Selectin ligands on human melanoma cells

Nicholas Miller, Richard G. Vile, Ian R. Hart

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


Twelve established human melanoma lines were screened for surface expression of the carbohydrate antigens Lewisa (Lea), sialyl Lewisa (SLea), dimeric sialyl Lewisa (diSLea), sialyl Lewis(X) (SLe(X)) and dimeric sialyl Lewis(X) (diSLe(X)). None of the lines expressed SLe(X), but 11/12 were positive for diSLe(X)) and 7/12 were positive for SLea. Although both diSLe(X)) and SLea have been reported to bind to E-selectin, none of the melanoma lines exhibited E-selectin-dependent adhesion to activated human umbilical vein endothelial cells (HUVECs). Three melanoma lines infected with a retroviral vector carrying the cDNA for the human Lewis fucosyltransferase (FucT-III) subsequently expressed SLe(X) at their cell surface and exhibited E-selectin-dependent adhesion to activated HUVECs. Treatment of these transduced cells with inhibitors of O-linked or N-linked protein glycosylation significantly inhibited E-selectin -mediated adhesion, though fluorescence-activated cell sorter analysis indicated no decrease in cell surface expression of SLe(X), SLea or diSLe(X). This suggests that the majority of SLe(X)/SLea-type glycans endogenously produced by human melanoma cells are not protein-associated and do not mediate E-selectin-dependent adhesion. These results support the hypothesis that E-selectin-dependent adhesion requires presentation of SLe(X)-type moieties on appropriate glycoproteins.

Original languageEnglish (US)
Pages (from-to)33-43
Number of pages11
JournalGlycoconjugate Journal
Issue number1
StatePublished - 1996


  • Cell adhesion
  • E-Selectin
  • Lewis antigens
  • Lewis fucosyltransferase
  • Melanoma
  • Metastasis

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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