Encyclopedia of Signaling Molecules

2018 Edition
| Editors: Sangdun Choi

Caspase Family

  • Alexandre Desroches
  • Dave Boucher
  • Jean-Bernard DenaultEmail author
Reference work entry
DOI: https://doi.org/10.1007/978-3-319-67199-4_176


The importance of peptidases in cell signaling is well established. Unlike many pathways controlled by phosphorylation, glycosylation, ubiquitination, or other types of post-translational modifications, steps governed by proteases are essentially irreversible because there is no efficacious mechanism for peptide bond ligation. This chapter presents the peptidase family of caspases, which performs limited proteolysis on a wide range of substrates with molecular consequences ranging from inactivation to gain-of-function to accelerated degradation of their targets. It is important to emphasize that caspases are signaling peptidases and not degrading enzymes akin to lysosomal cathepsins or digestive enzymes. The caspases that are principally implicated in inflammation and apoptosis will be the focus of this chapter; we will not discuss the roles of caspase 14.

In 1842, Karl Christoph Vogt, a German scientist, recognized the presence of cell death during the neuronal...

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  1. Fuentes-Prior P, Salvesen GS. The protein structures that shape caspase activity, specificity, activation and inhibition. Biochem J. 2004b;384:201–32.PubMedPubMedCentralCrossRefGoogle Scholar
  2. Galluzzi L, Aaronson SA, Abrams J, Alnemri ES, Andrews DW, Baehrecke EH, Bazan NG, Blagosklonny MV, Blomgren K, Borner C, Bredesen DE, Brenner C, Castedo M, Cidlowski JA, Ciechanover A, Cohen GM, De Laurenzi V, De Maria R, Deshmukh M, Dynlacht BD, El-Deiry WS, Flavell RA, Fulda S, Garrido C, Golstein P, Gougeon ML, Green DR, Gronemeyer H, Hajnoczky G, Hardwick JM, Hengartner MO, Ichijo H, Jaattela M, Kepp O, Kimchi A, Klionsky DJ, Knight RA, Kornbluth S, Kumar S, Levine B, Lipton SA, Lugli E, Madeo F, Malomi W, Marine JC, Martin SJ, Medema JP, Mehlen P, Melino G, Moll UM, Morselli E, Nagata S, Nicholson DW, Nicotera P, Nunez G, Oren M, Penninger J, Pervaiz S, Peter ME, Piacentini M, Prehn JH, Puthalakath H, Rabinovich GA, Rizzuto R, Rodrigues CM, Rubinsztein DC, Rudel T, Scorrano L, Simon HU, Steller H, Tschopp J, Tsujimoto Y, Vandenabeele P, Vitale I, Vousden KH, Youle RJ, Yuan J, Zhivotovsky B, Kroemer G. Guidelines for the use and interpretation of assays for monitoring cell death in higher eukaryotes. Cell Death Differ. 2009;16:1093–107.PubMedPubMedCentralCrossRefGoogle Scholar
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  4. Lamkanfi M, Dixit VM. Mechanisms and functions of inflammasomes. Cell. 2014b;157:1013–22.PubMedCrossRefGoogle Scholar
  5. Mace PD, Riedl SJ. Molecular cell death platforms and assemblies. Curr Opin Cell Biol. 2010b;22:828–36.PubMedPubMedCentralCrossRefGoogle Scholar
  6. Tait SW, Green DR. Mitochondria and cell death: outer membrane permeabilization and beyond. Nat Rev Mol Cell Biol. 2010b;11:621–32.CrossRefGoogle Scholar
  7. Vanden Berghe T, Linkermann A, et al. Regulated necrosis: the expanding network of non-apoptotic cell death pathways. Nat Rev Mol Cell Biol. 2014b;15:135–47.PubMedCrossRefGoogle Scholar

Copyright information

© Springer International Publishing AG 2018

Authors and Affiliations

  • Alexandre Desroches
    • 1
  • Dave Boucher
    • 2
  • Jean-Bernard Denault
    • 1
    Email author
  1. 1.Department of Pharmacology and Physiology, Faculty of Medicine and Health SciencesUniversité de SherbrookeSherbrookeCanada
  2. 2.Institute for Molecular BioscienceUniversity of QueenslandSt LuciaAustralia