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

A low-molecular-weight acceptor of galactosyltransferase activity was detected in sera and effusions of patients with extensive maligant disease. This substance was purified to homogeneity from both human serum and effusion by using sequential charcoal/Celite and DEAE-cellulose column chromatography. The purified acceptor was shown to act as substrate for both purified normal and cancer-associated human galactosyltransferase (EC 2.4.1.22) isoenzymes, but had a higher affinity for the cancer-associated isoenzyme (Km = 20 microM) than for the normal isoenzyme (Km = 500 microM). The substrate was found to be a glycopeptide with mol.wt. approx. 3600 determined by polyacrylamide-gel chromatography. Carbohyydate analysis demonstrated only the presence of glucosamine and mannose. Amino acid analysis revealed that the peptide moiety consisted of eight different amino acids, including two residues of asparagine and one residue of serine, but no threonine. These structural data suggest that the acceptor is a fraction of an asparagine-glucosamine type of glycoprotein.
 ...
PMID:Detection, purification and characterization of a human cancer-associated galactosyltransferase acceptor. 8 90

Two cancer-associated proteins, carcinoembryonic antigen (CEA) and pregnancy-associated alpha2 glycoprotein (PAG), together with 13 normal serum proteins were measured in the serum and effusion fluid of patients with ascites and pleural effusions. The results indicate that CEA measurement in effusion fluid is more effective than serum measurement in distinguishing cancerous from congestive or inflammatory effusions. Comparisons with the results of cytological examination suggest that fluid CEA estimation may prove a useful clinical tool. Serum PAG levels were higher in patients with cancer, but fluid determination offers no advantage in separating the disease groups. Similarly, the estimation of individual normal serum proteins in effusion fluids is unlikely to be of diagnostic value.
 ...
PMID:Cancer-associated proteins in effusion fluids. 87 10

Double antibody radioimmunoassay of carcinoembryonic antigen (CEA), a cancer-associated antigen of the human digestive system, was subjected to certain modifications and critically evaluated. Modifications pertained to: (a) the production of a high titer goat anti-CEA antiserum that was rendered highly specific by solid phase immunoabsorption with cyanogen bromide-activated Sepharose conjugates of normal plasma liver, and colon perchloric acid-soluble glycoprotein antigens: (b) the introduction of suitable alterations in the experimental conditions of radioiodination procedure to minimize and to prevent breakdown of the antigen, thus prolonging the storage of the labeled antigen; (c) the extended incubation period of CEA-anti-CEA immune reaction; and (d) the use of sodium acetate buffer, pH 6.1. Furthermore, the use of an automatic pipetting station for accurate and rapid reagent dispensation and statistical analysis of the radioimmunoassay data on a modern computer to ensure strict quality control of the assay provided some definite improvement over the existing assay.
 ...
PMID:Modifications and evaluation of double antibody radioimmunoassay of human carcinoembryonic antigen. 94 17

A new antigen associated with pancreatic cancer was prepared by immunoaffinity chromatography using Fab'-Sepharose beads. This antigen was a glycoprotein of large molecular weight (Mr greater than 8,000,000) in its native state, estimated by size exclusion chromatography on Sephacryl S400. After sodium dodecyl sulfate-polyacrylamide gel electrophoresis and blotting analysis, several cancer-associated glycoconjugates, including CA19-9, CA50, Span-1, Dupan-2, and sialyl SSEA-1, were detected on the antigenic moiety of Mr 90,000. By an enzyme immunoassay for the antigen, elevated levels were found in pooled sera obtained from patients with various malignant and non-malignant diseases and normal subjects. However, the enhanced expression of CA19-9, Lewisa, or Lewisb epitope on the antigen molecule was restricted to the pooled sera from patients with pancreatic cancer. Furthermore, antigens from pancreatic or gastric cancer expressed ligands with intense and specific reactivity for Bauhinia purpurea (BPA), peanut (PNA), and Vicia villosa (VVA) lectins. The present assay system of the antigen, using both monoclonal antibodies (CA19-9, Lewisa, and Lewisb) and lectins (BPA, VVA and PNA), will provide a useful approach to the diagnosis of pancreatic cancer.
 ...
PMID:Preparation of pancreatic cancer-associated mucin expressing CA19-9, CA50, Span-1, sialyl SSEA-1, and Dupan-2. 168 94

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.
 ...
PMID:Identification of glycoproteins expressing tumour-associated PNA-binding sites in colorectal carcinomas by SDS-GEL electrophoresis and PNA-labelling. 243 45

The Thomsen, Friedenreich (TF) and Tn carbohydrate antigens are expressed on the vast majority of human adenocarcinomas and are associated with aggressive behavior of certain tumors. TF and Tn antigens are also expressed on certain murine cancer cell lines including TA3-Ha, a highly lethal, transplantable mammary adenocarcinoma. TF and Tn cancer-associated carbohydrate haptens were synthesized, conjugated to protein carriers and used to demonstrate that delayed-type hypersensitivity (DTH) effector T cells can specifically recognize and respond to carbohydrate determinants on the TA3-Ha tumor-associated glycoprotein, epiglycanin. The effector cells were shown to have the helper DTH phenotype (Lyt1+, Lyt2-, Thy1+) and it was demonstrated that they respond to specific carbohydrate determinants in an MHC-restricted fashion. These experiments provide the rationale for the use of synthetic tumor-associated glycoconjugates (S-TAGs) to stimulate anticancer T cell immunity. In support of this hypothesis, it was shown that preimmunization with the appropriate S-TAGs could provide a degree of protection against a subsequent tumor transplant and that antitumor effector Lyt1+, Lyt2- T cells could be generated in vitro using the appropriate S-TAGs as antigens.
 ...
PMID:T cell recognition of a tumor-associated glycoprotein and its synthetic carbohydrate epitopes: stimulation of anticancer T cell immunity in vivo. 244 86

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.
 ...
PMID:Bovine leukaemia virus ISCOMs: biochemical characterization. 254 75

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.
 ...
PMID:Formation and characterization of FeLV ISCOMs. 275 Feb 72

Adenosine deaminase complexing protein (ADCP), a dimeric glycoprotein, has been reported to be decreased or deficient in transformed or cancer-derived cell lines, indicating its potential significance as an indicator of malignant transformation. A similar deficiency was reported in total homogenates of tumours of colon, kidney, lung and liver. In previous biochemical studies we failed to confirm the consistent reduction in ADCP concentration in cancer tissues. A possible explanation for our findings was thought to be intercellular heterogeneity in ADCP expression in individual tumour cells. To study ADCP expression in individual cells, we developed an immunohistochemical method which was applied to tissue sections. Paraformaldehyde--lysine--periodate (PLP) solution was found to be a suitable fixative. Fixed tissue samples were paraffin-embedded, sectioned and stained for ADCP, using an indirect peroxidase-labelled antibody procedure. The protein was localized in normal colonic mucosa, mainly in the brush border region of the luminal epithelium and in cytoplasmic granules. Intense ADCP immunoreactivity was found also in the basal part of some cells. In cancer cells, three staining patterns were observed: membranous, diffuse cytoplasmic and granular cytoplasmic. The adenocarcinomas exhibited significant intratumour and intertumour heterogeneity in their staining types. Further studies on ADCP expression in colorectal cancer in relation to clinical and histopathological characteristics are warranted in order to fully evaluate the potential significance of ADCP as a cancer associated antigen.
 ...
PMID:Immunohistochemical localization of adenosine deaminase complexing protein in intestinal mucosa and in colorectal adenocarcinoma as a marker for tumour cell heterogeneity. 285 62

Advances in the understanding of biochemical and molecular processes associated with cellular growth and differentiation, as well as colonic carcinogenesis hold promise for the development of new diagnostic and therapeutic modalities for this disease. Altered glycosylation of cell surface and secreted glycoconjugates appear to be useful markers in differentiating normal from malignant colonic tissue. New information regarding deletion and inappropriate expression of several blood group-related carbohydrate antigens as well as the synthesis of unique cancer-related carbohydrate structures has been derived from the use of monoclonal antibody technology, and may lead to more sensitive and specific screening tests and targeted therapies. Several glycoprotein markers for colon cancer have been studied whose diagnostic accuracy may surpass the limited sensitivity and specificity of traditional markers such as CEA. Colorectal cancers contain numerous quantitative and qualitative differences in metabolic and synthetic enzyme activities compared with normal colonic mucosa, which may be of potential importance in designing chemotherapeutic regimens or for following disease activity. Other cancer-associated markers, such as increases in orthinine decarboxylase activity and crypt cell labeling reflect abnormal proliferative activity and may be correlated with premalignant states. Studies of protooncogene expression and certain chromosomal deletions will provide insight into mechanisms of carcinogenesis and may also serve to define high-risk individuals. It is likely that as the biochemical and molecular mechanisms underlying malignancy are further delineated, cancer-associated markers will be defined that will improve diagnostic and more importantly, therapeutic efficacy.
 ...
PMID:Biochemical and other markers of colon cancer. 306 43


1 2 3 4 5 6 7 8 9 10 Next >>