Comparative lectin-binding and agglutination properties of the strain-specific, TA-3-St, and the non-strain-specific, TA3-Ha, murine mammary carcinoma ascites sublines. Further studies of receptors in epiglycanin.
The complex carbohydrates at the cell surfaces of two TA3, murine mammary carcinoma ascites sublines (the strain-specific, TA3-St subline and the nonstrain-specific. TA3-Ha line) were compared by binding studies with 125I-labelled concanavalin A (con A), Ricinis communis agglutinin (RCA), and eel-serum agglutinin (ESA). The TA3-Ha cell bound equal amounts of con A, 1.5-fold more RCA, and 4-fold more ESA than the TA3-St cell. Binding-inhibition studies by these lectins and two others [wheat-germ agglutinin (WGA) and potato lectin (STA)] suggest complementary binding-sites between con A and both RCA and ESA. Quantitative agglutination studies with the five lectins, and inhibition determinations by both neuraminidase-treated and untreated epiglycanin revealed that TA3-St, but not TA3-Ha, cells were agglutinated by con A, and that epiglycanin inhibited this agglutination, as well as the agglutination of rabbit erythrocytes by con A. The presence of a con A receptor on epiglycanin was also suggested by the binding of epiglycanin to con A-Sepharose, and its specific elution with methyl alpha-D-mannopyranoside. TA3-St cells were agglutinated at a 10-15-fold lower concentration of either STA or RCA than TA3-Ha cells, but both cells were agglutinated by the same concentration of WGA and ESA. Inhibition by epiglycanin of agglutination of TA3-St cells by either STA or ESA occurred at a concentration lower than that of TA3-Ha cells, but epiglycanin inhibited RCA agglutination of TA3-Hs cells at a concentration lower than that of TA3-St cells. Epiglycanin, but not asialoepiglycanin, inhibited the agglutination of TA3-Ha cells by WGA.
D000371:Agglutination / Q000187:drug effects; D000818:Animals; D001202:Ascitic Fluid / Q000166:cytology; D002460:Cell Line; D003208:Concanavalin A / Q000494:pharmacology; D004524:Eels; D006023:Glycoproteins / Q000494:pharmacology*; D007457:Iodine Radioisotopes; D007785:Lactose / Q000494:pharmacology; D037102:Lectins / Q000494:pharmacology; D008325:Mammary Neoplasms, Experimental / Q000276:immunology*; D008562:Membrane Glycoproteins; D051379:Mice; D037121:Plant Lectins; D010947:Plants, Toxic; D011975:Receptors, Mitogen / Q000378:metabolism*; D012278:Ricinus
D006023:Glycoproteins; D007457:Iodine Radioisotopes; D037102:Lectins; D008562:Membrane Glycoproteins; D037121:Plant Lectins; D011975:Receptors, Mitogen; C016424:epiglycanin protein, mouse; D003208:Concanavalin A; D007785:Lactose