Cathepsin B

Best known among lysosomal cysteine cathepsins for its unusual dual specificity, Cathepsin B (CTSB) functions as both an endopeptidase and a carboxypeptidase, a property arising from a distinctive occluding loop that partially covers the active-site cleft. The enzyme is synthesized as a preproenzyme with a signal peptide and a propeptide, is activated in the acidic lysosomal environment, and is inhibited by cystatins and stefins. Elevated CTSB levels have been documented in numerous tumors, where the protease contributes to extracellular matrix degradation, invasion, and metastatic spread, and it also participates in processing of proinflammatory mediators such as pro-IL-1β.