Mammalian initiator apoptotic caspases
- 21 October 2005
- journal article
- review article
- Published by Wiley in The FEBS Journal
- Vol. 272 (21), 5436-5453
- https://doi.org/10.1111/j.1742-4658.2005.04966.x
Abstract
Caspases are a conserved family of cysteine proteases. They play diverse roles in inflammatory responses and apoptotic pathways. Among the caspases is a subgroup whose primary function is to initiate apoptosis. Within their long prodomains, caspases-2, -9 and -12 contain a caspase activation and recruitment domain while caspases-8 and -10 bear death effector domains. Activation follows the recruitment of the procaspase molecule via the prodomain to a high molecular mass complex. Despite sharing some common features, other aspects of the biochemistry, substrate specificity, regulation and signaling mechanisms differ between initiator apoptotic caspases. Defects in expression or activity of these caspases are related to certain pathological conditions including neurodegenerative disorders, autoimmune diseases and cancer.Keywords
This publication has 180 references indexed in Scilit:
- Structure of the apoptotic protease-activating factor 1 bound to ADPNature, 2005
- Dual Role of BRUCE as an Antiapoptotic IAP and a Chimeric E2/E3 Ubiquitin LigaseMolecular Cell, 2004
- IAP proteins: blocking the road to death's doorNature Reviews Molecular Cell Biology, 2002
- Human caspase 12 has acquired deleterious mutationsBiochemical and Biophysical Research Communications, 2002
- IFNγ sensitizes for apoptosis by upregulating caspase-8 expression through the Stat1 pathwayOncogene, 2002
- Activation of Caspase-8 in the Alzheimer's Disease BrainNeurobiology of Disease, 2001
- Evidence That Caspase-13 Is Not a Human but a Bovine GeneBiochemical and Biophysical Research Communications, 2001
- Caspase-8 specificity probed at subsite S4:crystal structure of the caspase-8-Z-DEVD-cho complexJournal of Molecular Biology, 2000
- Activation of a pro‐apoptotic amplification loop through inhibition of NF‐κB‐dependent survival signals by caspase‐mediated inactivation of RIPFEBS Letters, 2000
- Akt Phosphorylation Site Found in Human Caspase-9 Is Absent in Mouse Caspase-9Biochemical and Biophysical Research Communications, 1999