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. The CASP recruitment domain (CARD) mediates signaling events that are associated with various human diseases including cancer, neuro-degenerative diseases and immune disorders[1].
- 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[2].
- 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.
[3][4]
3D structures of caspase
Caspase 3D structures
