Sandbox/ caspase-3 regulation: Difference between revisions
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S-nitrosylation of cysteine also regulates activity of caspase-3 in response of NO in the cell (Maejima, Adachi et al. 2005). As the previous discovery of nitosylated catalytic cysteine in the other caspases, S-nitrosylation directly inhibits the function of C163 of caspase-3. This kind of regulation is sufficiently strong and is a new anti-cancer pathway. For example, induced NO stress could definitely inhibit the myocardial apoptosis at the treatment of DOX. | S-nitrosylation of cysteine also regulates activity of caspase-3 in response of NO in the cell (Maejima, Adachi et al. 2005). As the previous discovery of nitosylated catalytic cysteine in the other caspases, S-nitrosylation directly inhibits the function of C163 of caspase-3. This kind of regulation is sufficiently strong and is a new anti-cancer pathway. For example, induced NO stress could definitely inhibit the myocardial apoptosis at the treatment of DOX. | ||
Phosphorylation consists in another important signaling pathway in biological system. Caspase-3 can be phosphorylated by many kinases like p38a MAPK, PAK2 and PKCdelta. However the site and function of phosphorylation is still unclear. | |||
====Natural Inhibitors==== | ====Natural Inhibitors==== | ||
X-linked inhibitor of apoptosis proteins (XIAP) contains the second baculovirus IAP repeat domain (BIR2) targeting caspase-3 and caspase-7. | X-linked inhibitor of apoptosis proteins (XIAP) contains the second baculovirus IAP repeat domain (BIR2) targeting caspase-3 and caspase-7. | ||
<StructureSection load='1I30' size='350' side='right' caption='Structure of complex of caspase-3 with XIAP-BIR2' scene=''> | |||
</StructureSection> | |||
Reference: | Reference: | ||