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Cathepsin B

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Synonyms

CatB; CathB; CB1; CPSB; CTSB; EC 3.4.22.1

Historical Background

Cathepsin derives from the Greek word “kathepsein” (i.e., to digest) and was coined in 1929 to describe digestive peptidases that are active in a slightly acidic environment (Willstätter and Bamann 1929). Cathepsin B, originally named cathepsin B1, was the first and remains the best-characterized member of the C1 family of papain-like, lysosomal cysteine peptidases. First purified from human liver in 1973 (Barrett 1973), cathepsin B is ubiquitously expressed in most cell and tissue types. The first complete protein sequence for cathepsin B, isolated from rat liver, was reported in 1983 (Takio et al. 1983). The first cDNA sequences for cathepsin B were published in 1985 (San Segundo et al. 1985). Cathepsin B exhibits both endopeptidase and exopeptidase activities, which are modulated by its occluding loop (Illy et al. 1997) and blocked by endogenous inhibitors of cysteine cathepsins (Barrett 1986). The main role...

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Cavallo-Medved, D., Sloane, B.F., Moin, K. (2018). Cathepsin B. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_101523

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