title: Further studies on the relationship between allotransplantability and the presence of the cell surface glycoprotein epiglycanin in the TA3-MM mouse mammary carcinoma ascites cell.
abstract: The loss of strain specificity in the TA3-St mammary carcinoma ascites cell during passage in ascites form in diseased syngeneic strain A mice was confirmed by the observation that TA3-MM/2 ascites cells were capable of progressive growth in 7 foreign mouse strains. Support for the hypothesis that allotransplantability in the TA3-MM lines may be due to masking of cell surface histocompatibility H-2a antigens by large glycoprotein (epiglycanin) molecules was obtained from the finding that the capacity of the TA3-MM/2 ascites cell to absorb anti-H-2a antibody was several times less than that of the parent TA3-St ascites cell, although it was greater than the capacity of the non-strain-specific TA3-Ha line. Further support for the location of epiglycanin molecules at the cell surface was obtained by transmission electron-microscopic observation of a high concentration of filamentous structures, usually 20-40 nm long, but often extending to 200-300 nm length at the TA3-MM/2 cell surface. Similar structures were also observed at the TA3-Ha cell surface but were not observed at the surface of the TA3-St ascites cell, a cell known to contain no detectable epiglycanin. Epiglycanin molecules, obtained by two different methods from TA3-MM/1, TA3-MM/2, and TA3-Ha ascites cells, were shown to be similar with respect to their capacities to inhibit the binding of 125I-labeled epiglycanin to its antibody, induced in the rabbit by TA3-Ha ascites cells in a radioimmunoassay.
mesh_terms: D000818:Animals; D000912:Antibodies, Neoplasm / Q000276:immunology; D002460:Cell Line; D002462:Cell Membrane / Q000032:analysis / Q000648:ultrastructure; D005260:Female; D006023:Glycoproteins / Q000032:analysis* / Q000276:immunology; D006183:H-2 Antigens / Q000276:immunology*; D008325:Mammary Neoplasms, Experimental / Q000032:analysis / Q000276:immunology* / Q000648:ultrastructure; D008562:Membrane Glycoproteins; D008565:Membrane Proteins / Q000032:analysis*; D051379:Mice; D008854:Microscopy, Electron; D008871:Microvilli / Q000648:ultrastructure; D009363:Neoplasm Proteins / Q000032:analysis*; D009368:Neoplasm Transplantation; D014181:Transplantation Immunology
chemical_list: D000912:Antibodies, Neoplasm; D006023:Glycoproteins; D006183:H-2 Antigens; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D009363:Neoplasm Proteins; C016424:epiglycanin protein, mouse