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Chapter category: Apoptosis

Apoptosis Dependent and Independent Functions of Caspases

This chapter appears in the following book:

Caspases: Their Role in Cell Death and Cell Survival

Edited by: Marek Los and Henning Walczak
ISBN: 0-306-47441-7
» Get more information about this book at landesbioscience.com «

Chapter authors:
Alicia Algeciras-Schimnich, Bryan C. Barnhart and Marcus E. Peter


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The study of cell death in the nematode Caenorhabditis elegans has led to the identification of several proteins which are responsible for orchestrating cell death. For each of these proteins, termed Ced for cell death defective, numerous mammalian homologues have been described (for review see ref. 1). The mammalian homologues of Ced-3, caspases, are a family of proteases involved in apoptosis execution. Caspases require an aspartic acid residue in the P1 position of their substrates and have an active site cysteine that mediates such cleavage. To date, 14 mammalian caspases have been identified. Caspases are divided into three groups: Group I caspases (caspases -1, -4, -5, -14, and murine -11, and -12) cleave the substrate sequence (W/L)EHD. This sequence is absent in most apoptosis substrates and these caspases are responsible for the generation of inflammatory signals and immune regulation rather than in the signaling of cell death. Group II (caspases -2, -3, -7) which prefer a DEXD motif, and group III caspases (caspases -6, -8, -9, -10) which prefer a (L/V)E(T/H)D sequence are involved in the execution of apoptosis.2 Caspases -8, -9, and -10 (initiator caspases) initiate the propagation of the apoptotic signals whereas caspases -3, -6, and -7 (effector caspases) execute the apoptotic program by cleaving numerous cellular proteins.

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The study of cell death in the nematode Caenorhabditis elegans has led to the identification of several proteins which are responsible for orchestrating cell death. For each of these proteins,...


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