Proteolytic regulation of apoptosis

Vincent J. Kidd, Jill M. Lahti, Tal Teitz

Research output: Contribution to journalArticlepeer-review

75 Scopus citations

Abstract

Much of the proteolysis that occurs during apoptosis is directed by caspases, a family of related cysteinyl proteases. A relatively small number of cellular proteins are targeted by caspases, yet their function is dramatically affected and apoptosis is triggered. Other proteases, such as granzymes and calpain, are also involved in the apoptotic signaling process, but in a much more cell type- and/or stimulus type-specific manner. At least three distinct caspase-signaling pathways exist; one activated through ligand-dependent death receptor oligomerization, the second through mitochondrial disruption, and the third through stress-mediated events involving the endoplasmic reticulum. These pathways also appear to interact to amplify weak apoptotic signals and shorten cellular execution time. Finally, defects in caspases contribute to autoimmune disease, cancer and certain neurological disorders.

Original languageEnglish (US)
Pages (from-to)191-201
Number of pages11
JournalSeminars in Cell and Developmental Biology
Volume11
Issue number3
DOIs
StatePublished - 2000
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Developmental Biology
  • Cell Biology

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