Expression levels of FUT6 gene transfected into human colon carcinoma cells switch two sialyl-Lewis X-related carbohydrate antigens with distinct properties in cell adhesion.

A human colon carcinoma cell line KM12-LX, expressing low levels of monoclonal antibody (mAb) FH6 epitope, was transfected with alpha 1,3-fucosyltransferase VI cDNA. Clonal populations with high or intermediate expression levels of the mRNA, shown by RT-PCR (FT6hi and FT6in cells, respectively) were obtained. FT6hi cells were found to express both mAb FH6 and KM93 epitopes by flow-cytometric analysis, whereas FT6in cells expressed mAb FH6 epitopes but not mAb KM93 epitopes. The mAb FH6-binding was abrogated by endo-beta-galactosidase treatment of FT6in, but not FT6hi, cells. FT6hi but not FT6in cells adhered to Chinese-hamster-ovary cells expressing human E-selectin. FT6in cells adhered to sections of mouse liver and the adhesion was blocked by treatment of the cells with endo-beta-galactosidase. The results indicate that endo-beta-galactosidase-sensitive and mAb FH6-reactive carbohydrate chains are generated under the control of expression levels of FUT6 and involved in the adhesion of colon carcinoma cells to liver sections.