Caspase: Difference between revisions

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Michal Harel, Alexander Berchansky

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 <StructureSection load='1pyo' size='350' side='right' scene='45/458455/Cv/1' caption='CASP-2 subunit P18 (purple, yellow) and subunit P12 (green, cyan) complex with polypeptide inhibitor (salmon, blue), aspartic aldehyde and acetyl group, [[1pyo]]'>
-'''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.  The CASP recruitment domain (CARD) mediates signaling events that are associated with various human diseases including cancer, neuro-degenerative diseases and immune disorders<ref>PMID:30664151</ref>.<br />
 *  '''CASP-1''' (or '''Interleukin-1 beta converting enzyme, ICE''') cleaves precursor cytokine interleukin 1-β and interleukin 18 into mature protein.  See:<br />
 [[Human Caspase-1]]<br />