Induction of cell death via Fas (CD95, Apo-1) may be associated with but is not dependent on Fas-induced tyrosine phosphorylation

Ottmar Janssen, Beate Lengl-Janßen, Hans Heinrich Oberg, Michael J. Robertson, Dieter Kabelitz

Research output: Contribution to journalArticle

18 Scopus citations

Abstract

Cross-linking of the Fas-antigen (CD95, Apo-1) triggers apoptosis in activated T cells and transformed T cell lines. Fas-induced apoptosis has been previously reported to require Fas-triggered tyrosine phosphorylation of various proteins. In the present study, we have compared the protein tyrosine phosphorylation pattern and the apoptosis sensitivity in a set of Jurkat variants selected for the absence or presence of T cell receptor (TCR)/CD3 expression and resistance or sensitivity to Fas-mediated apoptosis. While tyrosine phosphorylation upon Fas-ligation was readily apparent in wild-type Jurkat cells (which are sensitive to anti-Fas-induced apoptosis), drastically reduced tyrosine phosphorylation was observed in Fas-resistant Jurkat subclones (which still express CD95 on their surface). More importantly, TCR/CD3-negative Jurkat variants which expressed normal levels of CD95 and were fully susceptible to Fas-triggered cell death, did not show any protein tyrosine phosphorylation upon Fas-ligation. Taken together, our data demonstrate that Fas-induced cell death can be associated with but is not dependent on protein tyrosine phosphorylation.

Original languageEnglish (US)
Pages (from-to)63-69
Number of pages7
JournalImmunology Letters
Volume49
Issue number1-2
DOIs
StatePublished - Jan 1996
Externally publishedYes

Keywords

  • Apoptosis
  • CD95
  • Fas antigen
  • Signaling
  • T cells
  • Tyrosine phosphorylation

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

Fingerprint Dive into the research topics of 'Induction of cell death via Fas (CD95, Apo-1) may be associated with but is not dependent on Fas-induced tyrosine phosphorylation'. Together they form a unique fingerprint.

  • Cite this