Mammalian initiator apoptotic caspases

Authors

  • Po-ki Ho,

    1. Murdoch Children's Research Institute, Parkville, Victoria, Australia
    2. Children's Cancer Centre, Royal Children's Hospital, Parkville, Victoria, Australia
    3. Department of Paediatrics, University of Melbourne, Parkville, Victoria, Australia
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  • Christine J. Hawkins

    1. Murdoch Children's Research Institute, Parkville, Victoria, Australia
    2. Children's Cancer Centre, Royal Children's Hospital, Parkville, Victoria, Australia
    3. Department of Paediatrics, University of Melbourne, Parkville, Victoria, Australia
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C. Hawkins, Murdoch Children's Research Institute, Royal Children's Hospital, Flemington Road, Parkville, VIC 3052, Australia
Fax: +61 3 93454993
Tel: +61 3 93455823
E-mail: chris.hawkins@mcri.edu.au

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.

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