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August 15, 1997Biochemical JournalOpen Access

Caspases: the executioners of apoptosis

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Authors

GCGerald M. Cohen

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Overview

Molecular review reveals an enzymatic activation cascade in eukaryotic cells, highlighting direct mechanisms connecting death receptors to caspase execution.

Key Points

  • To delineate the structural composition, enzymatic activation pathways, and signaling hierarchy of caspases during programmed apoptotic cell death.
  • Synthesized biochemical and crystal structure analyses of caspase-1 and caspase-3 heterotetramers.
  • Evaluated evolutionary conservation and catalytic sequence identity between Caenorhabditis elegans CED-3 and mammalian cysteine proteases.
  • Examined death receptor signaling pathways involving CD95, tumor necrosis factor, and adapter proteins like RAIDD/CRADD.
  • Caspases exist as inactive proenzymes containing a conserved QACXG pentapeptide active site and assemble upon activation into heterotetramers with two large and two small subunits.
  • Activated caspases cleave substrate targets including poly(ADP-ribose) polymerase and structural lamins, precipitating characteristic morphological death.
  • Death receptor triggering recruits initiator caspase-8 via death effector domains, establishing an enzymatic hierarchy that drives downstream caspase activation.

Cite This Study

Gerald M. Cohen (1997) studied this question.

synapsesocial.com/papers/6a02432aa9a0df4cf49f472dhttps://doi.org/10.1042/bj3260001
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