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Abz-KQSRKFVPY(3-NO2) + H2O
Abz-KQSR + KFVPY(3-NO2)
-
peptide sequence from trask
-
-
?
Abz-RAARVVGGY(3-NO2) + H2O
Abz-RAAR + VVGGY(3-NO2)
-
-
-
-
?
Abz-RKRRGSRGY(3-NO2) + H2O
Abz-RKRR + GSRGY(3-NO2)
-
peptide sequence from filaggrin
-
-
?
Abz-RLARVVGGY(3-NO2) + H2O
Abz-RLAR + VVGGY(3-NO2)
-
-
-
-
?
Abz-RQARAVGGY(3-NO2) + H2O
Abz-RQAR + AVGGY(3-NO2)
-
-
-
-
?
Abz-RQARVVGGY(3-NO2) + H2O
Abz-RQAR + VVGGY(3-NO2)
Abz-RQARYVGGY(3-NO2) + H2O
Abz-RQAR + YVGGY(3-NO2)
-
-
-
-
?
Abz-RQLRVVGGY(3-NO2) + H2O
Abz-RQLR + VVGGY(3-NO2)
-
-
-
-
?
Abz-RQRRALEKY(3-NO2) + H2O
Abz-RQRR + ALEKY(3-NO2)
-
peptide sequence from alphaEbeta7 integrin
-
-
?
Abz-RQRRVVGGY(3-NO2) + H2O
Abz-RQRR + VVGGY(3-NO2)
-
-
-
-
?
Abz-RQYRVVGGY(3-NO2) + H2O
Abz-RQYR + VVGGY(3-NO2)
-
-
-
-
?
Abz-RRARVVGGY(3-NO2) + H2O
Abz-RRAR + VVGGY(3-NO2)
-
-
-
-
?
Abz-SKGRSLIGY(3-NO2) + H2O
Abz-SKGR + SLIGY(3-NO2)
-
peptide sequence from PAR-2
-
-
?
Abz-SKLRVVGGY(3-NO2) + H2O
Abz-SKLR + VVGGY(3-NO2)
-
peptide sequence from proMSP-1
-
-
?
acetyl-DQLR-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
acetyl-KKTR-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
acetyl-KQLR-7-amido-4-methylcoumarin + H2O
?
-
most active tetrapeptide substrate
-
-
?
acetyl-PVDR-7-amido-4-methylcoumarin + H2O
?
-
least active tetrapeptide substrate
-
-
?
blood clotting factor IX + H2O
active blood clotting factor IX
-
-
-
-
?
blood clotting factor VII + H2O
active blood clotting factor VII
-
-
-
-
?
blood clotting factor XII + H2O
active blood clotting factor XII
-
-
-
-
?
Boc-Gln-Ala-Arg-AMC + H2O
?
-
-
-
-
?
Boc-QAR-7-amido-4-methylcoumarin + H2O
Boc-QAR + 7-amino-4-methylcoumarin
-
-
-
?
epidermal growth factor receptor + H2O
?
-
hepsin cleavage of epidermal growth factor receptor is not dependent on receptor tyrosine phosphorylation
-
-
?
factor X + H2O
?
-
activates factor X in the presence of factor VII
-
?
Glu-Pro-Arg-4-nitroanilide + H2O
?
-
-
-
?
hepatocyte growth factor precursor + H2O
?
L-Asp-L-Ala-L-Ala-L-Arg-4-nitroanilide + H2O
L-Asp-L-Ala-L-Ala-L-Arg + 4-nitroaniline
-
-
-
-
?
L-Asp-L-Lys-(gamma-Cbo)-L-Pro-L-Arg-4-nitroanilide + H2O
L-Asp-L-Lys-(gamma-Cbo)-L-Pro-L-Arg + 4-nitroaniline
-
-
-
-
?
laminin-332 + H2O
?
-
by Western blotting and mass spectrometry, it is shown that hepsin cleaves the beta3 chain of rat Laminin-332. N-terminal sequencing identifies the cleavage site at beta3 Arg245, in a sequence context (SQLR245 cleavage LQGSCFC) conserved among species and in remarkable agreement with reported consensus target sequences for hepsin activity
-
-
?
microsomal glutathione S-transferase 1 + H2O
active microsomal glutathione S-transferase
-
hepsin seems to activate through microsomal glutathione S-transferase 1 dimer formation
-
-
?
N-acetyl-KQLR-7-amido-4-methylcoumarin + H2O
N-acetyl-KQLR + 7-amino-4-methylcoumarin
-
-
-
?
N-acetyl-L-Lys-L-Arg-L-Leu-L-Arg-7-amido-4-carbamoylmethylcoumarin + H2O
?
-
-
-
-
?
N-benzoyl-Ile-Glu-Phe-Ser-Arg-4-nitroanilide + H2O
?
N-benzoyl-Leu-Ser-Arg-4-nitroanilide + H2O
?
N-benzoyl-Phe-Val-Arg-4-nitroanilide + H2O
?
N-benzyloxycarbonyl-Ala-Arg-Arg 4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-Ala-Arg-Arg + 7-amino-4-methylcoumarin
-
weak substrate
-
?
N-tert-butyloxycarbonyl-Gly-Lys-Arg 4-methylcoumarin 7-amide + H2O
N-tert-butyloxycarbonyl-Gly-Lys-Arg + 7-amino-4-methylcoumarin
-
weak substrate
-
?
pro-hepatocyte growth factor + H2O
active hepatocyte growth factor
pro-macrophage-stimulating protein + H2O
?
-
the cleavage site is between Arg(483) and Val(484). At least 50% of the substrate is processed within 1 h at a hepsin concentration of 2.4 nM and at a molar enzyme to substrate ratio of 1:500
-
-
?
pro-urokinase + H2O
active urokinase
-
-
-
-
?
pro-urokinase-type plasminogen activator + H2O
active high molecular weight urokinase-type plasminogen activator
-
cleavage at the Lys158-Ile159 (P1-P1') peptide bond
-
-
?
prostasin pro-peptide + H2O
prostasin
-
hepsin activates prostasin, cleavage occurs at Arg44
-
-
?
single-chain hepatocyte growth factor + H2O
two-chain hepatocyte growth factor
efficiently converted by soluble form of hepsin comprising the entire extracellular domain
-
-
?
Suc-Leu-Leu-Val-Tyr-4-methylcoumaryl-7-amide + H2O
?
-
2% active with the purifed enzyme
-
-
?
t-butyloxycarbonyl-Ala-Gly-Pro-Arg-4-methylcoumaryl-7-amide + H2O
?
-
12% active with the purifed enzyme
-
-
?
t-butyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-Gln-Arg-Arg-4-methylcoumaryl-7-amide + H2O
?
-
100% active with the purifed enzyme
-
-
?
t-butyloxycarbonyl-Gln-Gly-Arg-4-methylcoumaryl-7-amide + H2O
?
-
58% active with the purifed enzyme
-
-
?
t-butyloxycarbonyl-Glu-Ala-Arg-4-methylcoumaryl-7-amide + H2O
?
-
41% active with the purifed enzyme
-
-
?
t-butyloxycarbonyl-Glu-Lys-Lys-4-methylcoumaryl-7-amide + H2O
?
-
8% active with the purifed enzyme
-
-
?
t-butyloxycarbonyl-Gly-Lys-Arg-4-methylcoumaryl-7-amide + H2O
?
-
25% active with the purifed enzyme
-
-
?
t-butyloxycarbonyl-Leu-Lys-Arg-4-methylcoumaryl-7-amide + H2O
?
-
19% active with the purifed enzyme
-
-
?
t-butyloxycarbonyl-Leu-Ser-Thr-Arg-4-methylcoumaryl-7-amide + H2O
?
-
13% active with the purifed enzyme
-
-
?
t-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
?
-
20% active with the purifed enzyme
-
-
?
tert-butyloxycarbonyl-Gln-Ala-Arg 4-methylcoumarin 7-amide + H2O
tert-butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
weak substrate
-
?
tert-butyloxycarbonyl-Gln-Arg-Arg 4-methylcoumarin 7-amide + H2O
tert-butyloxycarbonyl-Gln-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
tert-Butyloxycarbonyl-Val-Pro-Arg 4-methylcoumarin 7-amide + H2O
tert-Butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
weak substrate
-
?
Z-Phe-Arg-4-methylcoumaryl-7-amide + H2O
?
-
9% active with the purifed enzyme
-
-
?
zymogen factor VII + H2O
factor VIIa
-
cleaves between Arg152 and Ile153
-
?
additional information
?
-
Abz-RQARVVGGY(3-NO2) + H2O
Abz-RQAR + VVGGY(3-NO2)
-
-
-
-
?
Abz-RQARVVGGY(3-NO2) + H2O
Abz-RQAR + VVGGY(3-NO2)
-
peptide sequence from matriptase
-
-
?
hepatocyte growth factor precursor + H2O
?
-
-
-
?
hepatocyte growth factor precursor + H2O
?
-
potential substrate for hepsin in vivo
-
-
?
hepatocyte growth factor precursor + H2O
?
-
the catalytic domain of hepsin is a highly efficient activator (50% activation at 3.4 nM) of hepatocyte growth factor, the optimal P4-P1 substrate preference for hepsin sequence is Lys-Gln-Leu-Arg which exactly matches the activation sequence of hepatocyte growth factor precursor
-
-
?
N-benzoyl-Ile-Glu-Phe-Ser-Arg-4-nitroanilide + H2O
?
-
-
-
?
N-benzoyl-Ile-Glu-Phe-Ser-Arg-4-nitroanilide + H2O
?
-
-
-
?
N-benzoyl-Ile-Glu-Phe-Ser-Arg-4-nitroanilide + H2O
?
-
-
-
?
N-benzoyl-Leu-Ser-Arg-4-nitroanilide + H2O
?
-
-
-
?
N-benzoyl-Leu-Ser-Arg-4-nitroanilide + H2O
?
-
-
-
?
N-benzoyl-Leu-Ser-Arg-4-nitroanilide + H2O
?
-
-
-
?
N-benzoyl-Leu-Ser-Arg-4-nitroanilide + H2O
?
-
-
-
?
N-benzoyl-Phe-Val-Arg-4-nitroanilide + H2O
?
-
-
-
?
N-benzoyl-Phe-Val-Arg-4-nitroanilide + H2O
?
-
-
-
?
N-benzoyl-Phe-Val-Arg-4-nitroanilide + H2O
?
-
-
-
?
pro-hepatocyte growth factor + H2O
active hepatocyte growth factor
-
hepsin-mediated pro-HGF activation may be critical in the pathogenesis of human prostate cancer
-
-
?
pro-hepatocyte growth factor + H2O
active hepatocyte growth factor
-
-
-
-
?
Protein + H2O
?
-
-
-
?
additional information
?
-
-
biological role in cell growth
-
?
additional information
?
-
-
enzyme does not cleave factor VII R152E mutant
-
?
additional information
?
-
-
biological role in cell growth
-
?
additional information
?
-
-
hepsin reduces cell growth, cell invation and soft agar colony formation after expression in PC-3, LNCaP and DU145 cells
-
?
additional information
?
-
-
P1-P4 substrate specificity, hepsin exhibits strong preference at the P1 position for arginine over lysine, favours theonine, leucine or asparagine at the P2, glutamine or lysine at the P3, and proline or lysine at the P4 position
-
-
?
additional information
?
-
-
does not cleave pro-tissue-type plasminogen activator
-
-
?
additional information
?
-
-
hepsin exhibits trypsin-like catalytic activity that favores Arg at the P1, Thr/Leu/Asn at the P2, Gln/Lys at the P3, and Pro/Lys at the P4 positions
-
-
?
additional information
?
-
-
to study the substrate specificity of type II transmembrane serine proteases internally quenched fluorogenic peptide substrates are used based on the autoactivation sequence of matriptase (RQARVVGG). Positions P4, P3, P2 and P1 are substituted with nonpolar (Ala, Leu), aromatic (Tyr), acid (Glu) and basic (Arg) amino acids, whereas P1 is fixed to Arg. Hepsin shares similarities with matriptase and DESC1, but is markedly more permissive at P2
-
-
?
additional information
?
-
-
biological role in cell growth
-
?
additional information
?
-
-
cleaves after basic amino acid residues, Arg being preferable to Lys
-
?
additional information
?
-
-
hepsin stimulates disulfide-linked microsomal glutathione transferase 1 dimer formation resulting in activation of microsomal glutathione transferase 1 and preferential degradation of microsomal glutathione transferase 1 dimer
-
-
?
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(S)-N-(4-bromobenzyl)-4-(3-(3-carbamimidoylphenyl)-2-(naphthalene-2-sulfonamido)propanoyl)piperazine-1-carboxamide
inhibitor shows potency and selectivity for hepsin over matriptase and hepatocyte growth factor activator
1-[6-(6-methyl-3H-indol-2-yl)pyridin-2-yl]cyclohexan-1-ol
compounds exhibits inhibition of invasion and migration of hepsin-overexpressing cell line. The selective inhibition of hepsin is likely due to interactions of the midine group at the S1 site with the cyclohexyl ring from the 2-aryl group projecting towards the S1' site and the tert-hydroxyl group interacting with His57 side-chain
3,4-dichloroisocoumarin
-
94% inhibition at 0.1 mM
4-(2-aminoethyl)-benzenesulfonylfluoride hydrochloride
-
residual hepsin activity: 0%
4-amidinophenylmethylsulfonyl fluoride
-
complete inhibition at 1 mM
4-methylumbelliferyl p-guanidinobenzoate
-
irreversible inhibitor
9-fluorenylmethyloxycarbonyl-NR-ketobenzothiazole
potent and selective inhibitor for hepsin over matriptase
alpha1-Aantichymotrypsin
-
residual hepsin activity: 88%
-
alpha1-antitrypsin
-
residual hepsin activity: 67%
-
alpha2-antiplasmin
-
residual hepsin activity: 1%
-
anthralin
-
at 0.067 mM anthralin the hepsin activity is reduced by more than 70%
CaCl2
-
43% inhibition at 1 mM, with t-butyloxycarbonyl-Gln-Arg-Arg-4-methylcoumaryl-7-amide as substrate
diisopropylfluorophosphate
-
complete inhibition at 5 mM
dithiothreitol
-
94% inhibition at 10 mM, with t-butyloxycarbonyl-Gln-Arg-Arg-4-methylcoumaryl-7-amide as substrate
E64
-
31% inhibition at 0.1 mM, with t-butyloxycarbonyl-Gln-Arg-Arg-4-methylcoumaryl-7-amide as substrate
EDTA
-
8% inhibition at 1 mM, with t-butyloxycarbonyl-Gln-Arg-Arg-4-methylcoumaryl-7-amide as substrate
Glu-Gly-Arg-chloromethyl ketone
-
irreversible covalent inhibitor
HAI-2
-
is a potent inhibitor
-
hepatocyte growth factor activator inhibitor-1
-
potent inhibitor of hepsin activity
-
hepatocyte growth factor activator inhibitor-1-derived Kunitz domain inhibitor
-
KD1, inhibits cleavage of laminin-332 in a dose-dependent manner
-
hepatocyte growth factor activator inhibitor-1B
potent inhibitor of hepsin
-
hepatocyte growth factor activator inhibitor-2
-
HI-10331
-
reversible active site inhibitor
KD1
-
HAI-1B-derived Kunitz domain inhibitor
-
MgCl2
-
21% inhibition at 1 mM, with t-butyloxycarbonyl-Gln-Arg-Arg-4-methylcoumaryl-7-amide as substrate
N-alpha-p-tosyl-L-lysine chloromethyl ketone
-
12% inhibition at 0.1 mM, with t-butyloxycarbonylc-Gln-Arg-Arg-4-methylcoumaryl-7-amide as substrate
N-ethylmaleimide
-
25% inhibition at 1 mM, with t-butyloxycarbonyl-Gln-Arg-Arg-4-methylcoumaryl-7-amide as substrate
N-tosyl-L-phenylalanine chloromethyl ketone
-
13% inhibition at 0.1 mM, with t-butyloxycarbonyl-Gln-Arg-Arg-4-methylcoumaryl-7-amide as substrate
N-[1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]-N2-(20-[3,3-dimethyl-5-sulfo-2-[(1E)-3-[(4E)-4-[(2E)-2-(1,3,3-trimethyl-5-sulfo-1,3-dihydro-2H-indol-2-ylidene)ethylidene]cyclohex-1-en-1-yl]prop-1-en-1-yl]-3H-indolium-1-yl]-16-oxo-4,7,10,13-tetraoxa-15-azaicosan-1-oyl)-L-leucinamide
Leu-Arg dipeptide, attached to dye SulfoCy7. Compound shows 1000fold selectivtiy for hepsin over matriptase and selective uptake and retention in hepsin-overexpressing cells
N2-acetyl-N-[1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]-L-leucinamide
inhibitor based on tetrapeptide hepsin inhibitor acetyl-KQLR-ketothiazole. Hepsin affinity of the (R)-epimer is similar to that of the corresponding (S)-epimer
N2-acetyl-N-[5-carbamimidamido-1-oxo-1-(1,3-thiazol-2-yl)pentan-2-yl]-L-leucinamide
inhibitor based on tetrapeptide hepsin inhibitor acetyl-KQLR-ketothiazole. Hepsin affinity of the (R)-epimer is similar to that of the corresponding (S)-epimer
NaN3
-
34% inhibition at 1 mM, with t-butyloxycarbonyl-Gln-Arg-Arg-4-methylcoumaryl-7-amide as substrate
PEGylated Kunitz domain-1
-
potent hepsin active site inhibitor derived from hepatocyte growth factor activator inhibitor-1
-
phenylmethanesulfonyl fluoride
-
80% inhibition at 1 mM
plasminogen activator inhibitor-1
-
residual hepsin activity: 0%
serpinB12
forms a covalent complex with hepsin. Hepsin cleaves the reactive-site loop after the Arg residue
-
Soybean trypsin inhibitor
-
residual hepsin activity: 78%
-
antithrombin III
-
76% inhibition at 0.003 mM, 1U/ml heparin enhances inhibition
-
antithrombin III
-
residual hepsin activity: 0%
-
Aprotinin
-
90% inhibition at 0.008 mM
Aprotinin
-
residual hepsin activity: 1%
hepatocyte growth factor activator inhibitor-2
-
potent inhibitor of hepsin activity
-
hepatocyte growth factor activator inhibitor-2
potent inhibitor of hepsin
-
leupeptin
-
residual hepsin activity: 4%
leupeptin
-
99% inhibition at 0.1 mM
leupeptin
-
96% inhibition at 0.1 mM, with t-butyloxycarbonyl-Gln-Arg-Arg-4-methylcoumaryl-7-amide as substrate
ZnSO4
-
26% inhibition at 1 mM
ZnSO4
-
59% inhibition at 1 mM, with t-butyloxycarbonyl-Gln-Arg-Arg-4-methylcoumaryl-7-amide as substrate
additional information
-
no inhibition by soybean trypsin inhibitor and tissue factor pathway inhibitor
-
additional information
-
hepatocyte growth factor activator inhibitor 1 and hepatocyte growth factor activator inhibitor 2
-
additional information
antibody hH35 potently inhibits hepsin enzymatic activity at nanomolar concentrations, showing non-linear, slow, tight-binding inhibition
-
additional information
-
antibody hH35 potently inhibits hepsin enzymatic activity at nanomolar concentrations, showing non-linear, slow, tight-binding inhibition
-
additional information
synthesis of a heterobivalent inhibitor, targeting both hepsin and prostate-specific membrane antigen, EC 3.4.17.21. The compound is based on an amidine-containing indole analog linked with Lys-urea-Glu for binding to prostate-specific membrane antigen, and the optical dye SulfoCy7. Compound shows selective binding and retention in both prostate-specific membrane antigen and hepsin high-expressing cells
-
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Leytus, S.P.; Loeb, K.R.; Hagen, F.S.; Kurachi, K.; Davie, E.W.
A novel trypsin-like serine protease (hepsin) with a putative transmembrane domain expressed by human liver and hepatoma cells
Biochemistry
27
1067-1074
1988
Homo sapiens
brenda
Zhukov, A.; Hellman, U.; Ingelman-Sundberg, M.
Purification and characterization of hepsin from rat liver microsomes
Biochim. Biophys. Acta
1337
85-95
1997
Rattus norvegicus
brenda
Tsuji, A.; Torres-Rosado, A.; Arai, T.; Chou, S.H.; Kurachi, K.
Characterization of hepsin, a membrane bound protease
Biomed. Biochim. Acta
50
791-793
1991
Homo sapiens, Papio ursinus
brenda
Srikantan, V.; Valladares, M.; Rhim, J.S.; Moul, J.W.; Srivastava, S.
Hepsin inhibits cell growth/invasion in prostate cancer cells
Cancer Res.
62
6812-6816
2002
Homo sapiens
brenda
Tsuji, A.; Torres-Rosado, A.; Arai, T.; Le Beau, M.M.; Lemons, R.S.; Chou, S.H.; Kurachi, K.
Hepsin, a cell membrane-associated protease. Characterization, tissue distribution, and gene localization
J. Biol. Chem.
266
16948-16953
1991
Homo sapiens, Papio ursinus
brenda
Kazama, Y.; Hamamoto, T.; Foster, D.C.; Kisiel, W.
Hepsin, a putative membrane-associated serine protease, activates human factor VII and initiates a pathway of blood coagulation on the cell surface leading to thrombin formation
J. Biol. Chem.
270
66-72
1995
Homo sapiens
brenda
Kurachi, K.; Torres-Rosado, A.; Tsuji, A.
Hepsin
Methods Enzymol.
244
100-114
1994
Cricetulus griseus, Homo sapiens, Papio ursinus
brenda
Torres-Rosado, A.; O'Shea, K.S.; Tsuji, A.; Chou, S.H.; Kurachi, K.
Hepsin, a putative cell-surface serine protease, is required for mammalian cell growth
Proc. Natl. Acad. Sci. USA
90
7181-7185
1993
Homo sapiens
brenda
Somoza, J.R.; Ho, J.D.; Luong, C.; Ghate, M.; Sprengeler, P.A.; Mortara, K.; Shrader, W.D.; Sperandio, D.; Chan, H.; McGrath, M.E.; Katz, B.A.
The structure of the extracellular region of human hepsin reveals a serine protease domain and a novel scavenger receptor cysteine-rich (SRCR) domain
Structure
11
1123-1131
2003
Homo sapiens
brenda
Zhang, J.L.; Zhao, W.G.; Wu, K.L.; Wang, K.; Zhang, X.; Gu, C.F.; Li, Y.; Zhu, Y.; Wu, J.G.
Human hepatitis B virus X protein promotes cell proliferation and inhibits cell apoptosis through interacting with a serine protease hepsin
Arch. Virol.
150
721-741
2005
Homo sapiens (P05981), Homo sapiens
brenda
Herter, S.; Piper, D.E.; Aaron, W.; Gabriele, T.; Cutler, G.; Cao, P.; Bhatt, A.S.; Choe, Y.; Craik, C.S.; Walker, N.; Meininger, D.; Hoey, T.; Austin, R.J.
Hepatocyte growth factor is a preferred in vitro substrate for human hepsin, a membrane-anchored serine protease implicated in prostate and ovarian cancers
Biochem. J.
390
125-136
2005
Homo sapiens
brenda
Li, Y.; Yu, Z.; Zhao, X.; Shen, S.
Identification and characterization of hepsin/-TM, a non-transmembrane hepsin isoform
Biochim. Biophys. Acta
1681
157-165
2005
Homo sapiens
brenda
Klezovitch, O.; Chevillet, J.; Mirosevich, J.; Roberts, R.L.; Matusik, R.J.; Vasioukhin, V.
Hepsin promotes prostate cancer progression and metastasis
Cancer Cell
6
185-195
2004
Mus musculus
brenda
Kirchhofer, D.; Peek, M.; Lipari, M.T.; Billeci, K.; Fan, B.; Moran, P.
Hepsin activates pro-hepatocyte growth factor and is inhibited by hepatocyte growth factor activator inhibitor-1B (HAI-1B) and HAI-2
FEBS Lett.
579
1945-1950
2005
Homo sapiens (P05981)
brenda
Nakamura, K.; Nasu, Y.; Hongo, A.; Matsuo, T.; Kodama, J.; Ebara, S.; Nagai, A.; Abrzua, F.; Kumon, H.; Hiramatsu, Y.
Hepsin shows inhibitory effects through apoptotic pathway on ovarian cancer cell lines
Int. J. Oncol.
28
393-398
2006
Homo sapiens
brenda
Roemer, A.; Schwettmann, L.; Jung, M.; Stephan, C.; Roigas, J.; Kristiansen, G.; Loening, S.A.; Lichtinghagen, R.; Jung, K.
The membrane proteases adams and hepsin are differentially expressed in renal cell carcinoma. Are they potential tumor markers?
J. Urol.
172
2162-2166
2004
Homo sapiens (P05981), Homo sapiens
brenda
Guipponi, M.; Tan, J.; Cannon, P.Z.; Donley, L.; Crewther, P.; Clarke, M.; Wu, Q.; Shepherd, R.K.; Scott, H.S.
Mice deficient for the type II transmembrane serine protease, TMPRSS1/hepsin, exhibit profound hearing loss
Am. J. Pathol.
171
608-616
2007
Mus musculus
brenda
Matsuo, T.; Nakamura, K.; Takamoto, N.; Kodama, J.; Hongo, A.; Abrzua, F.; Nasu, Y.; Kumon, H.; Hiramatsu, Y.
Expression of the serine protease hepsin and clinical outcome of human endometrial cancer
Anticancer Res.
28
159-164
2008
Homo sapiens
brenda
Kunii, D.; Shimoji, M.; Nakama, S.; Ikebe, M.; Hachiman, T.; Sato, I.; Tamaki, A.; Yamazaki, K.; Aniya, Y.
Purification of liver serine protease which activates microsomal glutathione S-transferase: possible involvement of hepsin
Biol. Pharm. Bull.
29
868-874
2006
Rattus norvegicus
brenda
Wu, Q.; Parry, G.
Hepsin and prostate cancer
Front. Biosci.
12
5052-5059
2007
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Pal, P.; Xi, H.; Kaushal, R.; Sun, G.; Jin, C.H.; Jin, L.; Suarez, B.K.; Catalona, W.J.; Deka, R.
Variants in the HEPSIN gene are associated with prostate cancer in men of European origin
Hum. Genet.
120
187-192
2006
Homo sapiens
brenda
Moran, P.; Li, W.; Fan, B.; Vij, R.; Eigenbrot, C.; Kirchhofer, D.
Pro-urokinase-type plasminogen activator is a substrate for hepsin
J. Biol. Chem.
281
30439-30446
2006
Homo sapiens
brenda
Beliveau, F.; Desilets, A.; Leduc, R.
Probing the substrate specificities of matriptase, matriptase-2, hepsin and DESC1 with internally quenched fluorescent peptides
FEBS J.
276
2213-2226
2009
Homo sapiens
brenda
Miao, J.; Mu, D.; Ergel, B.; Singavarapu, R.; Duan, Z.; Powers, S.; Oliva, E.; Orsulic, S.
Hepsin colocalizes with desmosomes and induces progression of ovarian cancer in a mouse model
Int. J. Cancer
123
2041-2047
2008
Homo sapiens (P05981)
brenda
Nakamura, K.; Takamoto, N.; Abarzua, F.; Hongo, A.; Kodama, J.; Nasu, Y.; Kumon, H.; Hiramatsu, Y.
Hepsin inhibits the cell growth of endometrial cancer
Int. J. Mol. Med.
22
389-397
2008
Homo sapiens
brenda
Tripathi, M.; Nandana, S.; Yamashita, H.; Ganesan, R.; Kirchhofer, D.; Quaranta, V.
Laminin-332 is a substrate for hepsin, a protease associated with prostate cancer progression
J. Biol. Chem.
283
30576-30584
2008
Homo sapiens
brenda
Halabian, R.; Roudkenar, M.H.; Esmaeili, N.S.; Masroori, N.; Roushandeh, A.M.; Najafabadi, A.J.
Establishment of a cell line expressing recombinant factor VII and its subsequent conversion to active form FVIIa through hepsin by genetic engineering method
Vox Sang.
96
309-315
2009
Homo sapiens
brenda
Owen, K.A.; Qiu, D.; Alves, J.; Schumacher, A.M.; Kilpatrick, L.M.; Li, J.; Harris, J.L.; Ellis, V.
Pericellular activation of hepatocyte growth factor by the transmembrane serine proteases matriptase and hepsin, but not by the membrane-associated protease uPA
Biochem. J.
426
219-228
2010
Homo sapiens
brenda
Nakama, S.; Oshiro, N.; Aniya, Y.
Activation of rat liver microsomal glutathione transferase by hepsin
Biol. Pharm. Bull.
33
561-567
2010
Rattus norvegicus
brenda
Li, W.; Wang, B.E.; Moran, P.; Lipari, T.; Ganesan, R.; Corpuz, R.; Ludlam, M.J.; Gogineni, A.; Koeppen, H.; Bunting, S.; Gao, W.Q.; Kirchhofer, D.
Pegylated kunitz domain inhibitor suppresses hepsin-mediated invasive tumor growth and metastasis
Cancer Res.
69
8395-8402
2009
Mus musculus
brenda
Chen, M.; Chen, L.M.; Lin, C.Y.; Chai, K.X.
Hepsin activates prostasin and cleaves the extracellular domain of the epidermal growth factor receptor
Mol. Cell. Biochem.
337
259-266
2010
Homo sapiens
brenda
Holt, S.K.; Kwon, E.M.; Lin, D.W.; Ostrander, E.A.; Stanford, J.L.
Association of hepsin gene variants with prostate cancer risk and prognosis
Prostate
70
1012-1019
2010
Homo sapiens
brenda
Nandana, S.; Ellwood-Yen, K.; Sawyers, C.; Wills, M.; Weidow, B.; Case, T.; Vasioukhin, V.; Matusik, R.
Hepsin cooperates with MYC in the progression of adenocarcinoma in a prostate cancer mouse model
Prostate
70
591-600
2010
Mus musculus
brenda
Koschubs, T.; Dengl, S.; Duerr, H.; Kaluza, K.; Georges, G.; Hartl, C.; Jennewein, S.; Lanzendoerfer, M.; Auer, J.; Stern, A.; Huang, K.S.; Packman, K.; Gubler, U.; Kostrewa, D.; Ries, S.; Hansen, S.; Kohnert, U.; Cramer, P.; Mundigl, O.
Allosteric antibody inhibition of human Hepsin protease
Biochem. J.
442
483-494
2012
Homo sapiens (P05981), Homo sapiens
brenda
Raevskaya, A.A.; Kuznetsova, E.M.; Savvateeva, M.V.; Severin, S.E.
Isolation, purification, and study of properties of recombinant hepsin from Escherichia coli
Biochemistry
75
866-872
2010
Homo sapiens
brenda
Ganesan, R.; Kolumam, G.A.; Lin, S.J.; Xie, M.H.; Santell, L.; Wu, T.D.; Lazarus, R.A.; Chaudhuri, A.; Kirchhofer, D.
Proteolytic activation of pro-macrophage-stimulating protein by hepsin
Mol. Cancer Res.
9
1175-1186
2011
Homo sapiens
brenda
Khandekar, G.; Jagadeeswaran, P.
Role of hepsin in factor VII activation in zebrafish
Blood Cells Mol. Dis.
52
76-81
2014
Danio rerio
brenda
Zhang, C.; Zhang, M.; Wu, Q.; Peng, J.; Ruan, Y.; Gu, J.
Hepsin inhibits CDK11p58 IRES activity by suppressing unr expression and eIF-2alpha phosphorylation in prostate cancer
Cell. Signal.
27
789-797
2015
Homo sapiens (P05981)
brenda
Hsu, Y.C.; Huang, H.P.; Yu, I.S.; Su, K.Y.; Lin, S.R.; Lin, W.C.; Wu, H.L.; Shi, G.Y.; Tao, M.H.; Kao, C.H.; Wu, Y.M.; Martin, P.E.; Lin, S.Y.; Yang, P.C.; Lin, S.W.
Serine protease hepsin regulates hepatocyte size and hemodynamic retention of tumor cells by hepatocyte growth factor signaling in mice
Hepatology
56
1913-1923
2012
Mus musculus (O35453), Mus musculus
brenda
Niehaus, J.Z.; Miedel, M.T.; Good, M.; Wyatt, A.N.; Pak, S.C.; Silverman, G.A.; Luke, C.J.
SERPINB12 is a slow-binding inhibitor of granzyme A and hepsin
Biochemistry
54
6756-6759
2015
Homo sapiens (P05981)
brenda
Kim, K.; Kwon, H.; Choi, D.; Lim, T.; Minn, I.; Son, S.H.; Byun, Y.
Design and synthesis of dye-conjugated hepsin inhibitors
Bioorg. Chem.
89
102990
2019
Homo sapiens (P05981)
brenda
Franco, F.M.; Jones, D.E.; Harris, P.K.; Han, Z.; Wildman, S.A.; Jarvis, C.M.; Janetka, J.W.
Structure-based discovery of small molecule hepsin and HGFA protease inhibitors Evaluation of potency and selectivity derived from distinct binding pockets
Bioorg. Med. Chem.
23
2328-2343
2015
Homo sapiens (P05981)
brenda
Goswami, R.; Wohlfahrt, G.; Toermaekangas, O.; Moilanen, A.; Lakshminarasimhan, A.; Nagaraj, J.; Arumugam, K.N.; Mukherjee, S.; Chacko, A.R.; Krishnamurthy, N.R.; Jaleel, M.; Palakurthy, R.K.; Samiulla, D.S.; Ramachandra, M.
Structure-guided discovery of 2-aryl/pyridin-2-yl-1H-indole derivatives as potent and selective hepsin inhibitors
Bioorg. Med. Chem. Lett.
25
5309-5314
2015
Homo sapiens (P05981)
brenda
Kwon, H.; Kim, Y.; Park, K.; Choi, S.A.; Son, S.H.; Byun, Y.
Structure-based design, synthesis, and biological evaluation of Leu-Arg dipeptide analogs as novel hepsin inhibitors
Bioorg. Med. Chem. Lett.
26
310-314
2016
Homo sapiens (P05981)
brenda
Brunati, M.; Perucca, S.; Han, L.; Cattaneo, A.; Consolato, F.; Andolfo, A.; Schaeffer, C.; Olinger, E.; Peng, J.; Santambrogio, S.; Perrier, R.; Li, S.; Bokhove, M.; Bachi, A.; Hummler, E.; Devuyst, O.; Wu, Q.; Jovine, L.; Rampoldi, L.
The serine protease hepsin mediates urinary secretion and polymerisation of Zona Pellucida domain protein uromodulin
eLife
4
e08887
2015
Mus musculus (O35453)
brenda
Subedi, M.; Minn, I.; Chen, J.; Kim, Y.; Ok, K.; Jung, Y.W.; Pomper, M.G.; Byun, Y.
Design, synthesis and biological evaluation of PSMA/hepsin-targeted heterobivalent ligands
Eur. J. Med. Chem.
118
208-218
2016
Homo sapiens (P05981)
brenda
Sroka, W.D.; Adamowski, M.; Slupski, P.; Siodmiak, J.; Jarzemski, P.; Odrowaz-Sypniewska, G.; Marszall, M.P.
Alpha-methylacyl-CoA racemase and hepsin as urinary prostate cancer markers
Int. J. Biol. Markers
30
e401-e406
2015
Homo sapiens (P05981)
brenda
Damalanka, V.C.; Han, Z.; Karmakar, P.; ODonoghue, A.J.; La Greca, F.; Kim, T.; Pant, S.M.; Helander, J.; Klefstroem, J.; Craik, C.S.; Janetka, J.W.
Discovery of selective matriptase and hepsin serine protease inhibitors useful chemical tools for cancer cell biology
J. Med. Chem.
62
480-490
2019
Homo sapiens (P05981)
brenda
Wilkinson, D.J.; Desilets, A.; Lin, H.; Charlton, S.; Del Carmen Arques, M.; Falconer, A.; Bullock, C.; Hsu, Y.C.; Birchall, K.; Hawkins, A.; Thompson, P.; Ferrell, W.R.; Lockhart, J.; Plevin, R.; Zhang, Y.; Blain, E.; Lin, S.W.; Leduc, R.; Milner, J.M.; Rowan, A.D.
The serine proteinase hepsin is an activator of pro-matrix metalloproteinases molecular mechanisms and implications for extracellular matrix turnover
Sci. Rep.
7
16693
2017
Homo sapiens (P05981)
brenda