Cathepsin-W, also known as lymphopain, is a cysteine protease that belongs to the peptidase C1 family of cysteine cathepsins. This enzyme is encoded by the CTSW gene in humans . Cathepsin-W is predominantly expressed in cytotoxic cells, particularly natural killer (NK) cells and cytotoxic T lymphocytes (CTLs) .
Cathepsin-W shares structural similarities with other members of the papain-like cysteine protease family. It is characterized by its unique enzymatic activities and substrate specificity . The enzyme is glycosylated with high mannose-type glycans and is mainly localized in the endoplasmic reticulum (ER) .
Cathepsin-W plays a crucial role in the immune response. It is predominantly expressed in NK cells, which are preactivated cytotoxic cells capable of mediating their effector function without depending on presented antigenic peptides (MHC class I independent) . The enzyme is also expressed in CTLs, which require activation by antigen-derived peptides bound to the MHC class I complex .
The involvement of cathepsin-W in various physiological and pathological processes is an area of active research. It has been implicated in the modulation of immune responses and may have potential roles in autoimmune and neurodegenerative diseases . Additionally, cathepsin-W is being studied for its potential as a biomarker and therapeutic target in cancer progression .
Human recombinant cathepsin-W is produced using recombinant DNA technology. This involves the insertion of the CTSW gene into an expression vector, which is then introduced into a host cell system for protein production. The recombinant enzyme is subsequently purified for research and therapeutic applications.