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Intracellular Protein Catabolism pp 173–176Cite as

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

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 389))

Abstract

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].

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Author information

Authors and Affiliations

  1. Department of Pathology, Duke University Medical Center, Durham, 27710, North Carolina, USA

    Tomoko Komiyama, Long T. Quan & Guy S. Salvesen

Authors
  1. Tomoko Komiyama
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  2. Long T. Quan
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  3. Guy S. Salvesen
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Editor information

Editors and Affiliations

  1. University of Tokyo, Tokyo, Japan

    Koichi Suzuki

  2. College of Medicine, Penn State University, Hershey, Pennsylvania, USA

    Judith S. Bond

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© 1996 Plenum Press, New York

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Komiyama, T., Quan, L.T., Salvesen, G.S. (1996). Inhibition of Cysteine and Serine Proteinases by the Cowpox Virus Serpin CRMA. In: Suzuki, K., Bond, J.S. (eds) Intracellular Protein Catabolism. Advances in Experimental Medicine and Biology, vol 389. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0335-0_21

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  • DOI: https://doi.org/10.1007/978-1-4613-0335-0_21

  • Publisher Name: Springer, Boston, MA

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  • Online ISBN: 978-1-4613-0335-0

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