Cathepsin Z (CTSZ)

Cathepsin Z is a lysosomal cysteine-type carboxypeptidase encoded by the CTSZ gene, best known for its strict carboxypeptidase exopeptidase activity, which distinguishes it from other cathepsins that are mostly endopeptidases[1][3]. It is widely expressed, especially in cancer cell lines and tumors, and plays important roles in protein degradation, immune regulation, and extracellular matrix remodeling[1][3]. Cathepsin Z contains a unique insertion in its active site region and an exposed integrin-binding Arg-Gly-Asp motif, allowing interaction with integrins and heparin sulfate proteoglycans, with implications in cellular adhesion and phagocytosis[1]. It has been implicated in tumor cell invasion, migration (via noncatalytic mechanisms), neurodegeneration (dopamine neuron death), inflammation (protective roles in gastric disease), and infection susceptibility (notably tuberculosis)[1][3][7]. While considered a potential therapeutic target, there are currently no approved drugs specifically targeting Cathepsin Z. Expression and genetic variants (SNPs) in CTSZ are being explored for biomarker utility in cancer and infectious disease[1][3].

Other names

Cathepsin XCathepsin PCTSXCathepsin IVCathepsin B2Cathepsin YCathepsin Z1cysteine-type carboxypeptidaselysosomal carboxypeptidase Bcarboxypeptidase LBpreprocathepsin P

Inhibition of protease activity, modulation of cell invasion/migration