Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q86TM3 (cage)
 29,987 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An antigen, protein X (Px), was purified from immune complexes isolated from malignant pleural effusions from patients with adenocarcinoma of the lung by EDTA treatment, PEG 8000 precipitation, protein A affinity chromatography, and Sephadex G-200 separation in the presence of 3 M NaCl. The purified antigen had a M(r) 17,000 by SDS-PAGE, and consisted of isoelectric species of pI 6.3 and 6.6. Purified Px recombined with Ig isolated from pleural fluids from patients with lung adenocarcinoma, but not with Ig from patients with breast carcinoma. Using an autologous human and heterologous chicken antibody, Px was found, by immunohistology, in the cytoplasm of some of the well-differentiated lung adenocarcinoma cells, but was not seen in normal lung or a variety of other malignant tissues. A liquid-phase competitive-inhibition RIA was developed. Over 30 ng/ml of Px were found in 9 of 15 pleural fluids from patients with lung carcinoma, none of 20 from patients with breast, ovary, stomach or colon cancer, and in 3 of 15 patients with unknown primary tumor. Our data suggest that Px may be a lung-cancer-associated autoantigen which can elicit a host humoral response in vivo.
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PMID:Characterization of a lung-cancer-associated auto-antigen. 139 30

Pancreatic and mammary cancer cells are reported to have different oligosaccharides on the same apomucin, the MUCI gene product. A better understanding of the tissue specificity of these sugar structures may help in identifying the source of mucins when they are found in the sera. Serum levels of 3 pancreatic-cancer-associated carbohydrate epitopes identified by monoclonal antibodies (MAbs) SPan-1, 19-9 and DU-PAN-2, were compared to those of CA15-3 in a variety of malignant conditions. CA15-3 identifies both carbohydrate and peptide determinants associated with the MUC1 apomucin in breast tissues. SPan-1 antigen was elevated in a high percentage of patients with pancreatic, gastric and colorectal cancer but in only a few of the patients with malignancies of non-GI origin such as breast, ovary and lung. The 19-9 and DU-PAN-2 antigens had a similar pattern of much greater sensitivity for pancreatic cancer than for these non-gastrointestinal cancers. The levels of these 3 markers showed significant correlations in pancreatic cancer. In contrast, CA15-3 was elevated in a large number of patients with breast, lung, ovarian and pancreatic cancers. There was no correlation of CA15-3 with the 3 other markers in pancreatic cancer. SPan-1 and DF3/115D8 antigens in blood have different mobilities in SDS-PAGE and buoyant densities. Moreover, SPan-1 and DF3 antigenic determinants are localized in different regions of the same normal and malignant pancreas and breast tissues. Thus the SPan-1 determinant can be dissociated from the breast peptide and/or carbohydrate determinants.
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PMID:Differences in expression of SPan-1 and CA15-3 antigens in blood and tissues. 142 28

A total of 72 human leukemia-lymphoma cell lines were studied for reactivity with the monoclonal antibody (MAb) A7, an anti-human colon-cancer-cell-associated antigen reagent, by indirect membrane immunofluorescence. Nine of the 72 cell lines expressed the antigen recognized by A7 MAb. Five of the 34 T-cell lines, 2 of the 21 B-cell lines, and 2 of the 3 non-lymphoid-non-myeloid cell lines were reactive with A7 MAb. By means of SDS-PAGE and immunoblotting, the antigens isolated from both colon cancer cell lines (WiDr, SW1116 and LoVo) and leukemia cell lines (A3/KAWAKAMI, H9, RPMI 8226 and SPI-801) showed an identical MW of 42-43 kDa. The non-glycosylated antigen recognized by A7 MAb, which was expressed on both the colon cancer line (SW1116) and the leukemia line (H9) in the presence of tunicamycin, also showed an identical MW of 36 kDa. However, the quantity of the antigen in the leukemia cells was significantly lower than in the colon cancer cells. Although expression of this colon-cancer-associated antigen in the non-colon cancer cells is real, the significant expression of this antigen in colon-cancer cells makes it useful for clinical monitoring of colon cancer patients.
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PMID:Identification and characterization of a colon-cancer-associated antigen expressed on leukemia-lymphoma cell lines. 199 51

Many tumour-specific antigens in gastrointestinal cancers have carbohydrate immuno-determinants. These epitopes can be identified by lectins and monoclonal antibodies. By using fluorescein-isothiocyanate (FITC)-conjugated peanut agglutinin (PNA) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) we have investigated glycoproteins carrying altered carbohydrate epitopes in normal and carcinomatous human colorectal mucosa. In normal mucosa PNA stained goblet cell glycoconjugates in the supranuclear (Golgi) distribution. After neuraminidase pretreatment PNA stained actual mucin goblet itself at all levels of the crypts. Colorectal carcinomas displayed a strong and direct binding of PNA to apical cell membranes of carcinomatous cells and intraluminal secretions. Analysis of the glycoproteins by SDS-PAGE and PNA-labelling revealed four carcinoma-associated glycoproteins (26kD, 32kD, 35kD and 50kD). In addition, four glycoproteins (29kD, 30kD, 33kD and 36kD) common to normal and carcinomatous colorectal mucosa could be identified. All of these glycoproteins differed in their molecular weight from those in red cell controls which bind PNA only after desialylation. The study shows that the expression of PNA-binding sites in colorectal carcinomas signifies a cancer-associated carbohydrate alteration. Four carcinoma-associated glycoprotein antigens could be detected by this lectin. The antigens we have identified might be useful in the isolation and purification of more selective reagents for the serologic detection of colorectal cancer.
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PMID:Identification of glycoproteins expressing tumour-associated PNA-binding sites in colorectal carcinomas by SDS-GEL electrophoresis and PNA-labelling. 243 45

The glycoprotein gp51 of bovine leukaemia virus (BLV) has been included in an immunostimulating complex (ISCOM). The ISCOM was characterized biochemically in SDS-polyacrylamide gel electrophoresis showing the presence of proteins of estimated molecular weights of 50 and 30 kDa. Immunoblotting showed that gp51 was present in the ISCOM. The BLV-ISCOM had a S-value of 19 S and the electronmicrograph showed the cage-like structure as previously reported for other ISCOMs. About 17% of the total amount of gp51 in the cell culture fluid was recovered in the ISCOMs. The largest loss of gp51 was encountered during the sedimentation of the virus. An ELISA, utilizing monoclonal antibodies to defined epitopes for capture was developed to control the antigenicity of epitopes, e.g. those known to induce neutralizing antibodies. Using this device as a quality control for epitopes the following could be stated. First, ISCOMs prepared from virus solubilized with the non-ionic detergents Triton X-100 or MEGA did not react with neutralizing monoclonal antibodies. In contrast, ISCOMs prepared from virus solubilized with the non-ionic detergents Tween-20, Tween-80 or octyl glucoside did react with the neutralizing antibodies. Second, the neutralizing epitopes were better exposed in ISCOMs than the other epitopes of gp51. In a preliminary experiment it was shown that gp51 in ISCOMs was highly immunogenic.
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PMID:Bovine leukaemia virus ISCOMs: biochemical characterization. 254 75

The pharmacokinetics of 111In-labeled 260F9, a murine monoclonal antibody directed against a breast-cancer-associated antigen, was determined in seven patients with advanced breast cancer. Six patients were administered 1 mg antibody containing 1 mCi 111In. The seventh patient was administered 20 mg unlabeled antibody followed by 1 mg 111In-labeled antibody all via a peripheral vein. Immunoprecipitation, HPLC and SDS-PAGE gels demonstrated the stability of radiolabel on the antibody. The serum clearance of the radiolabel closely fits (r2 greater than 0.95) a two-compartment model for the first six patients. The apparent volume of distribution of the radiolabel approximated to the plasma volume (31) and its mean residence time was 23.7 h. The radiolabel had an average t 1/2 beta of 22.9 +/- 12.21 h at the 1-mg dose. At the 20-mg dose one-compartment elimination kinetics were observed with the radiolabel and antibody showing similar mean residence times (36-41 h) and a t 1/2 beta of 26-28 h. Whole-body imaging showed that the blood-pool: liver ratio of radioactivity increased fourfold (at 48 h postinfusion) at the higher dose and the percentage of the injected dose of radioactivity in the liver decreased from 25% to 8% (24 h postinfusion). In one patient 7-14 times more radioactivity was localized in a breast tumor than in fat (normal breast). Over the first 25 h an average (cumulative) 7.5% of the total dose was excreted in urine. A study of 260F9 in CDF-1 mice demonstrated that the radiolabel remained associated with the antibody in serum. The antibody, however, cleared 60-fold slower in mice than in patients and showed an increased mean residence time of 191 h. The disparity in the pharmacokinetics of the antibody seen in the mouse and in the clinic, points to the different behavior shown by murine monoclonal antibodies in humans. This points to the need for preliminary studies of antibodies in patients for preclinical evaluations of their effectiveness as drug-targeting agents.
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PMID:A preliminary pharmacokinetic study of 111In-labeled 260F9 anti-(breast cancer) antibody in patients. 270 39

Immunostimulating complexes (ISCOMs) have been prepared from feline leukaemia virus (FeLV) envelope proteins. The ISCOMs were characterized biochemically in SDS-polyacrylamide gel electrophoresis showing the presence of proteins of estimated molecular weights of 15,000, 27,000 and 70,000. Immunoblotting showed that both the transmembrane protein p15E and the external glycoprotein gp70 (making up the gp85 protein) were present in the ISCOM. Furthermore, a degradation product of gp70 with an estimated molecular weight of 32,000 was identified in the immunoblot. The FeLV ISCOM was shown by electron microscopy to have the characteristic cage-like structure of an ISCOM with a mean diameter of 37 nm. About 10% of the total amount of gp70 in the culture fluid was recovered in the ISCOMs. The largest loss was encountered during the sedimentation of the virus. In a preliminary immunization experiment in mice the FeLV ISCOMs elicited after a booster gave a clear-cut immune response against gp70.
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PMID:Formation and characterization of FeLV ISCOMs. 275 Feb 72

The GABA receptor of mammalian brain is a ligand-gated channel protein with allosteric binding sites for the benzodiazepines and barbiturate drugs. The receptor is an acidic oligomeric membrane glycoprotein and it has been purified to homogeneity from bovine cerebral cortex, bovine cerebellum and rat cerebral cortex by benzodiazepine affinity chromatography. In each case, extraction and purification with the zwitterionic detergent CHAPS and exogenous phospholipid has demonstrated the coexistence of GABA, benzodiazepine and cage convulsant ligand binding sites on a single protein complex; in addition the allosteric interactions between these sites are preserved in the isolated protein. The receptor has a heterologous structure that is conserved at the subunit level between the aforementioned mammalian species and brain regions. SDS-PAGE has shown that the receptor consists of two subunits, alpha (Mr 53000) and beta (Mr 57000) present in equal stoichiometry. A model consistent with the determination of the molecular weight of the native protein, i.e., Mr 230,000, is that of a tetramer alpha 2 beta 2. [3H]Flunitrazepam and [3H]muscimol have been employed as photoaffinity labels to map the benzodiazepine and GABA binding polypeptides respectively. Polyclonal and monoclonal antibodies have been raised to the native bovine GABAA receptor and these have been employed for the further characterisation of the receptor protein.
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PMID:Progress towards the understanding of the GABAA receptor structure. 304 Sep 81

An experimental infectious model in rabbits was used to study the release of bacterial substances in vivo in relation to the development of renal lesions, using three different group A Streptococci (type M56, M12 and T3). Three weeks post infection, renal lesions were confirmed in animals infected with M56 and M12, but not T3 streptococci, by histological and immunohistological analyses of the kidneys. Tissue-cage fluid (TCF) from the potentially nephritogenic strains (M56 and M12) showed a time-related increase of proteins and a production of streptococcal antibodies in serum. Isoelectrofocusing of TCF from nephritogenic and non-nephritogenic strains showed the presence of "nephritogenic-strain-specific" proteins in the most cationic region as well as in pH region 5.8-6.4. Immunoblotting after SDS-PAGE of TCF revealed a nephritogenic-strain-restricted protein that, by means of a mouse-monoclonal antibody, identified with the NSAP (Nephritic-Strain-Associated Protein). The biological activity demonstrated in the focus of infection using the M56 and M12 strains thus seems to be related in time to the induction of the nephritic process.
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PMID:Demonstration of streptococcal antigens produced in vivo and identification of a nephritis associated protein. 390 68

Porcine brain coated vesicles were isolated from crude fractions of tissue homogenates by affinity separation using anticlathrin-coated STaphylococcus aureus (Staph A) cells as a solid-phase immunoadsorbent. The specificity of the immunoadsorption was monitored by SDS PAGE analysis and by competitive ELISA assays. SDS PAGE of the material immunoadsorbed from a fraction of porcine bran smooth microsomes showed a selective enrichment in a 180,000 mol wt protein. In an ELISA assay, this protein competed effectively--in binding anticlathrin--with clathrin extracted from a coated vesicle preparation. When the immunoadsorbed fraction was examined by electron microscopy, coated vesicles and vesicle-free cages were found forming a quasicontinuous monolayer on the surface of the Staph A cells. Other particles were not adsorbed, and the controls were free of either clathrin cages or coated vesicles. Upon extensive dialysis (against MES buffer, pH 6.5), similar cages appeared on the surface of anticlathrin-coated Staph A cells reacted with extracted clathrin. This study demonstrates that anticlathrin-coated Staph A cells can be used for the isolation and purification of a homogeneous population of coated vesicles. In addition, the ability of extracted clathrin to bind and to polymerize onto the Staph A cells raises the possibility of using this technique to further explore the conditions required for cage and/or vesicle reconstitution.
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PMID:Coated vesicle isolation by immunoadsorption on Staphylococcus aureus cells. 704 38


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