Caspase
From Proteopedia
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'''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.<br /> | '''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.<br /> | ||
| - | * '''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]]<br /> | + | * '''CASP-1''' (or '''Interleukin-1 beta converting enzyme, ICE''') cleaves precursor cytokine interleukin 1-β and interleukin 18 into mature protein. See:<br /> |
| - | * '''CASP-3''' or ('''Apopain; Cysteine protease CPP32''') interacts with CASP-8 and CASP-9 during cell apoptosis. See [[Sandox Bay Serrano]] | + | [[Human Caspase-1]]<br /> |
| - | * '''CASP-6''' is involved in the activation of cascade of caspases during apoptosis. See [[Molecular Playground/Caspase-6 (new)]] | + | * '''CASP-3''' or ('''Apopain; Cysteine protease CPP32''') interacts with CASP-8 and CASP-9 during cell apoptosis. See:<br /> |
| - | * '''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]] | + | [[Sandox Bay Serrano]]<br /> |
| - | * '''CASP-9''' is an aspartic protease linked to mitochondrial death pathway. See [[Molecular Playground/Caspase-9 Regulation]].<br /> | + | [[Student Projects for UMass Chemistry 423 Spring 2012-5]]<br /> |
| + | [[Caspase-3 Regulatory Mechanisms]]<br /> | ||
| + | * '''CASP-6''' is involved in the activation of cascade of caspases during apoptosis. See:<br/> | ||
| + | [[Molecular Playground/Caspase-6 (new)]]<br /> | ||
| + | [[Caspase-6 and neurodegeneration]]<br /> | ||
| + | * '''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:<br /> [[Molecular Playground/Caspase-7 Dynamics]]<br /> | ||
| + | [[Molecular Playground/Executioner Caspase-7]]<br /> | ||
| + | * '''CASP-9''' is an aspartic protease linked to mitochondrial death pathway. See:<br /> | ||
| + | [[Molecular Playground/Caspase-9 Regulation]].<br /> | ||
* '''Metacaspase''' (MCASP) are arginine/lysine specific CASP. MCASP are found in plants and fungi. | * '''Metacaspase''' (MCASP) are arginine/lysine specific CASP. MCASP are found in plants and fungi. | ||
<ref>PMID:12920126</ref><ref>PMID:8035875</ref> | <ref>PMID:12920126</ref><ref>PMID:8035875</ref> | ||
Revision as of 08:16, 20 January 2020
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References
- ↑ 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:http://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:http://dx.doi.org/10.1038/370270a0
