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7-amido-4-carbamoylmethylcoumarin-KHYRSVAS-K(DNP)R + H2O
?
-
-
-
-
?
7-amido-4-carbamoylmethylcoumarin-KHYRSVAW-K(DNP)R + H2O
?
-
-
-
-
?
acetyl-DHYR-7-amido-4-carbamoylmethylcoumarin + H2O
acetyl-DHYR + 7-amino-4-carbamoylmethylcoumarin
-
suboptimal substrate
-
-
?
acetyl-KDYR-7-amido-4-carbamoylmethylcoumarin + H2O
acetyl-KDYR + 7-amino-4-carbamoylmethylcoumarin
-
suboptimal substrate
-
-
?
acetyl-KHDR-7-amido-4-carbamoylmethylcoumarin + H2O
acetyl-KHDR + 7-amino-4-carbamoylmethylcoumarin
-
suboptimal substrate
-
-
?
acetyl-KHYR-7-amido-4-carbamoylmethylcoumarin + H2O
acetyl-KHYR + 7-amino-4-carbamoylmethylcoumarin
acetyl-KHYR-7-amido-4-methylcoumarin + H2O
acetyl-KHYR + 7-amino-4-methylcoumarin
acetyl-PRLR-7-amido-4-carbamoylmethylcoumarin + H2O
acetyl-PRLR + 7-amino-4-carbamoylmethylcoumarin
benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-trifluoromethylcoumarin
benzyloxycarbonyl-Gly-Pro-Arg + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
D-Phe-Phe-Arg 4-methylcoumarin 7-amide
?
-
-
-
?
D-Phe-Phe-Arg-7-amido-4-methylcoumarin + H2O
D-Phe-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
D-Pro-Phe-Arg 4-methylcoumarin 7-amide
?
-
-
-
?
D-Pro-Phe-Arg 4-methylcoumarin 7-amide + H2O
?
-
fluorogenic substrate
-
?
D-Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
D-Pro-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
D-Val-Leu-Arg 4-methylcoumarin 7-amide
?
-
-
-
?
D-Val-Leu-Arg-7-amido-4-methylcoumarin + H2O
D-Val-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
dumpy + H2O
?
i.e. a zona pellucida-domain protein
-
-
?
epithelial sodium channel gamma subunit + H2O
?
-
the enzyme activates epithelial sodium channels by inducing cleavage of the gamma-subunit at a site distal to the furin cleavage site
-
-
?
human Toll-like receptor 4 + H2O
truncated Toll-like receptor 4 + ectodomain
reduction in the full-length form and reduction of the activation of the substrate. Substrate mutations K560A/K561A, K595A and R598A in the ectodomain abolish or reduce the enzyme activity, respectively
-
-
?
N-t-Boc-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
proform epithelial sodium channel + H2O
mature epithelial sodium channel + ?
-
-
-
?
proform filaggrin + H2O
mature filaggrin + ?
-
-
-
?
proform G protein-coupled protease activated receptor-2 + H2O
mature G protein-coupled protease activated receptor-2 + ?
-
-
-
?
Toll-like receptor 4 + H2O
truncated Toll-like receptor 4 + ectodomain
tosyl-Gly-L-Pro-L-Arg-4-nitroanilide + H2O
?
-
-
-
-
?
Z-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
Z-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
additional information
?
-
acetyl-KHYR-7-amido-4-carbamoylmethylcoumarin + H2O
acetyl-KHYR + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
acetyl-KHYR-7-amido-4-carbamoylmethylcoumarin + H2O
acetyl-KHYR + 7-amino-4-carbamoylmethylcoumarin
-
optimal substrate
-
-
?
acetyl-KHYR-7-amido-4-methylcoumarin + H2O
acetyl-KHYR + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-KHYR-7-amido-4-methylcoumarin + H2O
acetyl-KHYR + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-PRLR-7-amido-4-carbamoylmethylcoumarin + H2O
acetyl-PRLR + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
acetyl-PRLR-7-amido-4-carbamoylmethylcoumarin + H2O
acetyl-PRLR + 7-amino-4-carbamoylmethylcoumarin
-
suboptimal substrate
-
-
?
Protein + H2O
?
-
-
-
?
Toll-like receptor 4 + H2O
truncated Toll-like receptor 4 + ectodomain
reduction in the full-length form and reduction of the activation of the substrate
-
-
?
Toll-like receptor 4 + H2O
truncated Toll-like receptor 4 + ectodomain
reduction in the full-length form and reduction of the activation of the substrate
-
-
?
additional information
?
-
-
7-amido-4-carbamoylmethylcoumarin-KHYRIVAS-K(DNP)R completely inactive
-
-
?
additional information
?
-
critical role in the regulation of extracellular sodium ion transport via its activation of the epithelial cell sodium channel
-
-
?
additional information
?
-
-
critical role in the regulation of extracellular sodium ion transport via its activation of the epithelial cell sodium channel
-
-
?
additional information
?
-
-
active prostasin does not cleave the epidermal growth factor receptor extracellular domain directly, purified active prostasin also does not cleave purified epidermal growth factor receptor
-
-
?
additional information
?
-
activated prostasin appears to target several downstream effector proteins, including the epithelial sodium channel and the G protein-coupled protease activated receptor-2, which are both matriptase substrates
-
-
?
additional information
?
-
Lys or Arg residues are amino acids targeted by the enzyme
-
-
?
additional information
?
-
the matriptase zymogen is no substrate of prostasin
-
-
?
additional information
?
-
Lys or Arg residues are amino acids targeted by the enzyme
-
-
?
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(3R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-3-phenyl-L-prolinamide
-
(3S)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-3-methyl-L-prolinamide
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-(cyclohexylmethoxy)-L-prolinamide
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-(cyclopentylmethoxy)-L-prolinamide
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-([[4-(methylsulfonyl)benzyl]carbamoyl]oxy)-L-prolinamide
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-hydroxy-L-prolinamide
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(4-chlorobenzyl)oxy]-L-prolinamide
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(4-fluorobenzyl)oxy]-L-prolinamide
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(4-methylbenzyl)oxy]-L-prolinamide
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(dimethylcarbamoyl)oxy]-L-prolinamide
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(morpholin-4-ylcarbonyl)oxy]-L-prolinamide
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(phenylcarbamoyl)oxy]-L-prolinamide
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(piperidin-1-ylcarbonyl)oxy]-L-prolinamide
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[(pyrrolidin-1-ylcarbonyl)oxy]-L-prolinamide
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[[3-(trifluoromethyl)benzyl]oxy]-L-prolinamide
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-4-[[4-(trifluoromethyl)benzyl]oxy]-L-prolinamide
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-4-(benzyloxy)-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-L-prolinamide
-
(4R)-N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-4-[(benzylcarbamoyl)oxy]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-L-prolinamide
-
bacterial lipopolysaccharide
-
benzyl [(1S)-2-[[(1S)-1-[[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]carbamoyl]-3-phenylpropyl]amino]-1-(1H-imidazol-4-ylmethyl)-2-oxoethyl]carbamate
-
benzyl [(1S)-5-amino-1-[[(1S)-1-[[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]carbamoyl]-3-phenylpropyl]carbamoyl]pentyl]carbamate
-
Brij 35
-
activity decreases with increasing detergent concentration
camostat mesilate
-
potent inhibitor; potent prostasin inhibitor, 0.1 mM almost completely inhibits prostasin activity in vitro by 98.3%
EDTA
-
reduces enzyme activity by 30%
HAI-1
inhibitor of prostasin in skin
hepatocyte growth factor activator inhibitor-1
-
hepatocyte growth factor activator inhibitor-1A
-
-
-
hepatocyte growth factor activator inhibitor-1B
-
-
-
N-[(1S)-1-[[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]carbamoyl]-3-methylbutyl]-N2-[(benzyloxy)carbonyl]-L-lysinamide
-
N-[(1S)-1-[[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]carbamoyl]-3-methylbutyl]-Nalpha-[(benzyloxy)carbonyl]-L-histidinamide
-
N-[(1S)-5-amino-1-(1,3-benzoxazol-2-ylcarbonyl)pentyl]-1-[(2R)-2-[[(benzyloxy)carbonyl]amino]-4-phenylbutanoyl]-L-prolinamide
-
prostasin-binding protein
-
saline
-
reduces prostasin in nomotensive subjects
-
Soybean trypsin inhibitor
-
-
-
spironolactone
-
decreases urinary prostasin in nomotensives in whom the renin/aldosterone axis is activated by a low Na+ intake, ineffective in individuals with high Na+ intake
TGF-beta1
-
suppresses prostasin promoter activity in a time- and concentration-dependent manner, inhibition of prostasin expression by the induction of IkappaBalpha and the subsequent inhibition of NF-kappaB/Rel activity, may inhibit sodium reabsorption through a reduction in prostasin expression and subsequent inhibition of ENaC activity
-
Tween 20
-
activity decreases with increasing detergent concentration
ZnCl2
-
with acetyl-KHYR-7-amino-3-carbamoylmethyl-4-methylcoumarin
additional information
-
not inhibited by alpha1-antitrypsin, alpha1-antitrypsinPDX, alpha1-antichymotrypsin, and soybean trypsin inhibitor
-
antipain
-
50% inhibition at 0.0064 mM
Aprotinin
-
50% inhibition at 0.0000018 mM
Aprotinin
-
reversible binding to prostasin
Aprotinin
-
completely inhibits
Aprotinin
-
0.02 mg/ml, 41% inhibition within 60 min
bacterial lipopolysaccharide
viral promoter-driven expression of the human prostasin in the bladder of transgenic mice attenuates the bacterial lipopolysaccharide induction of nitric oxide synthase, whereas induction of cyclooxygenase-2, TNF-alpha, IL-1beta and IL-6 expression is not reduced
-
bacterial lipopolysaccharide
-
downregulation of mPro mRNA expression in the bladder, upregulation of inducible nitric oxide synthase, cyclooxygenase-2, interferon-gamma, TNF-alpha, IL-1beta, and IL-6
-
benzamidine
-
50% inhibition at 0.86 mM
benzamidine
-
completely inhibits
hepatocyte growth factor activator inhibitor-1
-
-
-
hepatocyte growth factor activator inhibitor-1
HAI-1
-
leupeptin
-
50% inhibition at 0.1 mM
prostasin-binding protein
-
of mouse seminal vesicle fluid, binds covalently to prostasin, complete inhibition
-
prostasin-binding protein
-
-
-
prostasin-binding protein
-
-
-
Protease nexin-1
inhibits prostasin´s serine protease activity, capable of binding to membrane-anchored prostasin
-
Protease nexin-1
-
forms an inactive complex with prostasin
-
Protease nexin-1
-
also known as glia-derived nexin or serpin E2
-
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additional information
spatial and temporal co-expression of matriptase and prostasin
malfunction
-
loss of prostasin expression in the transitional cell carcinoma cell lines is correlated with loss of or reduced E-cadherin expression, loss of epithelial morphology, and promoter DNA hypermethylation and may have functional implications in tumor invasion and resistance to chemotherapy
malfunction
-
prostasin silencing in BPH-1 cells is associated with up-regulation of iNOS, ICAM-1, interleukin-6, and interleukin-8, and down-regulation of cyclin D1, as well as reduced proliferation and invasion
malfunction
liver-specific PRSS8 enzyme knockout mice develop insulin resistance associated with the increase in hepatic Toll-like receptor 4, the knockout mice show an excessive response to lipopolysacchrides. Restoration of enzyme expression in livers of high-fat diet, knockout, and db/db mice decreases the TLR4 level and ameliorates insulin resistance, phenotypes, overview
malfunction
matriptase and prostasin null mice have identical phenotypes. mice deficient for matriptase phenocopy mice deficient for epidermal prostasin and show impaired corneocyte differentiation, imparied lipid matrix formation, loss of profilaggrin processing and loss of tight junction formation and function. Together, these defects lead to a compromised epidermal barrier and result in fatal dehydration during the neonatal period. The proteolytic processing of prostasin as well as profilaggrin is greatly reduced in matriptase hypomorphic mice
malfunction
prostasin null mice lack barrier formation and display fatal postnatal dehydration. But mice homozygous for a point mutation in the Prss8 gene, which causes the substitution of the active site serine within the catalytic histidine-aspartate-serine triad with alanine and renders prostasin catalytically inactive, develop barrier function and are healthy when followed for up to 20 weeks. Phenotypes, overview
malfunction
-
prostasin null mice lack barrier formation and display fatal postnatal dehydration. But mice homozygous for a point mutation in the Prss8 gene, which causes the substitution of the active site serine within the catalytic histidine-aspartate-serine triad with alanine and renders prostasin catalytically inactive, develop barrier function and are healthy when followed for up to 20 weeks. Phenotypes, overview
-
metabolism
high-fat diet triggers the suppression of the enzyme expression by inducing endoplasmic reticulum stress and increases the Toll-like receptor 4 level in the liver. Serum enzyme levels are correlated to body mass index and homoeostasis model assessment-insulin resistance
metabolism
high-fat diet triggers the suppression of the enzyme expression by inducing endoplasmic reticulum stress and increases the Toll-like receptor 4 level in the liver. Serum enzyme levels are correlated to body mass index and homoeostasis model assessment-insulin resistance
metabolism
matriptase and not prostasin is the primary effector protease of tight junction assembly in simple columnar epithelia
physiological function
-
prostasin inhibits cell invasion in human choriocarcinomal JEG-3 cells. Prostasin participates in the proteolytic activation of epithelial sodium channel as well as cleavage of epidermal growth factor receptor extracellular domain in human epithelial cells. Prostasin functions as an invasion suppressor in human trophoblast, participating in the invasion-restrictive regulation of trophoblasts to avoid their over-penetration into the uterine wall
physiological function
-
prostasin is essential for terminal epithelial differentiation, prostasin is involved in the extracellular proteolytic modulation of the epidermal growth factor receptor and is an invasion suppressor
physiological function
-
prostasin regulates human placental trophoblast cell proliferation via modulating the epidermal growth factor receptor-mitogen-activated protein kinase signaling pathway
physiological function
-
prostasin regulates iNOS and cyclin D1 expression by modulating protease-activated receptor-2 signaling in prostate epithelial cells. Prostasin plays a negative regulatory role on protease-activated receptor-2-mediated signaling in prostate epithelial cell
physiological function
-
prostasin significantly increases both CYP11B2 mRNA expression and aldosterone production in a dose-dependent manner
physiological function
-
prostasin significantly increases both CYP11B2 mRNA expression and aldosterone production in a dose-dependent manner. Prostasin has a stimulatory effect on the aldosterone synthesis by adrenal gland through the nonproteolytic action
physiological function
Prostasin catalyzed activation of ENaC induces an open channel conformation associated with sodium influx that results in membrane depolarization. Prostasin together with matriptase comprise a single common proteolytic pathway,that is required for barrier formation. Prostasin is activated through proteolytic cleavage by matriptase, but prostasin is also required for matriptase activation in intestinal epithelial cells to regulate closure of the paracellular pathway
physiological function
prostasin interacts with the epithelial Na+ channel, the catalytically inactive prostasin facilitates the cleavage of the gamma-subunit by an endogenous protease in Xenopus oocytes, cleavage of the gamma-subunit by furin at the consensus site gammaRKRR143 and subsequent cleavage by a second protease at a distal site strongly activate the channel
physiological function
prostasin is also a regulator of the epidermal sodium channel like matriptase
physiological function
prostasin supports epidermal development and postnatal homeostasis independent of its enzymatic activity
physiological function
the enzyme has the ability to activate epithelial sodium channels and effect the sodium current across the plasma membrane in vitro. In the epidermis, the glycosylphosphatidylinositol anchored membrane serine protease prostasin is activated by matriptase to initiate a proteolytic cascade that is required for the development of the stratum corneum barrier function. Proteolytic activity of the matriptase-prostasin cascade is regulated in the epidermis via inhibition by the Kunitz-type serine protease inhibitor hepatocyte growth factor activator inhibitor-1
physiological function
the serine protease prostasin regulates hepatic insulin sensitivity by modulating Toll-like receptor 4-mediated signalling, the enzyme decreases TLR4 levels by the proteolytic shedding
physiological function
the serine protease prostasin regulates hepatic insulin sensitivity by modulating Toll-like receptor 4-mediated signalling, the enzyme decreases TLR4 levels by the proteolytic shedding
physiological function
HAI-1 but not HAI-2 is the prominent inhibitor for prostasin and matriptase in skin. The limited role for HAI-2 in the inhibition of matriptase and prostasin is the result of its primarily intracellular localization in basal and spinous layer keratinocytes, which probably prevents the HAI-2 from interacting with active prostasin or matriptase
physiological function
knock-in mice expressing catalytically inactive prostasin display normal prenatal and postnatal survival. Catalytically inactive prostasin causes embryonic lethality in mice lacking its cognate inhibitors HAI-1 (SPINT1) or HAI-2 (SPINT2). Proteolytically inactive prostasin, unlike the wild-type protease, is unable to activate matriptase during placentation. All essential functions of prostasin in embryonic and postnatal development are compensated for by loss of HAI-1
physiological function
prostasin is found in the epidermis as one-chain zymogen and as two-chain proteolytically active form. Mice expressing only activation site cleavage-resistant (zymogen-locked) endogenous prostasin display normal interfollicular epidermal development and postnatal survival, but have defects in whisker and pelage hair formation
physiological function
tracheal-prostasin is a functional homologue of prostasin. Tracheal-prostasin degrades the zona pellucida-domain protein Dumpy, a component of the transient tracheal apical extracellular matrix. The tracheal-prostasin zymogen in vitro is activated by notopleural. RNAi-mediated knockdown embryos lack tracheal liquid clearance and die during the first instar larval stage
physiological function
-
prostasin supports epidermal development and postnatal homeostasis independent of its enzymatic activity
-
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Liu, L.; Hering-Smith, K.S.; Schiro, F.R.; Hamm, L.L.
Serine protease activity in M-1 cortical collecting duct cells
Hypertension
39
860-864
2002
Mus musculus
brenda
Yu, J.X.; Chao, L.; Chao, J.
Prostasin is a novel human serine proteinase from seminal fluid. Purification, tissue distribution, and localization in prostate gland
J. Biol. Chem.
269
18843-18848
1994
Homo sapiens
brenda
Chen, L.M.; Skinner, M.L.; Kauffman, S.W.; Chao, J.; Chao, L.; Thaler, C.D.; Chai, K.X.
Prostasin is a glycosylphosphatidylinositol-anchored active serine protease
J. Biol. Chem.
276
21434-21442
2001
Homo sapiens
brenda
Tong, Z.; Illek, B.; Bhagwandin, V.J.; Verghese, G.M.; Caughey, G.H.
Prostasin, a membrane-anchored serine peptidase, regulates sodium currents in JME/CF15 cells, a cystic fibrosis airway epithelial cell line
Am. J. Physiol. Lung Cell Mol. Physiol.
287
L928-L935
2004
Homo sapiens
brenda
Chen, L.M.; Wang, C.; Chen, M.; Marcello, M.R.; Chao, J.; Chao, L.; Chai, K.X.
Prostasin attenuates inducible nitric oxide synthase expression in lipopolysaccharide-induced urinary bladder inflammation
Am. J. Physiol. Renal Physiol.
291
F567-F577
2006
Mus musculus, Homo sapiens (Q16651), Homo sapiens
brenda
Shipway, A.; Danahay, H.; Williams, J.A.; Tully, D.C.; Backes, B.J.; Harris, J.L.
Biochemical characterization of prostasin, a channel activating protease
Biochem. Biophys. Res. Commun.
324
953-963
2004
Homo sapiens
brenda
Chao, J.
Prostasin
Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , Eds. ) Academic Press
2
1708-1709
2004
Homo sapiens, Mus musculus, Rattus norvegicus, Xenopus laevis
-
brenda
Olivieri, O.; Castagna, A.; Guarini, P.; Chiecchi, L.; Sabaini, G.; Pizzolo, F.; Corrocher, R.; Righetti, P.G.
Urinary prostasin: a candidate marker of epithelial sodium channel activation in humans
Hypertension
46
683-688
2005
Homo sapiens
brenda
Tuyen, d.o.G.; Kitamura, K.; Adachi, M.; Miyoshi, T.; Wakida, N.; Nagano, J.; Nonoguchi, H.; Tomita, K.
Inhibition of prostasin expression by TGF-beta1 in renal epithelial cells
Kidney Int.
67
193-200
2005
Rattus norvegicus
brenda
Chen, L.M.; Zhang, X.; Chai, K.X.
Regulation of prostasin expression and function in the prostate
Prostate
59
1-12
2004
Homo sapiens (Q16651)
brenda
Verghese, G.M.; Gutknecht, M.F.; Caughey, G.H.
Prostasin regulates epithelial monolayer function: cell-specific Gpld1-mediated secretion and functional role for GPI anchor
Am. J. Physiol.
291
C1258-C1270
2006
Mus musculus (Q99L44), Mus musculus
brenda
Myerburg, M.M.; McKenna, E.E.; Luke, C.J.; Frizzell, R.A.; Kleyman, T.R.; Pilewski, J.M.
Prostasin expression is regulated by airway surface liquid volume and is increased in cystic fibrosis
Am. J. Physiol. Lung Cell Mol. Physiol.
294
L932-L941
2008
Homo sapiens
brenda
Chen, M.; Chen, L.M.; Chai, K.X.
Mechanisms of sterol regulatory element-binding protein-2 (SREBP-2) regulation of human prostasin gene expression
Biochem. Biophys. Res. Commun.
346
1245-1253
2006
Homo sapiens
brenda
Chen, M.; Fu, Y.; Lin, C.; Chen, L.; Chai, K.X.
Prostasin induces protease-dependent and independent molecular changes in the human prostate carcinoma cell line PC-3
Biochim. Biophys. Acta
1773
1133-1140
2007
Homo sapiens
brenda
Netzel-Arnett, S.; Currie, B.M.; Szabo, R.; Lin, C.Y.; Chen, L.M.; Chai, K.X.; Antalis, T.M.; Bugge, T.H.; List, K.
Evidence for a matriptase-prostasin proteolytic cascade regulating terminal epidermal differentiation
J. Biol. Chem.
281
32941-32945
2006
Mus musculus
brenda
Bruns, J.B.; Carattino, M.D.; Sheng, S.; Maarouf, A.B.; Weisz, O.A.; Pilewski, J.M.; Hughey, R.P.; Kleyman, T.R.
Epithelial Na+ channels are fully activated by furin- and prostasin-dependent release of an inhibitory peptide from the gamma-subunit
J. Biol. Chem.
282
6153-6160
2007
Mus musculus
brenda
List, K.; Hobson, J.P.; Molinolo, A.; Bugge, T.H.
Co-localization of the channel activating protease prostasin/(CAP1/PRSS8) with its candidate activator, matriptase
J. Cell. Physiol.
213
237-245
2007
Mus musculus
brenda
Lin, H.Y.; Zhang, H.; Yang, Q.; Wang, H.X.; Wang, H.M.; Chai, K.X.; Chen, L.M.; Zhu, C.
Expression of prostasin and protease nexin-1 in rhesus monkey (Macaca mulatta) endometrium and placenta during early pregnancy
J. Histochem. Cytochem.
54
1139-1147
2006
Macaca mulatta
brenda
Zhang, H.; Lin, H.Y.; Yang, Q.; Wang, H.X.; Chai, K.X.; Chen, L.M.; Zhu, C.
Expression of prostasin serine protease and protease nexin-1 (PN-1) in rhesus monkey ovary during menstrual cycle and early pregnancy
J. Histochem. Cytochem.
55
1237-1244
2007
Macaca mulatta
brenda
Chen, M.; Chen, L.; Chai, K.X.
Androgen regulation of prostasin gene expression is mediated by sterol-regulatory element-binding proteins and SLUG
Prostate
66
911-920
2006
Homo sapiens (Q16651), Homo sapiens
brenda
Zhu, H.; Guo, D.; Li, K.; Yan, W.; Tan, Y.; Wang, X.; Treiber, F.A.; Chao, J.; Snieder, H.; Dong, Y.
Prostasin: a possible candidate gene for human hypertension
Am. J. Hypertens.
21
1028-1033
2008
Homo sapiens (Q16651), Homo sapiens
brenda
Tully, D.C.; Vidal, A.; Chatterjee, A.K.; Williams, J.A.; Roberts, M.J.; Petrassi, H.M.; Spraggon, G.; Bursulaya, B.; Pacoma, R.; Shipway, A.; Schumacher, A.M.; Danahay, H.; Harris, J.L.
Discovery of inhibitors of the channel-activating protease prostasin (CAP1/PRSS8) utilizing structure-based design
Bioorg. Med. Chem. Lett.
18
5895-5899
2008
Homo sapiens (Q16651)
brenda
Rickert, K.W.; Kelley, P.; Byrne, N.J.; Diehl, R.E.; Hall, D.L.; Montalvo, A.M.; Reid, J.C.; Shipman, J.M.; Thomas, B.W.; Munshi, S.K.; Darke, P.L.; Su, H.P.
Structure of human prostasin, a target for the regulation of hypertension
J. Biol. Chem.
283
34864-34872
2008
Homo sapiens (Q16651), Homo sapiens
brenda
Spraggon, G.; Hornsby, M.; Shipway, A.; Tully, D.C.; Bursulaya, B.; Danahay, H.; Harris, J.L.; Lesley, S.A.
Active site conformational changes of prostasin provide a new mechanism of protease regulation by divalent cations
Protein Sci.
18
1081-1094
2009
Homo sapiens (Q16651), Homo sapiens
brenda
Selzer-Plon, J.; Bornholdt, J.; Friis, S.; Bisgaard, H.C.; Lothe, I.M.; Tveit, K.M.; Kure, E.H.; Vogel, U.; Vogel, L.K.
Expression of prostasin and its inhibitors during colorectal cancer carcinogenesis
BMC Cancer
9
201
2009
Homo sapiens
brenda
Chen, L.; Verity, N.; Chai, K.
Loss of prostasin (PRSS8) in human bladder transitional cell carcinoma cell lines is associated with epithelial-mesenchymal transition (EMT)
BMC Cancer
9
377
2009
Homo sapiens
brenda
Costa, F.P.; Batista, E.L.; Zelmanowicz, A.; Svedman, C.; Devenz, G.; Alves, S.; Silva, A.S.; Garicochea, B.
Prostasin, a potential tumor marker in ovarian cancer--a pilot study
Clinics (Sao Paulo)
64
641-644
2009
Homo sapiens
brenda
Ma, X.J.; Fu, Y.Y.; Li, Y.X.; Chen, L.M.; Chai, K.; Wang, Y.L.
Prostasin inhibits cell invasion in human choriocarcinomal JEG-3 cells
Histochem. Cell Biol.
132
639-646
2009
Homo sapiens
brenda
Fu, Y.Y.; Gao, W.L.; Chen, M.; Chai, K.X.; Wang, Y.L.; Chen, L.M.
Prostasin regulates human placental trophoblast cell proliferation via the epidermal growth factor receptor signaling pathway
Hum. Reprod.
25
623-632
2010
Homo sapiens
brenda
Chen, Y.W.; Wang, J.K.; Chou, F.P.; Chen, C.Y.; Rorke, E.A.; Chen, L.M.; Chai, K.X.; Eckert, R.L.; Johnson, M.D.; Lin, C.Y.
Regulation of the matriptase-prostasin cell surface proteolytic cascade by hepatocyte growth factor activator inhibitor-1 (HAI-1) during epidermal differentiation
J. Biol. Chem.
285
31755-31762
2010
Homo sapiens
brenda
Ko, T.; Kakizoe, Y.; Wakida, N.; Hayata, M.; Uchimura, K.; Shiraishi, N.; Miyoshi, T.; Adachi, M.; Aritomi, S.; Konda, T.; Tomita, K.; Kitamura, K.
Regulation of adrenal aldosterone production by serine protease prostasin
J. Biomed. Biotechnol.
2010
793843
2010
Homo sapiens
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
Chen, L.M.; Hatfield, M.L.; Fu, Y.Y.; Chai, K.X.
Prostasin regulates iNOS and cyclin D1 expression by modulating protease-activated receptor-2 signaling in prostate epithelial cells
Prostate
69
1790-1801
2009
Homo sapiens
brenda
Bergum, C.; Zoratti, G.; Boerner, J.; List, K.
Strong expression association between matriptase and its substrate prostasin in breast cancer
J. Cell. Physiol.
227
1604-1609
2012
Homo sapiens (Q16651)
brenda
Carattino, M.D.; Mueller, G.M.; Palmer, L.G.; Frindt, G.; Rued, A.C.; Hughey, R.P.; Kleyman, T.R.
Prostasin interacts with the epithelial Na+ channel and facilitates cleavage of the gamma-subunit by a second protease
Am. J. Physiol. Renal Physiol.
307
F1080-F1087
2014
Xenopus laevis (Q9ES87)
brenda
Miller, G.S.; List, K.
The matriptase-prostasin proteolytic cascade in epithelial development and pathology
Cell Tissue Res.
351
245-253
2013
Mus musculus (Q9ESD1)
brenda
Buzza, M.S.; Martin, E.W.; Driesbaugh, K.H.; Desilets, A.; Leduc, R.; Antalis, T.M.
Prostasin is required for matriptase activation in intestinal epithelial cells to regulate closure of the paracellular pathway
J. Biol. Chem.
288
10328-10337
2013
Homo sapiens (Q16651)
brenda
Peters, D.E.; Szabo, R.; Friis, S.; Shylo, N.A.; Uzzun Sales, K.; Holmbeck, K.; Bugge, T.H.
The membrane-anchored serine protease prostasin (CAP1/PRSS8) supports epidermal development and postnatal homeostasis independent of its enzymatic activity
J. Biol. Chem.
289
14740-14749
2014
Mus musculus (Q99L44), Mus musculus C57BL/6N (Q99L44)
brenda
Uchimura, K.; Hayata, M.; Mizumoto, T.; Miyasato, Y.; Kakizoe, Y.; Morinaga, J.; Onoue, T.; Yamazoe, R.; Ueda, M.; Adachi, M.; Miyoshi, T.; Shiraishi, N.; Ogawa, W.; Fukuda, K.; Kondo, T.; Matsumura, T.; Araki, E.; Tomita, K.; Kitamura, K.
The serine protease prostasin regulates hepatic insulin sensitivity by modulating TLR4 signalling
Nat. Commun.
5
3428
2014
Homo sapiens (Q16651), Mus musculus (Q9ESD1)
brenda
Chai, A.C.; Robinson, A.L.; Chai, K.X.; Chen, L.M.
Ibuprofen regulates the expression and function of membrane-associated serine proteases prostasin and matriptase
BMC Cancer
15
1025
2015
Homo sapiens (Q16651), Homo sapiens
brenda
Szabo, R.; Lantsman, T.; Peters, D.E.; Bugge, T.H.
Delineation of proteolytic and non-proteolytic functions of the membrane-anchored serine protease prostasin
Development
143
2818-2828
2016
Mus musculus (Q9ESD1), Mus musculus
brenda
Friis, S.; Madsen, D.H.; Bugge, T.H.
Distinct developmental functions of prostasin (CAP1/PRSS8) zymogen and activated prostasin
J. Biol. Chem.
291
2577-2582
2016
Mus musculus (Q9ESD1)
brenda
Buzza, M.S.; Johnson, T.A.; Conway, G.D.; Martin, E.W.; Mukhopadhyay, S.; Shea-Donohue, T.; Antalis, T.M.
Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis
J. Biol. Chem.
292
10801-10812
2017
Homo sapiens (Q16651), Homo sapiens, Mus musculus (Q9ESD1)
brenda
Frederiksen-Moeller, B.; Joergensen, J.S.; Hansen, M.R.; Krigslund, O.; Vogel, L.K.; Andersen, L.B.; Jensen, B.L.
Prostasin and matriptase (ST14) in placenta from preeclamptic and healthy pregnant women
J. Hypertens.
34
298-306
2016
Homo sapiens (Q16651), Homo sapiens
brenda
Lin, C.K.; Tseng, C.K.; Wu, Y.H.; Lin, C.Y.; Huang, C.H.; Wang, W.H.; Liaw, C.C.; Chen, Y.H.; Lee, J.C.
Prostasin impairs epithelial growth factor receptor activation to suppress Dengue virus propagation
J. Infect. Dis.
219
1377-1388
2019
Homo sapiens (Q16651), Homo sapiens, Mus musculus (Q9ESD1)
brenda
Tamir, A.; Gangadharan, A.; Balwani, S.; Tanaka, T.; Patel, U.; Hassan, A.; Benke, S.; Agas, A.; DAgostino, J.; Shin, D.; Yoon, S.; Goy, A.; Pecora, A.; Suh, K.
The serine protease prostasin (PRSS8) is a potential biomarker for early detection of ovarian cancer
J. Ovarian Res.
9
20
2016
Homo sapiens (Q16651), Homo sapiens
brenda
Drees, L.; Koenigsmann, T.; Jaspers, M.H.J.; Pflanz, R.; Riedel, D.; Schuh, R.
Conserved function of the matriptase-prostasin proteolytic cascade during epithelial morphogenesis
PLoS Genet.
15
e1007882
2019
Drosophila melanogaster (Q9W2C8)
brenda
Lee, S.P.; Kao, C.Y.; Chang, S.C.; Chiu, Y.L.; Chen, Y.J.; Chen, M.G.; Chang, C.C.; Lin, Y.W.; Chiang, C.P.; Wang, J.K.; Lin, C.Y.; Johnson, M.D.
Tissue distribution and subcellular localizations determine in vivo functional relationship among prostasin, matriptase, HAI-1, and HAI-2 in human skin
PLoS ONE
13
e0192632
2018
Homo sapiens (Q16651), Homo sapiens
brenda