caspase45

Caspase-45 is a name that has appeared in some scientific databases and discussions as a proposed member of the caspase protease family, but its status as a distinct, functionally characterized enzyme is not established in widely used public resources. In several entries, CASP45 is listed as a predicted gene or transcript, yet there is no consensus on whether it encodes an active protease, and it may reflect annotation artifacts, alternative splicing, or naming inconsistencies with other caspases.

Caspases are cysteine proteases that cleave substrates after aspartate residues and play central roles in apoptosis and inflammatory signaling. They are typically synthesized as inactive zymogens and activated via proteolytic processing. If caspase-45 were confirmed as a genuine enzyme, it would be evaluated for its domain architecture, catalytic residues, and classification as an initiator or executioner caspase, as well as its expression pattern, regulation, and substrate specificity.

Current evidence for caspase-45 remains inconclusive. There are no widely cited experimental studies detailing its expression, enzymatic activity, substrates, or physiological function. Consequently, the scientific community treats CASP45 as a tentative annotation rather than a validated caspase with an established role.

Future research would require robust validation, including transcript and protein detection, demonstration of catalytic activity in vitro, substrate profiling, and functional studies in cellular or organismal models to determine whether caspase-45 constitutes a real caspase with a defined biological role. See also: Caspase family; Apoptosis; Inflammation.