caspase-7; ICE-like apoptotic protease 3; ICE-LAP3; Mch-3 protein (CASP7, MCH3)
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Function
- role in the activation cascade of caspases responsible for apoptosis execution
- cleaves sterol regulatory element binding proteins (SREBPs) & activates them
- proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-gly-217' bond
- cleavages by granzyme B or caspase-10 generate the two active subunits
- propeptide domains can also be cleaved efficiently by caspase-3
- strict requirement for an Asp residue at position P1 & has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-
Inhibition: inhibited by isatin sulfonamides
Structure
- active heterodimers between the small subunit of caspase-7 & the large subunit of caspase-3, & vice versa, also occur
- overexpression promotes programmed cell death heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 20 kD (p20) & a 11 kD (p11) subunit
- belongs to the peptidase C14 family
Compartment
Alternative splicing
named isoforms=3
Expression
- expressed in lung, skeletal muscle, liver, kidney, spleen & heart > testis
- no expression in brain