Activation of caspases ensures that the cellular components are degraded in a controlled manner, carrying out cell death with minimal effect on surrounding tissues.

These forms of cell death are important for protecting an organism from stress signals and pathogenic attack.

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.

[7] Note that in addition to apoptosis, caspase-8 is also required for the inhibition of another form of programmed cell death called necroptosis.

Caspase-14 plays a role in epithelial cell keratinocyte differentiation and can form an epidermal barrier that protects against dehydration and UVB radiation.

[13] Some activating multiprotein complexes includes: Once appropriately dimerised, the Caspases cleave at inter domain linker regions, forming a large and small subunit.

The cell shrinks and condenses - the cytoskeleton will collapse, and the nuclear envelope disassembles the DNA fragments up.

This results in the cell forming self-enclosed bodies called 'blebs', to avoid release of cellular components into the extracellular medium.

Examples of caspase cascade during apoptosis: Pyroptosis is a form of programmed cell death that inherently induces an immune response.

[citation needed] Caspase-1 activation is mediated by a repertoire of proteins, allowing detection of a range of pathogenic ligands.

This cellular ion imbalance leads to oligomerisation of NLRP3 molecules to form a multiprotein complex called the NLRP3 inflammasome.

[22] A crucial downstream substrate for pyroptotic caspases is Gasdermin D (GSDMD)[23] Inflammation is a protective attempt by an organism to restore a homeostatic state, following disruption from harmful stimulus, such as tissue damage or bacterial infection.

[7] H. Robert Horvitz initially established the importance of caspases in apoptosis and found that the ced-3 gene is required for the cell death that took place during the development of the nematode C. elegans.

Horvitz and his colleague Junying Yuan found in 1993 that the protein encoded by the ced-3 gene is cysteine protease with similar properties to the mammalian interleukin-1-beta converting enzyme (ICE) (now known as caspase 1).