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nature portfolio permissions reprints privacy policy 100 research drive tissue research advertising social media subscribe nature interleukin-lβ-converting enzyme including fas-mediated apoptosis3–8 nature 356 nature 375 nature 376 nature 371 nature 364 nature 380 nature apoptosis-related gene expression inhibit fas-mediated apoptosis inhibited ice-induced apoptosis springerlink instant access cancer stem cell fas-activated cells personal data data protection permissions mouse lymphoma supplemented fas-mediated apoptosis article enari privacy antitumoral effects induced fas-bearing cells1 cell-free system cpp32 induced apoptosis cpp32-induced apoptosis explore content subscription content european economic area institutional subscriptions read comparative proteomic analysis death receptor pathway accepting optional cookies fernandes-alnemri journals search log issue learn tran-sient ice manage preferences activity gradually accumulated access apoptosis induced

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         headline:Sequential activation of ICE-like and CPP32-like proteases during Fas-mediated apoptosis
         description:BINDING of Fas ligand or an agonistic anti-Fas antibody induces apoptosis in Fas-bearing cells1. The interleukin-lβ-converting enzyme (ICE) is a cysteine protease2 that is involved in apoptosis induced by various stimuli, including Fas-mediated apoptosis3–8. Several ICE homologues have been identified, and these are subdivided into three groups (ICE-, CPP32- and Ich-1-like pro-teases)9–18. We show here that specific inhibitors of ICE- or CPP32-like proteases can inhibit Fas-mediated apoptosis. Tran-sient ICE-like activity was found in the cytosolic fraction of Fas-activated cells, whereas ICE-dependent, CPP32-like activity gradually accumulated in the cytosol. Cell lysates from mouse lymphoma supplemented with either recombinant ICE or CPP32 induced apoptosis of nuclei. The CPP32 inhibitor inhibited ICE-or CPP32-induced apoptosis in the cell-free system, whereas the ICE-inhibitor only inhibited ICE-induced apoptosis. Cell extracts from thymocytes from ICE-null mice induced apoptosis in the cell-free system when it was supplemented with CPP32. These results indicate that Fas sequentially activates ICE- and CPP32-like proteases, and that downstream CPP32, together with a component(s) in the cytoplasm, causes apoptosis of nuclei.
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      headline:Sequential activation of ICE-like and CPP32-like proteases during Fas-mediated apoptosis
      description:BINDING of Fas ligand or an agonistic anti-Fas antibody induces apoptosis in Fas-bearing cells1. The interleukin-lβ-converting enzyme (ICE) is a cysteine protease2 that is involved in apoptosis induced by various stimuli, including Fas-mediated apoptosis3–8. Several ICE homologues have been identified, and these are subdivided into three groups (ICE-, CPP32- and Ich-1-like pro-teases)9–18. We show here that specific inhibitors of ICE- or CPP32-like proteases can inhibit Fas-mediated apoptosis. Tran-sient ICE-like activity was found in the cytosolic fraction of Fas-activated cells, whereas ICE-dependent, CPP32-like activity gradually accumulated in the cytosol. Cell lysates from mouse lymphoma supplemented with either recombinant ICE or CPP32 induced apoptosis of nuclei. The CPP32 inhibitor inhibited ICE-or CPP32-induced apoptosis in the cell-free system, whereas the ICE-inhibitor only inhibited ICE-induced apoptosis. Cell extracts from thymocytes from ICE-null mice induced apoptosis in the cell-free system when it was supplemented with CPP32. These results indicate that Fas sequentially activates ICE- and CPP32-like proteases, and that downstream CPP32, together with a component(s) in the cytoplasm, causes apoptosis of nuclei.
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