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)

Rivalta reaction is still used as a puncture fluid test for differentiation of exudate and transudate. However, the test method of Rivalta reaction has not been standardized, or positive precipitates for the reaction have not been investigated. Thus, we clarified the measurement method, and investigated Rivalta reaction-positive proteins. Rivalta reaction-positive punctuates converted to negative when pH increased to 4.6 or higher, showing the necessity of pH adjustment of acetic acid solution to 3.6-4.2 in Rivalta reaction. Using pH 4.0 acetic acid solution, 8 types of proteins were identified in Rivalta reaction-positive turbid precipitates: C-reactive protein (CRP), alpha1-antitrypsin (alpha1-AT), alpha1-acid glycoprotein (alpha1-AG), haptoglobin (Hp), transferrin (Tf), ceruloplasmin (Cp), fibrinogen (Fg), and hemopexin (Hpx). Since these are acute reactive proteins, or proteins increased in malignant tumors and infections, positivity for Rivalta reaction at the specified pH may suggest pathological inflammation.
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PMID:Reinvestigation of clinical value of Rivalta reaction of puncture fluid. 1565 65

We investigated the influence of two different light intensities, dim (100 lx) and bright (5000 lx), during the daytime on the circadian rhythms of selected acute phase proteins of C-reactive protein (CRP), alpha1-acid glycoprotein (AGP), alpha1-antichymotrypsin (ACT), transfferin (TF), alpha2-macroglobulin (alpha2-m), haptoglobin (HP), and ceruloplasmin (CP). Serum samples were collected from 7 healthy volunteers at 4 h intervals during two separate single 24 h spans during which they were exposed to the respective light intensity conditions. A circadian rhythm was detected only in ACT concentration in the bright light condition. The concentration of ACT, a positive acute phase protein (APP), increased (significantly significant differences in the ACT concentration were detected at 14:00 and 22:00 h) and AGP showed a tendency to be higher under the daytime bright compared to dim light conditions. There were no significant differences between the time point means under daytime dim and bright light conditions for alpha2-M, AGP, Tf, Cp, or Hp. The findings suggest that some, but not all, APP may be influenced by the environmental light intensity.
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PMID:Circadian rhythm of acute phase proteins under the influence of bright/dim light during the daytime. 1586 27

"Acute phase proteins" comprise a group of proteins whose concentrations increase or decrease by at least 25% after a damaging stimulus (burn, trauma, tissue damage, etc.) or during inflammation. We investigated the seasonal variation in the concentrations of several acute phase proteins--alpha1-antichymotrypsin (ACT), alpha1-acid glycoprotein (AGP), transferrin (Tf), alpha2-macroglobulin (alpha2-M), ceruloplasmin (Cp), antitrypsin (AT), and haptoglobin (Hp). Blood samples were collected from 15 healthy volunteers, who were subjected to the seasonal changes in illumination, were drawn at 08:00 h every 3 months (August, November, January/February, March/April, June/July). With the exception of Hp, all acute phase proteins showed an annual rhythm (ANOVA; p < 0.01). Lowest concentrations occurred in the winter months (November through February), with the exception of Tf, which was oppositely phased.
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PMID:Seasonal rhythms of "acute phase proteins" in humans. 1607 57

Zn is an essential trace element required throughout the life cycle. Although suboptimal Zn status is thought to be common in many sub-Saharan countries, there is a paucity of data in the Democratic Republic of Congo. The objective of the study was to determine Zn status in non-pregnant Congolese women. We measured plasma Zn and indicators of nutritional status (albumin, prealbumin, retinol-binding protein) and inflammation (C-reactive protein (CRP), ceruloplasmin, alpha1-acid glycoprotein (AGP)) in seventy-seven lactating and thirty non-lactating women (mean age 28 and 31 years, respectively). Blood samples were collected in summer 1989 in rural Bas-Congo during a survey on Fe status. Mean lactation period was 8.3 months. Mean parity was higher in lactating (3.6) than in non-lactating (2.2) women (P < 0.05). Mean biochemical indicators of nutritional status, CRP and ceruloplasmin were within normal range and not different between groups. Mean AGP concentrations were above normal (>1.2 g/l) and higher in lactating (1.365 g/l) than in non-lactating (1.178 g/l) women (P < 0.05). Mean Zn concentration (540 microg/l) of the overall study population was below normal (700 microg/l); and the mean was lower in lactating (455 microg/l) than in non-lactating (759 microg/l) women (P < 0.05). Multiple regression analysis suggested that parity (P < 0.05), but not inflammation, was the most important factor associated with low Zn levels. Despite the lack of data on dietary intake, the results suggest that suboptimal Zn status may be common in the studied population.
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PMID:Unusual low plasma levels of zinc in non-pregnant Congolese women. 1905 55

Fucosylation of N-glycoproteins has been implicated in various diseases, such as hepatocellular carcinoma (HCC). However, few studies have performed site-specific analysis of fucosylation in liver-secreted proteins. In this study, we characterized the fucosylation patterns of liver-secreted proteins in HCC plasma using a workflow to identify site-specific N-glycoproteins, where characteristic B- and/or Y-ion series with and without fucose in collision-induced dissociation were used in tandem mass spectrometry. In total, 71 fucosylated N-glycopeptides from 13 major liver-secreted proteins in human plasma were globally identified by LC-MS/MS. Additionally, 37 fucosylated N-glycopeptides were newly identified from nine liver-secreted proteins, including alpha-1-antichymotrypsin, alpha-1-antitrypsin, alpha-2-HS-glycoprotein, ceruloplasmin, alpha-1-acid glycoprotein 1/2, alpha-2-macroglobulin, serotransferrin, and beta-2-glycoprotein 1. Of the fucosylated N-glycopeptides, bi- and tri-antennary glycoforms were the most common ones identified in liver-secreted proteins from HCC plasma. Therefore, we suggest that this analytical method is effective for characterizing fucosylation in liver-secreted proteins. Graphical abstract A global map of fucosylated and non-fucosylated glycopeptides from 13 liver-secreted glycoproteins in hepatocellular carcinoma plasma.
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PMID:Analysis of fucosylation in liver-secreted N-glycoproteins from human hepatocellular carcinoma plasma using liquid chromatography with tandem mass spectrometry. 2756 92

We analyzed the tear film proteome of patients with dry eye (DE), meibomian gland dysfunction (MGD), and normal volunteers (CT). Tear samples were collected from 70 individuals. Of these, 37 samples were analyzed using spectral-counting-based LC-MS/MS label-free quantitation, and 33 samples were evaluated in the validation of candidate biomarkers employing customized antibody microarray assays. Comparative analysis of tear protein profiles revealed differences in the expression levels of 26 proteins, including protein S100A6, annexin A1, cystatin-S, thioredoxin, phospholipase A2, antileukoproteinase, and lactoperoxidase. Antibody microarray validation of CST4, S100A6, and MMP9 confirmed the accuracy of previously reported ELISA assays, with an area under ROC curve (AUC) of 87.5%. Clinical endpoint analysis showed a good correlation between biomarker concentrations and clinical parameters. In conclusion, different sets of proteins differentiate between the groups. Apolipoprotein D, S100A6, S100A8, and ceruloplasmin discriminate best between the DE and CT groups. The differences between antileukoproteinase, phospholipase A2, and lactoperoxidase levels allow the distinction between MGD and DE, and the changes in the levels of annexin A1, clusterin, and alpha-1-acid glycoprotein 1, between MGD and CT groups. The functional network analysis revealed the main biological processes that should be examined to identify new candidate biomarkers and therapeutic targets.
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PMID:Tear proteome analysis in ocular surface diseases using label-free LC-MS/MS and multiplexed-microarray biomarker validation. 2923 88


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