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Hepsin plays a physiologically important role in factor VII (show TH Proteins) activation and hemostasis in zebrafish.
These data demonstrate that the membrane-bound serine protease hepsin is the enzyme responsible for the physiological cleavage of uromodulin (show UMOD Proteins).
The findings suggest that the oncogenic activity of hepsin arises not only from elevated expression level but also from depletion of HAI-1 (show SPINT1 Proteins), events which together trigger gain-of-function activity impacting HGF (show HGF Proteins)/MET signalling and epithelial cohesion
The Hepsin pathway acts in concert with Wnt (show WNT2 Proteins) pathway to promote prostate cancer progression.
Low expression levels of hepsin and TMPRSS3 (show TMPRSS4 Proteins) are associated with poor breast cancer survival
Hepsin suppressed CDK11p58 internal ribosome entry site activity in prostate cancer cells by modulating UNR (show P2RY4 Proteins) expression and eIF-2alpha (show EIF2S1 Proteins) phosphorylation.
The results of this study suggest that, in Korean men, some polymorphisms in the HPN gene might be associated with the risk of developing prostate cancer.
hepsin expression is frequently up-regulated in breast cancer tissues, which is associated with tumor growth and progression
These findings suggest that the MSP (show MSMB Proteins)/RON (show MST1R Proteins) signaling pathway may be regulated by hepsin in tissue homeostasis and in disease pathologies, such as in cancer and immune disorders.
Elevated levels of hepsin interfere with cell adhesion and viability in the background of prostate cancer as well as other tissue types, the details of which depend on the microenvironment provided.
Hepsin activity was inhibited by anthralin and increased by resveratrol.
crystal structure of human hepsin, confirming cleavage and association of the two chains
Hepsin cooperates with MYC (show MYC Proteins) in the progression of adenocarcinoma in a prostate cancer mouse model.
Results suggest that upregulation of the cell surface serine protease hepsin in a primary tumor promotes cancer progression and metastasis.
the ability of hepsin to efficiently activate pro-uPA (show PLAU Proteins) suggests that it may initiate plasmin (show PLG Proteins)-mediated proteolytic pathways at the tumor/stroma interface that lead to basement membrane disruption and tumor progression
Hearing impairment present in hepsin/Tmprss1-null mice is characterized by a combination of various structural, cellular, and molecular abnormalities that are likely to affect different cochlear processes.
The ability of ectopic hepsin to induce tumor growth in mice is abrogated by the mutation of 3 critical residues in the catalytic domain, thus implicating the enzymatic activity of hepsin in promoting tumor progression.
Ln-332 may be one mechanism by which hepsin promotes prostate tumor progression and metastasis, possibly by up-regulating prostate cancer cell motility.
This gene encodes a type II transmembrane serine protease that may function in diverse processes, including regulation of cell growth. Deficiency in this gene results in hearing loss. The protein is cleaved into a catalytic serine protease chain and a non-catalytic scavenger receptor cysteine-rich chain, which associate via a single disulfide bond. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
hepsin (transmembrane protease, serine 1)
, serine protease hepsin
, Serine protease hepsin
, transmembrane protease serine 1
, transmembrane protease, serine 1