Caspase (CASP) are cysteine-aspartic proteases (see Protease) which function in apoptosis, necrosis and inflammation. Twelve CASP have been identified in human. CASP is synthesized as an inactive pro-CASP with a prodomain which is being cleaved off to render them active. The X-linked inhibitor of apoptosis protein (XIAP) with its baculoviral IAP repeat (BIR) domain is an inhibitor of CASP.
- CASP-1 (or Interleukin-1 beta converting enzyme, ICE) cleaves precursor cytokine interleukin 1-β and interleukin 18 into mature protein. See:
Human Caspase-1
- CASP-3 or (Apopain; Cysteine protease CPP32) interacts with CASP-8 and CASP-9 during cell apoptosis. See:
Sandox Bay Serrano
Student Projects for UMass Chemistry 423 Spring 2012-5
Caspase-3 Regulatory Mechanisms
- CASP-4 binds the lipid moiety of lipopolysaccharide to induce the activation of non-canonical inflammasome[1].
- CASP-6 is involved in the activation of cascade of caspases during apoptosis. See:
Molecular Playground/Caspase-6 (new)
Caspase-6 and neurodegeneration
- CASP-7 is a heterodimer consisting of P20 (human residues 1-198) and P11 (human residues 199-303) subunits. CASP-7 catalytic domain consists of residues 57-303. is an important initiator CASP and drICE is an effector of apoptosis CASP in Drosophila melanogaster. See:
Molecular Playground/Caspase-7 Dynamics
Molecular Playground/Executioner Caspase-7
- CASP-9 is an aspartic protease linked to mitochondrial death pathway. See:
Molecular Playground/Caspase-9 Regulation.
- Metacaspase (MCASP) are arginine/lysine specific CASP. MCASP are found in plants and fungi.
[2][3]
3D structures of caspase
Caspase 3D structures
- ↑ Lagrange B, Benaoudia S, Wallet P, Magnotti F, Provost A, Michal F, Martin A, Di Lorenzo F, Py BF, Molinaro A, Henry T. Human caspase-4 detects tetra-acylated LPS and cytosolic Francisella and functions differently from murine caspase-11. Nat Commun. 2018 Jan 16;9(1):242. doi: 10.1038/s41467-017-02682-y. PMID:29339744 doi:https://dx.doi.org/10.1038/s41467-017-02682-y
- ↑ Schweizer A, Briand C, Grutter MG. Crystal structure of caspase-2, apical initiator of the intrinsic apoptotic pathway. J Biol Chem. 2003 Oct 24;278(43):42441-7. Epub 2003 Aug 14. PMID:12920126 doi:https://dx.doi.org/10.1074/jbc.M304895200
- ↑ Wilson KP, Black JA, Thomson JA, Kim EE, Griffith JP, Navia MA, Murcko MA, Chambers SP, Aldape RA, Raybuck SA, et al.. Structure and mechanism of interleukin-1 beta converting enzyme. Nature. 1994 Jul 28;370(6487):270-5. PMID:8035875 doi:https://dx.doi.org/10.1038/370270a0
