Caspase-7/CASP7 Protein, Human (His)

Caspase-7/CASP7 Protein, a thiol protease, intricately participates in various programmed cell death processes, including apoptosis, pyroptosis, or granzyme-mediated programmed cell death. This multifaceted protein catalyzes the proteolytic cleavage of target proteins, such as CLSPN, PARP1, PTGES3, and YY1, upon activation by initiator caspases (CASP8, CASP9, and/or CASP10), thereby mediating the execution phase of apoptosis. Notably, CASP7 displays a preference for Asp-Glu-Val-Asp (DEVD) consensus sequences and exhibits plasticity for alternate non-canonical sequences. In the inflammatory response to bacterial infection, CASP7 plays a crucial role by cleaving and activating sphingomyelin phosphodiesterase SMPD1 in the extracellular milieu, promoting membrane repair. Moreover, CASP7 regulates pyroptosis in intestinal epithelial cells and granzyme-mediated programmed cell death in hepatocytes, contributing to membrane repair and counteracting the action of gasdermin-D (GSDMD) pores and perforin (PRF1) pores, respectively. Additionally, CASP7 inhibits type I interferon production during virus-induced apoptosis by cleaving antiviral proteins CGAS, IRF3, and MAVS. Despite its diverse roles, CASP7 lacks enzymatic activity itself.