basically similar to that of the original HCC. Thus, these findings suggest that the KYN-2 cell line is available as a new human HCC cell line and should be useful for various studies on HCC.
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PMID:A new human pleomorphic hepatocellular carcinoma cell line, KYN-2. 284 82

Eight liver biopsy specimens from five patients with PAS-negative intracisternal hyalin were investigated by immunofluorescence for: (1) immunoglobulins (Ig) G, A, M, D, E; (2) light chains (kappa and lambda); (3) complement components C1q, C4, C3c, C5, C9; (4) C1-inactivator; (5) C3-activator; (6) alpha 1-antitrypsin; (7) alpha 1-antichymotrypsin; (8) plasminogen; (9) fibrinogen; (10) fibrinogen breakdown products D and E; (11) fibronectin; (12) prealbumin; (13) albumin; (14) betalipoprotein; (15) apolipoprotein; (16) alpha 1- and alpha 2-glycoprotein; (17) cholinesterase; (18) ceruloplasmin; (19) haemopexin; (20) myoglobin; (21) placenta lactogen; (22) transferrin; (23) actin; (24) myosin; (25) cathepsin D; and (26) hepatitis B surface and core antigens (HBsAg and HBcAg). The globules reacted significantly with antisera against C3c (three patients), C4 (three patients), C3-activator (one patient) and fibrinogen (two patients). The cause of the protein accumulation is not clear. Serial studies indicate the possibility of a disturbance of protein secretion and an as yet unidentified immune complex disorder.
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PMID:Immunohistological investigations of PAS-negative globular intracisternal hyalin in human liver biopsy specimens. 285 88

The growth of Treponema denticola in a complex medium was stimulated by human ceruloplasmin and, to a lesser extent, albumin, alpha-1-antitrypsin, alpha-1-acid glycoprotein, and alpha-2-macroglobulin. Human ceruloplasmin could stimulate growth of T. denticola as well as or better than 5% rabbit serum, with a dose-response relationship of between 1 and 5 mg of ceruloplasmin per ml of culture medium. These results suggest that ceruloplasmin could substitute for rabbit serum in stimulating the growth of T. denticola.
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PMID:Ceruloplasmin can substitute for rabbit serum in stimulating the growth of Treponema denticola. 291 1

Mouse ceruloplasmin, the level of which in serum increases on administration of antitumor polysaccharides, was shown to have enhancing effects on the antibody production of mouse spleen cells toward sheep red blood cells and restorative effects on the suppressed mixed lymphocyte reaction of spleen cells of tumor-bearing mice. The proliferation of interleukin-2 dependent cytotoxic T cells and the suppressed concanavalin A response of the tumor bearing mice spleen cells were also enhanced by this serum glycoprotein, weakly but reproducibly. Furthermore, this serum glycoprotein was found to enhance glucose consumption and interleukin-1 production and cytotoxic activities of mouse peritoneal macrophages. These results suggest that mouse ceruloplasmin plays some roles in the natural resistance surveillance against tumors.
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PMID:Immunological effects of mouse ceruloplasmin. 294 Mar 56

We have previously shown that newly synthesized liver secretory proteins are exported at three distinct characteristic rates, with intracellular retention half-times of 110-120 min (e.g. transferrin), 75-80 min (e.g. ceruloplasmin), and 30-40 min (e.g. alpha 1-protease inhibitor) (J. B. Parent, H. Bauer, and K. Olden (1985) Biochim. Biophys. Acta, in press). In the present study we have determined the average time required for specific glycoproteins to move through the various compartments of the intracellular transport pathway, consisting of endoplasmic reticulum and Golgi complex. Localization in particular compartments was monitored by the use of the following complementary approaches: (i) Percoll density gradient fractionation of the subcellular organelles, (ii) sensitivity of the glycan moiety of N-linked glycosylation to endo-beta-N-acetylglucosaminidase H, and (iii) by the lectin-binding characteristics. The cell fractionation studies revealed that alpha 1-protease inhibitor, ceruloplasmin, and transferrin were transported from the rough endoplasmic reticulum with a retention half-time of 10, 30, or 45 min, respectively. Measurements of the rate at which newly synthesized glycoprotein became endo H-resistant (an event localized near the medial region of Golgi) demonstrated that it took 60-70, 30, and 18 min for 50% of transferrin, ceruloplasmin, and alpha 1-protease inhibitor, respectively, to reach the medial Golgi. Consistent with this finding, maximal binding of transferrin to wheat germ agglutinin (also a medial Golgi event) and Ricinus communis agglutinin I (a trans Golgi event) required 75 and 90 min, respectively, and maximal binding of ceruloplasmin to both lectins occurred in approximately 30 min. Maximal binding of alpha 1-protease inhibitor to wheat germ agglutinin and Ricinus communis agglutinin I required 15 and 30 min, respectively. The results presented here clearly indicate that (i) the time required for protein secretion cannot be entirely accounted for by lag in transport from the rough endoplasmic reticulum to the Golgi since the glycoproteins examined are retained in the former organelle for no more than two-fifths of the total intracellular retention half-time, and (ii) the variability in rates of protein secretion is not due solely to differences in rates of transport from the rough endoplasmic reticulum to the Golgi as variability in retention within the Golgi is also demonstrated. The results are discussed in terms of their compatibility with receptor-mediated transport of glycoproteins in both the endoplasmic reticulum and Golgi.
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PMID:Variability in transport rates of secretory glycoproteins through the endoplasmic reticulum and Golgi in human hepatoma cells. 298 65

We studied the effect of the plant alkaloid castanospermine on the biosynthesis and secretion of human hepatoma glycoproteins. The HepG-2 cells, grown in the presence or absence of the alkaloid, were labelled with [2-3H]mannose and then the labelled glycopeptides were prepared by Pronase digestion. This material was analysed by gel filtration on Bio-Gel P-4 before and after treatment with endo-beta-N-acetylglucosaminidase H. Castanospermine caused an accumulation of high-mannose oligosaccharides, by 70-75% over control. The major accumulated product, which could also be labelled with [3H]galactose and was only partially susceptible to alpha-mannosidase digestion, was identified by h.p.l.c. as a Glc3Man9GlcNAc. Thus the alkaloid inhibits glucosidase I in the human hepatoma cells. Analysis of total glycoproteins secreted by the cells into the medium revealed the presence of only complex oligosaccharides in both control and treated cultures, and the amount of the oligosaccharides labelled with radioactive mannose, galactose or N-acetylmannosamine, secreted by treated cells, was decreased by about 60%. The rate of secretion of total protein labelled with [35S]methionine and precipitated from the medium with trichloroacetic acid was inhibited by up to 40% in the presence of castanospermine. Pulse-chase studies utilizing [35S]methionine labelling were performed to study the effect of the alkaloid on secretion of individual plasma proteins. Immunoprecipitation at different chase times with monospecific antisera showed that castanospermine markedly decreased the secretion rates of alpha 1-antitrypsin, caeruloplasmin and, to a lesser extent, that of antithrombin-III. Secretions of apolipoprotein E, a glycoprotein containing only O-linked oligosaccharide(s), and albumin, a non-glycosylated protein, were not affected by the drug. It is suggested that castanospermine inhibits secretion of at least some glycoproteins containing N-linked oligosaccharides, owing to the inhibition of oligosaccharide processing.
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PMID:Castanospermine inhibits glucosidase I and glycoprotein secretion in human hepatoma cells. 300 19

Several human glycoproteins, including alpha 1-antitrypsin, alpha 1-acid glycoprotein, transferrin, caeruloplasmin and alpha 2HS-glycoprotein, synthesized by the hepatoma-derived cell line HepG2 were observed to contain covalently linked sulphate. These proteins were estimated to contain about 0.1 mol of sulphate/mol of protein. The most abundant of the sulphated glycoproteins, alpha 2HS-glycoprotein, was analysed in detail. All of the sulphate on this protein was attached to N-linked oligosaccharides which contained sialic acid and resisted release by endoglycosidase H. Several independent analytical approaches established that approx. 10% of the molecules of alpha 2HS-glycoprotein contained sulphate. Our results suggest that a number of human plasma proteins contain small amounts of sulphate linked to oligosaccharides.
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PMID:Sulphation of proteins secreted by a human hepatoma-derived cell line. Sulphation of N-linked oligosaccharides on alpha 2HS-glycoprotein. 301 4

The experimental data reveal that ceruloplasmin is a serum nonspecific factor acting during the early and late stages of infection with some respiratory viruses. This complex action seems to be based both on the enzymatic activity and on the copper-glycoprotein structure of ceruloplasmin. The changes in progen antigenicity produced by ceruloplasmin are probably involved in the mechanism of the antigenic shift and drift.
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PMID:Considerations about the possible function of ceruloplasmin in influenza and parainfluenza virus infections. 302 49

The structural characterization of glycoproteins by high-performance liquid chromatography (HPLC) is often difficult because of microheterogeneity of their oligosaccharide groups. To investigate this phenomenon, a series of human plasma glycoproteins of known amino acid sequence and carbohydrate structure was subjected to comparative study by HPLC. Methods for the isolation of singly glycosylated glycopeptides were developed. The chromatographic behavior in reversed-phase HPLC of mono-, di-, and multiglycosylated glycopeptides was compared with that of unglycosylated peptides of known amino acid sequence. Glycopeptides tended to be eluted earlier than non-glycopeptides, but the major factor governing retention was hydrophobicity. As shown by comparative study of five plasma glycoproteins by four chromatographic methods, microheterogeneity of the oligosaccharides affects chromatographic characterization of glycoproteins. In anion-exchange HPLC, carbohydrate charge heterogeneity is reflected by the broadening or asymmetry of peaks. Hydroxyapatite chromatography is useful for the purification of several forms of ceruloplasmin and other glycoproteins. The effect of carbohydrate is small in reversed-phase chromatography, but some proteins are denatured by the stringent conditions. Carbohydrate does not have much effect in hydrophobic interaction chromatography, which is more gentle. Because the chromatographic behavior of a glycoprotein may vary significantly with the procedure applied, several types of HPLC methods should be used for the characterization of glycoproteins.
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PMID:Structural characterization of glycoproteins. 304 48


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