Molecular pathology of cancer cell adhesiveness

A new cell surface-associated adhesive glycoprotein with a molecular weight of 70,000 was separated from differentiated rat ascites hepatoma cells forming cell islands in vivo (but not from undifferentiated rat ascites hepatoma cells present as single cells in vivo) and highly purified by chromatography; it was synthesized by the cells and localized on the cell surface. Its synthesis began to rise rapidly and reached its peak in 24 hr cultivation, i.e., a 10-fold increase. This substance induced not only aggregation but also adhesiveness of the cells characterized by junctional complexes including tight junctions, desmosomes, and intermediate junctions, closely resembling the frequency and distribution of junctional complexes observed on the above cell islands. Its potency was inhibited specifically by D-mannose and alpha-methyl-D-mannoside; the numbers of the binding sites per cell were calculated as 6 x 10(5). Its activity was concerned with the protein portion of the molecule, and not with the carbohydrate portion. Thus, it seemed reasonable that the adhesive glycoprotein may play a key role in the cell adhesiveness and island formation. In contrast, serum-associated adhesive glycoprotein, separated from normal rat serum, could aggregate the cells but not develop junctional complex.