Expression of Ia-like antigens on cultured human malignant melanoma cell lines (original) (raw)
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Ia-like antigen expression on biologically different human melanoma cell lines
European journal of cancer & clinical oncology, 1984
Ia-like antigen binding of a large panel of monoclonal antibodies (six anti-human Ia-like monoclonal antibodies and ten murine anti-Ia monoclonal antibodies cross-reactive with human Ia-like antigens) were compared on seven permanent human melanoma cell lines by radioimmunoassay. Cell lines were initiated from primary or metastatic tumors and presented various levels of tumorigenicity (assessed by heterotransplantation in nude mice) and pigmentation (shown by 5-S-cysteinyldopa determination and cytological data). Two cell lines originated from the same primary melanoma, while two other pairs of cell lines originated from superficial spreading melanoma or metastatic lymph node of the same patients. Identical Ia-like allodeterminants were found in cell lines of the same individual origin. Quantitative expression of beta 2-microglobulin and Ia-like antigens was similar in all cell lines except for one, in which these molecules were expressed in lower amounts. These results indicate tha...
Cancer Immunology Immunotherapy, 1981
Human malignant melanoma cell lines were assayed for secretion of plasminogen activator (PA) and for growth in the nude mouse. It was observed that cell lines that were high producers of PA also grew in the nude mouse. In order to detect differences in membrane constituents of cells related to these parameters of malignancy, antisera were raised in non-human primates against the high producer (Mel A-375) and the non-producer cell of PA (SK-Me125). After extensive absorption the two antisera showed little or no cross-reactivity with the other cell line. Several subclones were isolated from SK-Me125 and assayed for PA production and growth in the nude mouse. Two sublines (S 5 and S 13) were found that produced moderate amounts of PA and grew in the nude mouse, whereas five other sublines were negative in both respects. By means of antisera against sublines it could be shown that patterns of surface antigens were distinct from that of the parental line.
Cell surface antigens of human melanoma identified by monoclonal antibody
Proceedings of the National Academy of Sciences, 1979
Mouse NS-1 myeloma cells were fused with spleen cells from mice that had been immunized with cells from a human melanoma, M1804. Hybrid cells were grown in selective medium and tested for production of antibody to surface antigens of M1804 cells. Three hybrids that produced antibodies that bound to the melanoma cells but not to autologous skin fibroblasts were cloned. Antibodies produced by two of the clones were cytotoxic to M1804 cells in the presence of rabbit complement. Extensive specificity tests showed that the antibodies produced by the clones bound strongly only to M1804 cells; significant, although weaker, binding occurred with 2 of 11 allogeneic melanomas. Apart from weak binding of the antibody produced by one of the clones to a breast carcinoma, binding assays of five carcinomas, one sarcoma, and fibroblasts from 17 individuals were negative, as were cytotoxic tests of 10
Cancer Research, 1987
To identify melanoma associated antigens (MAAs) shared by human and guinea pig melanoma cells, a battery of murine monoclonal antibodies (MoAl>s) to human MAA and an antiserum to S100 protein were tested with four newly established guinea pig melanoma cell lines. Only the monoclonal antibodies 149.53 and 225.28 which recognize distinct deter minants of the human high molecular weight-MAA (HMW-MAA) re acted with all four guinea pig melanoma cell lines. To compare the binding site of MoAbs 149.53 and 225.28 with guinea pig and human melanoma cells, inhibition binding experiments were performed with antiidiotypic monoclonal antibodies which completely inhibit the binding of MoAbs 149.53 and 225.28 to human melanoma cells. The binding of M«Ah149.53 to guinea pig melanoma cells was partially inhibited by antiidiotypic MoAbs MF9-10 and MK1-180 which recognize distinct private idiotopes within the antigen combining site of MoAb 149.53. On the other hand the binding of MoAb 225.28 to guinea pig melanoma cells was completely inhibited by antiidiotypic MoAbs MF11-30 and I M-12 which recognize distinct private idiotopes within the antigen combining site of MoAb 225.28. These results suggest that the determinant recog nized by MoAb 149.53 on guinea pig melanoma cells is similar but not identical to that recognized on human melanoma cells, while the deter minants recognized by MoAb 225.28 on the two types of cells do not display any detectable differences under the experimental conditions tested. The target structure on the guinea pig melanoma cells identified by MoAbs 149.53 and 225.28 is a M, 280,000 molecule which has the same apparent molecular weight as one of the two subunits of the HMW-MAA synthesized by human melanoma cells. Sequential immunoprecipitation experiments with guinea pig melanoma cells showed that the determinant recognized by MoAb 149.53 is expressed on a subpopulation of the molecules recognized by MoAb 225.28. Immunohistochemical staining with MoAb 225.28 of a variety of different tissues from normal adult guinea pigs showed that the corresponding antigenic determinant is detectable only in basal cells of epidermis and hair follicles of skin. SIIMI protein, which is a cytoplasmic constituent of normal human melanocytes, benign nevi, and malignant melanocytes, was also detected in the cyto plasm of the four cultured guinea pig melanoma cells lines. The results of the present investigation may lead to a better understanding of the phylogenetic evolution of the human HMW-MAA and suggest that guinea pig melanoma may serve as a useful animal model for immunobiological studies and carcinogen-induced tumorigenesis investigations.
Cancer research, 1985
Mouse monoclonal antibodies (mAb) detecting 13 distinct systems of surface antigens on cultured melanocytes and melanomas were tested for reactivity with panels of (a) normal and malignant cultured cells; (b) normal adult and fetal tissues; and (c) specimens of metastatic melanoma and other tumor types. The objectives of this study were to compare antigen expression in cultured versus noncultured cells, to develop a panel of mAbs that identify subsets of melanomas, and to provide requisite information about antibody specificity in preparation for the use of antibodies in the diagnosis, imaging, and therapy of melanoma. Five of the melanoma surface antigens have been well characterized biochemically [GD3, chondroitin sulfate proteoglycan, HLA Class II antigens, glycoprotein of molecular weight 130,000 (gp130), and glycoprotein Mr 95,000/protein Mr 97,000 (gp95/p97)]. Three antigens have been related to melanocyte differentiation (HLA Class II, M111/M231, and M144), and six provide ad...
International Journal of Clinical & Laboratory Research, 1981
Summary Analysis of the tissue distribution of human Ia-like antigens has shown that they have a wider distribution than originally reported. Furthermore, the expression of Ia-like antigens may change when cells undergo malignant transformation: for instance, melanoma cells acquire Ia-like antigens, while breast carcinoma cells lose them. Serological and immunochemical analysis of Ia-like antigens with monoclonal antibodies has shown a cellular
International Journal of Cancer, 1986
The functional properties of the melanoma-associ ated antigens detected by monoclonal antibodies (MAbs) A M F-6 and A M F-7 w ere investigated. These MAbs w ere selected previously because of their capac ity to block the anti-m elanom a reactivity of cytotoxic T-lymphocyte clones A M F-6 and AMF-7 detect a me(anoma-associated proteoglycan (M W > 450-250 kDa) and a molecular complex, which under reducing con ditions consists of 4 compounds of 120, 95, 29 and 25 kDa respectively. A M F-6 reacted strongly with all 30 cultured melanomas and all 41 melanomas in frozen tissue sections. Significant cross-reactivity was only observed with nevi and perineurium, whereas normal skin melanocytes w ere negative. AMF-7 reacted with all 25 cultured melanomas and all 34 melanomas in frozen sections. A M F-7 cross-reacted with a propor tion of nevi and endothelial cells from small vessels. The antigen detected by A M F-6 and AMF-7 could not be modulated by retinoic acid or recombinant 7-IFN, which induced or enhanced the expression of HLA-DR, H L AD Q and Class-1 M H C antigens. In addition, the antigens w ere not readily modulated when cells were incubated in excess amounts of A M F-6 and AMF-7. Interestingly, the antigen detected by AMF-7 was strongly associated w ith the adhesion and cytoplasmic spreading of m elanom a cells to plastic surfaces and monolayers of vascular endothelial cells. A M F-6 did not block the adhesion of melanoma cells but delayed cytoplasmic spreading. Both A M F-6 and AMF-7 blocked fibronectin-induced chemotaxic m otility and chemokinesis of m elanom a cells. In addition to their m em brane localization, the antigens detected by AMF-6 and AM F-7 w ere also abundant in extracellular adhe sion plaques deposited by cultured melanoma ceils. O u r results indicate th at the high-MW melanomaassociated proteoglycan and the antigen detected by A M F-7 are associated w ith adhesion and/or cyto plasmic spreading and m o tility of human melanoma cells, suggesting that these antigens ¿ire associated with the (hematogenic) dissemination of human mela noma« This is supported by the finding that AMF-7 stained prim ary tum ors heterogeneously, whereas metastases w ere homogeneously stained.