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)

We have grown a human hepatoma cell line, designated as HA22T/VGH, from a 52-yr-old male hepatoma patient since July 1, 1980. This cell line has been subcultured more than 100 passages. The chromosome analysis of HA22T/VGH indicated that the chromosome numbers varied from 70 to 146, with the mode of 73. Methylcellulose soft agar assay showed that approximately 40% of the HA22T/VGH cells formed colonies. The HA22T/VGH produced tumors in nude mice. Histopathological studies of the tumor revealed the arrangement of hepatoma. Detected by the complement fixation method HA22T/VGH cells secreted ceruloplasmin, Factor B, C3, C4, Gc-globulin and alpha 1-acid-glycoprotein. These cells contained the liver associated enzymes: alanine amino transferase, tyrosine amino transferase and gamma-glutamyl transferase. HBsAg and alpha-fetoprotein were not detectable in the HA22T/VGH culture media or cell lysates by the radioimmunoassay.
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PMID:[A new human hepatoma cell line: establishment and characterization]. 629 75

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

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), a multifunctional, highly polymorphic glycoprotein responsible for the transport of vitamin D and for sequestering extracellular actin, was isolated from human serum and crystallized using vapour diffusion methods. The crystals were grown from 7.5% v/v polyethylene glycol 400 and 0.1 M acetate buffer at pH 4.6. These crystals show diffraction patterns consistent with the tetragonal space groups P4(1) and P4(3) with unit cell dimensions a = b = 135.5(4) A and c = 75.9(4) A. They diffract to 2.3 A. Using polyacrylamide gel electrophoresis it was shown that according to their electrophoretic mobility the O-glycosylated isoforms, with a terminal sialic acid residue, are absent in the crystals.
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PMID:Crystallization and X-ray investigation of vitamin D-binding protein from human serum. Identification of the crystal content. 763 9

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

In vitro treatment of mouse peritoneal cells with 1 micrograms lysophosphatidylcholine (lyso-Pc)/mL in serum free-0.1% egg albumin-supplemented RPMI 1640 medium for 30 min, followed by 3 h cultivation in a medium supplemented with human serum, resulted in a greatly enhanced Fc-receptor-mediated phagocytic activity of macrophages. Vitamin D-binding protein (group-specific component [Gc]) of alpha 2-globulin fraction was shown to be the sole serum glycoprotein required for the generation of a potent macrophage-activating factor. When a mixture of lysophosphatidylcholine (lyso-Pc)-treated nonadherent and adherent cells were cultured in a medium supplemented with a small amount of purified Gc protein (1 ng/mL), a greatly enhanced activation of macrophages was demonstrated. The generation of macrophage-activating factor from purified Gc protein was far more efficient than that from whole serum, indicating that a serum component is inhibitory to the activation process of macrophages. While three other major serum glycoproteins (alpha 2-macroglobulin, alpha 2-HS-glycoprotein and haptoglobin) were neither stimulatory nor inhibitory to lyso-Pc-primed macrophage activation, serum albumin (competitively with Gc protein) appeared to be inhibitory to the process of macrophage activation.
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PMID:Vitamin D-binding protein (group-specific component) is the sole serum protein required for macrophage activation after treatment of peritoneal cells with lysophosphatidylcholine. 822 94

Plasma/serum proteins of fetal blood samples (N = 88) obtained under ultrasound guidance between the 18th and the 39th week of pregnancy, of blood samples collected from premature infants (N = 19), newborns at term (N = 20) and children of less than 5 years of age (N = 55) were analysed by high-resolution two-dimensional polyacrylamide gel electrophoresis. By comparison with adult 'reference' protein maps, tens of different proteins (and some of their genetic variants) were identified on the electrophoretograms. After the 18th week of gestation, albumin, transferrin, Factor B, glu- and lys-plasminogen, antithrombin III, Gc-globulin, alpha 1-antitrypsin, alpha 2-HS-glycoprotein, several apolipoproteins (apo A-I, A-II, A-IV, C-II, C-III, D, E, J), retinol-binding protein, transthyretin and alpha-fetoprotein could be observed. During intrauterine life, the size of the spots corresponding to alpha-fetoprotein progressively decreased, whereas the protein pattern globally showed an increase in the number and in the size of the spots. These modifications were particularly apparent in the regions of the electrophoretograms restricted to the heavy and light chains of IgG and to alpha 1-antichymotrypsin. In addition, we observed an unidentified fetal polypeptide characterized by an apparent molecular weight (M(r)) of 46 kDa (P46) and a pI of 5.0. P46 was present in all fetuses and all infants of less than 2 years of age.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Plasma/serum protein patterns in human fetuses and infants: a study by high-resolution two-dimensional polyacrylamide gel electrophoresis. 851 49

Two-dimensional (2-D) gel analysis was used to examine differences in the levels of 19 plasma proteins: before and after an acute inflammatory reaction (parenteral typhoid vaccination) in normal subjects, between rheumatoid arthritis (RA) patients and normals and in RA patients treated with tenidap (120 mg) and piroxicam (20 mg). Typhoid vaccination increased levels of SAA, haptoglobin alpha1, haptoglobin alpha2, haptoglobin beta and alpha1-anti-chymotrypsin but decreased transthyretin and apolipoprotein E. In RA patients, serum amyloid A (SAA), haptoglobin alpha2, haptoglobin beta, alpha1-antichymotrypsin and C3 proactivator levels were elevated while apolipoprotein A-I, apolipoprotein A-IV, transthyretin, Gc-globulin, alpha2-HS glycoprotein, alpha2-macroglobulin and alpha1-B glycoprotein levels were decreased, compared to normals. Compared to piroxicam, tenidap lowered levels of alpha1-antiprotease and SAA but raised the levels of transthyretin, Gc-globulin, alpha2-HS-glycoprotein and alpha2-macroglobulin in RA patients. C-reactive protein (CRP) could not be quantified on 2-D gels but, when measured by rate nephelometry, levels were reduced after treatment with tenidap compared to piroxicam. The general pattern of the acute phase protein response to an acute inflammatory response to typhoid vaccination is similar to that in the chronic inflammatory condition, RA. The impact of tenidap on both positive and negative acute-phase proteins in RA patients could clearly be distinguished from that of piroxicam.
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PMID:Analysis of changes in acute-phase plasma proteins in an acute inflammatory response and in rheumatoid arthritis using two-dimensional gel electrophoresis. 954 3

The separation of human serum globulins into individual components was investigated by capillary zone electrophoresis (CZE) using a linear polyacrylamide-coated capillary at pH 7.4. Prior to CZE analysis of globulin components present in serum, it was found that it was necessary to remove albumin. Preparation of albumin-depleted human serum with a HiTrap Blue column allowed the detection of alpha- and beta-globulin components as a series of peaks. Almost all the peaks, both narrow and broad, observed in CZE analysis could be assigned to six globulin components (alpha1-acid-glycoprotein, alpha1 -antitrypsin, haptoglobin, alpha2-macroglobulin, Gc-globulin, and transferrin) by using the technique of antibody-based indirect detection. The CZE results, obtained from serum preparations from three healthy adults and six patients, showed that the CZE system might be capable of detecting qualitative differences among individuals with regard to individual globulin components.
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PMID:Capillary zone electrophoresis of albumin-depleted human serum using a linear polyacrylamide-coated capillary: separation of serum alpha-and beta-globulins into individual components. 1067 21


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