| pubmed-article:4018461 | pubmed:abstractText | The components involved in cell adhesion were studied using the H6 line of embryonal carcinoma cells. H6 cells are especially suitable for studies on cell interactions, since genetic mutants can be selected, and various processes of cell adhesion can be controlled by regulating the calcium concentration in the medium. Three aggregation-defective variants of H6 were isolated, all of which showed reduced binding of the lectin, peanut agglutinin (PNA). Quantitation of PNA receptors on the cell surface by immunoprecipitation of iodinated surface proteins indicated that these receptors were reduced on the variants by one-half to one-quarter. The separation of immunoprecipitated PNA receptors on sodium-dodecyl-sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) demonstrated that one type of receptor, with an apparent molecular weight of 94 kilodaltons, was reduced. Parental and variant cells bind similar quantities of concanavalin A and soybean agglutinin, suggesting that there is no generalized effect on major glycoproteins. Thus, the defect in aggregation and the defect in the 94-kilodalton protein may be correlated, and this glycoprotein may have a role in the mediation of H6 cell-cell adhesion. | lld:pubmed |
