Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0025202 (melanoma)
 69,561 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The expression of a human melanoma-associated antigen, p97, in cultured melanoma cells was investigated using a modification of the Sternberger peroxidase-antiperoxidase (PAP) technique. Explant cultures of two skin melanomas were found to consist of a mixture of cells, some positive and some negative, for the expression of p97. From two other melanomas two cell lines were newly established. All cells from these lines expressed detectable p97 over a period up to 18 months. With the cell lines and the explant cultures we have initiated an investigation of the expression of p97 at the ultrastructural level, using the PAP technique. Antigen expression was detected as a continuous, strongly stained band at the cell surface of the melanoma cells.
 ...
PMID:Localization of melanoma-associated antigen p97 in cultured human melanoma, as visualized by light and electron microscopy. 684

The authors sought S-100 protein in sections cut from formalin- or glutaraldehyde-fixed, paraffin-embedded tumors from the eye and other sites by an immunoperoxidase technique, using rabbit antibovine S-100 protein antiserum, swine antirabbit serum, a peroxidase-antiperoxidase preparation, and amino-ethylcarbizole as developer. Tissue from 26 intraocular tumors was examined, the pathologic diagnosis being unknown to the investigators at that time that the tests were performed. Thirteen of 16 malignant melanomas of the choroid contained S-100 protein (81%), while only one of seven retinoblastomas contained S-100 protein (14%). One cutaneous malignant melanoma metastatic to the eye contained S-100 protein, while none of three metastatic nonmelanocytic, nonneural tumors contained the protein. These results are similar to our findings with nonocular tumors, in which 56 of 56 cutaneous melanomas contained S-100 protein (100%) and only 1 of 51 nonneural, nonmelanocytic tumors contained S-100 protein (2%). S-100 protein may be useful as a marker for ocular malignant melanoma.
 ...
PMID:Detection of cytoplasmic S-100 protein in primary and metastatic intraocular melanomas. 687 80

A xenoantiserum to murine B16 melanoma cells was developed by immunizing rabbits with cultured B16 melanoma cells. This antiserum could, after extensive absorption with normal C57BL/6 mouse tissues, react with syngeneic (B16) and allogeneic (HP) melanomas as well as with other murine neoplasms, including syngeneic 75S adenocarcinoma, allogeneic myeloma and leukemic T cell lines. The antiserum also cross-reacted with syngeneic fetal fibroblasts and with an allogeneic fetal fibroblast cell line (SC-1) either uninfected or infected with murine leukemia virus (MuLV). Immunoprecipitated material from B16 melanoma cell-surface glycoproteins that had been labeled with [125I] by lactoperoxidase and purified by a Lentil lectin column was analyzed by one-dimensional SDS- and two-dimensional polyacrylamide gel electrophoresis, which disclosed an acidic glycoprotein with a molecular weight (mol. wt) of 90 K daltons. Absorption studies suggested that the 90 K mol. wt gylcoprotein represented the oncofetal moiety expressed in murine medanoma, carcinoma and fetal tissues. When the amount of this antigen in developing C57BL/6 mouse fetuses was measured by absorption assays, we found that it was expressed strongly in those fetuses just before birth. Binding and absorption studies demonstrated that the 90 K mol. wt glycoprotein, while being expressed on a variety of fetal and neoplastic cells in mice, did not exist at detectable levels in normal tissues of adult C57BL/6 mice, including tissues of the thymus, lymph node, spleen, liver, brain, lung and kidney.
 ...
PMID:Identification of an oncofetal antigen (gp90) on murine B16 melanoma cells. 688 31

Xenoantiserum to human malignant melanoma was prepared by immunizing rabbits with melanoma associated antigens (MAA) solubilized from melanoma cell membrane by limited papain digestion. The antiserum was absorbed extensively with red cells, leukemia cells and cultured lymphoid cell lines, and was assayed for its reactivity with different human cell types by the indirect membrane immunofluorescence and radioimmunoprecipitation techniques. The data obtained suggest that there are at least two different MAA on human melanoma cells. The first is melanoma-group specific and can be detected commonly on different melanoma cell lines. The second is oncofetal and is shared by melanoma, carcinoma, and fetal cells tested thus far. Immunoprecipitated material from melanoma cell membrane that had been radioiodinated with lactoperoxidase and solubilized with a non-ionic detergent was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, which showed two major peaks with estimated molecular weights of 90,000 and 120,000 daltons. The 90,000 molecular weight component appears to be oncofetal, as it disappeared when the antiserum was absorbed with either melanoma or carcinoma cell lines.
 ...
PMID:Surface antigenic characteristics of human melanoma cells defined by xenoantiserum raised against papain-solubilized melanoma-associated antigens. 702 33

Surface macromolecules on cultured human melanoma cells wee radioiodinated by a lactoperoxidase method. Macromolecules shed into culture medium were collected, concentrated, and fractionated on Sepharose 6B and lentil lectin-Sepharose. Radioactivity associated with macromolecules was assayed by precipitation with trichloracetic acid, and that associated with melanoma-associated antigens (MAA) was assayed by specific immunoprecipitation with xenogeneic anti-melanoma serum. Following the last step in purification, approximately two-thirds of the acid-insoluble radioactivity in the most MAA-active fraction was associated with this antigen. MAA concentration in this fraction was approximately 200-fold greater than that in cells, and it contained a single labeled protein band by polyacrylamide gel electrophoresis in sodium dodecyl sulfate. The MAA was a glycoprotein consisting of a single polypeptide chain with a molecular weight of approximately 75,000. This antigen was common to several but not to all melanomas. It was not detected, or was present in much decreased concentration, in 16 other unrelated allogeneic or xenogeneic normal and malignant cells. It was immunologically unrelated to serum albumin or fibronectin. These observations indicate that we have highly purified a Mr 75,000 cell surface component of human melanoma cell which appears to be a MAA.
 ...
PMID:Identification and purification of a Mr 75,000 cell surface human melanoma-associated antigen. 704 82

A monoclonal antibody, F11, was produced against a tumor-associated antigen from the spent medium of the M14 human malignant melanoma cell line which was grown continuously in serum-free medium. Ouchterlony double-diffusion study revealed that the F11 monoclonal antibody is an immunoglobulin G1. The F11 monoclonal antibody reacted positively with seven of eight (88%) melanoma, five of five (100%) carcinoma, zero to five normal, and zero of two lymphoblastoid cell lines by indirect immunofluorescence test. Also, by indirect immunofluorescence test, F11 monoclonal antibody reacted with cryostat sections from four of five (80%) melanomas, six of seven (86%) carcinomas, zero of one benign nevus, and zero of two benign breast diseases. By the indirect avidin:biotin:peroxidase complex immunoperoxidase method, the F11 monoclonal antibody reacted positively with cryostat sections from five of five (100%) melanomas, five of five (100%) breast cancers, two of two (100%) colon cancers, zero of one benign nevus, and zero of one Hodgkin's disease spleen. Thus, the tumor-associated antigen that the F11 monoclonal antibody recognizes appears to be expressed by melanomas and carcinomas, hence the designation melanoma-carcinoma-associated antigen. Microscopic observations disclosed that the melanoma-carcinoma-associated antigen is present in the cytoplasm, on the membrane of melanoma and carcinoma cells, and in the lumen of glandular structures of breast and colon carcinomas. The molecular weight of the melanoma-carcinoma-associated antigen in spent medium from the M14 CEM cell line is 100,000 as determined by sodium dodecyl sulfate:polyacrylamide gel electrophoretic analysis of indirect immunoprecipitates obtained with the F11 monoclonal antibody.
 ...
PMID:Mouse monoclonal antibody to a melanoma-carcinoma-associated antigen synthesized by a human melanoma cell line propagated in serum-free medium. 704 18

The fate of cell surface macromolecules released by human melanoma cells in vitro was studied. Labeled surface macromolecules released by lactoperoxidase-radioiodinated melanoma cells were incubated cells. It was found that some of these macromolecules were autocatabolized to acid-soluble fragments by the cells which had released them. Degradation did not occur in the absence of cells, was almost completely inhibited at 4 degrees, and was partially suppressed by cytochalasin B (10 micrograms/ml) and by some inhibitors of energy production, i.e., iodoacetamide (10(-4) M) and a combination of 2-deoxyglucose (18 mg/ml) and 2,4-dinitrophenol (10(-4) M). Radioiodinated surface macromolecules were degraded much more rapidly than radioiodinated serum proteins. Thus, degradation required the presence of cells, was in part an active process, and was selective. These results suggest that one of the pathways for the turnover of surface macromolecules on tumor cells is shedding followed by autocatabolism of the shed material by the cells which they have released.
 ...
PMID:Autocatabolism of surface macromolecules shed by human melanoma cells. 707 5

The surface proteins of seven human cell lines (three bladder carcinomas (TCC), two normal urothelial lines, one colon carcinoma, and one malignant melanoma) were labelled with 125I by the glucose oxidase-lactoperoxidase technique. Plasma membranes of the cells were isolated and analysed by sodium dodecyl sulphate electrophoresis (SDS-PAGE). When analysed under reducing conditions by staining with protein stain, approximately 45 distinct membrane polypeptides were detected in all membrane preparations. Although the banding patterns for all cell lines were very similar, a 23 K and a 110 K band were only seen in the five unrothelial lines. When the same gels were analysed by autoradiography, between 13 and 17 bands were detected for each of the cell lines. However, in this case, analysis revealed individual and stable banding profiles for each. One 180 K band and one 100 K band were only seen in the autoradiographs of the two normal lines but not in those of the tumor membranes. Analysis under non-reducing conditions gave similar results. The antigenicity of these surface components was analysed by incubating detergent extracts of surface-iodinated cells with IgG from a rabbit anti-TCC serum, absorbed with fetal bovine serum and bound to protein A (from Staphylococcus aureus) on a matrix of Sepharose 4B. Analysis of the eluates by autoradiography after SDS-PAGE under reducing conditions showed that many of the labelled polypeptides were antigenic and shared by all seven cell lines. Analysis of eluates from IgG preparations, exhaustively absorbed with human spleen, revealed the presence of at least one antigenic 110 K polypeptide confined to the membrane of the urothelial cells. Preparation of a rabbit antiserum to this 110 K component, isolated from one of the TCC-lines and tested by ADCC, indicated that this polypeptide constitutes an important surface antigen, present on urothelial cells of both TCC- and normal origin but absent from the colon carcinoma and malignant melanoma used for control.
 ...
PMID:Plasma membrane-associated antigens on tumor cells derived from transitional-cell carcinoma of the human urinary bladder. II. Identification at the molecular level of plasma membrane-associated antigens. 720 13

The role of cell surface glycoproteins in determining in vivo blood-borne arrest and survival characteristics of murine melanoma sublines of low (B16-F1) or high (B16-F10) potential to form experimental lung metastases after injection i.v. was assessed after inhibiting tumor cell protein glycosylation with tunicamycin. Incubation of B16-F1 or B16-F10 cells with 0.5 micrograms (or above) tunicamycin per ml for 12 to 36 hr inhibited significantly lung tumor colony formation. Examination of B16 cells in the presence of 0.5 micrograms drug per ml indicated that complex oligosaccharide synthesis was inhibited greater than 90%, while protein synthesis remained at about 50% of the control levels. Tunicamycin induced morphological changes in B16-F1 and B16-F10 cells such as cellular rounding. Cell growth was also inhibited by tunicamycin. These effects were reversible, and B16 cells recovered their normal morphologies and growth rates within 24 hr after removal of the drug. Exposed cell surface protein analyzed by lactoperoxidase-catalyzed 125I iodination-sodium dodecyl sulfate-polyacrylamide gel electrophoresis-autoradiography showed few changes after tunicamycin treatment; however, sialogalactoproteins (detected by the binding of 125I-labeled R. communis agglutinin I to polyacrylamide gels containing desialized B16 cell surface components) were reduced dramatically by the drug. The adhesive properties of untreated and tunicamycin-treated B16 cells were assessed by the binding of 51Cr-labeled B16 cells to endothelial cell monolayers. Tunicamycin-treated B16-F1 and B16-F10 cells adhered at lower rates to endothelial cells such that after 24 to 36 hr of drug (0.5 micrograms/ml) treatment adhesion was almost completely blocked, suggesting that tunicamycin-induced cell surface glycoprotein changes in B16 melanoma cells may interfere with tumor cell-host cell interactions that lead to arrest and survival of blood-borne malignant cells.
 ...
PMID:Effects of tunicamycin on B16 metastatic melanoma cell surface glycoproteins and blood-borne arrest and survival properties. 726 Sep 6

Glycoproteins of a metastasizing line of B16 mouse melanoma and a poorly metastasizing wheat germ agglutinin-resistant clone were compared. Cell surface proteins and glycoproteins were isotopically labeled by lactoperoxidase-catalyzed iodination and by NaB3H4 reduction after oxidation by periodate or galactose oxidase and subsequently analyzed by gel electrophoresis and autoradiography. Differences were observed in the relative mobilities of several major cell surface components. Binding of 125I-labeled lectins to total cellular proteins on polyacrylamide gels following electrophoresis showed that the major wheat germ agglutinin-binding components of F1 cells were altered in Wa-4 cells. Similar differences were not observed in concanavalin A-binding components. Total cellular glycopeptides were analyzed after separation into structurally distinct classes. The acidic "complex" N-glycosidic glycopeptides from the resistant cells were of lower molecular weight than those from the parent cells. No differences were observed among the mannose-rich N-glycosidic glycopeptides or the alkali-labile O-glycosidic oligosaccharides. Structural studies involving methylation analysis revealed that in the altered glycopeptides of the resistant cells the amount of neuraminic acid residues was decreased to one-half, concomitant with an increase in the amount of fucose. The lost sialic acid was bound to C-3 of galactose, whereas the increased fucose was found on C-3 of 4-substituted N-acetylglucosamine. A possible basis for the glycosylation change and its relation to the biological behavior are discussed.
 ...
PMID:Carbohydrate changes in glycoproteins of a poorly metastasizing wheat germ agglutinin-resistant melanoma clone. 738 14


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