CASP4


Description

The CASP4 (caspase 4) is a protein-coding gene located on chromosome 11.

Caspase 4 is an enzyme that proteolytically cleaves other proteins at an aspartic acid residue (LEVD-), and belongs to a family of cysteine proteases called caspases. The function of caspase 4 is not fully known, but it is believed to be an inflammatory caspase, along with caspase 1, caspase 5 (and the murine homolog caspase 11), with a role in the immune system. The anti-inflammatory drug indoprofen is an inhibitor of the activity of the caspase-4 enzyme.

CASP4, also known as caspase-4, is an inflammatory caspase that plays a crucial role in the innate immune response. It acts as the effector of the non-canonical inflammasome, a protein complex that is activated by direct binding of lipopolysaccharide (LPS) to CASP4. This activation triggers pyroptosis, a form of programmed cell death that helps to eliminate infected cells and limit bacterial replication. CASP4 also indirectly activates the NLRP3 and NLRP6 inflammasomes, which promote the release of inflammatory cytokines. CASP4 cleaves a variety of proteins, including GSDMD, IL18, and CGAS. Cleavage of GSDMD leads to pyroptosis, while cleavage of IL18 promotes the recruitment and activation of immune cells. Cleavage of CGAS may play a role in the regulation of antiviral innate immune activation. CASP4 is involved in a variety of cellular processes, including cell death induced by endoplasmic reticulum stress, and by treatment with cytotoxic amyloid precursor protein (APP) peptides found in Alzheimer's patient brains. It interacts with a number of proteins, including CASP1, NOD2, SERPINB1, and TMEM214. In its precursor form, CASP4 interacts with TMEM214, which is required for association with the endoplasmic reticulum membrane.

CASP4 is also known as ICE(rel)II, ICEREL-II, ICH-2, Mih1, Mih1/TX, TX.

Associated Diseases



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