ERICE, a novel FLICE-activatable caspase.

The Journal of biological chemistry (1998-06-23)
E W Humke, J Ni, V M Dixit
ABSTRACT

Programmed cell death, or apoptosis, is a process of fundamental importance to cellular homeostasis in metazoan organisms (Ellis, R. E., Yuan, J., and Horvitz, H. R. (1991) Annu. Rev. Cell Biol. 7, 663-698). The caspase family of mammalian proteases, related to the nematode death protein CED-3, plays a crucial role in apoptosis and inflammation. We report here the isolation and characterization of a new caspase, tentatively termed ERICE (Evolutionarily Related Interleukin-1beta Converting Enzyme). Based on phylogenetic analysis, ERICE (caspase-13) is a member of the ICE subfamily of caspases which includes caspase-1 (ICE), caspase-4 (ICErel-II, TX, ICH-2), and caspase-5 (ICErel-III, TY). Overexpression of ERICE induces apoptosis of 293 human embryonic kidney cells and MCF7 breast carcinoma cells. Like other members of the subfamily, ERICE is not activated by the serine protease granzyme B, a caspase-activating component of cytotoxic T cell granules. Therefore, ERICE most likely does not play a role in granzyme B-induced cell death. ERICE, however, was activated by caspase-8 (FLICE, MACH, Mch-5), the apical caspase activated upon engagement of death receptors belonging to the tumor necrosis factor family. This is consistent with a potential role for ERICE in this receptor-initiated death pathway.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Caspase 13 Substrate
Sigma-Aldrich
Caspase 13 Substrate
Sigma-Aldrich
N-Acetyl-Leu-Glu-Glu-Asp-7-amido-4-trifluoromethylcoumarin, ≥90% (HPLC), powder
Sigma-Aldrich
Anti-Caspase 13 (ERICE) antibody produced in rabbit, ~0.5 mg/mL, IgG fraction of antiserum, buffered aqueous solution