CASP5


Description

The CASP5 (caspase 5) is a protein-coding gene located on chromosome 11.

Caspase 5 (CASP5) is an enzyme that breaks down other proteins at a specific point called an aspartic acid residue. It belongs to a family of enzymes called caspases that use cysteine to cut proteins. CASP5 is classified as an inflammatory caspase, along with caspase 1, caspase 4, and the mouse caspase 11, and plays a role in the immune system.

Caspase-5 (CASP5) is a thiol protease involved in programmed cell death, specifically the process of pyroptosis. It initiates pyroptosis by cleaving Gasdermin-D (GSDMD), releasing the N-terminal gasdermin moiety that forms pores in cell membranes, leading to cell lysis. Additionally, CASP5 mediates the cleavage and maturation of IL18, a pro-inflammatory cytokine. Interestingly, the cleavage of GSDMD and IL18 is not solely dependent on the consensus cleavage site but also relies on an exosite interface on CASP4. CASP5 also participates in non-canonical inflammasome activation by cleaving cGAS, potentially playing a role in regulating antiviral innate immune responses. {ECO:0000269|PubMed:28314590, ECO:0000269|PubMed:29898893, ECO:0000269|PubMed:37993714}

CASP5 is also known as ICE(rel)III, ICEREL-III, ICH-3.

Associated Diseases


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