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Query: UMLS:C0025202 (melanoma)
 69,561 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An immunogen consisting of a 4M urea extract derived from human melanoma cells (M14), that was devoid of HLA-A,B,C, HLA-DR antigens and fibronectin was adsorbed to lens culinaris lectin-Sepharose 4B and used to immunize mice for production of monoclonal antibody to a melanoma-specific glycoprotein. Screening for hybridomas secreting antibodies to melanoma associated antigens was facilitated by use of a solid phase target antigen of chemically defined medium of melanoma cells (CDM). Use of these procedures allowed us to select 40 hybridomas secreting antibody which recognized determinants on melanoma cells not found on lymphoid cells. Further characterization of one of these hybridomas, 9.2.27, indicated that the antibody it secreted recognized a 240K dalton glycoprotein found on all melanoma cell lines tested but not on carcinoma, lymphoid, or fibroblastoid cultures. These results demonstrate the utility of soluble antigen preparations devoid of strongly immunogenic non tumor-specific molecules in the elicitation of tumor specific antibody. Preliminary results suggest that immunogens of this kind are superior to intact melanoma cells for production of tumor specific hybridomas.
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PMID:Production and characterization of monoclonal antibody to a melanoma specific glycoprotein. 620 19

Two monospecific human antibodies (anti-OFA-I-1 and anti-OFA-I-2) produced in vitro by lymphoblast cell lines originating from melanoma patients have been shown previously to recognize cell surface antigens (OFA-I-1 and OFA-I-2) on human tumors and fetal brain: OFA-I-1 is expressed on a variety of human tumors, while OFA-I-2 has been detected only on tumors of neuroectodermal origin. Evidence presented in this report suggests that the two antigens expressed by a cultured human melanoma cell line (M14) are chemically distinct and that OFA-I-2 is a cell surface glycolipid, ganglioside GD2: GalNAc beta 1 leads to 4 NeuAc alpha 2 leads to 8NeuAc alpha 2 leads to 3 Gal beta 1 leads to 4Glc-ceramide.
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PMID:Identification of a human neuroectodermal tumor antigen (OFA-I-2) as ganglioside GD2. 629 43

Interferon-gamma affected the expression of the products of the immunoassociated antigen complex by a differential modulation of DR- and DC-locus-controlled molecules. In melanoma M14 cells treated with interferon-gamma, levels of DR molecules were increased two- to threefold, whereas levels of DC molecules were increased six- to sevenfold. Similar effects were induced on the two allelic products of each locus.
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PMID:Differential effects of gamma interferon on expression of HLA class II molecules controlled by the DR and DC loci. 641 9

UCLA-SO-M14, a human melanoma cell line, was cultured for ten passages in vitro. The line was converted to an ascitic form, M14-A, by transplanting M14 into CD-1 nude mice and back into tissue culture. The minimum number of M14-A cells that formed ascites in all mice (within 10-21 days) was 5 X 10(5), and over 80% of such mice developed macroscopic liver metastases. M14-A inoculated subcutaneously formed tumor at the site of injection, but rarely led to the development of metastases. However, when M14-A was inoculated subcutaneously in young mice (1-14 days old), more than 50% developed lung (but not liver) metastases. The reproducibility of the formation of ascites and metastases was confirmed by testing M14-A at various passages. M14-A may be useful as a model for the metastatic process in human melanoma.
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PMID:Establishment of an ascitic human melanoma cell line that metastasizes to lung and liver in nude mice. 647 27

A human IgM monoclonal antibody was produced in vitro against OFA-I-2, a human tumor membrane antigen. This antigen is expressed on tumors of neuroectodermal origin, and has been identified as the ganglioside GD2. This study examines the anti-tumor effect of the monoclonal antibody against a GD2-positive human melanoma cell line, M14, inoculated subcutaneously into athymic CD-1 nude mice. Tumor-free survival was prolonged markedly when the monoclonal antibody and M14 cells were inoculated simultaneously. When antibody and complement were also injected into established tumor nodules, M14 tumor growth was suppressed. However, intraperitoneal injection of the antibody did not alter the growth of the subcutaneously inoculated M14 cells. The antibody has no effect on the growth of a GD2-negative melanoma cell line, M24. These results indicate that the human monoclonal antibody to GD2 may be useful for the suppression of GD2-positive tumor cells in cancer patients if the tumor can be directly exposed to the antibody and complement.
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PMID:Human monoclonal antibody to ganglioside GD2-inhibited human melanoma xenograft. 654 Jun 88

Human IgM kappa monoclonal antibody (anti-GD2) to a tumor antigen, ganglioside GD2, has been produced by Epstein-Barr virus-transformed human B lymphoblasts. In the present study, we demonstrated the anti-tumor effects of passively administered anti-GD2 against an ascites-form human melanoma cell line, M14-A, transplanted into athymic nude mice. M14-A expresses GD2 in vivo. Cells (5 X 10(5) were inoculated intraperitoneally (i.p.) or subcutaneously (s.c.) into CD-1 nude mice that had received i.p. injections of 200 micrograms anti-GD2 and rabbit complement. Significant tumor-free intervals were observed in the treated mice (P less than 0.005) for i.p. tumors and P less than 0.025 for s.c. tumors). M14-A formed well-vascularized s.c. tumors if injected into young nude mice. Three-wk-old CD-1 nude mice bearing 2-3 mm M14-A s.c. tumor nodules were treated i.p. with anti-GD2 and rabbit complement. Tumor growth was delayed for 25 days. On day 15, treated tumors were 20% the size of control tumors. Because most biopsied or autopsied melanomas express GD2, and because patients with melanoma produce autoantibodies to GD2, the results in this study may provide important information for future passive immunization with human monoclonal antibody and for active specific immunization with GD2 antigen.
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PMID:Human monoclonal antibody to tumor-associated ganglioside GD2: suppressed growth of human melanoma in nude mice. 654 67

A tumor-associated antigen (TAA) was isolated from spent culture medium (chemically defined serum-free medium) of human melanoma cell line UCLA-SO-M14 (M14). The isolation procedures included concentration, ultrafiltration, gel filtration chromatography, and chloroform:methanol (C:M) extraction. The melanoma TAA activity recovered from the organic phase of the C:M extract was subsequently fractionated by gel filtration and radiolabeled with Na125I. The radioiodinated antigen was further purified by Sephacryl S-200 gel filtration and allogeneic antibody affinity chromatography. With the use of previously characterized anti-TAA allogeneic sera from melanoma patients and 125I-labeled TAA, a radioimmunoassay (RIA) was developed. Protein A-bearing Staphylococcus aureus was used to separate bound and unbound 125I-labeled TAA. The coefficient of variation between experiments and within experiments with unlabeled melanoma TAA as the competitor in the competitive RIA ranged from 8.9 to 20.4%. These variations were consistently lower (8.9-13.6%) at high levels (6 micrograms melanoma TAA/ml) of the competitor than they were (17.3-20.5%) at low levels (0.5 microgram melanoma TAA/ml), suggesting reasonable reproducibility of the assay. A logit versus log plot of the competitive RIA data and analysis by linear regression yielded a straight line. This line represented a 5- to 1,000-ng detection range for melanoma TAA. Analysis of C:M-extracted and Sephacryl S-200-purified melanoma TAA by the competitive RIA revealed a 695-fold purification of the antigen that represented a 37.5% recovery from the spent culture medium. The greatest enrichment of the melanoma TAA was achieved by the C:M extraction step. This step separated the melanoma TAA from other antigens, e.g., fetal antigen and human leukocyte antigens.
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PMID:Studies of a melanoma tumor-associated antigen detected in the spent culture medium of a human melanoma cell line by allogeneic antibody. I. Purification and development of a radioimmunoassay. 658 4

A tumor-associated antigen (TAA) was isolated from spent culture medium of human melanoma cell line UCLA-SO-M14 (M14). After radioiodination and further purification, it was used in a radioimmunoassay (RIA). When tested in RIA for anti-TAA activity, 56% (111/200) of sera from melanoma patients, 21% (21/100) of sera from sarcoma patients, and 19% (19/100) of sera from carcinoma patients, as well as 12% (6/50) sera from pregnant women and 10% (10/100) apparently normal sera, were positive. The variations (0.25-3.8 micrograms/mg total protein) in specific TAA activity in 20 different batches of spent media collected for 18 months exhibited patterns of gradual increases and decreases, suggesting a cell growth cycle-related phenomenon. Binding between the allogeneic antibody and 125I-labeled TAA was inhibited by 70% (32/47) of melanoma spent media and cells (from culture or biopsy). Conversely, only 7% (3/33) spent medium or membrane extracts of other tumor cells and 0% (1/69) of human normal, fetal, or placental cells were positive in competitive RIA. The TAA was immunologically different from normal tissue antigens, blood-group antigens, human leukocyte antigens, and microbial antigens. These immunobiologic properties of the TAA isolated from M14 spent culture medium and used in the RIA suggested that such TAA was melanoma associated.
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PMID:Studies of a melanoma tumor-associated antigen detected in the spent culture medium of a human melanoma cell line by allogeneic antibody. II. Immunobiologic characterization. 658 5

A melanoma tumor-associated antigen (TAA), isolated from spent culture medium of human melanoma cell line UCLA-SO-M14, was purified to mean homogeneity to determine its physical and biochemical nature. Gel filtration and native polyacrylamide gel electrophoretic analyses of the 125I-labeled melanoma TAA revealed that the antigen had a molecular weight in the range of 180,000-190,000. However, ultracentrifugation of melanoma 125I-labeled TAA in a 5-20% sucrose density gradient revealed a sedimentation coefficient to be 4.96 +/- 0.24. Melanoma 125I-labeled TAA focused at a pH of 6.5 by isoelectric focusing. No carbohydrates were detectable by various colorometric methods in the highly purified melanoma TAA fraction, and melanoma TAA failed to bind with several lectins. Its antigenic activity was destroyed by the proteolytic enzymes but was not affected by the glycosidic enzymes or phospholipase A2. The results suggested that the melanoma TAA was most likely a lipoprotein that had a molecular weight of 180,000-190,000, a sedimentation coefficient of approximately 5, and a pl value of 6.5. The protein portion apparently formed the antibody binding site(s).
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PMID:Studies of a melanoma tumor-associated antigen detected in the spent culture medium of a human melanoma cell line by allogeneic antibody. III. Physicochemical properties. 658 6

A human melanoma cell line, M14 , adapted to grow in serum free synthetic media was examined for its expression and secretion of several serologically defined melanoma associated antigens (MAA) previously described in this laboratory. Melanoma associated antigen expression and secretion was identical to that of M14 cells grown in parallel in serum supplemented medium. Spent synthetic media was found to be an enriched serum free source for the initial isolation of 100 kilodalton secreted glycoprotein MAA. M14 melanoma cells grown in synthetic media were also shown to be adaptable to the double agar clonogenic assay facilitating the examination of clonal heterogeneity in functional studies of MAA in melanoma tumor biology. Recent investigations from this laboratory have focused on characterizing human melanoma associated antigens (MAA) found either as secreted or cell surface associated glycoproteins in human melanoma cell lines. In these studies, monoclonal and polyclonal antiserums to melanoma cell components have been developed to specifically identify these MAAs immunochemically and provide a means to study the structural biochemistry of these determinants. At this time we have identified two antigens on which our research efforts are targeted: 1) a 100,000 dalton secreted glycoprotein (100K) common to melanoma, sarcoma and neuroblastoma tumor cell lines, and 2) a 250,000 dalton-high molecular weight component glycoprotein-proteoglycan complex which is thus far restricted to melanoma cells. The ultimate goal of our efforts is two-fold. Initially, we hope to develop schemes to isolate these melanoma associated antigens in sufficient quantities to obtain detailed structural information on these molecules, and secondly, we wish to implicate these glycoproteins in functional aspects of the biology of metastatic human melanoma in vitro.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Antigenic expression of human melanoma cells in serum-free medium. 673 Nov 48


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