Caspase Recruitment Domain Family, Member 18 (CARD18), also known as ICEBERG, is a protein-coding gene that plays a crucial role in the regulation of inflammatory responses and apoptosis. This protein is part of the death domain superfamily, which includes other domains such as the death effector domain and the pyrin domain .
CARD18 contains a caspase recruitment domain (CARD), which is a well-known protein interaction module. This domain is essential for mediating protein-protein interactions necessary for apoptosis and immune cell signaling pathways . CARD18 specifically inhibits the generation of interleukin-1 beta (IL-1β) by interacting with caspase-1 and preventing its association with RIP2 . This interaction down-regulates the release of IL-1β, thereby modulating inflammatory responses .
The primary function of CARD18 is to act as an inhibitor of cysteine-type endopeptidase activity. It is involved in the negative regulation of interleukin-1 beta production and protein binding activity . By inhibiting caspase-1, CARD18 plays a significant role in controlling inflammation and preventing excessive immune responses, which can lead to tissue damage.
Mutations or dysregulation of CARD18 can have significant implications for human health. Abnormalities in the function of CARD18 may contribute to various inflammatory diseases and conditions characterized by excessive apoptosis. Understanding the role of CARD18 in these processes can provide insights into potential therapeutic targets for treating inflammatory and autoimmune diseases.
Human recombinant CARD18 is used in various research applications to study its function and interactions with other proteins. It is particularly valuable in investigating the mechanisms of inflammation and apoptosis, as well as in the development of potential therapeutic interventions for related diseases .