The adhesion molecules E-selectin (ELAM-1) and P-selectin (GMP-140/CD62) recognize the carbohydrate motives sialyl-Lex, sialyl-diLex, or sialyl-Lea, though with different affinity. We found that the melanoma cell line NKI-4 bound to E-selectin, but not to P-selectin. This melanoma cell line did not express sialyl-Lex, but was positive for sialyl-diLex and sialyl-Lea. In contrast, 2 other melanoma cell lines, MeWo and SK-MEL-28, expressing either sialyl-diLex or sialyl-Lea on the cell surface, bound neither E-selectin nor P-selectin. Transfection of the fucosyltransferases Fuc-TIII, Fuc-TIV, and Fuc-TV mediates cell surface expression of sialyl-Lex in many cell lines. We detected transcripts of the fucosyltransferases Fuc-TIII and Fuc-TV in 4 melanoma cell lines despite the absence of cell surface sialyl-Lex. Our observations indicate that expression of fucosyltransferases (Fuc-TIII and -TV) and generation of cell-surface sialyl-diLex are not sufficient to permit adherence to E-selectin or P-selectin. Furthermore, it seems possible that a yet undefined ligand different from sialyl-Lex, sialyl-diLex, or sialyl-Lea enables melanoma cells to adhere to E-selectin.

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Supported by the Deutsche Forschungsgemeinschaft.

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©1994 American Association for Cancer Research.
1994
American Association for Cancer Research, Inc.