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A Sialyl-Le^x-negative Melanoma Cell Line Binds to E-Selectin but not to P-Selectin¹

Department of Internal Medicine [U. K., M. N.], Universitätsklinikum Steglitz, Berlin, Germany, Institute of Immunology [S. K-K., H. H., T. D.], Universitätsklinikum Steglitz, Berlin, Germany, and Department of Internal Medicine, Beth Israel Hospital, Boston, Massachusetts 02114 [(G. W.]

² To whom requests for reprints should be addressed, at Universitätsklinikum Steglitz, Abt. für Innere Medizin, Hindenburgdamm 30, D-1000 Berlin 45, Germany.

The adhesion molecules E-selectin (ELAM-1) and P-selectin (GMP-140/CD62) recognize the carbohydrate motives sialyl-Lex, sialyl-diLe^x, or sialyl-Le^a, 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-Le^x, but was positive for sialyl-diLe^x and sialyl-Le^a. In contrast, 2 other melanoma cell lines, MeWo and SK-MEL-28, expressing either sialyl-diLe^x or sialyl-Le^a 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-Le^x 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-Le^x. 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-Le^x, sialyl-diLe^x, or sialyl-Le^a enables melanoma cells to adhere to E-selectin.

¹ Supported by the Deutsche Forschungsgemeinschaft.

The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked advertisement in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Received 7/16/93. Accepted 12/15/93.

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