Inhibition of Cysteine and Serine Proteinases by the Cowpox Virus Serpin CRMA

  • Tomoko Komiyama
  • Long T. Quan
  • Guy S. Salvesen
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 389)


Interleukin lß converting enzyme (ICE) is the founding member of a family of cysteine proteinases active in the metabolism of intracellular proteins [1]. Other members of this family include Ich-1, CPP32, Ced-3, all of which have been implicated in apoptosis (programmed cell death) [2–4]. Though ICE itself may also be involved in apoptosis, its main role is probably to activate pro-interleukin-lß (proIL-lß) via specific cleavage following Asp residues [1,5].


Serine Proteinase Cysteine Proteinase Thyroxin Binding Globulin Squamous Cell Carcinoma Antigen Tight Binding Inhibitor 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Plenum Press, New York 1996

Authors and Affiliations

  • Tomoko Komiyama
    • 1
  • Long T. Quan
    • 1
  • Guy S. Salvesen
    • 1
  1. 1.Department of PathologyDuke University Medical CenterDurhamUSA

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