Cell surface sialylation plays a role in modulating sensitivity towards APO-1-mediated apoptotic cell death

Marcus E. Peter*, Stefan Hellbardt, Reinhard Schwartz-Albiez, Michael O. Westendorp, Henning Walczak, Gerhard Moldenhauer, Matthias Grell, Peter H. Krammer

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

80 Scopus citations


APO-1/Fas(CD95), a member of the tumour necrosis factor (TNF)/nerve growth factor (NGF) receptor superfamily transduces apoptotic signals into apoptosis sensitive cells. In metabolic labelling experiments using the highly APO-1 positive cell lines HUT78 (adult T cell leukemia) and SKW6.4 (B lymphoblastoid cell line) APO-1 was characterised as a long living protein with a complex glycosylation pattern involving terminal sialic acid groups which account for 8-kDa of its apparent molecular weight on SDS-PAGE. APO-1 expression and the degree of sialylation were determined in additional T and B cell lines. On the group I Burkitt's lymphoma cell line BL60 transfected with human APO-1 (K50) low sialylated species were detected only on the cell surface, suggesting that sialylation might be functionally important. Removal of terminal sialic acid groups by treatment of B and T cell lines with Vibrio cholerae neuraminidase (VCN) augmented sensitivity towards anti-APO-1 and human APO-1 ligand induced apoptosis. Similarly, VCN-treated U937 cells were rendered more sensitive to TNFα-induced cell death. Thus, sialylation may be one mechanism to regulate sensitivity towards ligand-mediated cell death in this receptor family.

Original languageEnglish (US)
Pages (from-to)163-171
Number of pages9
JournalCell Death and Differentiation
Issue number3
StatePublished - Dec 1 1995


  • Apoptosis
  • Glycosylation
  • Neuraminidase
  • Surface biotinylation

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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