Please use this identifier to cite or link to this item: https://doi.org/10.1074/jbc.274.15.10301
Title: Molecular cloning and characterization of two novel pro-apoptotic isoforms of caspase-10
Authors: Ng, P.W.P. 
Porter, A.G. 
Jänicke, R.U. 
Issue Date: 9-Apr-1999
Citation: Ng, P.W.P., Porter, A.G., Jänicke, R.U. (1999-04-09). Molecular cloning and characterization of two novel pro-apoptotic isoforms of caspase-10. Journal of Biological Chemistry 274 (15) : 10301-10308. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.274.15.10301
Abstract: Caspase-10/a (Mch4) and caspase-10/b (FLICE2) are related death effector domain-containing cysteine aspartases presumed to be at or near the apex of apoptotic signaling pathways. We report the cloning and characterization of two novel proteins that are splice isoforms of the caspase-10 family. Caspase-10/c is a truncated protein that is essentially a prodomain-only form of the caspase that lacks proteolytic activity in vitro but efficiently induces the formation of perinuclear filamentous structures and cell death in vivo. Caspase-10/c mRNA is specifically up-regulated upon TNF stimulation, suggesting a potential role of this isoform in amplifying the apoptotic response to extracellular stimuli such as cytokines. Caspase-10/d is a hybrid of the known caspases Mch4 and FLICE2, as it is identical to FLICE2 except for the small (p12) catalytic subunit, which is identical to Mch4. Caspase- 10/d is proteolytically active in vitro and also induces cell death in vivo, although it is less active than Mch4. The mRNAs for all known isoforms of caspase-10 are abundantly expressed in fetal lung, kidney, and skeletal muscle but are very poorly expressed or absent in these tissues in the adult, implying a possible role for the caspase-10 family in fetal development.
Source Title: Journal of Biological Chemistry
URI: http://scholarbank.nus.edu.sg/handle/10635/111974
ISSN: 00219258
DOI: 10.1074/jbc.274.15.10301
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