Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.16.3.1 (ceruloplasmin)
5,074 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

116 women 21-36 years old, who had been taking oral contraceptives (OC) for at least 1 and 1/2 years and, at the most, for 4 years, were studied. The subjects underwent detailed clinical, biochemical, and immunological tests using samples of their blood sera. Their OC was Neogest consisting of .15 mg levonorgestrel and .03 mg ethinyl estradiol. Prealbumin values were higher than normal .40 g/l ) in 23 of 83 women studied. Alpha-1-antitrypsin values were below normal in 55 and above normal 4.0 g/l in 13 of 114 subjects studied. Alpha-2-macroglobulin was below normal (1.75 g/l) in 18 and above normal 4.20 g/l in 3 women of 67 studied. In 26 women, orosomucoid (alpha-1-glycoprotein) values were below normal (.55 g/l) and in 2 women the values were above normal (1.40 g/l) among 116 women. The ceruloplasmin values were below normal in 2 (.15 g/l) and above normal in 51 women (.60 g/l) of 115 studied. The effect of OCs on these proteins and possible metabolic changes and pathological associations were also addressed. All of these differences were statistically significant (p 0.01). The relationship of deviation from normal was the largest for alpha-1-antitrypsin with a below normal direction (1/1 = .482) and for ceruloplasmin with an above normal direction (1/1 = .440). The main reason of departure was the large number of above normal values in the case of prealbumin and ceruloplasmin and the large number of below normal values for alpha-1-antitrypsin, alpha-2-macroglobulin, and orosomucoid.
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PMID:[Hormonal contraception and levels of selected serum proteins]. 213 7

Adult male Sprague-Dawley rats with streptozotocin-induced diabetes (6 to 8 wk duration), treated or untreated with insulin, were studied with two aims: (a) to ascertain whether protracted diabetes in the rat is associated with changes in circulating plasma protein levels analogous to those reported in human diabetic patients with clinical evidence of complications; (b) to evaluate the effects of experimental diabetes on the net cumulative biosynthesis of 10 specific plasma proteins by the isolated liver, perfused for 24 hr. Samples of liver donor plasma and samples of perfusate were analyzed by single radial immunodiffusion or by rocket immunoelectrophoresis for albumin, alpha 1-macroglobulin and the acute phase glycoproteins: fibrinogen, alpha 1-acid glycoprotein (Darcy), alpha 1-acid glycoprotein (Kawasaki), haptoglobin, alpha 2-(acute phase) globulin, hemopexin, C3-complement and ceruloplasmin. Diabetes (6 to 8 wk), untreated with insulin, resulted in significantly increased liver donor plasma levels of alpha 1-acid glycoprotein (Darcy) and alpha 1-acid glycoprotein (Kawasaki); plasma levels of hemopexin and of C3 decreased to 75% and 30% of normal, respectively. Insulin treatment of diabetic liver donors for 6 to 8 wk prevented the increase in alpha 1-acid glycoprotein (Darcy) and alpha 1-acid glycoprotein (Kawasaki) and minimized the decrease in C3 to 75% of normal. Perfused livers from untreated diabetic rats (6 to 8 wk) showed slightly decreased cumulative synthesis and secretion of alpha 1-acid glycoprotein (Darcy); however, synthesis of albumin was reduced to 35% of normal and that of eight glycoproteins ranged from 25% of normal (fibrinogen) to 12% of normal (C3). The striking in vitro induction of increased synthesis of acute-phase proteins by cortisol plus insulin in the isolated perfused normal liver was in contrast to the severely attenuated induction in perfused livers of untreated diabetic rats, which ranges from 50% of normal for alpha 1-acid glycoprotein (Darcy) to 5% of normal (C3). Severely negative perfusate nitrogen balance and impaired glucose utilization by perfused untreated diabetic livers contrasted with positive nitrogen balance and good glucose utilization of normal livers in response to insulin plus cortisol. The plasma protein synthetic capacity and the in vitro response to insulin plus cortisol of perfused livers from insulin-treated diabetic rats were normal for seven of the proteins but moderately decreased for albumin, haptoglobin and C3.
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PMID:Effects of streptozotocin diabetes in the rat on blood levels of ten specific plasma proteins and on their net biosynthesis by the isolated perfused liver. 213 29

Eleven potential biochemical markers were measured in serum from 33 patients with malignant and 13 with benign colorectal disease: four isoenzymes (creatine kinase-BB, homoarginine-sensitive alkaline phosphatase, salivary-type amylase, and macro-creatine kinase type 2), five specific proteins (ferritin, alpha 1-acid glycoprotein, C-reactive protein, alpha 1-antitrypsin, and ceruloplasmin), one oncofetal antigen (carcinoembryonic antigen, CEA), and one hormone (beta human choriogonadotropin). The sensitivity of individual markers for the detection of early-stage malignancy (n = 11) ranged from 0% to 64% (CEA 18%); for late-stage colon malignancy (n = 12) from 8% to 83% (CEA 83%). Specificity in patients (n = 10) with benign intestinal disease ranged from 80% to 100% (CEA 100%). The five most-sensitive markers--C-reactive protein, alpha 1-glycoprotein, CEA, macrocreatine kinase type 2, and homoarginine-sensitive alkaline phosphatase--were selected for use as a "colon panel." In retrospective comparison, use of the colon panel instead of CEA alone increased sensitivity by 17% and 64% for late-and early-stage cancer, respectively; specificity, however, decreased by 30%, but should improve with serial testing.
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PMID:Multiple markers of malignancy in sera of patients with colorectal carcinoma: preliminary clinical studies. 241 37

Monitoring of plasma proteinases, proteinase inhibitors and other selective plasma proteins was evaluated in patients undergoing Y-graft aortofemoral bypass operation. Fast-reacting acute-phase proteins (C-reactive protein, antichymotrypsin, alpha 1-acid glycoprotein) and slow-reacting proteins (haptoglobin, alpha 1-antitrypsin) increased significantly 48-120 h after operation. By contrast, no significant increase was found between plasma ceruloplasmin levels before clamping and after declamping. Activity and concentration of alpha 2-macroglobulin decreased postoperatively and remained significantly lowered throughout the observation period. Plasma levels of granulocyte elastase were elevated significantly 1 h after declamping, whereas trypsin-binding capacity decreased immediately after the release of the clamp. Aprotinin pretreatment caused higher trypsin-binding capacity of the plasma, significantly lower 'unspecific' proteolytic (azocasein-hydrolyzing) activity and significantly lower non-TCA precipitable low molecular weight plasma protein concentration. Our results confirm the data of several authors that monitoring of plasma proteinases, proteinase inhibitors and other selective plasma proteins may be helpful in evaluating surgical patients postoperatively.
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PMID:Plasma proteinases, proteinase inhibitors and other selective plasma proteins following aortofemoral bypass operation. 242 35

To investigate our earlier hypothesis that carbohydrates play a regulatory role in the intracellular transport of secretory glycoproteins, we used 1-deoxynojirimycin (DNJ), and inhibitor of glucosidase I and II of the rough endoplasmic reticulum (RER), to modify the structure of N-linked glycan moieties of secretory glycoproteins of human hepatoma (Hep G2) cells in culture. Using a pulse-chase protocol, we found that treatment of Hep G2 cultures with 1.25 mM DNJ markedly reduced the rate of secretion of alpha 1-protease inhibitor, ceruloplasmin, and alpha 2-macroglobulin, but had no effect on the export of fibronectin, alpha-fetoprotein and transferrin, nor on albumin which lacks carbohydrate. For example, 50% of newly synthesized alpha 1-protease inhibitor, the glycoprotein most dramatically affected, was secreted by 27 min in control cultures versus 110 min in DNJ-treated cultures. Percoll gradient cell fractionation analyses revealed that DNJ inhibited transport of the affected secretory glycoproteins in the RER segment of the ER/Golgi pathway. For example, 50% of newly synthesized alpha 1-protease inhibitor was lost from the RER fraction by 10 min in untreated cells, but 70 min was required for the transport of a similar amount of protein in DNJ-treated cells. DNJ treatment also inhibited the rate at which the N-linked glycan moieties of the affected glycoproteins became resistant to endo H in the Golgi. Since the glycan moiety of secreted forms of the affected glycoproteins were fully processed to the complex structure, suggesting escape from DNJ inhibition, we concluded that removal of terminal glucose residues from the glycan chain of secretory glycoproteins is required for their transport from the RER to the Golgi. We suggest that the oligosaccharide moieties on alpha 1-protease inhibitor, ceruloplasmin and alpha 2-macroglobulin form part of the binding site for a receptor which regulates transport of these glycoproteins.
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PMID:Differential effects of 1-deoxynojirimycin on the intracellular transport of secretory glycoproteins of human hepatoma cells in culture. 243 31

Ceruloplasmin is a copper containing serum glycoprotein. It is an acute-phase protein and its levels are increased in inflammation and in a number of experimental and human tumors. It is normally synthesized in the liver and not in fibroblasts. In this paper we present evidence that ceruloplasmin mRNA is synthesized in Balb/C 3T3 cells and its levels are increased about 3-fold in Rous-Sarcoma virus (RSV) transformed cells. The ceruloplasmin mRNAs from rat liver and RSV 3T3 cells have the same electrophoretic mobility.
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PMID:Induction of the ceruloplasmin mRNA in Balb/C 3T3 cells after Rous-Sarcoma virus transfection. 243 32

The main 'acute-phase proteins' were determined in serum of 20 patients with presenile Alzheimer's disease (AD) and compared with values in 18 age-matched healthy control subjects. Following parameters were evaluated: alpha 1-antitrypsin (alpha AT), haptoglobin (HPT), transferrin (TRF), acidic alpha 1-glycoprotein (A alpha G), ceruloplasmin (CER), alpha 2-macroglobulin (alpha MG), C-reactive protein (CRP), albumin (ALB), together with the immunoglobulins IgG, IgM and IgA, and some of the most significant factors of the classic (C3, C4) and alternative (properdin factor B) pathways of complement activation. The results showed a statistically significant increase in the levels of alpha AT (p less than 0.001), CER (p less than 0.001) and of all the complement factors studied (p less than 0.005). The levels of other acute-phase protein (HPT, TRF, A alpha G, alpha MG, CRP, ALB) and immunoglobulins (IgG, IgM, IgA) were similar in AD patients and normal controls. These results give rise the possibility that these elements indicate an altered immunoregulation compatible with chronic cell damage and/or chronic inflammation conditions. Moreover, the increased level of alpha AT can be related to the low production of interleukin-1 (IL-1) reported in AD, which supports the hypothesis of a relative derangement of the macrophage function in presenile AD patients.
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PMID:Acute-phase proteins in Alzheimer's disease. 245 38

Serum concentrations of sex hormone binding globulin (SHBG), pregnancy associated alpha 2-glycoprotein (alpha 2-PAG), caeruloplasmin (Cp), alpha 1-antitrypsin (alpha 1-At) and transferrin (Tf), unconjugated and total estrone, and unconjugated estradiol-17 beta were measured twice at a 4-5 week interval in 43 cases of early normal pregnancy (gestational weeks 6-19). Significant correlations between estrogen and protein levels in the total material were observed for all proteins except for Tf. However, within 2-week intervals of pregnancy, significant correlations were obtained only in certain intervals between estrogens on one hand and SHBG, Cp and alpha 1-At on the other. Significant correlations between rates of increase of estrogens and of proteins were obtained only at certain occasions for SHBG, Cp, Tf and alpha 1-At. The results indicate that, although estrogens may have a modulatory function in 'steroid-sensitive' protein synthesis, they are probably not the main physiological regulator.
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PMID:Serum levels of estrogens and of five 'steroid sensitive' proteins in early normal pregnancy. 245 29

We have studied the role of the liver in the relative increase of Concanavalin A (Con A)-reactive molecular forms of various positive rat acute-phase glycoproteins (APGPs) occurring in serum during inflammation. Secretion media of hepatocytes isolated from inflamed rats showed a 2 to 5-fold increase of the total amounts of four APGPs studied in comparison to secretion media of control hepatocytes. These changes were in analogy with those observed for corresponding sera, except for alpha 1-antitrypsin. All the different Con A-reactive molecular forms were present in the media, with exception of the most reactive form of ceruloplasmin. In vitro and in vivo, dexamethasone augmented the secretion of three APGPs, and especially of the Con A-most reactive forms. The in vitro effect of dexamethasone--augmented secretion of Con A-reactive molecular forms of alpha 1-acid glycoprotein and haptoglobin--was comparable with the results obtained for hepatocytes isolated from inflamed rats. In vivo, dexamethasone treatment resulted in an even higher increase of the serum concentration of the Con A-most reactive forms of both APGPs than experimental inflammation did. Although an extrahepatic contribution cannot be excluded, these results suggest that alterations in the Con A reactivity of APGPs as observed during the acute-phase of inflammation have their origin in the liver. A change in the Con A reactivity of glycoprotein indicates a modulation of its glycosylation. Since dexamethasone can affect these changes in vivo and in vitro, glucocorticoids most probably are involved in the regulation of the glycosylation of the APGPs during biosynthesis in the liver.
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PMID:Glycosylation of four acute-phase glycoproteins secreted by rat liver cells in vivo and in vitro. Effects of inflammation and dexamethasone. 245 14

There is a very important modification of the plasma protein equilibrium during an inflammatory reaction. Most of the proteins, except the immunoglobulins, have their biosynthesis or catabolic rate modified. The plasma concentration of these proteins may be increased, decreased or equal to the normal values. Clinically, the term "Acute Phase Protein" APP is reserved for the proteins whose plasma concentration is at least 50 per cent higher than normal values. These APP are: alpha-1 acid-glycoprotein, alpha-1 proteinase inhibitor, alpha-1 antichymotrypsin, haptoglobin, ceruloplasmin, fibrinogen, C-reactive protein, serum amyloid A protein. Interleukin-1 induces the APP's hepatic biosynthesis. The APP and, more generally, a lot of plasma proteins play a role during inflammatory reaction. They have some real functions of metabolic regulators. The functions result from the interaction of these proteins with ligands of various origins which give "protein-ligands" complexes. These complexes are cleared by the RES or by the hepatocyte. The results are protease inhibition, neutralization of toxic molecules such as hemoglobin or the superoxide anion, clearance of cell membranes and chromatin. The interaction of plasma proteins and particularly the APP's with different ligands issued from the inflammatory site, is an example of physiopathological self regulation.
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PMID:[Proteins of the inflammatory reaction. Regulatory functions]. 245 87


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