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Mammalian initiator apoptotic caspases
Author(s) -
Ho Poki,
Hawkins Christine J.
Publication year - 2005
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2005.04966.x
Subject(s) - caspase , proteases , intrinsic apoptosis , apoptosis , microbiology and biotechnology , effector , xiap , caspase 2 , caspase 7 , biology , programmed cell death , chemistry , biochemistry , enzyme
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.