Differential role of tyrosine phosphorylation in the induction of apoptosis in T cell clones via CD95 or the TCR/CD3-complex

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

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

Activated T cells undergo apoptosis when the Fas-antigen (APO-1, CD95) is ligated by Fas Ligand (FasL) or agonistic anti-Fas antibodies. Repeated stimulation of T lymphocytes via the TCR/CD3-complex induces activation-induced cell death (AICD) associated with FasL surface expression. FasL binding to Fas molecules triggers the Fas-dependent death signaling cascade. Since it is still controversial whether Fas-induced cell death is associated with tyrosine kinase activity, we investigated the tyrosine kinase activation requirements in anti-Fas antibody-induced cell death and AICD in human T cell clones. We report that cell death triggered by anti-Fas antibody is not accompanied by an increase in tyrosine phosphorylation and cannot be blocked by inhibitors of protein tyrosine kinases (PTK). Under the same conditions, AICD of T cell clones is clearly associated with tyrosine kinase activation. In fact, semiquantitative RT-PCR analysis of FasL mRNA expression triggered in T cell clones via the TCR/CD3-complex revealed that tyrosine phosphorylation is required for functional FasL mRNA and surface expression.

Original languageEnglish (US)
Pages (from-to)403-412
Number of pages10
JournalCell Death and Differentiation
Volume4
Issue number5
DOIs
StatePublished - Jan 1 1997

Keywords

  • Apoptosis
  • CD95
  • Human
  • Signal transduction
  • T cell receptor
  • T lymphocytes
  • Tyrosine phosphorylation

ASJC Scopus subject areas

  • Cell Biology

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