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Mammalian initiator apoptotic caspases.

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  • Author(s): Ho PK;Ho PK; Hawkins CJ
  • Source:
    The FEBS journal [FEBS J] 2005 Nov; Vol. 272 (21), pp. 5436-53.
  • Publication Type:
    Journal Article; Review
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 101229646 Publication Model: Print Cited Medium: Print ISSN: 1742-464X (Print) Linking ISSN: 1742464X NLM ISO Abbreviation: FEBS J Subsets: MEDLINE
    • Publication Information:
      Original Publication: Oxford, UK : Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies, c2005-
    • Subject Terms:
      Apoptosis*; Caspases/*metabolism; Animals ; Caspase Inhibitors ; Caspases/chemistry ; Caspases/genetics ; Enzyme Activation ; Gene Expression Regulation, Enzymologic ; Humans ; Protein Binding ; Substrate Specificity
    • 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.
    • Number of References:
      186
    • Accession Number:
      0 (Caspase Inhibitors)
      EC 3.4.22.- (Caspases)
    • Publication Date:
      Date Created: 20051103 Date Completed: 20051213 Latest Revision: 20220410
    • Publication Date:
      20250114
    • Accession Number:
      10.1111/j.1742-4658.2005.04966.x
    • Accession Number:
      16262685