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Unless otherwise stated all data on this page refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).
Caspases, (E.C. 3.4.22.-) which derive their name from Cysteine ASPartate-specific proteASES, include at least two families; initiator caspases (caspases 2, 8, 9 and 10), which are able to hydrolyse and activate a second family of effector caspases (caspases 3, 6 and 7), which themselves are able to hydrolyse further cellular proteins to bring about programmed cell death. Caspases are heterotetrameric, being made up of two pairs of subunits, generated by a single gene product, which is proteolysed to form the mature protein. Members of the mammalian inhibitors of apoptosis proteins (IAP) are able to bind the procaspases, thereby preventing maturation to active proteinases.
Caspase 1 Show summary »« Hide summary More detailed page
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Caspase 2 Show summary »« Hide summary More detailed page
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Caspase 3 Show summary »« Hide summary More detailed page
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Caspase 4 Show summary »« Hide summary More detailed page
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Caspase 5 Show summary »« Hide summary More detailed page
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Caspase 6 Show summary »« Hide summary More detailed page
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Caspase 7 Show summary »« Hide summary More detailed page
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Caspase 8 Show summary »« Hide summary More detailed page
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Caspase 9 Show summary »« Hide summary More detailed page
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Caspase 10 Show summary »« Hide summary More detailed page
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Caspase 14 Show summary »« Hide summary More detailed page
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9. Putt KS, Chen GW, Pearson JM, Sandhorst JS, Hoagland MS, Kwon JT, Hwang SK, Jin H, Churchwell MI, Cho MH et al.. (2006) Small-molecule activation of procaspase-3 to caspase-3 as a personalized anticancer strategy. Nat Chem Biol, 2 (10): 543-50. [PMID:16936720]
10. Ruchaud S, Korfali N, Villa P, Kottke TJ, Dingwall C, Kaufmann SH, Earnshaw WC. (2002) Caspase-6 gene disruption reveals a requirement for lamin A cleavage in apoptotic chromatin condensation. EMBO J, 21 (8): 1967-77. [PMID:11953316]
11. Scott CW, Sobotka-Briner C, Wilkins DE, Jacobs RT, Folmer JJ, Frazee WJ, Bhat RV, Ghanekar SV, Aharony D. (2003) Novel small molecule inhibitors of caspase-3 block cellular and biochemical features of apoptosis. J Pharmacol Exp Ther, 304 (1): 433-40. [PMID:12490620]
Database page citation:
C14: Caspase. Accessed on 04/12/2024. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=734.
Concise Guide to PHARMACOLOGY citation:
Alexander SPH, Fabbro D, Kelly E, Mathie AA, Peters JA, Veale EL, Armstrong JF, Faccenda E, Harding SD, Davies JA et al. (2023) The Concise Guide to PHARMACOLOGY 2023/24: Enzymes. Br J Pharmacol. 180 Suppl 2:S289-373.
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CARD16 (Caspase recruitment domain-containing protein 16, caspase-1 inhibitor COP, CARD only domain-containing protein 1, pseudo interleukin-1β converting enzyme, pseudo-ICE, ENSG00000204397) shares sequence similarity with some of the caspases.