Executioner caspase-3 and caspase-7 are functionally distinct proteases

Proceedings of the National Academy of Sciences of the United States of America

Volumn 105, Issue 35, 2008, Pages 12815-12819

  Walsh, John G ^a   Cullen, Sean P ^a   Sheridan, Clare ^a   Lüthi, Alexander U ^a   Gerner, Christopher ^a,b   Martin, Seamus J ^a  

^a TRINITY COLLEGE DUBLIN   (Ireland)

^b MEDICAL UNIVERSITY OF VIENNA   (Austria)

Author keywords

Apoptosis; Caspase substrates; Proteolysis

Indexed keywords

CASPASE 3; CASPASE 6; CASPASE 7; GELSOLIN; PROTEIN BID; PROTEIN P23; PROTEINASE; X LINKED INHIBITOR OF APOPTOSIS;

ANIMAL CELL; APOPTOSIS; ARTICLE; CELL DEATH; CONTROLLED STUDY; ENZYME ACTIVITY; HUMAN; HUMAN CELL; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN FUNCTION;

AMINO ACID SEQUENCE; ANIMALS; BH3 INTERACTING DOMAIN DEATH AGONIST PROTEIN; CASPASE 3; CASPASE 7; CASPASE 9; CELL LINE, TUMOR; CELL-FREE SYSTEM; CYTOCHROMES; HUMANS; HYDROLYSIS; INTRAMOLECULAR OXIDOREDUCTASES; JURKAT CELLS; MICE; MOLECULAR SEQUENCE DATA; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEOME; PROTEOMICS; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

MUS;

EID: 51349139607     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0707715105     Document Type: Article

References (17)

1. Lüthi AU, Martin SJ (2007) The CASBAH: A searchable database of caspase substrates. Cell Death Differ 14:641-650.
2. Timmer JC, Salvesen GS (2007) Caspase substrates. Cell Death Differ 14:66-72.
3. Stennicke HR, et al. (1998) Pro-caspase-3 is a major physiologic target of caspase-8. J Biol Chem 273:27084-27090.
4. Slee EA, et al. (1999) Ordering the cytochrome c-initiated caspase cascade: Hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner. J Cell Biol 144:281-292.
5. Thornberry NA, et al. (1997) A combinatorial approach defines specificities of members of the caspase family and granzyme B: Functional relationships established for key mediators of apoptosis. J Biol Chem 272:17907-17911.
6. Stennicke HR, Renatus M, Meldal M, Salvesen GS (2000) Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8. Biochem J 350:563-568.
7. Kuida K, et al. (1996) Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice. Nature 384:368-372.
8. Houde C, et al. (2004) Caspase-7 expanded function and intrinsic expression level underlies strain-specific brain phenotype of caspase-3-null mice. J Neurosci 24:9977-9984.
9. Lakhani SA, et al. (2006) Caspases 3 and 7: Key mediators of mitochondrial events of apoptosis. Science 311:847-851.
10. Leonard JR, Klocke BJ, D'Sa C, Flavell RA, Roth KA, (2002) Strain-dependent neurodevelopmental abnormalities in caspase-3-deficient mice. J. Neuropathol. Exp Neurol 61:673-677.
11. Slee EA, Adrian C, Martin SJ (2001) Executioner caspase-3, -6, and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis. J Biol Chem 276:7320-7326.
12. Srinivasula SM, Ahmad M, Fernandes-Alnemri T, Alnemri ES (1998) Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization. Mol Cell 1:949-957.
13. Jänicke RU, Sprengart ML, Wati MR, Porter AG (1998) Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis. J Biol Chem 273:9357-9360.
14. Taylor RC, Cullen SP, Martin SJ (2008) Apoptosis: Controlled demolition at the cellular level. Nat Rev Mol Cell Biol 9:231-241.
15. Hill MM, Adrian C, Duriez PJ, Creagh EM, Martin SJ (2004) Analysis of the composition, assembly kinetics and activity of native Apaf-1 apoptosomes. EMBO J 23:2134-2145.
16. Martin SJ, et al. (1996) The cytotoxic cell protease granzyme B initiates apoptosis in a cell-free system by proteolytic processing and activation of the ICE/CED-3 family protease, CPP32, via a novel two-step mechanism. EMBO J 15:2407-2416.
17. Adrain C, Murphy BM, Martin SJ (2005) Molecular ordering of the caspase activation cascade initiated by the cytotoxic T lymphocyte/natural killer (CTL/NK) protease granzyme B. J Biol Chem 280:4663-4673.