Caspase-2 can function upstream of bid cleavage in the TRAIL apoptosis pathway

J Biol Chem. 2004 Aug 13;279(33):35047-52. doi: 10.1074/jbc.M400708200. Epub 2004 Jun 1.

Abstract

In many mammalian cell types, engagement of the TRAIL/Apo2L death receptors DR4 and DR5 alters mitochondrial physiology, thereby promoting the release of pro-apoptotic proteins normally contained within this organelle. A contemporary view of this process is that in so-called type II cells death receptor-activated caspase-8 cleaves the Bcl-2 family member Bid, which generates a truncated Bid fragment that collaborates with Bax, another Bcl-2 relative, to promote the release of mitochondrial factors necessary for activation of executioner caspases and apoptosis. Here we show that in some type II cells caspase-2 is necessary for optimal TRAIL-mediated cleavage of Bid. Down-regulation of caspase-2 using RNA interference significantly inhibited TRAIL-induced apoptosis. Analysis of the TRAIL proteolytic cascade following gene silencing of specific pathway components revealed that caspase-2 is necessary for efficient cleavage of Bid; however, caspase-2 proteolytic processing, which occurs downstream of Bax, is not necessary for its role in Bid cleavage.

MeSH terms

  • Animals
  • Apoptosis Regulatory Proteins
  • Apoptosis*
  • BH3 Interacting Domain Death Agonist Protein
  • Blotting, Western
  • Carrier Proteins / metabolism*
  • Caspase 2
  • Caspase 3
  • Caspase 7
  • Caspase 8
  • Caspases / metabolism
  • Caspases / physiology*
  • Cell Death
  • Cell Line
  • Cell Survival
  • Dose-Response Relationship, Drug
  • Down-Regulation
  • Enzyme Activation
  • Etoposide / pharmacology
  • Gene Silencing
  • Humans
  • Membrane Glycoproteins / metabolism*
  • Mitochondria / metabolism
  • Models, Biological
  • Proto-Oncogene Proteins / metabolism
  • Proto-Oncogene Proteins c-bcl-2*
  • RNA Interference
  • RNA, Small Interfering / metabolism
  • Staurosporine / pharmacology
  • TNF-Related Apoptosis-Inducing Ligand
  • Tetrazolium Salts / pharmacology
  • Thiazoles / pharmacology
  • Time Factors
  • Transfection
  • Tumor Necrosis Factor-alpha / metabolism*
  • bcl-2-Associated X Protein

Substances

  • Apoptosis Regulatory Proteins
  • BAX protein, human
  • BH3 Interacting Domain Death Agonist Protein
  • BID protein, human
  • Carrier Proteins
  • Membrane Glycoproteins
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • RNA, Small Interfering
  • TNF-Related Apoptosis-Inducing Ligand
  • TNFSF10 protein, human
  • Tetrazolium Salts
  • Thiazoles
  • Tumor Necrosis Factor-alpha
  • bcl-2-Associated X Protein
  • Etoposide
  • CASP3 protein, human
  • CASP7 protein, human
  • CASP8 protein, human
  • Caspase 2
  • Caspase 3
  • Caspase 7
  • Caspase 8
  • Caspases
  • thiazolyl blue
  • Staurosporine