Carbohydrate-mediated adhesion of human colon carcinoma cells to human liver sections.

Clinicopathological observations have revealed that the expression level of a carbohydrate antigen recognized by the monoclonal antibody (mAb) FH6 in colorectal carcinomas is higher at advanced stages than at early stages. The present study aimed to elucidate whether human colon carcinoma cell surface glycans recognized by mAb FH6 determine the ability of these cells to adhere to sections of human liver. Variant human colon carcinoma cell lines selected for high and low binding of mAb FH6 were compared with respect to their adhesive capacity. The cells expressing the higher level of FH6 binding also showed a greater ability to adhere to liver sections. This adhesion was not blocked by anti-E-selectin monoclonal antibodies, but pretreatment of the carcinoma cells with endo-beta-galactosidase significantly reduced both cell surface binding of mAb FH6 and the ability of the cells to adhere to liver sections. Our observations suggest that endo-beta-galactosidase-sensitive carbohydrate chains containing an epitope recognized by mAb FH6 play an important role in the adhesion of human colon carcinoma cells to human liver sections. Whether these interactions have any relationship to the mechanism(s) of liver metastasis remains to be elucidated.