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Introduction

Cathepsin B is one of approximately a dozen members of the Cathepsin (Greek kata- "down" and hepsein "boil”) family, a group of proteases widely distributed in animal cells with vital roles in a variety of processes, including intracellular protein turnover, immune response triggered apoptosis, and extracellular bone resorption. Because most of these enzymes are activated in low pH environments, their functions are generally localized to the interior of lysosomes. One notable exception to this rule is Cathepsin K, which is secreted extracellularly by osteoclasts during bone resorption. They share the general function of degrading polypeptides, and are differentiated by their respective structures, catalytic mechanisms, and substrate specificities ^{[1] [2]}. Cathepsin B is coded for by the gene CTSB (homo sapiens) located on chromosome 8 ^[3], and is conserved in chimpanzee, dog, cow, mouse, rat, chicken, zebrafish, fruit fly, and several other organisms ^[4](6).

Structure

Mechanism

Medical Implications