title: Patching, microvilli, and the agglutination of normal and transformed cells.
abstract: Transmission and scanning electron microscopy were used to study possible structural correlates in the process of agglutination of several types of normal and transformed cells by Concanavalin A. In parallel studies we found that post-confluence inhibition of cell division and agglutiniability of cells by Concanavalin A were not correlated with patching of surface bound lectin molecules as determined with a hemocyanin marker. Transformed cells growing in monolayer cultures were found to have many more microvilli than the corresponding normal cells. However, when cells were brought into suspension with EDTA, all cells developed numerous microvilli and we were not able to distinguish between agglutinable and nonagglutinable cells on the basis of morphological appearance. Cells agglutinated by Concanavalin A had numerous interdigitated microvilli at points of cell-cell contact. The appearance of spontaneously agglutinated cells and lectin agglutinated cells was very similar with respect to the involvement of microvilli in cell-cell attachments, and labeling studies with hemocyanin indicated that Concanavalin A bound to microvilli is rapidly cleared from these surface specializations in a manner analogous to that observed with patching of surface bound lectin. Several lines of SV-40 transformed fibroblasts were shown to be considerably more spontaneously agglutinable than untransformed cells. These results indicate that Concanavalin A may amplify an intrinsic membrane property common to many transformed cells that is expressed as an increase in the rate of adhesion of suspended cells. It is proposed that the membrane change detected by the agglutination reaction may also be involved in the loss of post-confluence inhibition of cell division and growth of transformed cells in semisolid media, due to a surface interaction that allows transformed cells to use each other as growth substrata.
mesh_terms: D000371:Agglutination; D001665:Binding Sites; D002460:Cell Line; D002462:Cell Membrane / Q000502:physiology* / Q000648:ultrastructure; D002471:Cell Transformation, Neoplastic; D003208:Concanavalin A; D003470:Culture Media; D006433:Hemocyanins; D008854:Microscopy, Electron; D008855:Microscopy, Electron, Scanning; D011485:Protein Binding
chemical_list: D003470:Culture Media; D003208:Concanavalin A; D006433:Hemocyanins