Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P02774 (Gc-globulin)
 196 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Vitamin D-binding protein (VDBP, known as Gc-globulin) was discovered by an immunochemical method in the urine of patients with Itai-itai disease. The urine and sera of Itai-itai disease patients produced specific precipitin lines with anti-human VDBP antisera. The electrophoretic mobility of the protein in the urine is the same as that in the serum. A significant correlation was found between VDBP and beta 2-microglobulin in the urine. Based on this result, it was concluded that Itai-itai disease is associated with disturbances of vitamin D transport and/or metabolism.
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PMID:Demonstration of vitamin D-binding protein (Gc-globulin) in the urine of Itai-itai disease patients. 668 43

The mechanism of the interaction between two genetically determined serum vitamin D-binding protein forms and the muscle skeletal actin was investigated. Vitamin D-binding protein was isolated in a good yield from human serum, using immunoaffinity chromatography. 16 mg of pure vitamin D-binding protein were obtained from 100 ml of serum. The interaction between purified vitamin D-binding protein and skeletal muscle actin was studied by viscosity, delta A (232 nm) measurements and by electron microscopy. The effect of vitamin D-binding protein on actin polymerization is characterized by the decrease of the nucleation and elongation rates and by the decrease of the final concentration of polymerized actin in the steady state. The depolymerizing effect is not the result of direct action on vitamin D-binding protein on F-actin but rather of an increased concentration of the complex of the former protein with G-actin. The characteristics of the vitamin D-binding protein and profilin interactions with actin are similar. Both proteins seem to react only with G-actin.
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PMID:The effect of serum vitamin D-binding protein on polymerization and depolymerization of actin is similar to the effect of profilin on actin. 668 65

Human and bovine milk were analyzed for vitamin D, 25-hydroxyvitamin D, 24,25-dihydroxyvitamin D, 25,26-dihydroxyvitamin D and 1,25-dihydroxyvitamin D using exhaustive chromatographic purification procedures coupled with ligand binding assays. Human milk contained the following amounts of antirachitic sterols (pg/ml, mean +/- SD, n = 5): 39 +/- 9 vitamin D; 311 +/- 31 25-hydroxyvitamin D; 52 +/- 8 24,25-hydroxyvitamin D; 32 +/- 9 25,26-dihydroxyvitamin D; 5.1 +/- 0.3 1,25-dihydroxyvitamin D. Normal bovine milk contained levels of these sterols comparable to those found in human milk. Increasing the oral dose of vitamin D to the cows was reflected by an increase of the parent vitamin and 25-hydroxyvitamin D in the milk. Vitamin D-binding protein concentration in human milk whey, determined by Ouchterlony immunodiffusion and radioimmunoassay, was 1--2% of the levels observed in the plasma and was dependent on the stage of lactation. Vitamin D and its metabolites were shown initially to be present in the whey portion but with time migrated into the fat portion of milk. The antirachitic sterols detected account for approximately 25 IU/liter and 27 IU/liter of antirachitic activity in human and bovine milk, respectively. In both species 25-hydroxyvitamin D comprised the majority of the antirachitic sterols detected in normal milk.
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PMID:Vitamin D and its metabolites in human and bovine milk. 678 13

Plasma proteins were measured in bronchoalveolar lavage effluents and serums from normal healthy nonsmokers and smokers, and their concentrations in the 2 fluids were compared. Two-dimensional polyacrylamide gel electropherograms suggested, and radial immunodiffusion assays confirmed, that the soluble proteins of the bronchoalveolar surface resemble serum in kind and amount with the following significant exceptions. Two immunoglobulins, IgG and IgA, were present in amounts that exceeded their concentrations in serum; of the 2, IgG was more abundant. Large nonimmunoglobulin proteins (greater than 300,000 daltons) were absent or present at very low concentrations compared with the amounts found in serum. Transferrin was the only nonimmunoglobulin with a concentration significantly higher at the bronchoalveolar surface than in serum. Smoking did not cause a significant change in the concentration of any protein in serum, but did cause an increase in IgG, C4, and C3 and a decrease in alpha 2-thioglycoprotein, alpha 1-acid glycoprotein, and Gc-globulin in lavage effluents from females.
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PMID:Plasma proteins of the bronchoalveolar surface of the lungs of smokers and nonsmokers. 678 30

Vitamin D-binding protein (DBP) concentrations were determined in the sera of 90 cystic fibrosis homozygotes, 57 obligate heterozygotes, and 46 normal controls. Very significantly lower mean concentrations were found in the sera of CF homozygotes compared with both heterozygotes and controls (P less than 0.01, Wilcoxon Rank Sums Test). Subdivision of the samples by Gc phenotype showed that this relationship held true both in the Gc1 and Gc2-1 phenotypes. The small sample size of the Gc2 genotype makes the significance levels of limited usefulness, but the pattern of variation of DBP levels among CF homozygotes, heterozygotes, and controls was consistent with that observed for the Gc1 and Gc2-1 classes. Haptoglobin levels showed high coefficients of variation when compared among CF homozygotes, obligate heterozygotes, and controls, presumably because of nonspecific elevation in the acute-phase response. Alpha 2-macroglobulin levels were, if anything, slightly elevated in CF homozygotes compared with controls, while albumin levels showed no significant mean differences between these groups. Since the DBP concentration does not vary with age nor with levels of vitamin D and its metabolites, we interpret our results to mean that DBP levels are specifically decreased in cystic fibrosis, perhaps as the result of impaired glycosylation of the protein.
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PMID:Serum concentrations of vitamin D-binding protein (group-specific component) in cystic fibrosis. 679 2

The approximate association constants of the plasma vitamin D binding globulin (Gc-globulin) for 25-hydroxycholecalciferol (25(OH)D3) and the plasma 25(OH)D3 binding capacities were measured in samples from 123 patients with a variety of disorders. No gross differences in binding affinities were observed between different groups of patients and controls. Many patients, however, had moderately reduced, and several had grossly reduced, plasma binding capacities. The changes in Gc-globulin relative to some other proteins are also described in detail in three patients during the course of their illness. Gc-globulin concentration and hence plasma vitamin D binding capacity can undergo rapid and marked changes during illness.
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PMID:Vitamin D binding globulin levels and affinity in various clinical conditions. 689 97

The common allele, GC/1, was subtyped into GC*IF and GC*IS by isoelectric focusing, increasing the proportion of heterozygotes from 0.42 to 0.58. In a series of 200 blood donors and 200 cord bloods the allele frequencies were found to be: GC*IS = 0.59, GC*IF = 0.11, GC*2 = 0.30; and GC*IS = 0.54, GC*IF = 0.16, GC*2 = 0.30, respectively. These values were similar to frequencies obtained in studies of other Caucasian populations. The average probability of detecting non-paternity for this population is increased from 17% to 30% after subtyping GC 1.
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PMID:Distribution of the GC (group-specific component) subtypes in cord bloods and blood donors. 689 51

Group-specific component (vitamin D-binding protein) was purified to homogeneity from human plasma by a three-step procedure involving pseudo-ligand affinity chromatography on immobilized Cibacron blue F3-GA followed by gel filtration and ion-exchange chromatography. Upon pseudo-ligand chromatography, Gc globulin was separated into two peaks. The first, which represented approx. 4% of the total Gc globulin, was eluted together with other alpha-globulins of similar Mr and/or pI, and the second (96% of Gc globulin) was clearly retarded. Collection of the latter provided a fraction 10-fold enriched in Gc globulin, with yields higher than 90%. Incubation of plasma with trace amounts of radioactively-labeled 25-OH vitamin D3 showed that the radioactivity coeluted with the first peak. In addition, after saturation with 25-OH vitamin D3, all the Gc globulin was eluted in the first peak. This indicates that the two peaks correspond to the holo and the apo forms of the protein, respectively, and suggests that either the interaction of the apo form with the Cibacron blue dye involves the binding site for vitamin D metabolites, or that the holo-protein undergoes a conformational change as a consequence of formation of the complex.
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PMID:Interaction of group-specific component (vitamin D-binding protein) with immobilized Cibacron blue F3-GA. 689 18

A group of 1916 Russian men donors was studied for 15 electrophoretic blood protein systems, coded by 22 protein loci: Transferrin (Tf), Haptoglobin (Hp)--2 loci, Group-specific component (Gc), Hemoglobin (Hb)--2 loci, Lactatdehydrogenase (LDH)--2 loci, Malatdehydrogenase (MDH), Erythrocyte esterase (Est)--4 loci, Albumen (Alb), 6-phosphogluconatdehydrogenase (6 PGD), Phosphoglucomutase (PGM)--2 loci, Esterase D (Est D), Adenosindesaminase (ADA), Acid Erythrocyte phosphatase (AcP), Glutamic transaminase (GPT) and Glioxalase-I (GLO-I). Ten loci were defined as polymorphic, the level of heterozygosity for cumulative loci was 0,1435 +/- 0,003. Moscow population was compared to major human races for the set of genetic characters--heterozygosity, correlation coefficient of single locus heterozygosity, a genetic distance. It has been shown that the extent of relation of ethnic groups to Moscow population decreases as follows: Caucasoids, Mongoloids, Negroids.
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PMID:[Polymorphism and heterozygosity levels of the Russian population of Moscow: data for 22 gene loci coding blood proteins]. 719 52

The changes in rat plasma protein distribution after carbon tetrachloride administration were examined using two-dimensional electrophoresis, utilizing isoelectric focusing in polyacrylamide gel in the first dimension and pore gradient polyacrylamide gel electrophoresis in the second dimension. Drastic changes in amount of protein were observed at more than 20 spot positions including those of transferrin, Gc-globulin and low-density lipoprotein. The time course of the changes was examined, and the most drastic changes were observed at 2 days after carbon tetrachloride administration.
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PMID:Detection of the changes in protein distribution of rat plasma induced by carbon tetrachloride administration by means of two-dimensional electrophoresis. 729 60


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