Caspase 1

Caspase 1/Interleukin-1 converting enzyme is an is_associated_with::enzyme that proteolytically cleaves other proteins, such as the precursor forms of the inflammatory is_associated_with::cytokines interleukin 1β and is_associated_with::interleukin 18, into active mature peptides.

Structure
Caspase 1 is produced as a is_associated_with::zymogen that is cleaved into 20 kDa (p20) and 10 kDa (p10) subunits that become part of the active enzyme. Active caspase 1 contains two is_associated_with::heterodimers of p20 and p10. It interacts with another is_associated_with::CARD domain containing protein called is_associated_with::PYCARD (or ASC) and is involved in is_associated_with::inflammasome formation and activation of inflammatory processes.

Function
Caspase 1 has been shown to induce cell is_associated_with::necrosis or is_associated_with::pyroptosis and may function in various developmental stages. Studies of a similar protein in mouse suggest a role in the pathogenesis of is_associated_with::Huntington's disease. is_associated_with::Alternative splicing of the gene results in five transcript variants encoding distinct isoforms. Recent studies implicated caspase 1 in promoting CD4 T-cell death and inflammation by HIV, two signature events that fuel HIV disease progression to AIDS.

Interactions
Caspase 1 has been shown to interact with is_associated_with::NLRC4.