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July 1, 1997Journal of Biological ChemistryOpen Access

I-FLICE, a Novel Inhibitor of Tumor Necrosis Factor Receptor-1- and CD-95-induced Apoptosis

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Authors

SHShimin HuCapital Medical UniversityCVClaudius VincenzUniversity of MichiganJNJian NiHebei University of Engineering

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Implication

Molecular study uncovers I-FLICE as an inactive caspase homolog that inhibits receptor-mediated apoptosis, indicating a novel dominant-negative regulatory mechanism.

Key Points

  • To identify and characterize I-FLICE and determine its function in tumor necrosis factor receptor-1- and CD-95-induced apoptotic signaling.
  • Cloned and structurally characterized the sequence of the novel protein I-FLICE.
  • Compared the domain architecture and catalytic motifs of I-FLICE with caspases 8 (FLICE) and 10 (Mch4/FLICE2).
  • Assessed the inhibitory capability of I-FLICE against receptor-mediated apoptotic pathways.
  • I-FLICE displays overall structural architecture remarkably similar to caspase 8 (FLICE) and caspase 10 (Mch4/FLICE2).
  • Sequence analysis confirmed I-FLICE lacks the catalytic active site residues and substrate-binding pocket necessary for protease activity.
  • I-FLICE acts as a dominant-negative inhibitor that blocks apoptosis initiated by CD-95 and tumor necrosis factor receptor-1.

Cite This Study

Hu et al. (1997) studied this question.

synapsesocial.com/papers/6a1e9ccfbf2a5d44faaf15f8https://doi.org/10.1074/jbc.272.28.17255
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Also Consider

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