| Activity |
|---|
| Catalytic type | Cysteine |
| Peplist | Included in the Peplist with identifier PL00067 |
| NC-IUBMB | Subclass 3.4 (Peptidases) >> Sub-subclass 3.4.22 (Cysteine endopeptidases) >> Peptidase 3.4.22.3
|
| Enzymology | BRENDA database |
| Proteolytic events | CutDB database (35 cleavages) |
| Activity status | human: active (Mort, 2004)
mouse: active (Mort et al., 1988)
|
| Physiology | Contributes to antigen processing for MHC II in mouse, but is not indespensable (Deussing et al., 1998). Suggested to mediate post-translational processing and activation of prorenin (Jutras & Reudelhuber, 1999). |
| Knockout | Antisense-transfected osteosarcoma cells with depressed expression of cathepsin B showed lower invasive activity in Transwell chambers, consistent with the proposal that cathepsin B is involved in the proteolytic processes in invasive osteosarcomas (Kruger et al., 1999). Combined deficiency of cathepsins B and L in mice is lethal during the second to fourth week, and associated with a degree of brain atrophy not previously seen in mice (Felbor et al., 2002). |
| Pharmaceutical relevance | Potential drug target for cancer (e.g. Bervar et al., 2003), but may be required for induction of caspase-independent cell death (Broker et al., 2004). Proposed to be responsible for premature activation of trypsinogen in acute pancreatitis (Figarella et al., 1988; Szilagyi et al., 2001). It has been reported that down-regulation of expression of both cathepsin B and u-plasminogen activator has anti-tumour activity in experimental systems (Gondi et al., 2004). |
| Pathways |
KEGG | Antigen processing and presentation |
|
KEGG | Lysosome |
|
Other databases
| WIKIPEDIA | http://en.wikipedia.org/wiki/Cathepsin_B |
| Cleavage site specificity |
Explanations of how to interpret the
following cleavage site sequence logo and specificity matrix can be found here. |
|---|
| Cleavage pattern | -/-/-/- -/-/-/- (based on 4712 cleavages) |
FFxx