Sequential activation of three distinct ICE-like activities in Fas-ligated Jurkat cells

Eric L. Greidinger, Douglas K. Miller, Ting Ting Yamin, Livia Casciola-Rosen, Antony Rosen

Research output: Contribution to journalArticlepeer-review

104 Scopus citations


ICE family proteases have been implicated as important effecters of the apoptotic pathway, perhaps acting hierarchically in a protease cascade. Using cleavage of endogenous protease substrates as probes, three distinct tiers of ICE-like activity were observed after Fas ligation in Jurkat cells. The earliest cleavage detected (30 min) was of fodrin, and produced a 150 kDa fragment. The second phase of cleavage (50 min) involved PARP, U1-70kDa and DNA-PK(cs), all substrates of the CPP32-11ke proteases. Lamin B cleavage was observed during the third cleavage phase (90 min). Distinct inhibition profiles obtained using a panel of peptide-based inhibitors of ICE-like proteases clearly distinguished the three different cleavage phases. These studies provide evidence for a sequence of ICE-like proteolytic activity during apoptosis. The early fodrin cleavage, producing a 150 kDa fragment, identifies an ICE-like activity proximal to CPP32 in Fas-induced Jurkat cell apoptosis.

Original languageEnglish (US)
Pages (from-to)299-303
Number of pages5
JournalFEBS letters
Issue number3
StatePublished - Jul 29 1996
Externally publishedYes


  • Apoptosis
  • CPP32
  • ICE
  • Protease

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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