Caspase 7

Caspase 7 is an executioner cysteine protease that cleaves after aspartate residues and participates in programmed cell death and inflammation[1][2]. Mechanistically, death receptor and DNA-damage pathways activate caspase 7 through caspase 8 and caspase 9, placing it within apoptosis signaling cascades[1]. In Fas-stimulated Jurkat cells, caspase 8 activates caspase 3 and caspase 7, supporting a branched protease cascade during apoptotic execution[3]. In inflammatory models, caspase 1 inflammasomes activate caspase 7, and caspase 7 can mediate caspase 1-induced apoptosis upstream of caspase 3[1][4]. Disease and model evidence links caspase 7 to endotoxemia resistance in deficient mice, Salmonella-infected macrophages, neuropathic rat spinal cord apoptosis, and CHO-cell viability studies[1][4][5][6]. Compared with caspase 3, caspase 7 shares substrate recognition and some endogenous substrates, but specific substrates, caspase 1-dependent activation, and endotoxemia phenotypes distinguish the isoforms[1]. For experimental applications, isatin sulfonamides inhibit caspases 3 and 7 and serve as PET or SPECT apoptosis-imaging recognition units after radiolabeling[7].