EC Number   |
General Information |
Reference |
|---|
   3.4.21.106 | physiological function |
addition of hepsin to osteoarthritis cartilage in explant culture induces significant collagen and aggrecan release and activates metalloproteinases proMMP-1 and proMMP-3. Hepsin directly cleaves the aggrecan core protein at a cleavage site within the interglobular domain. Hepsin expression correlates with synovitis as well as tumour necrosis factor alpha expression, and is induced in cartilage by a pro-inflammatory stimulus. Hepsin demonstrates markedly reduced capacity to activate proteinase-activated receptor-2, compared with matriptase |
755460 |
| 3.4.21.106 | physiological function |
deletion of hepsin in mice results in enlarged hepatocytes and narrowed liver sinusoids. Metastatic cancer cells preferentially colonize the hepsin-/- mouse liver as a result of the retention of tumor cells because of narrower sinusoids. The enlarged hepatocytes express increased levels of connexin, which results from defective prohepatocyte growth factor processing and decreased c-Met phosphorylation in the livers of hepsin-/- mice. Treatment of hepsin-/- mice with recombinant hepatocyte growth factor rescues these phenotypes, and treatment of wild-type mice with an hepatocyte growth fator antagonist recapitulates the phenotypes observed in hepsin-/- mice |
731887 |
| 3.4.21.106 | physiological function |
hepsin alone and not matriptase or HGFA plays a key role in diminishing epithelial cell membrane integrity through degradation of desmogelin-2 in breast cancer cells |
754402 |
| 3.4.21.106 | physiological function |
hepsin andmyc cooperate during the progression to high-grade prostatic adenocarcinoma |
710464 |
| 3.4.21.106 | physiological function |
hepsin inhibits the internal ribosome entry site activity and expression of CDK11p58,which is associated with cell cycle progression and pro-apoptotic signaling in prostate cancer. Hepsin suppresses CDK11p58 internal ribosome entry site activity in prostate cancer by modulating transacting factor unr expression and eIF-2alpha phosphorylation. Hepsin inhibits the expression of unr by directly binding to unr internal ribosome entry site element and suppressing its activity, and also represses eIF-2alpha phosphorylation through down-regulating the expression and phosphorylation of general control nonderepressible-2 |
731633 |
| 3.4.21.106 | physiological function |
hepsin knockdown increases the kinetic prothrombin time and significantly reduces the factor VIIa plasma levels |
731529 |
| 3.4.21.106 | physiological function |
hepsin promotes invasive prostate tumor growth and metastasis |
707989 |
| 3.4.21.106 | physiological function |
membrane-bound hepsin is the enzyme responsible for the physiological cleavage of uromodulin, the most abundant protein in the urine. Hepsin physically interacts with uromodulin and cleaves at the physiological site in vitro and in vivo |
753410 |
| 3.4.21.106 | physiological function |
the macrophage-stimulating protein/RON signaling pathway is regulated by hepsin in tissue homeostasis and in disease pathologies, such as in cancer and immune disorders |
718105 |
