Human Caspase-1: Difference between revisions
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==Activation and Regulation== | ==Activation and Regulation== | ||
Caspase-1 begins as a zymogen, with its two subunits and a CARD region all in one peptide sequence. Activation is thought to be initiated by removal of the CARD region and dimerization. Bonds between subunits can be cleaved, leading to the maturation of the enzyme, but this does not necessarily convey greater activity. ASC and Ipaf have been identified as possible regulators of caspase-1 in a structure called the inflammasome. ASC leads to ATP-driven activation of caspase-1, while Ipaf connects signals triggered by intracellular pathogens.<ref name=Mariathasan>PMID:15190255</ref> Both of these activators are essential for caspase-1 driven cell death, showing a link between inflammation and apoptosis. Adaptors in the inflammasome react to extracellular and endogenous danger signals, usually flaggelin, to activate caspase-1 and begin the inflammatory response.<ref name=Franchi>PMID:19221555</ref> | Caspase-1 begins as a [http://en.wikipedia.org/wiki/Zymogen zymogen], with its two subunits and a CARD region all in one peptide sequence. Activation is thought to be initiated by removal of the CARD region and dimerization. Bonds between subunits can be cleaved, leading to the maturation of the enzyme, but this does not necessarily convey greater activity. ASC and Ipaf have been identified as possible regulators of caspase-1 in a structure called the inflammasome. ASC leads to ATP-driven activation of caspase-1, while Ipaf connects signals triggered by intracellular pathogens.<ref name=Mariathasan>PMID:15190255</ref> Both of these activators are essential for caspase-1 driven cell death, showing a link between inflammation and apoptosis. Adaptors in the inflammasome react to extracellular and endogenous danger signals, usually flaggelin, to activate caspase-1 and begin the inflammatory response.<ref name=Franchi>PMID:19221555</ref> | ||
==Structure== | ==Structure== | ||