What happened to plant caspases?

J Exp Bot. 2008;59(3):491-9. doi: 10.1093/jxb/erm352. Epub 2008 Feb 13.


The extent of conservation in the programmed cell death pathways that are activated in species belonging to different kingdoms is not clear. Caspases are key components of animal apoptosis; caspase activities are detected in both animal and plant cells. Yet, while animals have caspase genes, plants do not have orthologous sequences in their genomes. It is 10 years since the first caspase activity was reported in plants, and there are now at least eight caspase activities that have been measured in plant extracts using caspase substrates. Various caspase inhibitors can block many forms of plant programmed cell death, suggesting that caspase-like activities are required for completion of the process. Since plant metacaspases do not have caspase activities, a major challenge is to identify the plant proteases that are responsible for the caspase-like activities and to understand how they relate, if at all, to animal caspases. The protease vacuolar processing enzyme, a legumain, is responsible for the cleavage of caspase-1 synthetic substrate in plant extracts. Saspase, a serine protease, cleaves caspase-8 and some caspase-6 synthetic substrates. Possible scenarios that could explain why plants have caspase activities without caspases are discussed.

Publication types

  • Review

MeSH terms

  • Caspases / metabolism*
  • Cell Death / physiology*
  • Cysteine Endopeptidases / metabolism
  • Plants / enzymology*


  • Caspases
  • Cysteine Endopeptidases
  • vacuolar processing enzyme