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)

Serum proteins in normal and ARDS bronchoalveolar lavages were analyzed using crossed immunoelectrophoresis. Normal lavages demonstrated relatively few proteins (albumin, alpha 1-antitrypsin, transferrin, and haptoglobin) in low concentrations. In contrast, substantial amounts of all identifiable serum proteins were detected in ARDS lavages. IgA was apparently locally produced. Two of the largest proteins, beta-lipoprotein (mol wt greater than 2 million) and IgM (mol wt approximately 900,000) were found to be complexed as evidenced by their coprecipitation in a single spike in ARDS lavage. Electrophoretic modifications of ARDS albumin and alpha 1-antitrypsin precipitation peaks and partial identity spurring of the alpha 1-lipoprotein peak with other precipitation loops indicated possible complex formation between these proteins and other possibly pathogenic lung fluid constituents. Similarly, modifications of orosomucoid and Gc-globulin peaks indicated possible molecular alterations resulting from interactions with other components. The relatively few protein modifications exhibited in ARDS lavages together with alpha 1-antitrypsin-protease complex formation confirm the relative absence of substantial proteolytic activity in ARDS edema fluids obtained within 12 hr of the onset of the syndrome demonstrated in previous studies.
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PMID:Crossed immunoelectrophoretic analysis of ARDS lavage proteins. 379 28

Total serum protein levels in 70 patients with urolithiasis were not significantly different from those in 20 control subjects, although certain variations were detected in individual protein patterns. In contrast, total urinary protein was significantly higher in patients with urolithiasis. 4-6 different components, i.e., albumin, alpha 1-acidic glycoprotein, alpha 1-antitrypsin, Gc-globulin, fibrinogen and immunoglobulin G, were found in the matrices of calculi and in urine, suggesting that proteinuria may play a role in the formation of stones in patients with urolithiasis.
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PMID:Immunochemical studies of serum, urine and calculus proteins in urolithiasis. 399 70

The beta-D-galactoside-specific lectin from Allomyrina dichotoma reacts with serum proteins which contain the corresponding carbohydrate moieties. By affinity chromatography of human serum using the insolubilized lectin coupled to Sepharose, it is possible to fractionate human serum proteins in 2 groups: those which react with the lectin (alpha 1-acid glycoprotein, haptoglobin, etc.) and those which do not (albumin, Gc-globulin, etc.). IgG is the only serum protein that can be found in both groups.
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PMID:Affinity chromatography of human serum proteins using immobilized lectin from Allomyrina dichotoma. 402 67

Urine was collected from 6 healthy male adults at rest and from 20 male adults after a marathon race (25 miles). The concentrated urines were quantitatively analyzed, by single radial immunodiffusion, for their content in 12 different plasma proteins: tryptophan-rich prealbumin, albumin, alpha(1)-acid glycoprotein, alpha(1)-antitrypsin, ceruloplasmin, haptoglobin, Gc-globulin, transferrin, hemopexin, beta(2)-glycoprotein I, gammaA-globulin, and gammaG-globulin.Albumin, gammaA-globulin, and gammaG-globulin represent the major part of the plasma proteins detected in normal urine excreted by humans at rest (12, 0.5, and 2.5 mg respectively, out of a total excretion of 17.5 mg of plasma proteins per 24 hr). The other plasma proteins were excreted at a lower rate (< 0.4 mg/24 hr). The relative content of tryptophan-rich prealbumin, alpha(1)-antitrypsin, Gc-globulin, transferrin, and gammaG-globulin was lower in normal urine than in normal serum, whereas that of alpha(1)-acid glycoprotein, beta(2)-glycoprotein I, and gammaA-globulin was higher. The ratio of gammaG-globulin to gammaA-globulin was 4.9:1. When plotted on a logarithmic scale, no direct relationship between the molecular weight of a protein and the value of its renal clearance could be observed.Strenuous exercise increased (up to 50-fold) the excretion of plasma proteins which represent 82% of the total proteins found in urine, instead of 57% in urine collected from humans at rest. There was particularly a significant rise of tryptophan-rich albumin, albumin, alpha(1)-acid glycoprotein, transferrin, gammaA-globulin, and gammaG-globulin (0.26, 127, 11.8, 3.3, 1.2, and 2.0 mug respectively, out of a total excretion of 167 mug of plasma proteins per min). The ratio of gammaG-globulin to gammaA-globulin was 16:1. After exercise, the renal clearance of proteins increased from 2 to 40 times, but, as for the urine of normal subjects at rest, no direct relationship between molecular weight and renal clearance could be observed.
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PMID:Quantitative immunological determination of 12 plasma proteins excreted in human urine collected before and after exercise. 417 Mar 90

Immunologic analyses of urinary proteins in patients with gestosis and related obstetrical conditions were performed and urinary protein patterns were compared with blood plasma protein patterns. Many kinds of proteins could be detected in urine of patients with gestosis beside albumin. Therefore, "proteinuria" should be chosen to characterise this state instead of the term "albuminuria". Generally speaking, when a total volume of protein contained in urine increases, its types or subfractions also increase in urine. Next to albumin, the most commonly detected proteins in urine of patients with gestosis were transferrin, IgG, inter-alpha-trypsin inhibitor, alpha 1-antitrypsin, IgA, alpha 2-HS-glycoprotein, alpha 1-acid glycoprotein, Gc-globulin, alpha 1-antichymotrypsin, hemopexin, ceruloplasmin, prealbumin, haptoglobin, anti-thrombin III, Cl-inactivator, IgM, and alpha 2-macroglobulin, in the descending order of their occurrence. Proteins that promptly became negative in urine of gestosis patients after delivery were inter-alpha-trypsin inhibitor, IgA, and ceruloplasmin. On the other hand, proteins most apt to persist in urine were albumin, alpha 2-HS-glycoprotein, and IgG. Generally speaking, lower molecular weight proteins were likely to persist in urine after delivery. Simultaneous determination of blood plasma and urinary proteins was performed for 18 kinds or subfractions of protein. A prognostic value of renal protein clearance was discussed.
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PMID:A study on proteins contained in urine of gestosis patients. 641 21

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 structure and organization of the human vitamin D-binding protein (DBP) gene has been determined. The gene is composed of 13 exons and 12 intervening sequences. With the help of the polymerase chain reaction (PCR) introns were amplified using exon-specific oligonucleotide primers, and were sequenced after subcloning; the exon/intron borders were determined. The introns 2, 5, 7, 9 and 10 were sequenced completely; the introns 1, 3, 4, 6, 8, 11 and 12 were sequenced in part. We designed intron-specific primers for the amplification of each exon by the PCR-method. This permits the analysis of mutational and function-related sites. By comparison with the genes for human albumin and alpha-fetoprotein the gene for DBP/GC is confirmed as a member of this multigene family. The location of the introns in the coding region of the human DBP-gene is identical with the position of the introns in the rat DBP-gene.
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PMID:Sequence and organization of the human vitamin D-binding protein gene. 750 19

The transporter of vitamin D and its metabolites in blood has received increasing attention in recent years, and is recognized to be a member of a gene family that includes albumin and alpha-fetoprotein. Identical to the group specific component (Gc-globulin) of serum, the protein is a single-chain polypeptide constitutively synthesized in liver that circulates in amounts in far excess of normal vitamin D metabolite concentrations in blood. It plays the major role in the egress of endogenously synthesized vitamin D, from skin and appears to restrain D-sterols from too rapid/excessive cell entry. Along with plasma gelsolin, it comprises the plasma actin-scavenger system that facilitates removal of actin, liberated from lysed cells, by depolymerization and prevention of polymerization. Recently, the protein has been shown to behave as a co-chemotaxin specific for the complement peptide C5a, and its sialic acid-free form has been reported to play a role in macrophage activation. The latter functions strongly implicate its participation in inflammation responses. A unifying hypothesis might also suggest the protein to provide focal D-sterol delivery to cells that are important to the resolution of tissue injuries.
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PMID:Plasma vitamin D-binding protein (Gc-globulin): multiple tasks. 762 13

The presence of the glycoproteins haptoglobin and hemopexin in human plasma albumin (HPA) solutions were demonstrated to be responsible for the formation of polymers and aggregates during heat treatment for 10 h at 60 degrees C. Apart from haptoglobin and hemopexin three other contaminating proteins were identified as transferrin, Gc-globulin and beta 2-glycoprotein. During heat treatment the antigenicity of haptoglobin and hemopexin changed markedly and more than 90% of the antigens appeared as aggregates in the void volume during the following size chromatography. Without loss of albumin haptoglobin and hemopexin were removed from the HPA preparation by lectin (concanavalin A) affinity chromatography. The haptoglobin- and hemopexin-depleted HPA preparation did not form aggregates or polymers during heat treatment.
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PMID:Identification and removal of polymer- and aggregate-forming proteins in human plasma albumin preparations. 780

Human urine contains a spectrum of proteins derived from various organs in the body. This investigation was undertaken to identify a group of proteins secreted primarily by bladder urothelium. Saline bladder washouts were collected from 9 male and 4 female patients undergoing routine cystoscopic examination. Each sample was sieved, desalted, freeze-dried and solubilized in urea mix. identical amounts of proteins were pooled according to donor sex. All individual and pooled samples were then subjected to 2-dimensional gel analysis using the ISO-DALT system. Profiles of both groups of subjects were highly reproducible, comparable and resembled those of urine and plasma. Several hundred spots were visualized although most of them as yet remain unrecognized. The proteins identified in bladder washouts include albumin, transferrin, IgG gamma-heavy chain, Gc-globulin, alpha 1-antichymotrypsin, alpha 1-antitrypsin, alpha 1-acid glycoprotein, G4, IgG light chains, alpha 1-microglobulin, and low and high density lipoproteins. Most importantly, while some abundant urinary macromolecules such as Tamm-Horsfall mucoprotein and most acidic urinary proteins were undetectable, albumin and transferrin were relatively less expressed. The 2-dimensional profiles we developed can be used as a data base to study urothelium derived proteins in various disease conditions such as bladder cancer.
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PMID:High resolution 2-dimensional electrophoretic analysis of proteins in saline bladder washings. 796 21


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