Caspase-7: A Protease Involved in Apoptosis and Inflammation

Int J Biochem Cell Biol. 2010 Jan;42(1):21-4. doi: 10.1016/j.biocel.2009.09.013. Epub 2009 Sep 25.

Abstract

Caspase-7 was considered to be redundant with caspase-3 because these related cysteine proteases share an optimal peptide recognition sequence and have several endogenous protein substrates in common. In addition, both caspases are proteolytically activated by the initiator caspase-8 and -9 during death receptor- and DNA-damage-induced apoptosis, respectively. However, a growing body of biochemical and physiological data indicate that caspase-7 also differs in significant ways from caspase-3. For instance, several substrates are specifically cleaved by caspase-7, but not caspase-3. Moreover, caspase-7 activation requires caspase-1 inflammasomes under inflammatory conditions, while caspase-3 processing proceeds independently of caspase-1. Finally, caspase-7 deficient mice are resistant to endotoxemia, whereas caspase-3 knockout mice are susceptible. These findings suggest that specifically interfering with caspase-7 activation may hold therapeutic value for the treatment of cancer and inflammatory ailments.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Apoptosis*
  • Caspase 7 / chemistry
  • Caspase 7 / metabolism*
  • Humans
  • Inflammation / enzymology*
  • Inflammation / pathology*
  • Inflammation / therapy

Substances

  • Caspase 7