UMLS:C0027651 - FACTA Search

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Query: UMLS:C0027651 (tumor)
685,946 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A membrane-associated glycoprotein fraction, referred to a CEA-M was isolated from human colonic tumor tissue by sodium dodecyl sulfate extraction of membrane fragments followed by wheat germ agglutinin affinity chromatography, Bio-Gel A-1.5 gel filtration and preparative slab gel electrophoresis. With a m.w. of approximately 200,000, isoelectric point of about 4.2 and carbohydrate:protein ratio of 2:1, this glycoprotein has physiocochemical and antigenic similarities to carcinoembryonic antigen, CEA. Immunochemical studies have shown that antiserum developed for this glycoprotein possesses relative specificity for human colonic carcinomas. Chemical cleavage of this glycoprotein by 2-nitro-5-thiocyanobenzoic acid resulted in three major Coomassie Blue and two periodic acid Schiff stainable fragments (one of which stains with both). It was found that one of the glycopeptides, labeled as TA, isolated by affinity and covalent chromatography, contained 77% carbohydrates and possessed antigenic determinants recognized by at least 70% of the antibody population raised against the total glycoprotein fraction; purified antibodies to this region of the molecule seem promising for the development of a specific assay for gastrointestinal tumors.
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PMID:Colonic tumor membrane-associated glycoprotein: isolation of antigenically-active peptides after chemical cleavage. 6 65

The distribution of mucosubstances in adenoid cystic carcinoma was investigated, and an attempt was made to characterize histochemically the various mucosubstances present. For these purposes the high iron diamine technique (HID), as well as the Astra blue, aldehyde fuchsin and Alcian blue staining methods were employed. Alcian blue was further combined with the periodic acid-Schiff (PAS) technique, the Alcian blue being applied at pH levels between 0.5 and 2.5. In addition the effect of neuraminidase and hyaluronidase treatment as well as methylation and acid hydrolysis procedures on the staining qualities were studied. Acidic mucosubstances with varying histochemical properties were present in different structures of the neoplasm. The characteristic pseudocyst, a major structural component of the neoplasm, stained strongly with HID, Astra blue, aldehyde fuchsin and Alcian blue at low pH. These staining reactions were markedly suppressed by hyaluronidase treatment, and are apparently attributable to the presence of chondroitin 4- and/or 6-sulfate. Employing the Alcian blue-critical electrolyte concentration technique, the basophilia of the pseudocysts was suppressed at a concentration of 0.5-0.6 M MgCl2, which might indicate polysaccharides of relatively low degree of sulfation. An additional, non-sulfated acid mucin could also be demonstrated in these structures. In certain duct and gland like structures of the tumours, a change in staining pattern from blue or blue-red to red could be observed after exposure of the sections to neuraminidase and subsequent staining with the Alcian blue (pH 2.5)-PAS sequence. Similar observations were also made when the pH of the Alcian blue was lowered to 1.5-1.0, as well as after acid hydrolysis. These findings afford evidence for the presence of a neuraminidase susceptive sialomucin in certain epithelial secretions of the tumor. At the ultrastructural level the replicated basement lamina of the pseudocysts displayed a strong positive reaction with the PA-CrA-silver staining technique. Furthermore, amorphous material within the lumina of small duct like structures also displayed a positive reaction. The amorphous material of the cystic compartments was less reactive.
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PMID:Distribution of mucosubstances in adenoid cystic carcinoma. 7 83

An experimental procedure for detecting and characterizing tumor-associated, virion, and histocompatibility antigens has been developed. The method takes advantage of the high resolution that proteins, solubilized by Triton X-100 and reduced, display after sodium dodecyl sulfate gel electrophoresis. The antigens can be detected as distinct molecular weight species by a highly sensitive inhibition of cytotoxic reaction. When coupled to the lactoperoxidase-catalyzed iodination of intact cells, the procedure permits the determination of externally exposed antigens. In the present study, the method has been applied to the Moloney leukemia virus-induced YAC lymphoma cells of strain A mice, which express a Moloney leukemia virus-determined cell surface antigen (MCSA) in addition to the type C viral proteins gp71, p30, p15, p15(E), p12, and p10. MCSA was identified as an exposed surface protein distinct in size and antigenic determinants from the major envelope and core protein of Moloney leukemia virus and the histocompatibility antigens. Multiple molecular weight species possessing antigenic determinants for MCSA, gp71, and H-2(a) have been detected. These results provide direct confirmation that MCSA is unrelated to the known virion structural proteins or to the H-2(a) antigen. This method should permit the direct identification and molecular weight characterization of any antigen whose determinants are not solely dependent on a complex quaternary structure and for which serological reagents are available.
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PMID:Moloney leukemia virus-induced cell surface antigen: detection and characterization in sodium dodecyl sulfate gels. 7 31

Murine spleen cells from normal donors were cultured in vitro with trinitrobenzene sulfonate (TNBS)-conjugated soluble proteins, i.e., bovine gamma globulin (TNP-BGG) or bovine serum albumin (TNP-BSA). Addition of 100 mug of any of these TNP-proteins to the spleen cell cultures led to the generation of cytotoxic T-cell effectors which were H-2-restricted and TNP- specific. The lytic potential of such effectors was comparable to that generated by sensitization with TNBS-modified syngeneic cells, and was restricted to haplotypes shared at the K or K plus I-A, or the D regions of the H-2 complex. Greater effecter cell activity was generated by addition of TNP-BGG against TNBS-modified targets which shared K plus I-A than against modified targets which shared the D region with the responding cells, which suggests that the same immune response genes are involved when the response is generated by the addition of TNP-conjugated soluble proteins or of TNBS- modified cells. H-2-restricted, TNP-specific effecter cells were generated by culturing mouse spleen cells with syngeneic cells which had been preincubated with TNP- BGG or TNP-BSA for 1.5 h. The addition of unconjugated soluble proteins to the cultures did not result in cytotoxic effectors detectable on H-2-matched targets, whether the targets were prepared by modification with TNBS, or by incubation with either the unconjugated or TNP-conjugated proteins. Depletion of phagocytic cells in the tumor preparation by Sephadex G-10 column fractionation before incubation with TNP-BSA had no effect on their lysis by the relevant effector cells. Immunofluorescent staining of tumor target cells with anti-TNP antibodies indicated that TNP could be detected on the tumor cells within 10 rain of incubation with TNP-BSA. The cytotoxic response generated by addition of the TNP-proteins to spleen cell cultures was found to be T-cell dependent at the effector phase, as shown by the sensitivity of the lytic phase to absorbed RAMB and complement. Furthermore, the response did not appear to be attributable to antibody-dependent cellular cytotoxicity. Three mechanisms were considered which could account for the generation of H-2-restricted, TNP-specific, cytotoxic T-cell effectors by the addition of soluble TNP-proteins. These include covalent linkage of activated TNP groups from the soluble proteins to cell surface components, macrophage processing of the soluble conjugates and presentation to the responding lymphocytes in association with H-2-coded self structures, or hydrophobic interaction of the TNP-proteins to cell surfaces. Results obtained from sodium dodecyl sulfate gel patterns indicating that cell-bound TNP was still linked to BSA, and the observation that phagocytic-depleted cells could interact with the soluble TNP-proteins and function as H-2-restricted targets, appear not to favor the first two proposed mechanisms.
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PMID:H-2-restricted cytotoxic effectors generated in vitro by the addition of trinitrophenyl-conjugated soluble proteins. 7 37

Previous studies from this laboratory have mapped resistance and/or susceptibility to radiation-induced leukemia virus (RadLV)-induced neoplasia to the H-2D region. H-2 linked effects on virus replication can be detected subsequent to the initial virus infection, and clear-cut differences in numbers of virus infected thymus cells can be detected as early as 5 wk after RadLV inoculation. Rapid increases in cellular synthesis and cell surface expression of H-2 antigens are detectable immediately after virus inoculation. These changes have been studied by immunofluorescence, absorption, cell surface iodination followed by sodium dodecyl-sulfate-polyacrylamide gel electrophoresis, and two dimensional gel electrophoretic analysis of internally labeled lymphocyte proteins. Expression of H-2K molecules is significantly increased in cells of susceptible and resistant animals. However, significant increases in expression of H-2D antigens occurs only on thymus cells from resistant strains (H-2Dd). Transformed cells of resistant and susceptible H-2 haplotypes adapted to tissue culture lack detectable H-2 antigens as determined by serological absorption studies. It is argued that altered expression of H-2 antigens plays a very significant role in the mechanism of host defense to virus infection.
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PMID:Increased synthesis and expression of H-2 antigens on thymocytes as a result of radiation leukemia virus infection: a possible mechanism for H-2 linked control of virus-induced neoplasia. 7 39

The distribution of simian virus 40 (SV40)-specific proteins in nuclear subfractions of pulse-chase-labeled HeLa cells infected with nondefective adenovirus type 2 (Ad2)-SV40 hybrid viruses was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The SV40-specific proteins of Ad2+ND1, Ad2+ND2, and Ad2+ND5 specifically associate with the nuclear matrix and are virtually absent from the high-salt nuclear extract. In Ad2+ND4-infected HeLa cells, the SV40-specific proteins with molecular weights of 64,000 (64K) and lower also specifically associate with the nuclear matrix. The SV40-specific 72K, 74K, and 95K proteins were found both in the nuclear matrix and in the high-salt nuclear extract. Analyses of the nuclear matrices isolated from hybrid virus-infected cells by immunofluorescence microscopy showed that SV40 U-antigen-positive sera from SV40 tumor-bearing hamsters react with SV40-specific proteins integrated into nuclear matrices of HeLa cells infected by Ad2+ND1, Ad2+ND2, and Ad2+ND4, but not with nuclear matrices of HeLa cells infected by Ad2+ND5. This suggests that SV40-specific proteins of Ad2+ND1, Ad2+ND2, and Ad2+ND4 integrated into the nuclear matrix carry SV40 U-antigen determinants. The apparent discrepancy in the subcellular localization of SV40-specific proteins in hybrid virus-infected cells when analyzed by biochemical cell fractionation procedures and when analyzed by immunofluorescence staining is discussed.
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PMID:Simian virus 40 (SV40)-specific proteins associated with the nuclear matrix isolated from adenovirus type 2-SV40 hybrid virus-infected HeLa cells carry SV40 U-antigen determinants. 7 34

The simian virus 40-specific T-antigen has been extracted from SV AL/N mouse embryo tissue culture cells by treatment with Triton X-100 detergent. The extracts contained tumor-specific transplantation antigen (TSTA) and tumor-specific surface antigen. These extracts were purified by ammonium sulfate precipitation and diethyl-aminoethyl cellulose and phosphocellulose column chromatography and were assayed for the three antigens. We found that T-antigen, TSTA, and much of the tumor-specific surface antigen copurified through all purification steps. This finding is consistent with previous suggestions of the close degree of homology that must exist between the protein species carrying these three antigenic determinants. The antibody-mediated cytolytic assay appears to detect a new type of antigen on the cell surface, different from T-antigen and TSTA; two antigenic fractions were obtained from the phosphocellulose column that had tumor-specific surface antigen activity, but one of these did not have T-antigen or TSTA activities.
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PMID:Comparative behavior of simian virus 40 T-antigen and of tumor-specific surface and transplantation antigens during partial purification. 7 58

Tumor-specific and skin-reactive antigen of a syngeneic liposarcoma (H-10) of Hartley/F guinea pig was solubilized with 3M potassium chloride and purified by precipitation with 2M ammonium sulfate, followed by Sephadex G-200 gel filtration. The antigenic activity of 7 fractions obtained was estimated by the delayed-type skin reaction elicited in syngeneic animals immunized with H-10 cells admixed with BCG. Accurate relative activity of the fractions comparable to the skin reaction elicited by living H-10 cells was calculated by the parallel line assay method in which the dose-response curves of the fractions are compared with that of living cells. About 30 approximately 50 microgram protein of the 3 fractions eluted slowly from the Sephadex column elicited the skin reaction equivalent to that elicited with 1 X 10(6) of living H-10 cells. Tumor-specific skin reactivity per microgram protein of these 3 fractions was roughly 20 approximately 40 times higher than that of lyophilized cells.
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PMID:Tumor-specific skin-reactive antigen solubilized from a syngeneic guinea pig liposarcoma by 3M potassium chloride. 7 69

Rabbit antisera were prepared to chronic lymphatic leukemia (CLL) lymphocytes and were tested for their reaction with radioiodinated, solubilized, cell surface proteins of normal and CLL lymphocytes. A pooled, hyperimmune antiserum precipitated at least 16 polypeptides from both normal and CLL lymphocytes as shown by sodium-dodecyl sulfate polyacrylamide gel electrophoresis. These polypeptides varied in molecular weight from 11,000 to 180,000. None was prominent or unique to the CLL lymphocytes, although four peptide bands in the CLL cells usually showed more radioactivity than their counterparts in normal cells. Precipitation with antisera of known specificity showed that the cell surface proteins from CLL and normal lymphocytes included HLA antigens and beta2-microglobulin. IgM and IgD were found in preparations of normal cells and in cells of 3 of 5 CLL patients. Of cells from the other 2 patients, one showed only IgD and the other no Ig. An antigen-binding capacity test was employed to quantitate the antibody content of a pooled anti-CLL lymphocyte serum. The antiserum reacted with all Ig classes; however, after absorption with light chains and F(ab')2 fragments, the serum retained activity only for IgM and IgD. The absorbed antiserum bound 45 microgram IgM, 1.5 microgram IgD and 4.5 microgram beta2-microglobulin per milliliter. These data indicate that rabbit anti-CLL lymphocyte sera fail to detect a qualitatively unique tumor-specific polypeptide on the surfaces of CLL cells. However, such antisera contain antibodies to many cell surface proteins including IgM, IgD, HLA antigens and beta2-microglobulin.
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PMID:Quantitation of antibodies to IgM, IgD and beta2-microglobulin in antisera to chronic lymphatic leukemia lymphocytes. 7 57

A 32,000-dalton protein (p32) located in avian retrovirus cores was immunoprecipitated from [35S]methionine-labeled avian myeloblastosis virus (AMV) propagated in cultured chicken embryo fibroblast cells by an antiserum preparation (sarc III) derived from tumor-bearing hamsters injected with cloned and passaged cells from an avian sarcoma virus-induced primary hamster tumor. Since sarc III serum apparently contained antibodies only to virus-coded proteins and not to chicken cellular proteins, the immunoprecipitation of p32 from AMV by sarc III serum strongly suggested that p32 is virus coded. The origin of p32 was more definitively established by demonstrating the existence of a structural relationship between p32 and the AMV DNA polymerase. AMV p32 cross-reacted with the beta polypeptide of AMV alphabeta DNA polymerase in radioimmunoprecipitation and radioimmunoprecipitation inhibition assays, indicating that p32 and beta share common antigenic determinants. This relationship was clarified by sodium do-decyl sulfate-polyacrylamide gel electrophoretic analysis of the peptides generated by limited proteolysis of 125I-labeled AMV DNA polymerase polypeptides and of 125I-labeled AMV p32 by chymotrypsin or Staphylococcus aureus V-8 protease. The peptides which appeared during proteolytic digestion of p32 were a subset of those produced by digestion of the beta polypeptide; however, p32 had no discernible peptides in common with the alpha polypeptide. Further, all of the peptides produced by limited proteolysis of beta were present in the digests of either p32 or alpha. Our findings suggest that p32 is apparently derived by cleavage of the beta polypeptide of AMV DNA polymerase, presumably at a site near or identical to that at which alpha is generated from beta by proteolytic cleavage.
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PMID:Virus-coded origin of a 32,000-dalton protein from avian retrovirus cores: structural relatedness of p32 and the beta polypeptide of the avian retrovirus DNA polymerase. 8 16

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