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Query: UMLS:C0684249 (lung carcinoma)
 23,830 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Human embryonal carcinoma cells sometimes display the developmental potential of early embryonic stem cells. While available data do not clearly identify a counterpart of these tumor cells in normal development, previous comparisons of human embryonal carcinoma and yolk sac carcinomas indicated that these cell types are closely related, and suggested that embryonal carcinoma cells might resemble the progenitors of extraembryonic endoderm. To analyse further cell-differentiation lineage in these tumors, we produced monoclonal antibodies to cytostructurally associated antigens of human embryonal carcinoma cells. Spleen cells from mice immunized with a detergent-insoluble extract of cultured human embryonal carcinoma cells were fused to NS-1 myeloma cells, and hybridoma supernatants were screened by indirect immunofluorescence on the immunizing cell line, then on a panel of cell lines derived from human embryonal carcinomas, yolk sac carcinomas, and a range of neoplastic and normal tissues. Monoclonal antibody GCTM-1 stained the nuclei of all human cells tested and served as a positive control; this antibody immunoprecipitated proteins of 85 and 66 k Da from human embryonal carcinoma cells. GCTM-2 recognized an epitope on a 200-k Da extracellular protein present on the surface of embryonal carcinoma cells, and stained the surface of visceral yolk sac-type carcinoma and colorectal carcinoma cells as well. Enzymatic analysis of carbohydrate residues on the GCTM-2 antigen revealed that it was a keratan sulphate proteoglycan, and suggested that the epitope recognized by the antibody lies on the core protein. In immunoblots, antibody GCTM-3 bound to a 57-k Da cytoskeletal protein expressed in human embryonal carcinoma. This antibody decorated filamentous arrays in cell lines from human embryonal carcinoma, visceral yolk sac carcinoma, parietal yolk sac carcinoma (endodermal sinus tumour), and adenocarcinoma and large cell carcinoma of the lung. Antibody GCTM-4 recognized a determinant present on a 69-k Da polypeptide, associated with a component of the lysosomal compartment, which was expressed in embryonal carcinoma cells, but no other cell type tested. The results with this antibody panel thus allow distinction between human embryonal carcinoma and yolk sac carcinoma, but provide further evidence of a close relationship between these cell types.
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PMID:Analysis of cell-differentiation lineage in human teratomas using new monoclonal antibodies to cytostructural antigens of embryonal carcinoma cells. 324 84

The surface oligosaccharide residues, glycoproteins and sialyl components of CMT64 lung carcinoma cells and high-metastatic sublines CMT167 and CMT181 have been studied in culture. (1) The total cellular sialic acid content did not differ appreciably between the three lines. However, the accessibility of surface sialyl groups, measured by metabolic incorporation of [3H]NAcmannosamine followed by neuraminidase hydrolysis, was decreased from 42% in CMT64 to 25% hydrolyzed in CMT181. (2) The major plasma membrane glycoproteins of the lines were radiolabelled by lactoperoxidase iodination, metabolic incorporation of [3H]fucose or labelling in the terminal sialyl residues by the NaIO4-NaB[3H]4 method and the labelled glycoproteins were analyzed by two-dimensional gel electrophoresis. Each labelling technique identified a complex pattern of glycoproteins including a prominently labelled group of high-molecular-weight acidic sialoglycoproteins: GP200/4.9-5.1 (apparent molecular weight X 10(-3)/pl of iodoprotein); GP150/5.1-5.6; GP130/5.0-5.6; GP110/5.0; GP100/4.8 and GP100/5.0-5.4. (3) The neuraminidase-susceptible glycoproteins on CMT64 and CMT181 were identified in the isoelectric focusing separation of the two-dimensional gel separation by the charge difference caused by desialylation. The glycoproteins most susceptible to neuraminidase were the high-molecular-weight acidic glycoproteins which showed marked charge heterogeneity: GP150/5.1-5.6, GP130/5.0-5.6; GP100/5.0-5.4 and GP100/4.8. (4) Using these procedures we did not detect modifications between CMT181 and CMT64 and we conclude that the cultured cells of the sublines do not display marked surface glycoprotein alterations that reflect their enhanced spontaneous metastatic potential.
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PMID:Cell surface properties of high- and low-metastatic cell lines selected from a spontaneous mouse lung carcinoma. 665 29