EC Number   |
General Information |
Reference |
|---|
   3.4.22.B62 | more |
homology modeling of FhCL3 using the three dimensional structure of proFhCL1 C25G, PDB ID 2O6X, as a template |
755072 |
| 3.4.22.B62 | physiological function |
although no direct anticoagulant effect of the peptidases is observed, cathepsin peptidases from Fasciola are able to degrade purified fibrinogen, with FhCL1 having the highest fibrinogenolytic activity. FhCL1 and FhCL2 also both efficiently degrade fibrin, but FhCL3 does not. FhCL1 has a larger fibrinogenolytic activity than FhCL2 and FhCL3 and is capable of degradation of the fibrinogen alpha-chain, beta-chain, and gamma-chain. FhCL2 andFhCL3 demonstrate only minor cleavage of the gamma-chain and slower cleavage of the alpha-chain and beta-chain compared to FhCL1 |
754672 |
| 3.4.22.B62 | physiological function |
in the case of the helminth trematode Fasciola hepatica, the secretion of different cathepsin L cysteine peptidases (FhCL) is crucial for the parasite survival. Among these enzymes, cathepsin L3 (FhCL3) is expressed mainly in the juvenile or invasive stage. The ability of FhCL3 to digest collagen is critical for intestinal tissue invasion during juvenile larvae migration. FhCL3 induces a non-canonical inflammasome activation in dendritic cells (DCs) of C57BL/6 mice, leading to interleukin (IL)-1beta and IL-18 production without a previous microbial priming. This activation is depending on the cysteine protease activity of FhCL3 and the NLRP3 receptor, but independent of caspase activation. FhCL3 is internalized by DCs, promoting pro-IL-1beta cleavage to its mature and biologically active form IL-1beta, which is released to the extracellular environment. The FhCL3-induced NLRP3 inflammasome activation conditions DCs to promote a singular adaptive immune response, characterized by increased production of IFN-gamma and IL-13. Due to the poor colocalization of FhCL3 with endosomes or lysosomes, the mechanism of endocytosis could be different from that used by FhCL1. The lack of involvement of NF-kkappaB in FhCL3-induced DCs activation, suggests that other/s transcription factor might be involved in the synthesis of pro-IL-1beta |
753661 |
| 3.4.22.B62 | physiological function |
schistosomal cathepsin peptidases are not able to cleave fibrinogen or fibrin, which is in line with the presence of other anticoagulant and fibrinolytic strategies adopted by schistosomes. This allows schistosomes to counteract fibrin formation at their surface, allowing blood-feeding and survival of the parasite within its host |
754672 |
| 3.4.22.B62 | physiological function |
the dormant larvae of Fasciola hepatica express a specific cathepsin L protease, CL3, stored as an inactive zymogen that is rapidly secreted and activated following emergence from their cysts to become infective larvae |
709951 |
| 3.4.22.B62 | physiological function |
the enzyme enables the parasite penetrate the intestinal wall |
732674 |
