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Alterations in expression and synthesis of glycolipid antigens in human colonic tumor cell lines.

Incubation of human intestinal SW1116 tumor cells in serum-free medium containing butyric acid reduced their capacity to synthesize gastrointestinal carcinoma-associated (GICA) glycolipid antigen 4- to 8-fold as determined by a radioimmunobinding assay using anti-GICA monoclonal antibody:high-performance thin-layer chromatography; autoradiography; and densitometry. The structure of GICA has been described as a sialylated Lea glycolipid (J. L. Magnani, B. Nilsson, M. Brockhaus, D. Zopf, Z. Steplewski, A. Koprowski, and V. Ginsburg. J. Biol. Chem., 257: 14365-14369, 1982). Tritiated fucose incorporation into GICA was reduced per cell (7-fold), per mg protein (5-fold), and per mg lipid (4-fold). A purified organically soluble glycolipid fraction from control SW1116 cells contained more Lewis antigen than did butyrate-treated cells as determined by the high-performance thin-layer chromatography radioimmunobinding assay. Incorporation of radioactivity from [3H]fucose and guanosine diphosphate [14C]fucose into Lewis antigens in butyrate-treated cells was 2- to 3-fold lower than in control cells. HT29 cells carry the blood type of the original donor, Blood Group A. Isotope incorporation into A glycolipid antigen was reduced 2- to 8-fold upon exposure to butyrate. Commensurate with these results was a dramatic reduction in cell population-doubling rate. We propose that synthesis of these fucolipid antigens is associated more with dividing, undifferentiated tumor cell populations. The diminution in antigen levels may derive from diminished cells' capacity for fucosylation in the presence of butyrate.