A sialyl-Le(x)-negative melanoma cell line binds to E-selectin but not to P-selectin

Cancer Res. 1994 Feb 15;54(4):1109-12.


The adhesion molecules E-selectin (ELAM-1) and P-selectin (GMP-140/CD62) recognize the carbohydrate motives sialyl-Le(x), sialyl-diLe(x), 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-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-diLe(x) 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Cell Adhesion
  • Cell Adhesion Molecules / metabolism*
  • E-Selectin
  • Flow Cytometry
  • Fucosyltransferases / genetics
  • Humans
  • Lewis X Antigen / analysis*
  • Melanoma / metabolism*
  • Melanoma / pathology
  • Molecular Sequence Data
  • P-Selectin
  • Platelet Membrane Glycoproteins / metabolism*
  • Polymerase Chain Reaction
  • RNA, Messenger / analysis
  • Tumor Cells, Cultured


  • Cell Adhesion Molecules
  • E-Selectin
  • Lewis X Antigen
  • P-Selectin
  • Platelet Membrane Glycoproteins
  • RNA, Messenger
  • Fucosyltransferases