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The integral role caspases play in cell death and disease has led to research on using caspases as a drug target. For example, inflammatory caspase-1 has been implicated in causing autoimmune diseases; drugs blocking the activation of Caspase-1 have been used to improve the health of patients. Additionally, scientists have used caspases as ...
Caspase-1/Interleukin-1 converting enzyme (ICE) is an evolutionarily conserved enzyme that proteolytically cleaves other proteins, such as the precursors of the inflammatory cytokines interleukin 1β and interleukin 18 as well as the pyroptosis inducer Gasdermin D, into active mature peptides.
CARDs were originally characterized based on their involvement in the regulation of caspase activation and apoptosis. [2] The basic six-helix structure of the domain appears to be conserved as far back as the ced-3 and ced-4 genes in C. elegans, the organism in which several components of the apoptotic machinery were first characterized.
Inhibitors of apoptosis are a group of proteins that mainly act on the intrinsic pathway that block programmed cell death, which can frequently lead to cancer or other effects for the cell if mutated or improperly regulated. Many of these inhibitors act to block caspases, a family of cysteine proteases that play an integral role in apoptosis. [1]
67770 Ensembl ENSG00000120159 ENSMUSG00000028578 UniProt Q9H8G2 Q8VDY9 RefSeq (mRNA) NM_001167575 NM_024828 NM_026368 RefSeq (protein) NP_001161047 NP_079104 NP_080644 NP_001393278 NP_001393279 NP_001393280 Location (UCSC) Chr 9: 26.84 – 26.89 Mb Chr 4: 94.39 – 94.45 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Caspase activity and apoptosis inhibitor 1 is a protein that in ...
The death-effector domain (DED) is a protein interaction domain found only in eukaryotes that regulates a variety of cellular signalling pathways. [2] The DED domain is found in inactive procaspases (cysteine proteases) and proteins that regulate caspase activation in the apoptosis cascade such as FAS-associating death domain-containing protein ().
APO-1-mediated apoptosis can be inhibited by a variety of factors, including the viral caspase inhibitors CrmA and p35, as well as viral FLICE-inhibitory proteins known as v-FLIPs. When in the presence of APO-1, v-FLIPs preferentially bind and prevent procaspase-8 from being recruited; as such, apoptosis is stalled.
This functional apoptosome then can provide a platform activation of caspase 9. [1] [16] Caspase 9 exists as a zymogen in the cytosol and is thought to be found at 20 nM in cells. [16] Though it is known that the zymogen does not need to be cleaved in order to become active, [16] the activity of procaspase-9 may increase significantly once ...