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

1. The nutritional status of children showing no clinical signs of malnutrition, from the University School of Khon Kaen, Khon Kaen province, north-east Thailand and from two villages nearby, was tested. The children were grouped according to their body-weight expressed as a percentage of expected weight-for-height (Harvard standards (Stuart & Stevenson, 1959), as given by Jelliffe (1966)). 2. The differing prealbumin concentrations indicated that nutritional status differed between the groups. 3. The urinary urea: creatinine ratio was significantly lower in the village children compared with the children from Khon Kaen, indicative of the higher dietary protein intake of the latter. 4. alpha1-Acid glycoprotein and the first 'post-albumin peak' (obtained by polyacrylamide gel electrophoresis of serum and containing mainly mainly Gc-globulin, alpha1-antichymotrypsin and alpha1-B-glycoprotein) were found to be significantly higher in the village children compared with children from Khon Kaen. 5. The three main proteins of the first 'post-albumin peak' from polyacrylamide gel electrophoresis of serum were tested separately using the electroimmunoassay method. There was no significant difference in Gc-globulin between the children from Khon Kaen and the village children. The concentration of alpha1-B-glycoprotein from those Khon Kaen children whose body-weight was more than 95% expected weight-for-height was significantly lower compared with that of village children, alpha1-Antichymotrypsin concentration was significantly higher in serum from Khon Kaen children than in serum from village children.
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PMID:Serum protein fractions from children of differing nutritional status analysed by polyacrylamide gel electrophoresis and electroimmunoassay. 5 97

All seven pure yolk sac tumors of gonadal and extragonadal origin tested showed a bright positive fluorescence for alpha-fetoprotein in the tumor tissue. A positive reaction was seen in both the tumor cells and the hyaline globules. In all cases, however, the positive fluorescence was distributed in some focal areas of the tumor tissue. Certain tumor cells showed a strong granular intracytoplasmic fluorescence, whereas others showed a weak or a negative fluorescence. The fluorescence-positive tumor cells were located mainly in the areas rich in fluorescence-positive hyaline globules. Besides alpha-fetoprotein, certain plasma proteins--albumin, alpha-1 antitrypsin, and transferrin--were also demonstrated in all five yolk sac tumors tested. The pattern of the distribution of positive fluorescence was basically similar to that of alpha-fetroprotein. Other plasma proteins--orosomucoid, haptoglobin, Gc-globulin, alpha-2 macroglobulin, hemopexin, and ceruloplasmin--were present in certain tumors, and were distributed mainly in a limited number of hyaline globules. Both IgG and IgA were present in two tumors of ovarian origin. The immunoglobulins were for the most part present in extracellular hyaline globules, suggesting that these are taken up from the circulation. Test for fibrinogen, beta-lipoprotein, IgM, IgE, beta-1C/beta-1A and beta-1E globulins were negative or questionable. In a hepatoblastoma, tests for alpha-fetoprotein were positive, but those for other plasma proteins were negative. Fine granular fluorescence was seen in each hepatocellular tumor cell. Mesenchymal elements were virtually unstained.
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PMID:Immunofluorescent demonstration of alpha- fetoprotein and other plasma proteins in yolk sac tumor. 6 8

Serum-25-hydroxy-vitamin-D (25-OHD) nephrotic syndrome (N.S.) without renal insufficiency (urinary protein excretion greater than 3-5 g/24 h/1-73 m2; glomerular filtration-rate greater than 80 ml/min/1-73 m2). Serum-25-OHD levels were low in patients with N.S. (mean 19 nmol/1, range 4-41 nmol/1), compared with a normal range of 25-200 nmol/1. Serum-concentrations of Gc-globulin--the binding protein for vitamin D and its metabolites (D.B.P.)--were significantly (P less than 0-001) lower in patients with N.S. (mean 340 mg/1, range 190-480 mg/1) than in non-proteinuric controls (mean 440 mg/1, range 376-510 mg/1, measured by radial immunodiffusion). In contrast to non-proteinuric urine, urine of all N.S. patients contained a large amount of 25-OHD-binding capacity; D.B.P. could be detected in all N.S. urines after concentration. Scatchard analysis of the urine demonstrated the presence of a low-affinity and a high-affinity binding protein (tentatively identified as albumin and D.B.P.). These results suggest an acquired deficiency of circulating 25-OHD in N.S. secondary to urinary loss of protein-bound 25-OHD. The biological relevance of the low 25-OHD levels is unknown. There was no clinical evidence of osteomalacia (X-ray, serum-alkaline-phosphatase); however, slightly elevated serum-parathyroid-hormone (P.T.H.) levels would be compatible with borderline vitamin-D depletion.
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PMID:25-hydroxy-vitamin-D in nephrotic syndrome. 6 93

Untreated malaria for more than 4 days in eleven patients decreased significantly prealbumin, transferrin levels and increased SGOT activity when compared with a control group and a group of 10 malaria patients who were admitted to the hospital at an earlier stage of the infection. Total protein was significantly lower in the group of patients admitted after five to ten days to hospital compared with the control group. In all malaria patients independent of the duration of the acute infection the 1st post albumin peak in polyacrylamide gel electrophoresis (consisting mainly of Gc-globulin, alpha-1-antichymotrypsin and alpha-1 B-glycoprotein) and creatinine were found to be significantly higher compared with the control group.
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PMID:Alterations of human serum proteins and other biochemical parameters after five to ten days of untreated acute falciparum malaria. 33 73

Vitamin D-binding protein (DBP), a member of a multigene family including alpha-fetoprotein (AFP) and albumin, is a serum glycoprotein that reversibly binds and transports vitamin D and its metabolites to target cells. In this work, we demonstrate that normal and malignant human B-lymphocytes specifically bind and internalize DBP. Radioiodinated DBP (125I-DBP) was used to follow the uptake of the protein by Raji cells, a human pre-B-lymphoma cell line. Time course studies of DBP uptake by these cells exhibited a saturable profile at both 4 and 37 degrees C. The binding saturation curve obtained by incubating Raji cells at 4 degrees C with different concentrations (1.5 nM to 1.5 microM) of 125I-DBP showed two saturation plateaus; Scatchard analysis showed the presence of two groups of receptor sites with a Kd1 of 2.04 x 10(-7) M (n1 = 42,161 +/- 4,336 sites/cell) and a Kd2 of 1.01 x 10(-6) M (n2 = 198,000 +/- 48,000 sites/cell). After incubation of Raji cells at 37 degrees C with both fluorescein isothiocyanate (FITC) and horseradish peroxidase conjugates, DBP was internalized and could be localized in the cytoplasm. DBP-horseradish peroxidase conjugates were used to follow the uptake and to determine the endocytic pathway of the protein in Raji cells. The initial steps, contrary to those observed for AFP, did not apparently involve coated pits and vesicles. Small vesicles (approximately 50-60 nm) with electron-dense DBP-horseradish peroxidase reaction products were observed that could fuse with large endosomes. These endosomes appeared dispersed in the cytoplasm with some preferential localization in the Golgi centrosphere region. Pulse-chase experiments showed that only 10% of the uptaken protein was released in a nondegraded form. Accordingly, most DBP molecules accumulated in endosomes should be degraded in lysosomes, instead of being recycled back to the surface, as in the case of AFP. Contrary to malignant B-cells (Raji), the uptake ability for DBP of normal quiescent B-lymphocytes was very low. Specific binding and internalization of DBP-FITC by these cells were observed following mitogen-induced activation. Significant values of uptake were obtained at 37 degrees C after 72 h of incubation in the presence of pokeweed mitogen. The binding of DBP-FITC was partially inhibited in the presence of an excess of unlabeled protein. Taken together, the actual results suggest that DBP receptors are constitutively expressed by malignant B-cells and in a transitory form by normal B-lymphocytes undergoing mitogen-induced activation.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Receptor-mediated uptake and processing of vitamin D-binding protein in human B-lymphoid cells. 137 1

The vitamin D binding protein (DBP), alternatively known as Gc-globulin, is a member of the albumin (ALB) and alpha-fetoprotein (AFP) gene family. The rat DBP gene is expressed at high levels in liver and at moderate levels in kidney, testis, abdominal fat, and yolk sac. Very low levels of DBP as well as ALB and AFP transcripts can be detected in all other tissues studied by the reverse transcriptase/polymerase chain reaction technique. During development, liver DBP gene transcripts are detectable at 14 days of gestation and levels rise gradually until adulthood in parallel with ALB. DBP present on the surface of U937 monocyte-derived cells is acquired from serum, suggesting cell surface binding sites for DBP. The rat DBP gene has been cloned and characterized. It spans 35 kb and contains 13 exons and 12 introns. The DBP gene contains two fewer exons than the ALB or AFP genes, accounting for the shortest size of its mRNA and protein product. Its 5'-flanking region contains a high degree of structural similarity to both ALB and AFP promoters.
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PMID:Vitamin D binding protein: genomic structure, functional domains, and mRNA expression in tissues. 195 76

Group-specific component (Gc) and total albumin concentrations in the breast secretions from 20 full-term infants were measured. The Gc concentrations as well as the albumin concentrations correlated significantly (p less than 0.02) with the total cell count and the absolute concentration of each white blood cell type in the breast fluid. The ratio of albumin in neonatal breast secretion to that in neonatal serum was similar to the comparable ratio for Gc. Since albumin and Gc are of similar molecular size, these observations suggest leakage of these two proteins from serum to breast secretion and a possible chemotactic relationship between these proteins and the mononuclear cells in neonatal milk.
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PMID:Group-specific component in neonatal breast secretion: relationship to the cellular content. 232 9

The present study concerns the endotoxin neutralizing activity of human iron-free transferrin, and group-specific protein also called Gc-globulin. Iron-free transferrin was used because former studies showed that the endotoxin binding capacity is restricted to apotransferrin. The endotoxin neutralizing activity of the different protein preparations was tested by use of the limulus-amebocyte-lysate test after solubilizing in an isotonic electrolyte buffer at pH 7.0. Surprisingly, in the presence of transferrin the limulus test detected about 200% and 150%, respectively, of the endotoxin content measurable in the presence of human albumin or without any protein. The addition of Gc-globulin leads to a loss of endotoxin of about 40%.
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PMID:Influence of human transferrin and group-specific protein on endotoxicity in vitro. 238 16

A near full-length cDNA encoding the human vitamin D-binding protein (hDBP) was isolated from a human liver mRNA expression library. Complete sequence analysis of this clone predicts the full-length amino acid sequence of the pre-hDBP. Comparison of the sequence of the hDBP mRNA and protein to existing protein and nucleic acid data banks demonstrates a strong and highly characteristic homology of the hDBP with human albumin (hALB) and human alpha-fetoprotein (hAFP). Based upon this structural comparison, we establish that DBP is a member of the ALB and AFP gene family.
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PMID:Serum vitamin D-binding protein is a third member of the albumin and alpha fetoprotein gene family. 241 79

The strong sequence homology described recently between Gc (Vitamin D-binding protein) and albumin, and the ability of the latter, to bind 2-p-toluidinylnaphthylene sulfonate (TNS) promoted similar binding studies with Gc. TNS bound to native Gc as demonstrated by fluorescence, but chloroform:methanol extraction of Gc and gas chromatography revealed that large amounts of unsaturated fatty acids - 16:1, 18:1, 18:2 and 20:4 were also associated with Gc. In addition, TNS fluorescence was abolished by delipidation of Gc, and restored upon subsequent reconstitution with fatty acid. Finally, 70-80% of [3H]-arachidonic acid added to whole serum bound to Gc. These results demonstrated that TNS fluorescence of the native molecule reflects associated lipid, and suggest a novel role for Gc as a reservoir for a circulating pool of unsaturated fatty acids.
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PMID:Evidence of a novel association of unsaturated fatty acids with Gc (vitamin D-binding protein). 313 16


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