Caspase 13

Caspase 13 or ERICE ("evolutionarily related interleukin-1β converting enzyme") is a protein that was identified in cattle. It belongs to a family of enzymes called caspases that cleave their substrates at C-terminalaspartic acid residues. Although this enzyme was originally reported as a human caspase that could be activated by caspase 8, later studies confirmed the gene identified for caspase 13 came from bovine origin, and is the likely orthologue of human caspase 4.

Caspases are a large family of proteases that cleave their substrates at C-terminal aspartic acid residues, using a catalytic cysteine in their active site. They all play critical roles in programmed cell death (apoptosis) and inflammation. In apoptosis, initiator caspases activate executioner caspases. This triggers the dismantling of the cell by cleaving key cellular proteins. This results in DNA fragmentation or membrane blebbing. This process occurs when the cytoskeleton breaks down, causing protrusions to the cellular membrane during apoptosis.caspase proteins In recent years, research has shown that caspases are also involved in non-apoptotic cellular processes like necroptosis and autophagy. Apart from their primary roles, caspases are essential in development as they remove unnecessary cells during the formation of organs and tissues. However, each protein within the Caspase family has different functions according to where they are located. The dysregulation of the caspases can cause cancer, autoimmunity, and neurodegenerative diseases. They are essential to homeostasis and maintaining healthy cells.