Caspase-2 is resistant to inhibition by inhibitor of apoptosis proteins (IAPs) and can activate caspase-7

Author(s): Ho, PK; Jabbour, AM; Ekert, PG; Hawkins, CJ;
Details: Publication Year 2005-03,Volume 272,Issue #6,Page 1401-1414
Journal Title: FEBS JOURNAL
Publication Type: Journal Article
Abstract: Caspases are a family of cysteine proteases with roles in cytokine maturation or apoptosis. Caspase-2 was the first pro-apoptotic caspase identified, but its functions in apoptotic signal transduction are still being elucidated. This study examined the regulation of the activity of caspase-2 using recombinant proteins and a yeast-based system. Our data suggest that for human caspase-2 to be active its large and small subunits must be separated. For maximal activity its prodomain must also be removed. Consistent with its proposed identity as an upstream caspase, caspase-2 could provoke the activation of caspase-7. Caspase-2 was not subject to inhibition by members of the IAP family of apoptosis inhibitors.
Publisher: BLACKWELL PUBLISHING LTD
Keywords: CYTOCHROME-C RELEASE; CYSTEINE PROTEASE; ADAPTER MOLECULE; GRANZYME-B; FAMILY; YEAST; SPECIFICITIES; MITOCHONDRIA; MECHANISM; CLEAVAGE
Publisher's Version: https://doi.org/10.1111/j.1742-4658.2005.04573.x
Terms of Use/Rights Notice: Refer to copyright notice on published article.

Creation Date: 2005-03-01 12:00:00