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Information on EC 3.4.21.109 - matriptase and Organism(s) Homo sapiens and UniProt Accession Q8IU80
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3.4.21.109 matriptaseSpecify your search results
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- 3.4.21.109
- hepatocyte
- hepcidin
- hai-1
- anemia
- metastasis
- prostate
- hepsin
- zymogen
- transferrin
- prostasin
- overload
-
trypsin-like
-
irida
- plasminogen
- hemojuvelin
-
iron-refractory
-
kunitz-type
- inhibitor-1
-
kunitz
-
ttsps
- hemochromatosis
-
erythropoiesis
-
microcytic
-
membrane-anchored
-
urokinase-type
-
ferroportin
-
iron-deficiency
- pro-hgf
-
pericellular
- upa
-
autoactivation
-
two-chain
-
hypochromic
- medicine
-
protease-activated
-
tmprss4
-
spint2
-
corpuscular
-
erythroferrone
- profilaggrin
- camostat
- corin
-
epithelial-derived
- par-2
- hypotrichosis
- drug development
- diagnostics
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
cleaves various synthetic substrates with Arg or Lys at the P1 position and prefers small side-chain amino acids, such as Ala and Gly, at the P2 position
Synonyms
matriptase, tmprss6, matriptase-2, type ii transmembrane serine protease, mt-sp1, epithin, matriptase-1, tadg-15, st-14, snc19, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
epithin
matriptase
matriptase-1
membrane-type serine protease 1
MT-SP1
ST14
TADG-15
TADG15
type II transmembrane protease
additional information
matriptase
-
-
MT-SP1
-
-
additional information
-
matriptase is a member of the type II transmembrane serine protease family
additional information
-
matriptase is a member of the type II transmembrane serine protease family
additional information
-
matriptase-2 is a member of the type II transmembrane serine protease, TTSP, family
additional information
-
the enzyme belongs ot the type II transmembrane serine protease family
additional information
-
the enzyme belongs to the family of type II transmembrane serine proteases
additional information
-
the enzyme is a member of the type II transmembrane serine protease family
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cleaves various synthetic substrates with Arg or Lys at the P1 position and prefers small side-chain amino acids, such as Ala and Gly, at the P2 position
the basic group of the P1 arginine side chain makes a salt bridge with Asp 756 at the bottom of the S1 pocket, substrate docking study,overview
cleaves various synthetic substrates with Arg or Lys at the P1 position and prefers small side-chain amino acids, such as Ala and Gly, at the P2 position
cleaves various synthetic substrates with Arg or Lys at the P1 position and prefers small side-chain amino acids, such as Ala and Gly, at the P2 position
Asp771, His656, and Ser805 are the residues of the catalytic triad
-
cleaves various synthetic substrates with Arg or Lys at the P1 position and prefers small side-chain amino acids, such as Ala and Gly, at the P2 position
structure-function relationship, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
cleavage of C-N-linkage
hydrolysis of peptide bond
-
-
CAS REGISTRY NUMBER
COMMENTARY
241475-96-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ABZ-Ile-Arg-Ala-Arg-Ser-Ala-Ala-Tyr(3-NO2)-NH2 + H2O
ABZ-Ile-Arg-Ala-Arg + Ser-Ala-Ala-Tyr(3-NO2)-NH2
-
-
-
?
ABZ-Ile-Arg-Ala-Arg-Ser-Ala-Gly-Tyr(3-NO2)-NH2 + H2O
ABZ-Ile-Arg-Ala-Arg + Ser-Ala-Gly-Tyr(3-NO2)-NH2
-
-
-
?
ABZ-Ile-Arg-Ala-Arg-Ser-Ala-Ser-Tyr(3-NO2)-NH2 + H2O
ABZ-Ile-Arg-Ala-Arg + Ser-Ala-Ser-Tyr(3-NO2)-NH2
-
-
-
?
Boc-Gln-Ala-Arg-4-nitroanilide + H2O
Boc-Gln-Ala-Arg + 4-nitroaniline
-
-
-
?
Boc-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
Boc-Gln-Ala-Arg + 7-amino-4-methylcoumarin
fluorogenic substrate
-
-
?
Boc-QAR-Amc + H2O
?
matriptase-2 mediates efficient cleavage of artificial peptides corresponding to cleavage sites located in the proteins filaggrin, CUB-domain-containing protein 1 (CDCP1), and alphaE beta7 integrin
-
-
?
fetuin-A + H2O
?
a liver-derived alpha2-Heremans-Schmid glycoprotein from plasma, processing into a two-chain form, cleavage sites are Arg and Lys residues in the 40 amino acid sequence of the linker connceting the two peptides
-
-
?
N2-t-butyloxycarbonyl-QNR-7-amido-4-methylcoumarin + H2O
?
matriptase-2 mediates efficient cleavage of artificial peptides corresponding to cleavage sites located in the proteins filaggrin, CUB-domain-containing protein 1 (CDCP1), and alphaE beta7 integrin
-
-
?
proform matriptase + H2O
mature matriptase
matriptase is expressed as a zymogen and is autocatalytically processed and activated through cleavage at Arg614 within the RQAR614-VVGG activation sequence
-
-
?
proform matriptase-2 + H2O
mature matriptase
matriptase-2 is expressed as zymogen form and undergoes autocatalysis at Arg576 within the PSSR576-IVGG sequence located in the consensus activation site of its pro-domain
-
-
?
(DY-681)-Gly-Arg-Gln-Ser-Arg-Ala-Ile-Lys (DY-681)-NH + H2O
?
-
synthetic substrate, peptide sequence is derived from one of the preferred matriptase cleavage sequences, P4(Arg/Lys)-P3(Xxx)-P2(Ser)-P1(Arg)-P10(Ala), where Xxx is a nonbasic amino acid
-
-
?
acid-sensing ion channel 1 + H2O
?
-
the matriptase recognition sites Arg-145, Lys-185, and Lys-384 are identified in the specific substrate acid-sensing ion channel 1
-
-
?
Arg-Xaa-Ser-Arg-Ala + H2O
Arg-Xaa-Ser + Arg-Ala
-
X: non-basic amino acid, good substrate
-
?
benzoyl-L-arginine-4-methylcoumaryl-7-amide + H2O
benzoyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-Gln-Ala-Arg-4-nitroanilide + H2O
Boc-Gln-Ala-Arg + 4-nitroaniline
-
-
-
?
Boc-Glu-Ala-Arg-7-amido-4-methylcoumarin + H2O
Boc-Glu-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
butyloxycarbonyl-L-Gln-L-Ala-L-Arg-4-nitroanilide + H2O
butyloxycarbonyl-L-Gln-L-Ala-L-Arg + 4-nitroaniline
-
-
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
HGF/SF + H2O
?
-
i.e. hepatocyte growth factor/scatter factor, growth factor
-
-
?
influenza A H1 virus hemagglutinin + H2O
?
the soluble form of the protease is able to specifically cleave hemagglutinins from H1 virus, but not from H2 and H3 viruses, in a broad pH range
-
-
?
insulin growth factor binding protein-related protein-1 + H2O
?
-
cleaved by the soluble form of active matripase
-
-
?
Lys-Xaa-Ser-Arg-Ala + H2O
Lys-Xaa-Ser + Arg-Ala
-
X: non-basic amino acid, good substrate
-
?
methyl-sulfonyl-D-cyclo-hexyltyrosyl-glycyl-L-arginine-4-nitroanilide + H2O
?
-
-
-
?
N-succinyl-Ala-Phe-Lys-7-amido-4-methylcoumarin + H2O
N-succinyl-Ala-Phe-Lys + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxy-carbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin
N-tert-butoxy-carbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-benzyl-Asp-Pro-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-benzyl-Asp-Pro-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-benzyl-Glu-Gly-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-benzyl-Glu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-gamma-benzyl-Glu-Ala-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
N-tert-butoxycarbonyl-gamma-benzyl-Glu-Ala-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-gamma-benzyl-Glu-Ala-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-gamma-benzyl-Glu-Gly-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-gamma-benzyl-Glu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg 7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
N-tert-butoxycarbonyl-Gly-Lys-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gly-Lys-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Leu-Arg-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Leu-Gly-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Leu-Gly-Arg + 7-amino-4-methylcoumarin
N-tert-butoxycarbonyl-Leu-Ser-Thr-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Leu-Ser-Thr-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
?
pro matrix metalloproteinase 1 + H2O
?
-
matriptase activates pro-matrix metalloproteinase-1 and processes pro-matrix metalloproteinase-3 to its fully active form
-
-
?
pro matrix metalloproteinase 3 + H2O
?
-
matriptase activates pro-matrix metalloproteinase-1 and processes pro-matrix metalloproteinase-3 to its fully active form
-
-
?
pro-form GPI-anchored serine protease prostasin + H2O
mature GPI-anchored serine protease prostasin + ?
pro-form influenza hemagglutinin H2 + H2O
mature influenza hemagglutinin H2 + ?
subtype H2N2
-
-
?
pro-form influenza hemagglutinin H3 + H2O
mature influenza hemagglutinin H3 + ?
subtype H3N2
-
-
?
pro-form matriptase + H2O
mature matriptase + ?
autocatalytic activation
-
-
?
pro-HGF + H2O
?
-
matriptase is an efficient activator of hepatocyte growth factor
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
pro-urokinase-type plasminogen activator + H2O
?
-
-
-
-
?
proform epithelial sodium channel + H2O
mature epithelial sodium channel + ?
-
-
-
-
?
proform G protein-coupled protease activated receptor-2 + H2O
mature G protein-coupled protease activated receptor-2 + ?
-
-
-
-
?
single-chain urokinase-type plaminogen activator + H2O
?
-
is activated by matriptase
-
?
succinyl-Ala-Phe-Lys-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Phe-Lys + 7-amino-4-methylcoumarin
-
-
?
t-butoxycarbonyl-L-Gln-L-Ala-L-Arg-7-amido-4-methylcoumarin + H2O
t-butoxycarbonyl-L-Gln-L-Ala-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
enzymatic activity assay
-
-
?
urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
pro-uPA activation on THP-1 cells
-
-
?
VPEKQTRGL + H2O
?
influenza hemagglutinin H3 cleavage site peptide mimic
-
-
?
Xaa-Arg-Ser-Arg-Ala + H2O
Xaa-Arg-Ser + Arg-Ala
-
X: non-basic amino acid, good substrate
-
?
Xaa-Lys-Ser-Arg-Ala + H2O
Xaa-Lys-Ser + Arg-Ala
-
X: non-basic amino acid, good substrate
-
?
hemojuvelin + H2O
?
a glycosylphosphatidylinositol-linked membrane protein. inactivation
-
-
?
epidermal growth factor receptor + H2O
EGFR135 + EGFR110
-
-
fragments of 135 and 110 kDa, EGFR110 is constitutively active, while EGFR135 is inactive in terms of tyrosine phosphorylation
-
?
epidermal growth factor receptor + H2O
EGFR135 + EGFR110
-
the epidermal growth factor receptor, EGFR is proteolytically cleaved in the N-terminal extracellular domain by the matriptase-prostasin serine protease cascade in cultured epithelial cells
fragments of 135 and 110 kDa, no longer responsive to EGF stimulation
-
?
hepatocyte growth factor + H2O
activated hepatocyte growth factor + ?
-
proteolytic activation of hepatocyte growth factor/scatter factor, physiological function, overview
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
-
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
activation
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
seven proteases are involved in the activation of HGF/SF, involved in cell proliferation and adhesion, ECM degradation/remodeling, and migration/invasiveness, overview
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
the enzyme is involved in tumor progression and metastasis
-
-
?
IGFBP-rP1 + H2O
?
-
involved in involved in cell proliferation and adhesion
-
-
?
insulin-like growth factor binding protein related protein-1
?
-
IGFBP-rP1
-
-
?
insulin-like growth factor binding protein related protein-1
?
IGFBP-rP1
-
-
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
-
activation
-
-
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
-
proteolytical cleavage on the cell surface of a a single-chain IGFB-rP1 to a two-chain form, consisting of a 25 kDa chain and an 8 kDa chain, changing its biological in modulation of cellular adhesion and growth in an IGF/insulin-dependent or independent manner, as well as tumor-suppressive activity, the soluble form of active matriptase cleaves IGFBP-rP1 but HAI-1 or some other inhibitors block its activity in culture medium, overview
-
-
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
-
i.e. IGFBP-rP1
-
-
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
-
i.e. IGFBP-rP1 or angiomodulin or mac25
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Leu-Gly-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Leu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Leu-Gly-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Leu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
?
pro-form GPI-anchored serine protease prostasin + H2O
mature GPI-anchored serine protease prostasin + ?
activation
-
-
?
pro-form GPI-anchored serine protease prostasin + H2O
mature GPI-anchored serine protease prostasin + ?
activation, prostasin is also a regulator of the epidermal sodium channel like matriptase
-
-
?
pro-form influenza hemagglutinin H1 + H2O
mature influenza hemagglutinin H1 + ?
-
-
-
?
pro-form influenza hemagglutinin H1 + H2O
mature influenza hemagglutinin H1 + ?
preferred subtype H1N1
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
-
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
activation
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
activation at the cell surface, where uPA and matriptase co-localize, involved in cell proliferation and adhesion, ECM degradation/remodeling, and migration/invasiveness
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
the enzyme is involved in tumor progression and metastasis
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
-
involved in terminal epithelial cell differentiation, mechanism of enzyme access for direct cleavage in vivo, overview
-
-
?
prostasin + H2O
activated prostasin + ?
-
proteolytic activation by matriptase, when expressed without matriptase, prostasin remains in the zymogen form and no prostasin-PN-1 complex is formed, overview
-
-
?
prostasin + H2O
activated prostasin + ?
-
proteolytic activation by matriptase
-
-
?
stromelysin + H2O
activated stromelysin + propeptide of stromelysin
-
activation
-
-
?
stromelysin + H2O
activated stromelysin + propeptide of stromelysin
-
i.e. MMP-3 or matrix metalloproteinase-3, recombinant human substrate, activation
-
-
?
VEGFR-2 + H2O
?
-
i.e. vascular endothelial growth factor receptor 2, a growth factor receptor
-
-
?
additional information
?
-
the optimized peptide substrate sequence is Ile-Arg-Ala-Arg-Ser-Ala-Gly
-
-
?
additional information
?
-
-
the optimized peptide substrate sequence is Ile-Arg-Ala-Arg-Ser-Ala-Gly
-
-
?
additional information
?
-
cleaves synthetic substrates with arginine or lysine as their P1 sites and prefers small side chain amino acids, such as Ala and Gly, at P2 sites
-
?
additional information
?
-
-
cleaves synthetic substrates with arginine or lysine as their P1 sites and prefers small side chain amino acids, such as Ala and Gly, at P2 sites
-
?
additional information
?
-
-
preferred amino acid residues: at P4 position: Lys and Arg, at P3 position: basic residues and Glu, at P2 position: Gly, Ser and Phe
-
?
additional information
?
-
degrades extracellular matrix, matriptase-binding protein is a Kunitz-type serine protease inhibitor
-
?
additional information
?
-
-
degrades extracellular matrix, matriptase-binding protein is a Kunitz-type serine protease inhibitor
-
?
additional information
?
-
initiator of matrix-degrading protein cascade, activates hepatocyte growth factor scattering factor
-
?
additional information
?
-
-
initiator of matrix-degrading protein cascade, activates hepatocyte growth factor scattering factor
-
?
additional information
?
-
-
involved in multiple aspects of tumor progression and cancer invasion
-
?
additional information
?
-
-
enzyme regulation and deregulation in cancer, overview, matriptase is involved in cancer initiation and progression, it not only facilitates cellular invasiveness but may also activate oncogenic pathways, overview
-
-
?
additional information
?
-
-
matriptase blockade could potentially modulate tumorigenesis and metastasis in vivo
-
-
?
additional information
?
-
-
matriptase cleaves and activates proteins implicated in the progression of cancer
-
-
?
additional information
?
-
-
matriptase expression is correlated with tumor progression in epithelium-derived cancer cells
-
-
?
additional information
?
-
-
matriptase has an essential physiological role in profilaggrin processing, corneocyte maturation, and lipid matrix formation associated with terminal differentiation of the oral epithelium and the epidermis, and is also critical for hair follicle growth, matriptase and HAI expression are frequently dysregulated in human cancer, and matriptase expression, that is unopposed by HAI-1, potently promotes carcinogenesis and metastatic dissemination in animal models, matriptase dramatically increases apoptosis of immature thymocytes in the thymus, leading to thymocyte depletion, physiological functions of matriptase, the enzyme is involved in epithelial carcinogenesis, detailed overview
-
-
?
additional information
?
-
-
matriptase is a type II transmembrane serine protease and highly regulated in leukocytes, and correlates with the presence of active uPA on their surface, it is up-regulated in a variety of cancers and correlates closely with disease progression, it acts as initiator of protease cascades/signaling pathways, overview
-
-
?
additional information
?
-
-
matriptase promotes tumor growth and angiogenesis by enhancing extracellular matrix degradation in tumor cell microenvironments, overview
-
-
?
additional information
?
-
-
matriptase-1 enhances breast tumor growth and invasion and correlates with poor prognosis for breast cancer patients, while matriptase-2 shows the opposite effects, overview
-
-
?
additional information
?
-
matriptase-1 enhances breast tumor growth and invasion and correlates with poor prognosis for breast cancer patients, while matriptase-2 shows the opposite effects, overview
-
-
?
additional information
?
-
-
matriptase-2 inhibits breast tumor growth and invasion and correlates with favorable prognosis for breast cancer patients, while matriptase-1 shows the opposite effects, overview
-
-
?
additional information
?
-
matriptase-2 inhibits breast tumor growth and invasion and correlates with favorable prognosis for breast cancer patients, while matriptase-1 shows the opposite effects, overview
-
-
?
additional information
?
-
mutation in gene ST14 causes autosomal recessive ichthyosis with hypotrichosis syndrome, characterized by congenital ichthyosis associated with abnormal hair, overview
-
-
?
additional information
?
-
-
physiological functions, overview, MT-SP1 is a type II transmembrane serine protease implicated in a range of cancers including those of the breast, cervix, ovaries, prostate, colon and gastrointestinal tract, MT-SP1 plays a role in embryologic development
-
-
?
additional information
?
-
-
physiological regulatory mechanisms, overview, matriptase is involved in cancer invasion and metastasis by serving as a membrane activator directly on cancer cell surfaces to recruit and activate urokinase type plasminogen activator, MMP-3, hepatocyte growth factor, and insulin-like growth factor binding protein-related protein-1, all of which are important in various aspects of cancers, including extracellular matrix degradation, adhesion, cellular motility and tumor vascularization
-
-
?
additional information
?
-
-
reduced matriptase activity is associated with incomplete terminal differentiation of epidermis, epidermal appendages, oral epithelium, and, likely, other epithelial structures, matriptase activity must be tightly controlled in epithelial tissues by transcriptional and posttranslational mechanisms, as matriptase dysregulation can cause embryonic demise as well as malignant transformation
-
-
?
additional information
?
-
-
the G827R mutation in patients with autosomal recessive ichthyosis with hypotrichosis leads to the expression of an inactive protease
-
-
?
additional information
?
-
-
matriptase binds cytosolic proteins to regulate enzymatic activity and cellular distribution of the protease
-
-
?
additional information
?
-
-
R/KXSR-/-A is the cleavage sequence of matriptase
-
-
?
additional information
?
-
-
the enzyme is a type II transmembrane serine protease
-
-
?
additional information
?
-
-
matriptase does not cleave acid-sensing ion channel 2
-
-
?
additional information
?
-
-
the P1 residue for MT-SP1 substrates is either arginine or lysine
-
-
?
additional information
?
-
matriptase has an autocatalytic domain, RQAR. At physiological pH, matriptase is capable of cleaving both the H1 (IQSR-/-GLFG) and H3 (KQTR-/-GLFG) consensus cleavage sequences, whereas no cleavage is observed with the H2 (IESRGLFG) consensus sequence. RQRR-/-VVGG is the optimal cleavage sequence of matriptase
-
-
?
additional information
?
-
-
matriptase has an autocatalytic domain, RQAR. At physiological pH, matriptase is capable of cleaving both the H1 (IQSR-/-GLFG) and H3 (KQTR-/-GLFG) consensus cleavage sequences, whereas no cleavage is observed with the H2 (IESRGLFG) consensus sequence. RQRR-/-VVGG is the optimal cleavage sequence of matriptase
-
-
?
additional information
?
-
the enzyme shows low rate cleavage of the A/Japan/305/57 (H2) peptide mimic (VPQIESRGL) compared to that for the H1 consensus
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
proform matriptase + H2O
mature matriptase
matriptase is expressed as a zymogen and is autocatalytically processed and activated through cleavage at Arg614 within the RQAR614-VVGG activation sequence
-
-
?
proform matriptase-2 + H2O
mature matriptase
matriptase-2 is expressed as zymogen form and undergoes autocatalysis at Arg576 within the PSSR576-IVGG sequence located in the consensus activation site of its pro-domain
-
-
?
acid-sensing ion channel 1 + H2O
?
-
the matriptase recognition sites Arg-145, Lys-185, and Lys-384 are identified in the specific substrate acid-sensing ion channel 1
-
-
?
butyloxycarbonyl-L-Gln-L-Ala-L-Arg-4-nitroanilide + H2O
butyloxycarbonyl-L-Gln-L-Ala-L-Arg + 4-nitroaniline
-
-
-
-
?
epidermal growth factor receptor + H2O
EGFR135 + EGFR110
-
the epidermal growth factor receptor, EGFR is proteolytically cleaved in the N-terminal extracellular domain by the matriptase-prostasin serine protease cascade in cultured epithelial cells
fragments of 135 and 110 kDa, no longer responsive to EGF stimulation
-
?
hepatocyte growth factor + H2O
activated hepatocyte growth factor + ?
-
proteolytic activation of hepatocyte growth factor/scatter factor, physiological function, overview
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
HGF/SF + H2O
?
-
i.e. hepatocyte growth factor/scatter factor, growth factor
-
-
?
influenza A H1 virus hemagglutinin + H2O
?
the soluble form of the protease is able to specifically cleave hemagglutinins from H1 virus, but not from H2 and H3 viruses, in a broad pH range
-
-
?
pro matrix metalloproteinase 1 + H2O
?
-
matriptase activates pro-matrix metalloproteinase-1 and processes pro-matrix metalloproteinase-3 to its fully active form
-
-
?
pro matrix metalloproteinase 3 + H2O
?
-
matriptase activates pro-matrix metalloproteinase-1 and processes pro-matrix metalloproteinase-3 to its fully active form
-
-
?
pro-form GPI-anchored serine protease prostasin + H2O
mature GPI-anchored serine protease prostasin + ?
activation, prostasin is also a regulator of the epidermal sodium channel like matriptase
-
-
?
pro-form influenza hemagglutinin H1 + H2O
mature influenza hemagglutinin H1 + ?
-
-
-
?
pro-form matriptase + H2O
mature matriptase + ?
autocatalytic activation
-
-
?
pro-HGF + H2O
?
-
matriptase is an efficient activator of hepatocyte growth factor
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
profilaggrin + H2O
filaggrin + propeptide of filaggrin
-
involved in terminal epithelial cell differentiation, mechanism of enzyme access for direct cleavage in vivo, overview
-
-
?
proform epithelial sodium channel + H2O
mature epithelial sodium channel + ?
-
-
-
-
?
proform G protein-coupled protease activated receptor-2 + H2O
mature G protein-coupled protease activated receptor-2 + ?
-
-
-
-
?
prostasin + H2O
activated prostasin + ?
-
proteolytic activation by matriptase, when expressed without matriptase, prostasin remains in the zymogen form and no prostasin-PN-1 complex is formed, overview
-
-
?
stromelysin + H2O
activated stromelysin + propeptide of stromelysin
-
activation
-
-
?
urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
pro-uPA activation on THP-1 cells
-
-
?
hemojuvelin + H2O
?
a glycosylphosphatidylinositol-linked membrane protein. inactivation
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
activation
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
seven proteases are involved in the activation of HGF/SF, involved in cell proliferation and adhesion, ECM degradation/remodeling, and migration/invasiveness, overview
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
the enzyme is involved in tumor progression and metastasis
-
-
?
IGFBP-rP1 + H2O
?
-
involved in involved in cell proliferation and adhesion
-
-
?
insulin-like growth factor binding protein related protein-1
?
-
IGFBP-rP1
-
-
?
insulin-like growth factor binding protein related protein-1
?
IGFBP-rP1
-
-
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
-
activation
-
-
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
-
proteolytical cleavage on the cell surface of a a single-chain IGFB-rP1 to a two-chain form, consisting of a 25 kDa chain and an 8 kDa chain, changing its biological in modulation of cellular adhesion and growth in an IGF/insulin-dependent or independent manner, as well as tumor-suppressive activity, the soluble form of active matriptase cleaves IGFBP-rP1 but HAI-1 or some other inhibitors block its activity in culture medium, overview
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
-
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
activation
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
activation at the cell surface, where uPA and matriptase co-localize, involved in cell proliferation and adhesion, ECM degradation/remodeling, and migration/invasiveness
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
the enzyme is involved in tumor progression and metastasis
-
-
?
VEGFR-2 + H2O
?
-
i.e. vascular endothelial growth factor receptor 2, a growth factor receptor
-
-
?
additional information
?
-
the optimized peptide substrate sequence is Ile-Arg-Ala-Arg-Ser-Ala-Gly
-
-
?
additional information
?
-
-
the optimized peptide substrate sequence is Ile-Arg-Ala-Arg-Ser-Ala-Gly
-
-
?
additional information
?
-
degrades extracellular matrix, matriptase-binding protein is a Kunitz-type serine protease inhibitor
-
?
additional information
?
-
-
degrades extracellular matrix, matriptase-binding protein is a Kunitz-type serine protease inhibitor
-
?
additional information
?
-
initiator of matrix-degrading protein cascade, activates hepatocyte growth factor scattering factor
-
?
additional information
?
-
-
initiator of matrix-degrading protein cascade, activates hepatocyte growth factor scattering factor
-
?
additional information
?
-
-
involved in multiple aspects of tumor progression and cancer invasion
-
?
additional information
?
-
-
enzyme regulation and deregulation in cancer, overview, matriptase is involved in cancer initiation and progression, it not only facilitates cellular invasiveness but may also activate oncogenic pathways, overview
-
-
?
additional information
?
-
-
matriptase blockade could potentially modulate tumorigenesis and metastasis in vivo
-
-
?
additional information
?
-
-
matriptase cleaves and activates proteins implicated in the progression of cancer
-
-
?
additional information
?
-
-
matriptase expression is correlated with tumor progression in epithelium-derived cancer cells
-
-
?
additional information
?
-
-
matriptase has an essential physiological role in profilaggrin processing, corneocyte maturation, and lipid matrix formation associated with terminal differentiation of the oral epithelium and the epidermis, and is also critical for hair follicle growth, matriptase and HAI expression are frequently dysregulated in human cancer, and matriptase expression, that is unopposed by HAI-1, potently promotes carcinogenesis and metastatic dissemination in animal models, matriptase dramatically increases apoptosis of immature thymocytes in the thymus, leading to thymocyte depletion, physiological functions of matriptase, the enzyme is involved in epithelial carcinogenesis, detailed overview
-
-
?
additional information
?
-
-
matriptase is a type II transmembrane serine protease and highly regulated in leukocytes, and correlates with the presence of active uPA on their surface, it is up-regulated in a variety of cancers and correlates closely with disease progression, it acts as initiator of protease cascades/signaling pathways, overview
-
-
?
additional information
?
-
-
matriptase promotes tumor growth and angiogenesis by enhancing extracellular matrix degradation in tumor cell microenvironments, overview
-
-
?
additional information
?
-
-
matriptase-1 enhances breast tumor growth and invasion and correlates with poor prognosis for breast cancer patients, while matriptase-2 shows the opposite effects, overview
-
-
?
additional information
?
-
matriptase-1 enhances breast tumor growth and invasion and correlates with poor prognosis for breast cancer patients, while matriptase-2 shows the opposite effects, overview
-
-
?
additional information
?
-
-
matriptase-2 inhibits breast tumor growth and invasion and correlates with favorable prognosis for breast cancer patients, while matriptase-1 shows the opposite effects, overview
-
-
?
additional information
?
-
matriptase-2 inhibits breast tumor growth and invasion and correlates with favorable prognosis for breast cancer patients, while matriptase-1 shows the opposite effects, overview
-
-
?
additional information
?
-
mutation in gene ST14 causes autosomal recessive ichthyosis with hypotrichosis syndrome, characterized by congenital ichthyosis associated with abnormal hair, overview
-
-
?
additional information
?
-
-
physiological functions, overview, MT-SP1 is a type II transmembrane serine protease implicated in a range of cancers including those of the breast, cervix, ovaries, prostate, colon and gastrointestinal tract, MT-SP1 plays a role in embryologic development
-
-
?
additional information
?
-
-
physiological regulatory mechanisms, overview, matriptase is involved in cancer invasion and metastasis by serving as a membrane activator directly on cancer cell surfaces to recruit and activate urokinase type plasminogen activator, MMP-3, hepatocyte growth factor, and insulin-like growth factor binding protein-related protein-1, all of which are important in various aspects of cancers, including extracellular matrix degradation, adhesion, cellular motility and tumor vascularization
-
-
?
additional information
?
-
-
reduced matriptase activity is associated with incomplete terminal differentiation of epidermis, epidermal appendages, oral epithelium, and, likely, other epithelial structures, matriptase activity must be tightly controlled in epithelial tissues by transcriptional and posttranslational mechanisms, as matriptase dysregulation can cause embryonic demise as well as malignant transformation
-
-
?
additional information
?
-
-
the G827R mutation in patients with autosomal recessive ichthyosis with hypotrichosis leads to the expression of an inactive protease
-
-
?
additional information
?
-
-
matriptase does not cleave acid-sensing ion channel 2
-
-
?
additional information
?
-
-
the P1 residue for MT-SP1 substrates is either arginine or lysine
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
additional information
low intracellular iron increases the stability of matriptase-2, overview
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-arginyl-L-glutaminyl-N-[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-hydroxypentan-2-yl]-L-alaninamide
-
L-arginyl-N1-[(2S)-1-[[(2R)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
-
L-arginyl-N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
L-arginyl-N1-[(2S)-1-[[(2S)-6-amino-1-(1,3-benzothiazol-2-yl)-1-oxohexan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
-
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
inhibitor modeling in the wild-type enzyme active site, overview
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
-
N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
-
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
-
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
-
(1r,4r)-4-amino-N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)cyclohexanecarboxamide
-
(2R)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylic acid
-
-
(2S)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylic acid
-
-
1-(2-aminoethyl)-N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)piperidine-4-carboxamide
-
1-(3-aminopropanoyl)-N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)piperidine-4-carboxamide
-
1-(N-[[3-(b-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-3-carboxamide
-
-
1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-4-carboxamide
-
-
3,5-bis(4-carbamimidoylphenoxy)-N-((4-hydroxycyclohexyl)methyl)benzamide
-
3,5-bis(4-carbamimidoylphenoxy)-N-(1-(2-hydroxyethyl)piperidin-4-yl)benzamide
-
3-(3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-ethylbiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl)benzenecarboximidamide
-
inhibitor completely prevents matriptase zymogen activation in human adenocarcinoma cell lines AsPC-1 and BxPC-3. Pro-urokinase-type plasminogen activator activation is completely abolished by matriptase inhibition. Matriptase inhibitors reduce the phosphorylation of the HGF receptor/cMet and the overall cellular invasiveness of the human pancreatic adenocarcinoma cell line AsPC-1
3-[(2R)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
3-[(2R)-3-[4-(2-carbamimidamidoethyl)piperidin-1-yl]-2-[(naphthalen-2-ylsulfonyl)amino]propyl]benzenecarboximidamide
-
-
3-[(2S)-2-([[3-(4-aminobutyl)phenyl]sulfonyl]amino)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(1H-indol-5-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(2-methylpyrimidin-4-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-aminopyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[4'-(1-methylethoxy)biphenyl-3-yl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[(biphenyl-3-ylsulfonyl)amino]-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[(naphthalen-2-ylsulfonyl)amino]-3-oxopropoxy]benzenecarboximidamide
higher cytotoxic effect, enzyme-bound structure, crystal structure analysis, overview
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[([3-[(3-aminopropyl)amino]phenyl]sulfonyl)amino]-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(2'-chlorobiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(3',4'-dimethoxybiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(3'-chlorobiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-chlorobiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-ethoxybiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-ethylbiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-methoxybiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4-cyclohexylphenyl)sulfonyl]amino]-3-oxopropoxy]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxo-2-([[2,4,6-tri(propan-2-yl)phenyl]sulfonyl]amino)propoxy]benzenecarboximidamide
higher cytotoxic effect
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxo-2-[[(3-pyridin-3-ylphenyl)sulfonyl]amino]propyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxo-2-[[(3-pyridin-4-ylphenyl)sulfonyl]amino]propyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(4-aminobutanoyl)piperidin-1-yl]-3-oxo-2-([[2,4,6-tri(propan-2-yl)phenyl]sulfonyl]amino)propoxy]benzenecarboximidamide
-
3-[(2S)-3-[4-(b-alanyl)piperidin-1-yl]-3-oxo-2-([[2,4,6-tri(propan-2-yl)phenyl]sulfonyl]amino)propoxy]benzenecarboximidamide
-
3-[(2S)-3-[4-(N-carbamimidoyl-b-alanyl)piperazin-1-yl]-3-oxo-2-([[2,4,6-tris(1-methylethyl)phenyl]sulfonyl]amino)propyl]benzenecarboximidamide
-
3-[3-[4-(2-carbamimidamidoethyl)piperidin-1-yl]-2-[(naphthalen-2-ylsulfonyl)amino]-3-oxopropyl]benzenecarboximidamide
-
4,4'-((5-(1,2,3,4-tetrahydroisoquinoline-2-carbonyl)-1,3-phenylene)bis(oxy))dibenzimidamide
-
4,4'-((5-(4-(2-aminoethyl)piperidine-1-carbonyl)-1,3-phenylene)bis(oxy))dibenzimidamide
-
4,4'-((5-(4-fluorophenylsulfonamido)-1,3-phenylene)bis(oxy))dibenzimidamide
-
4,4'-((5-(decahydroquinoline-1-carbonyl)-1,3-phenylene)bis(oxy))dibenzimidamide
-
4,4'-((5-(naphthalene-2-sulfonamido)-1,3-phenylene)bis(oxy))dibenzimidamide
-
4,4'-[(3-[[(4-fluorophenyl)sulfonyl]amino]pyridine-2,6-diyl)bis(oxy)]dibenzenecarboximidamide
-
4,4'-[benzene-1,4-diylbis(oxy)]dibenzenecarboximidamide
binding structure, overview
4-(1-[3-carbamimidoyl-N-[(3-pyrrolidin-1-ylphenyl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
4-(1-[3-carbamimidoyl-N-[(4'-ethoxybiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
4-(1-[3-carbamimidoyl-N-[(4'-ethylbiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
4-(1-[N-[(4'-tert-butylbiphenyl-3-yl)sulfonyl]-3-carbamimidoyl-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
4-([1-[(2S)-3-(3-carbamimidoylphenyl)-2-([[2,4,6-tris(1-methylethyl)phenyl]sulfonyl]amino)propanoyl]piperidin-4-yl]carbonyl)piperidine-1-carboximidamide
-
4-([1-[(2S)-3-(3-carbamimidoylphenyl)-2-[[(4-cyclohexylphenyl)sulfonyl]amino]propanoyl]piperidin-4-yl]carbonyl)piperidine-1-carboximidamide
-
inhibitor completely prevents matriptase zymogen activation in human adenocarcinoma cell lines AsPC-1 and BxPC-3. Pro-urokinase-type plasminogen activator activation is completely abolished by matriptase inhibition. Matriptase inhibitor reduce the phosphorylation of the HGF receptor/cMet and the overall cellular invasiveness of the human pancreatic adenocarcinoma cell line AsPC-1
4-aminobenzamidine
-
weak competitive inhibition, competition assay with antibody inhibitors, overview
4-[(2-[[(2S)-6-carbamimidamido-1-oxohexan-2-yl]amino]-2-oxoethyl)carbamoyl]-6-methoxy-6-oxo-4-[3-(prop-1-en-2-yl)benzyl]hexanoic acid
-
4-[1-(3-carbamimidoyl-N-[[3-(1H-imidazol-1-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
4-[1-(3-carbamimidoyl-N-[[3-(2-oxopiperazin-1-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
4-[1-(3-carbamimidoyl-N-[[3-(2-oxopiperidin-1-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
4-[1-(3-carbamimidoyl-N-[[3-(6-oxopyridazin-1(6H)-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
4-[1-(N-[[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
4-[1-(N-[[3-(6-aminopyridin-3-yl)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]butanamide
-
-
4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]butanoic acid
-
-
4-[4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazin-1-yl]-N-methyl-4-oxobutanamide
-
-
9-fluorenylmethyloxycarbonyl-GR-ketobenzothiazole
potent and selective inhibitor for matriptase over hepsin
anti-matriptase LDL receptor domain 3-specific monoclonal antibodies
-
complete inhibition of enzyme activation
-
antisense-matripase
-
significantly reduces matripase protein expression by 70-80%, anti-tumoral activity on HRA cells intraperitoneal injected into nude mice
-
benzyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
benzylsulfonyl-D-arginyl-proline-(2-aminomethyl-5-chlorobenzyl)-amide bis(trifluoroacetate)
-
-
benzylsulfonyl-D-arginyl-proline-(4-amidinobenzyl)amide bis-(trifluoroacetate)
-
-
benzylsulfonyl-D-cyclohexylalanyl-proline-(2-aminomethyl-5-chlorobenzyl)amide
-
-
CJ-730
-
3-amidinophenylalanine-based inhibitor CJ-730, completely inhibits pro-HGF activation in PC3 cells
D-hTyr-Ala-4-amidinobenzylamide
compound has a 10fold reduced activity against thrombin and factor Xa
ethyl (3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)carbamate
-
ethyl 4-(3,5-bis(4-carbamimidoylphenoxy)benzamido)piperidine-1-carboxylate
-
ethyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
-
-
GAVCPKILKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGACPKILKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGRCPKALKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGRCPKILKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCAKILKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPAILKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKALKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKIAKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKILAKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKILKACRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKILKKCRRDSDCPGACICRGAGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKILKKCRRDSDCPGACICRGNGACGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKILKKCRRDSDCPGACICRGNGYCASGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKILKKCRRDSDCPGACICRGNGYCGAGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPKRLKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
GGVCPRILKKCRRDSDCPGACICRGNGYCGSGSD
a mutant of Momordica cochinchinensis trypsin inhibitor-II
hepatcyte growth factor activator inhibitor-1
-
in normal skin matriptase is complexed to hepatcyte growth factor activator inhibitor-1 wheras in squamous cell carcinoma the enzyme is present in an unassociated form
-
L-arginyl-N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
EC50 is 0.00564-0.0068 mM, the inhibitor contains a ketobenzothiazole serine trap designed based on matriptase's auto-catalytic domain (RQAR), it is a selective, slow, tight-binding inhibitor of matriptase that significantly reduces viral replication of H1N1 influenza virus, including the 2009 pandemic virus
methyl (2R)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylate
-
-
methyl (2S)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylate
-
-
methyl 4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]butanoate
-
-
N-((1r,4r)-4-aminocyclohexyl)-3,5-bis((3-carbamimidoylbenzyl)oxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3,5-bis((4-carbamimidoylbenzyl)oxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-((3-carbamimidoylbenzyl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-((4-bromobenzyl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-((4-carbamimidoylbenzyl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-((6-aminopyridin-3-yl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-((6-bromopyridin-3-yl)methoxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-(4-(3-aminopropanamido)phenoxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-(4-(aminomethyl)phenoxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-(4-aminophenoxy)-5-(4-carbamimidoylphenoxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-(4-carbamimidoylphenoxy)-5-((4-chlorobenzyl)oxy)benzamide
-
N-((1r,4r)-4-aminocyclohexyl)-3-(4-carbamimidoylphenoxy)-5-(4-carbamoylphenoxy)benzamide
-
N-(1-(3-aminopropyl)piperidin-4-yl)-3,5-bis(4-carbamimidoylphenoxy)benzamide
-
N-(2-aminoethyl)-1-(3-carbamimidoyl-N-[[2,4,6-tris(1-methylethyl)phenyl]sulfonyl]-L-phenylalanyl)piperidine-4-carboxamide
-
N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)-1-(2-hydroxyethyl)piperidine-4-carboxamide
-
N-(3-[[(1R)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)ethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-(2-methylpiperidin-1-yl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-(4-methylpiperidin-1-yl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-oxo-2-piperazin-1-ylethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-oxo-2-piperidin-1-ylethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-[4-[4-(methylamino)-4-oxobutyl]piperidin-1-yl]-2-oxoethyl]sulfamoyl]phenyl)azetidine-3-carboxamide
-
-
N-(3-[[(1S)-1-[[4-(2-aminoethyl)piperidin-1-yl]carbonyl]-3-phenylpropyl]sulfamoyl]phenyl)-beta-alaninamide
-
N-(3-[[(1S)-1-[[4-(2-aminoethyl)piperidin-1-yl]carbonyl]-4-phenylbutyl]sulfamoyl]phenyl)-beta-alaninamide
-
N-(3-[[(1S)-2-(4-benzylpiperidin-1-yl)-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-3-hydroxypropanamide
-
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-b-alaninamide
-
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)azetidine-3-carboxamide
-
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)propanamide
-
N-(3-[[(1S)-2-[4-(2-carbamimidamidoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
N-(3-[[(2S)-1-[4-(2-aminoethyl)piperidin-1-yl]-3-(3-carbamimidoylphenyl)-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
inhibitor completely prevents matriptase zymogen activation in human adenocarcinoma cell lines AsPC-1 and BxPC-3. Pro-urokinase-type plasminogen activator activation is completely abolished by matriptase inhibition. Matriptase inhibitors reduce the phosphorylation of the HGF receptor/cMet and the overall cellular invasiveness of the human pancreatic adenocarcinoma cell line AsPC-1
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-oxo-1-(piperazin-1-yl)propan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
inhibitor completely prevents matriptase zymogen activation in human adenocarcinoma cell lines AsPC-1 and BxPC-3. Pro-urokinase-type plasminogen activator activation is completely abolished by matriptase inhibition. Matriptase inhibitors reduce the phosphorylation of the HGF receptor/cMet and the overall cellular invasiveness of the human pancreatic adenocarcinoma cell line AsPC-1
N-(4-aminocyclohexyl)-O-(3-carbamimidoylphenyl)-N2-(naphthalen-2-ylsulfonyl)-L-serinamide
-
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
-
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
-
N-[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-[3-(aminomethyl)benzyl]-2-oxoethyl]-4'-methoxybiphenyl-3-sulfonamide
-
N-[3-([(1S)-1-(3-carbamimidoylbenzyl)-2-[4-(4-hydroxyphenyl)piperazin-1-yl]-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
-
N-[3-([(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-benzyl-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
N-[3-([(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-[3-(aminomethyl)benzyl]-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
N-[3-([(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-[4-(aminomethyl)benzyl]-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
N-[3-([1-[4-(2-aminoethyl)piperidin-1-yl]-3-(3-carbamimidoylphenyl)-1-oxopropan-2-yl]sulfamoyl)phenyl]-b-alaninamide
-
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
-
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
-
O-(3-carbamimidoylphenyl)-N-(4-methylcyclohexyl)-N2-(naphthalen-2-ylsulfonyl)-L-serinamide
-
R1K'4-eglin
-
different eglin c variants with differing inhibitory potential versus matriptase, construction, expression and purification of eglin c variants and screening for inhibitory potency, overview, R1K'4-eglin has the wild-type Pro45 at P1 position and Tyr49 at P4' position residues replaced with Arg and Lys, respectively, leads to the production of a selective, high affinity and proteolytically stable inhibitor of matriptase, molecular modeling of enzyme-inhibitor complex, overview
R1K4-eglin
-
wild type eglin c with Pro45 at P1 position and Tyr49 residues at P4 position replaced with Arg and Lys respectively, most potent, selective, high affinity and proteolytically stable inhibitor
R4R1-eglin
-
with substituted P42 and L45 for arginine residues, variants containing an Arg or Lys at position 49 instead of the original Tyr residue show enhanced inhibition
scFv antibody E2
-
competitive mechanism of inhibition of the scFv antibody enzyme inhibitors, which competes with substrate binding in the S1 site, the antibody binds to a number of residues flanking the active site, forming a unique three-dimensional binding epitope
-
scFv antibody S4
-
competitive mechanism of inhibition of the scFv antibody enzyme inhibitors, which competes with substrate binding in the S1 site, the antibody binds to a number of residues flanking the active site, forming a unique three-dimensional binding epitope
-
sulfated 3-amidinophenylalanine derivatives
deiverse variants, overview
-
L-arginyl-N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
-
L-arginyl-N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
docking of the inhibitor in the active site of matriptase, structure, overview
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
inhibitor completely prevents matriptase zymogen activation in human adenocarcinoma cell lines AsPC-1 and BxPC-3. Pro-urokinase-type plasminogen activator activation is completely abolished by matriptase inhibition. Matriptase inhibitors reduce the phosphorylation of the HGF receptor/cMet and the overall cellular invasiveness of the human pancreatic adenocarcinoma cell line AsPC-1
4-(1-[3-carbamimidoyl-N-[(4'-ethylbiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
4-(1-[3-carbamimidoyl-N-[(4'-ethylbiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
inhibitor completely prevents matriptase zymogen activation in human adenocarcinoma cell lines AsPC-1 and BxPC-3. Pro-urokinase-type plasminogen activator activation is completely abolished by matriptase inhibition. Matriptase inhibitors reduce the phosphorylation of the HGF receptor/cMet and the overall cellular invasiveness of the human pancreatic adenocarcinoma cell line AsPC-1
4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride
-
inhibition of IGFBP-rP1 processing
benzyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
-
-
benzyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
-
inhibitor completely prevents matriptase zymogen activation in human adenocarcinoma cell lines AsPC-1 and BxPC-3. Pro-urokinase-type plasminogen activator activation is completely abolished by matriptase inhibition. Matriptase inhibitors reduce the phosphorylation of the HGF receptor/cMet and the overall cellular invasiveness of the human pancreatic adenocarcinoma cell line AsPC-1
hepatocyte growth factor activator inhibitor
-
HAI-1, the cognate transmembrane inhibitor of the enzyme, which is coexpressed with matriptase in epithelium
-
hepatocyte growth factor activator inhibitor
HAI-1, conventional protease inhibitor
-
hepatocyte growth factor activator inhibitor
-
active protease is inhibited by, and forms complexes with, hepatocyte growth factor activator inhibitor (HAI-1)
-
hepatocyte growth factor activator inhibitor 1
-
following matriptase activation, the active enzyme is immediately inhibited by binding to hepatocyte growth factor activator inhibitor 1, resulting in stable matriptase-hepatocyte growth factor activator inhibitor 1 complexes that are rapidly secreted
-
hepatocyte growth factor activator inhibitor 1
-
HAI-1, a Kunitz-type inhibitor that functions both as a chaperone and a reversible inhibitor
-
hepatocyte growth factor activator inhibitor-1
i.e. HAI-1, binding is reversible and acid labile
-
hepatocyte growth factor activator inhibitor-1
-
HAI-1
-
hepatocyte growth factor activator inhibitor-1
-
HAI-1, a Kunitz-type transmembrane serine protease inhibitor, cognate inhibitor of matriptase with regulatory function, molecular mechanism of inhibition, domain structure of HAI-1, proteolytic processing during maturation, activation, and shedding, enzyme-inhibitor complex structure, overview, the level of HAI-1 expression seems to be an important factor in the regulation of matriptase zymogen activation
-
hepatocyte growth factor activator inhibitor-1
-
HAI-1, forms complexes wih the enzyme in vivo
-
hepatocyte growth factor activator inhibitor-1
-
HAI-1, without HAI-1 active matriptase may become unstable, leading to its degradation and low protein expression
-
hepatocyte growth factor activator inhibitor-1
-
is required for proper development of placenta, overview
-
hepatocyte growth factor activator inhibitor-1
-
activated matriptase is immediately inhibited by and forms complex with hepatocyte growth factor activator inhibitor-1
-
sunflower trypsin inhibitor-1
-
and several derivatives with different amino acid side chains, overview
sunflower trypsin inhibitor-1
SFTI-1, GRCTKSIPPICFPD, the plant-derived cyclic peptide is a promising drug scaffold with potent matriptase inhibitory activity, three-dimensional structure of the inhibitor and the protease domain of matriptase, molecular modeling, overview
additional information
analysis of interaction of matriptase-2 with prototype low-molecular weight ligands using site-directed mutagenesis, kinetic analysis and molecular modeling, substrate/inhibitor-enzyme interactions, overview
-
additional information
analysis of interaction of matriptase-2 with prototype low-molecular weight ligands using site-directed mutagenesis, kinetic analysis and molecular modeling, substrate/inhibitor-enzyme interactions, overview
-
additional information
design and synthesis of potent, selective inhibitors of matriptase, overview. Design of a class of potent and selective peptidomimetic inhibitors of matriptase based on the P4-P1 (Arg-Gln-Ala-Arg) portion of the activation peptide of matriptase, to which is linked a C-terminal serine trap in the form of a ketobenzothiazole group. The ketobenzothiazole serine trap is selected to form a covalent and reversible bond with the catalytic serine residue of the enzyme. Importance of stereochemistry at the P1 position for inhibitory potency
-
additional information
peptide inhibitor docking study with matriptase and matriptase-2, overview
-
additional information
-
not inhibited by leupeptin, pepstatin and N-(R)-(2-(hydroxyaminocarbonyl)methyl)-4-methylpentanoyl-L-3-(2'-naphthyl)alaninyl-L-alanine 2-aminoethyl amide
-
additional information
-
autoinhibitory role of the LDLRA modules that may prevent premature activation of matriptase in the absence of appropriate activation stimuli
-
additional information
-
inhibition of matriptase activation in vitro and in vivo, overview
-
additional information
-
inhibitor design and synthesis, inhibitory potency and structure-activity relationships, overview, matriptase blockade could potentially modulate tumorigenesis and metastasis in vivo
-
additional information
-
no inhibition of IGFBP-rP1 processing by leupeptin, pepstatin, and N-(R)-(2-(hydroxyaminocarbonyl)methyl)-4-methylpentanoyl-l-3-(2'-naphthyl)alaninyl-l-alanine 2-aminoethyl amide, i.e. TAPI-1
-
additional information
controlled by a serpin complex, consisting of antithrombin III, alpha1-antitrypsin and alpha2-antiplasmin
-
additional information
-
controlled by a serpin complex, consisting of antithrombin III, alpha1-antitrypsin and alpha2-antiplasmin
-
additional information
-
the enzyme is competitively inhibited by the anti-MT-SP1 antibody FabE2
-
additional information
inhibitor design, synthesis of diverse 5-substituted phenylene1,3-bis(oxy) dibenzimidamide analogues, overview. Anaysis of cytotoxic effects of inhibitors
-
additional information
-
inhibitor design, synthesis of diverse 5-substituted phenylene1,3-bis(oxy) dibenzimidamide analogues, overview. Anaysis of cytotoxic effects of inhibitors
-
additional information
O-(3-carbamimidoylphenyl)-L-serine amides as matriptase inhibitors, overview. Analysis of cytotoxic effects of inhibitors
-
additional information
synthesis of high-affinity cyclic peptide matriptase inhibitors. An analogue of Momordica cochinchinensis trypsin inhibitor-II (MCoTI-II) is one of the most potent inhibitors of matriptase, structure-activity relationships of SFTI-1 and MCoTI-II, which is a structurally divergent trypsin inhibitor also containing a cyclic backbone
-
additional information
generation of monoclonal antibodies against mutant N164Q/R614A and use as inhibitors. Two antibodies are competitive inhibitors and able to block the activity of wild-type full-length matriptase in complex biological samples by binding near the active site
-
additional information
-
generation of monoclonal antibodies against mutant N164Q/R614A and use as inhibitors. Two antibodies are competitive inhibitors and able to block the activity of wild-type full-length matriptase in complex biological samples by binding near the active site
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4,4'-diisothiocyanatostilbene-2,2' disulfonic acid
-
as an early response to acidosis, matriptase activation can also be induced by perturbation of intracellular pH homeostasis using substances inhibiting Na+/H+ exchangers or other acid-base ion channels
5-(N-ethyl-N-isopropyl)-amiloride
-
as an early response to acidosis, matriptase activation can also be induced by perturbation of intracellular pH homeostasis using substances inhibiting Na+/H+ exchangers or other acid-base ion channels
5-(N-methyl-N-isobutyl)-amiloride
-
as an early response to acidosis, matriptase activation can also be induced by perturbation of intracellular pH homeostasis using substances inhibiting Na+/H+ exchangers or other acid-base ion channels
C2 ceramide 1-phosphate
-
weaker activator than sphingosine 1-phosphate, activation at 0.000237 mM
C8 ceramide 1-phosphate
-
weaker activator than sphingosine 1-phosphate, activation at 0.001 mM
Epidermal growth factor
-
stimulates the release of matripase/hepatocyte growth factor activator inhibitor-1 complexes
H+
-
exposure of epithelial and carcinoma cells to a mildly acidic extracellular milieu pH 6.0 results in robust matriptase activation
hepatocyte growth factor activator inhibitor
HAI-1, zymogen activator of matriptase
-
Ibuprofen
-
matriptase zymogen is down-regulated in the UROtsa cells by ibuprofen
N-acetylglucosaminyltransferase V
-
the transient overexpression of N-acetylglucosaminyltransferase V, MGAT5, significantly enhances the activity of matriptase
-
prostasin
-
prostasin stimulates the conversion of the cell-associated 70-kDa matriptase zymogen to the two-chain active form. Prostasin induces matriptase zymogen activation in intestinal epithelial cells to regulate closure of the paracellular pathway. But active recombinant matriptase, however, does not require the expression of endogenous prostasin for barrier-forming activity
-
serum
from human, horse, mouse, rat, rabbit, duck, chicken, goat, calf, turtle and foetal bovine serum, leads to increase of the level of the active two-chain form
-
sphingosine 1-phosphate
-
activation at 0.00001 mg/ml, activation is dependent on Ca2+
sphingosine 1-phosphate
-
mediates translocation of the enzyme to cell-cell junctions, sphingosine 1-phosphate-induced matripase activation is enhancend by reduced hepatocyte growth factor activator inhibitor-1 expression
additional information
-
activation of the matriptase zymogen requires sequential N-terminal cleavage, activation site autocleavage, and transient association with HAI-1, different activation mechanisms, matriptase translocates to the cell surface and is activated within min after exposure of breast cancer cells to sphingosine-1-phosphate, a serum-derived lipid that signals through specific G-protein-coupled receptor, this activation process was shown to require actin cytoskeleton remodeling, overview
-
additional information
-
prolonged stabilization of matriptase by GnT-V-mediated glycosylation in vivo, thus extending its half-life and permitting it to play role in the early phases of papillary carcinoma, but not in its later phase progression, overview
-
additional information
-
the enzyme is induced by lysophospholipids, androgens, and the polyanionic suramin, the agents induce different signaling pathways and cellular events in a cell type-specific manner leading to matriptase activation, which requires an intact lipid bilayer microenvironment, enzyme activation within the range of pH 5.2-7.2, overview, inhibition of matriptase activation in vitro and in vivo, overview
-
additional information
-
zymogen activation is stimulated by suramin, lysophosphatidic acid, and sphingosine 1-phosphate, overview
-
additional information
controlled by a serpin complex, consisting of antithrombin III, alpha1-antitrypsin and alpha2-antiplasmin
-
additional information
-
controlled by a serpin complex, consisting of antithrombin III, alpha1-antitrypsin and alpha2-antiplasmin
-
additional information
-
under normal conditions the activity of matriptase is tightly regulated by the endogenous hepatocyte growth factor activator inhibitors HAI-1 and, or HAI-2
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
35.5
ABZ-Ile-Arg-Ala-Arg-Ser-Ala-Ala-Tyr(3-NO2)-NH2
pH and temperature not specified in the publication
8.35
ABZ-Ile-Arg-Ala-Arg-Ser-Ala-Gly-Tyr(3-NO2)-NH2
pH and temperature not specified in the publication
24.5
ABZ-Ile-Arg-Ala-Arg-Ser-Ala-Ser-Tyr(3-NO2)-NH2
pH and temperature not specified in the publication
0.38
Boc-Gln-Ala-Arg-4-nitroanilide
pH and temperature not specified in the publication, recombinant c-Myc-tagged mutant
0.00381
N-tert-butoxycarbonyl-gamma-benzyl-Glu-Ala-Arg-7-amido-4-methylcoumarin
pH 8.5
0.0475
N-tert-butoxycarbonyl-gamma-benzyl-Glu-Gly-Arg-7-amido-4-methylcoumarin
pH 8.5
0.024
Boc-Gln-Ala-Arg-4-nitroanilide
pH and temperature not specified in the publication, recombinant c-Myc-tagged mutant H665F
0.19
Boc-Gln-Ala-Arg-4-nitroanilide
pH and temperature not specified in the publication, recombinant c-Myc-tagged mutant A757S
0.21
Boc-Gln-Ala-Arg-4-nitroanilide
pH and temperature not specified in the publication, recombinant c-Myc-tagged wild-type enzyme
0.62
Boc-Gln-Ala-Arg-4-nitroanilide
pH and temperature not specified in the publication, recombinant c-Myc-tagged mutant L785S
0.83
Boc-Gln-Ala-Arg-4-nitroanilide
pH and temperature not specified in the publication, recombinant c-Myc-tagged mutant A757S/L785S
1
Boc-Gln-Ala-Arg-4-nitroanilide
above, pH and temperature not specified in the publication, recombinant c-Myc-tagged mutant E712Y
1
Boc-Gln-Ala-Arg-4-nitroanilide
above, pH and temperature not specified in the publication, recombinant c-Myc-tagged mutant E712Y/A757S/L785S
0.159
butyloxycarbonyl-L-Gln-L-Ala-L-Arg-4-nitroanilide
-
purified matriptase-2, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.21
butyloxycarbonyl-L-Gln-L-Ala-L-Arg-4-nitroanilide
-
matriptase-2 in conditioned medium of HEK-MT2 cells, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.381
butyloxycarbonyl-L-Gln-L-Ala-L-Arg-4-nitroanilide
-
recombinant human matriptase, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.00489
N-tert-butoxycarbonyl-Gln-Ala-Arg 7-amido-4-methylcoumarin
pH 8.5
additional information
additional information
-
pre-steady-state and steady-state kinetics, stopped-flow, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.24
ABZ-Ile-Arg-Ala-Arg-Ser-Ala-Ala-Tyr(3-NO2)-NH2
pH and temperature not specified in the publication
3.79
ABZ-Ile-Arg-Ala-Arg-Ser-Ala-Gly-Tyr(3-NO2)-NH2
pH and temperature not specified in the publication
2.66
ABZ-Ile-Arg-Ala-Arg-Ser-Ala-Ser-Tyr(3-NO2)-NH2
pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.2
ABZ-Ile-Arg-Ala-Arg-Ser-Ala-Ala-Tyr(3-NO2)-NH2
pH and temperature not specified in the publication
450.4
ABZ-Ile-Arg-Ala-Arg-Ser-Ala-Gly-Tyr(3-NO2)-NH2
pH and temperature not specified in the publication
109.8
ABZ-Ile-Arg-Ala-Arg-Ser-Ala-Ser-Tyr(3-NO2)-NH2
pH and temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000457
1-[(4S)-4-amino-5-(1,3-benzothiazol-2-yl)-5-oxopentyl]guanidine
matriptase, pH and temperature not specified in the publication
0.0000014
2-(L-alanyl-L-arginyl)-1,3-benzothiazole
matriptase, pH and temperature not specified in the publication
0.0061
L-arginyl-L-glutaminyl-N-[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-hydroxypentan-2-yl]-L-alaninamide
matriptase, pH and temperature not specified in the publication
0.0000046
L-arginyl-N1-[(2S)-1-[[(2R)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
matriptase, pH and temperature not specified in the publication
0.000000011 - 0.0000033
L-arginyl-N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
0.0000095
L-arginyl-N1-[(2S)-1-[[(2S)-6-amino-1-(1,3-benzothiazol-2-yl)-1-oxohexan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
matriptase, pH and temperature not specified in the publication
0.000052 - 0.1
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
0.003 - 0.28
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
0.000000088
N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
matriptase, pH and temperature not specified in the publication
0.000003
(1r,4r)-4-amino-N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)cyclohexanecarboxamide
pH 8.5, temperature not specified in the publication
0.000001
(1r,4r)-4-aminocyclohexyl 3,5-bis(4-carbamimidoylphenoxy)benzoate
pH 8.5, temperature not specified in the publication
0.00018
(2R)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylic acid
-
-
0.011
(2S)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylic acid
-
-
0.000018
1-(2-aminoethyl)-N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)piperidine-4-carboxamide
pH 8.5, temperature not specified in the publication
0.000061
1-(3-aminopropanoyl)-N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)piperidine-4-carboxamide
pH 8.5, temperature not specified in the publication
0.000031
1-(N-[[3-(b-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-3-carboxamide
-
-
0.000013
1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-4-carboxamide
-
-
0.00005
2-Nas-Phe(3-Am)-4-(2-guanidinoethyl)piperidide
pH 8.0, recombinant catalytic enzyme domain
0.001182
3,5-bis(4-carbamimidoylphenoxy)-N-((4-hydroxycyclohexyl)methyl)benzamide
pH 8.5, temperature not specified in the publication
0.000204
3,5-bis(4-carbamimidoylphenoxy)-N-(1-(2-hydroxyethyl)piperidin-4-yl)benzamide
pH 8.5, temperature not specified in the publication
0.000591
3,5-bis(4-carbamimidoylphenoxy)-N-(4-fluorophenyl)benzamide
pH 8.5, temperature not specified in the publication
0.000301
3,5-bis(4-carbamimidoylphenoxy)-N-(4-hydroxycyclohexyl)benzamide
pH 8.5, temperature not specified in the publication
0.00077
3,5-bis(4-carbamimidoylphenoxy)-N-(4-methylcyclohexyl)benzamide
pH 8.5, temperature not specified in the publication
0.000411
3,5-bis(4-carbamimidoylphenoxy)-N-(cyclohexylmethyl)benzamide
pH 8.5, temperature not specified in the publication
0.000592
3,5-bis(4-carbamimidoylphenoxy)-N-cyclohexylbenzamide
pH 8.5, temperature not specified in the publication
0.00162
3,5-bis(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.0000025
3-(3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-ethylbiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl)benzenecarboximidamide
-
-
0.000046
3-[(2R)-3-[4-(2-carbamimidamidoethyl)piperidin-1-yl]-2-[(naphthalen-2-ylsulfonyl)amino]propyl]benzenecarboximidamide
-
-
0.000001
3-[(2S)-2-([[3-(4-aminobutyl)phenyl]sulfonyl]amino)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxopropyl]benzenecarboximidamide
-
0.000013
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(1H-indol-5-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
0.000028
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(2-methylpyrimidin-4-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
0.00000008 - 0.0000001
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
0.0000016
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-aminopyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
0.000012
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[4'-(1-methylethoxy)biphenyl-3-yl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
0.00011
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[(biphenyl-3-ylsulfonyl)amino]-3-oxopropyl]benzenecarboximidamide
-
0.0003
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[(naphthalen-2-ylsulfonyl)amino]-3-oxopropoxy]benzenecarboximidamide
pH and temperature not specified in the publication
0.0000067
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[([3-[(3-aminopropyl)amino]phenyl]sulfonyl)amino]-3-oxopropyl]benzenecarboximidamide
-
0.000029
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(2'-chlorobiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
0.0000054
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(3',4'-dimethoxybiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
0.000091
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(3'-chlorobiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
0.000026
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-chlorobiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
0.000006
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-ethoxybiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
0.0000025
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-ethylbiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
0.000007
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4'-methoxybiphenyl-3-yl)sulfonyl]amino]-3-oxopropyl]benzenecarboximidamide
-
0.0003
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[[(4-cyclohexylphenyl)sulfonyl]amino]-3-oxopropoxy]benzenecarboximidamide
pH and temperature not specified in the publication
0.0001
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxo-2-([[2,4,6-tri(propan-2-yl)phenyl]sulfonyl]amino)propoxy]benzenecarboximidamide
pH and temperature not specified in the publication
0.000047
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxo-2-[[(3-pyridin-3-ylphenyl)sulfonyl]amino]propyl]benzenecarboximidamide
-
0.00006
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-3-oxo-2-[[(3-pyridin-4-ylphenyl)sulfonyl]amino]propyl]benzenecarboximidamide
-
0.0015
3-[(2S)-3-[4-(4-aminobutanoyl)piperidin-1-yl]-3-oxo-2-([[2,4,6-tri(propan-2-yl)phenyl]sulfonyl]amino)propoxy]benzenecarboximidamide
pH and temperature not specified in the publication
0.0017
3-[(2S)-3-[4-(b-alanyl)piperidin-1-yl]-3-oxo-2-([[2,4,6-tri(propan-2-yl)phenyl]sulfonyl]amino)propoxy]benzenecarboximidamide
pH and temperature not specified in the publication
0.000082
3-[(2S)-3-[4-(N-carbamimidoyl-b-alanyl)piperazin-1-yl]-3-oxo-2-([[2,4,6-tris(1-methylethyl)phenyl]sulfonyl]amino)propyl]benzenecarboximidamide
pH 8.0, recombinant catalytic enzyme domain
0.00073
4,4'-((5-(1,2,3,4-tetrahydroisoquinoline-2-carbonyl)-1,3-phenylene)bis(oxy))dibenzimidamide
pH 8.5, temperature not specified in the publication
0.000094
4,4'-((5-(4-(2-aminoethyl)piperidine-1-carbonyl)-1,3-phenylene)bis(oxy))dibenzimidamide
pH 8.5, temperature not specified in the publication
0.00198
4,4'-((5-(4-fluorophenylsulfonamido)-1,3-phenylene)bis(oxy))dibenzimidamide
pH 8.5, temperature not specified in the publication
0.000305
4,4'-((5-(decahydroquinoline-1-carbonyl)-1,3-phenylene)bis(oxy))dibenzimidamide
pH 8.5, temperature not specified in the publication
0.00179
4,4'-((5-(naphthalene-2-sulfonamido)-1,3-phenylene)bis(oxy))dibenzimidamide
pH 8.5, temperature not specified in the publication
0.000218
4,4'-[(3-[[(4-fluorophenyl)sulfonyl]amino]pyridine-2,6-diyl)bis(oxy)]dibenzenecarboximidamide
pH 8.5, temperature not specified in the publication
0.00106
4,4'-[(5-aminobenzene-1,3-diyl)bis(oxy)]dibenzenecarboximidamide
pH 8.5, temperature not specified in the publication
0.000177
4-(1-[3-carbamimidoyl-N-[(3-pyrrolidin-1-ylphenyl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
0.000028
4-(1-[3-carbamimidoyl-N-[(4'-ethoxybiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
0.000024 - 0.0000245
4-(1-[3-carbamimidoyl-N-[(4'-ethylbiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
0.000087
4-(1-[N-[(4'-tert-butylbiphenyl-3-yl)sulfonyl]-3-carbamimidoyl-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
0.000014
4-([1-[(2S)-3-(3-carbamimidoylphenyl)-2-([[2,4,6-tris(1-methylethyl)phenyl]sulfonyl]amino)propanoyl]piperidin-4-yl]carbonyl)piperidine-1-carboximidamide
pH 8.0, recombinant catalytic enzyme domain
0.000026
4-([1-[(2S)-3-(3-carbamimidoylphenyl)-2-[[(4-cyclohexylphenyl)sulfonyl]amino]propanoyl]piperidin-4-yl]carbonyl)piperidine-1-carboximidamide
-
-
0.000545
4-aminocyclohexyl 3,5-bis(4-carbamimidoylphenoxy)benzoate
pH 8.5, temperature not specified in the publication
0.2
4-[1-(3-carbamimidoyl-N-[[3-(1H-imidazol-1-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
0.000024
4-[1-(3-carbamimidoyl-N-[[3-(2-oxopiperazin-1-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
0.00003
4-[1-(3-carbamimidoyl-N-[[3-(2-oxopiperidin-1-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
0.000098
4-[1-(3-carbamimidoyl-N-[[3-(6-oxopyridazin-1(6H)-yl)phenyl]sulfonyl]-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
0.00000043
4-[1-(N-[[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
0.00001
4-[1-(N-[[3-(6-aminopyridin-3-yl)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
0.0000063
4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]-N-methylbutanamide
-
-
0.000012
4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]butanamide
-
-
0.000255
4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]butanoic acid
-
-
0.000053
4-[4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazin-1-yl]-N-methyl-4-oxobutanamide
-
-
0.00000013
9-fluorenylmethyloxycarbonyl-GR-ketobenzothiazole
pH not specified in the publication, temperature not specified in the publication
0.0000061 - 0.0000075
benzyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
0.00022 - 0.01
benzylsulfonyl-D-arginyl-proline-(2-aminomethyl-5-chlorobenzyl)-amide bis(trifluoroacetate)
0.000055 - 0.00019
benzylsulfonyl-D-arginyl-proline-(4-amidinobenzyl)amide bis-(trifluoroacetate)
0.0021 - 0.01
benzylsulfonyl-D-cyclohexylalanyl-proline-(2-aminomethyl-5-chlorobenzyl)amide
0.000026
D-hTyr-Ala-4-amidinobenzylamide
pH 8.0, temperature not specified in the publication
0.000041
ethyl (3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)carbamate
-
0.00185
ethyl 4-(3,5-bis(4-carbamimidoylphenoxy)benzamido)piperidine-1-carboxylate
pH 8.5, temperature not specified in the publication
0.000065
ethyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
-
-
0.0001
methyl (2R)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylate
-
-
0.0024
methyl (2S)-1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidine-2-carboxylate
-
-
0.0000061
methyl 4-[1-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperidin-4-yl]butanoate
-
-
0.000003
N-((1r,4r)-4-aminocyclohexyl)-3,5-bis((3-carbamimidoylbenzyl)oxy)benzamide
pH 8.5, temperature not specified in the publication
0.000023
N-((1r,4r)-4-aminocyclohexyl)-3,5-bis((4-carbamimidoylbenzyl)oxy)benzamide
pH 8.5, temperature not specified in the publication
0.001698
N-((1r,4r)-4-aminocyclohexyl)-3,5-bis(4-(aminomethyl)phenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.000006
N-((1r,4r)-4-aminocyclohexyl)-3-((3-carbamimidoylbenzyl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.00026
N-((1r,4r)-4-aminocyclohexyl)-3-((4-bromobenzyl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.00001
N-((1r,4r)-4-aminocyclohexyl)-3-((4-carbamimidoylbenzyl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.00203
N-((1r,4r)-4-aminocyclohexyl)-3-((6-aminopyridin-3-yl)oxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.000793
N-((1r,4r)-4-aminocyclohexyl)-3-((6-bromopyridin-3-yl)methoxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.000116
N-((1r,4r)-4-aminocyclohexyl)-3-(4-(3-aminopropanamido)phenoxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.00004
N-((1r,4r)-4-aminocyclohexyl)-3-(4-(aminomethyl)phenoxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.00113
N-((1r,4r)-4-aminocyclohexyl)-3-(4-aminophenoxy)-5-(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.00047
N-((1r,4r)-4-aminocyclohexyl)-3-(4-carbamimidoylphenoxy)-5-((4-chlorobenzyl)oxy)benzamide
pH 8.5, temperature not specified in the publication
0.000824
N-((1r,4r)-4-aminocyclohexyl)-3-(4-carbamimidoylphenoxy)-5-(4-carbamoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.000141
N-(1-(3-aminopropyl)piperidin-4-yl)-3,5-bis(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.000026
N-(2-aminoethyl)-1-(3-carbamimidoyl-N-[[2,4,6-tris(1-methylethyl)phenyl]sulfonyl]-L-phenylalanyl)piperidine-4-carboxamide
pH 8.0, recombinant catalytic enzyme domain
0.000018
N-(3,5-bis(4-carbamimidoylphenoxy)phenyl)-1-(2-hydroxyethyl)piperidine-4-carboxamide
pH 8.5, temperature not specified in the publication
0.0000067
N-(3-[[(1R)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)ethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.00047
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-(2-methylpiperidin-1-yl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.000053
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-(4-methylpiperidin-1-yl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.000037
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-oxo-2-piperazin-1-ylethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.000033
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-oxo-2-piperidin-1-ylethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.000016
N-(3-[[(1S)-1-(3-carbamimidoylbenzyl)-2-[4-[4-(methylamino)-4-oxobutyl]piperidin-1-yl]-2-oxoethyl]sulfamoyl]phenyl)azetidine-3-carboxamide
-
-
1
N-(3-[[(1S)-1-[[4-(2-aminoethyl)piperidin-1-yl]carbonyl]-3-phenylpropyl]sulfamoyl]phenyl)-beta-alaninamide
larger than 1
1
N-(3-[[(1S)-1-[[4-(2-aminoethyl)piperidin-1-yl]carbonyl]-4-phenylbutyl]sulfamoyl]phenyl)-beta-alaninamide
larger than 1
0.000017
N-(3-[[(1S)-2-(4-benzylpiperidin-1-yl)-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.00012
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-3-hydroxypropanamide
-
0.0000066
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-b-alaninamide
pH 8.0, recombinant catalytic enzyme domain
0.0000038
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
0.000003
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)azetidine-3-carboxamide
-
0.00018
N-(3-[[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)propanamide
-
0.0000018
N-(3-[[(1S)-2-[4-(2-carbamimidamidoethyl)piperidin-1-yl]-1-(3-carbamimidoylbenzyl)-2-oxoethyl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.0000038
N-(3-[[(2S)-1-[4-(2-aminoethyl)piperidin-1-yl]-3-(3-carbamimidoylphenyl)-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.000036
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-oxo-1-(piperazin-1-yl)propan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
-
0.00001
N-(4-aminocyclohexyl)-3,5-bis(4-carbamimidoylphenoxy)benzamide
pH 8.5, temperature not specified in the publication
0.0037
N-(4-aminocyclohexyl)-O-(3-carbamimidoylphenyl)-N2-(naphthalen-2-ylsulfonyl)-L-serinamide
pH and temperature not specified in the publication
0.00077
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C
0.0021
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C
0.000145
N-[(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-[3-(aminomethyl)benzyl]-2-oxoethyl]-4'-methoxybiphenyl-3-sulfonamide
-
0.00015
N-[3-([(1S)-1-(3-carbamimidoylbenzyl)-2-[4-(4-hydroxyphenyl)piperazin-1-yl]-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
-
0.01
N-[3-([(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-benzyl-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
0.000056
N-[3-([(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-[3-(aminomethyl)benzyl]-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
0.0028
N-[3-([(1S)-2-[4-(2-aminoethyl)piperidin-1-yl]-1-[4-(aminomethyl)benzyl]-2-oxoethyl]sulfamoyl)phenyl]-beta-alaninamide
-
0.000055
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C
0.00022
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C
0.000004
R1K'4-eglin
-
pH 9.0, recombinant His-tagged amino acids 596-855 of matriptase
0.000000011
L-arginyl-N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
matriptase, pH and temperature not specified in the publication
0.0000033
L-arginyl-N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide
matriptase-2, pH and temperature not specified in the publication
0.000052
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant H665F
0.00021
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S
0.00029
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged wild-type enzyme
0.015
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant L785S
0.02
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S/L785S
0.02
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y
0.1
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y/A757S/L785S
0.003
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant H665F
0.037
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged wild-type enzyme
0.075
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S
0.2
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y
0.2
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y/A757S/L785S
0.22
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant L785S
0.28
N-(benzylsulfonyl)-3-cyclohexylalanyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S/L785S
0.000046
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant H665F
0.00016
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S
0.00019
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged wild-type enzyme
0.0012
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant L785S
0.0016
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S/L785S
0.02
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y
0.03
N2-(benzylsulfonyl)arginyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y/A757S/L785S
0.0026
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant H665F
0.03
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged wild-type enzyme
0.054
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant L785S
0.069
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S
0.2
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y
0.2
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y/A757S/L785S
0.62
N2-(benzylsulfonyl)arginyl-N-[2-(aminomethyl)-5-chlorobenzyl]-L-prolinamide
pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S/L785S
0.00000008
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
0.0000001
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-([[3-(6-amino-2,3,4,5-tetrahydropyridin-3-yl)phenyl]sulfonyl]amino)-3-oxopropyl]benzenecarboximidamide
-
-
0.000024
4-(1-[3-carbamimidoyl-N-[(4'-ethylbiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
0.0000245
4-(1-[3-carbamimidoyl-N-[(4'-ethylbiphenyl-3-yl)sulfonyl]-L-phenylalanyl]piperidin-4-yl)-N-methylbutanamide
-
-
0.000005
Aprotinin
-
matriptase-2 in conditioned medium of HEK-MT2 cells, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.0000098
Aprotinin
-
recombinant human matriptase, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.000013
Aprotinin
-
purified matriptase-2, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.0000061
benzyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
-
-
0.0000075
benzyl 4-(N-[[3-(beta-alanylamino)phenyl]sulfonyl]-3-carbamimidoyl-L-phenylalanyl)piperazine-1-carboxylate
-
-
0.00022
benzylsulfonyl-D-arginyl-proline-(2-aminomethyl-5-chlorobenzyl)-amide bis(trifluoroacetate)
-
recombinant human matriptase, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.01
benzylsulfonyl-D-arginyl-proline-(2-aminomethyl-5-chlorobenzyl)-amide bis(trifluoroacetate)
-
Ki above 0.01 mM, matriptase-2 in conditioned medium of HEK-MT2 cells, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.01
benzylsulfonyl-D-arginyl-proline-(2-aminomethyl-5-chlorobenzyl)-amide bis(trifluoroacetate)
-
Ki above 0.01 mM, purified matriptase-2, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.000055
benzylsulfonyl-D-arginyl-proline-(4-amidinobenzyl)amide bis-(trifluoroacetate)
-
recombinant human matriptase, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.00017
benzylsulfonyl-D-arginyl-proline-(4-amidinobenzyl)amide bis-(trifluoroacetate)
-
purified matriptase-2, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.00019
benzylsulfonyl-D-arginyl-proline-(4-amidinobenzyl)amide bis-(trifluoroacetate)
-
matriptase-2 in conditioned medium of HEK-MT2 cells, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.0021
benzylsulfonyl-D-cyclohexylalanyl-proline-(2-aminomethyl-5-chlorobenzyl)amide
-
recombinant human matriptase, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.01
benzylsulfonyl-D-cyclohexylalanyl-proline-(2-aminomethyl-5-chlorobenzyl)amide
-
Ki above 0.01 mM, matriptase-2 in conditioned medium of HEK-MT2 cells, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.01
benzylsulfonyl-D-cyclohexylalanyl-proline-(2-aminomethyl-5-chlorobenzyl)amide
-
Ki above 0.01 mM, purified matriptase-2, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.00029
benzylsulfonyl-D-cyclohexylalanyl-proline-(4-amidinobenzyl)-amide
-
matriptase-2 in conditioned medium of HEK-MT2 cells, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.00046
benzylsulfonyl-D-cyclohexylalanyl-proline-(4-amidinobenzyl)-amide
-
purified enzyme, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.00077
benzylsulfonyl-D-cyclohexylalanyl-proline-(4-amidinobenzyl)-amide
-
recombinant human matriptase, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.0019
leupeptin
-
recombinant human matriptase, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.0024
leupeptin
-
matriptase-2 in conditioned medium of HEK-MT2 cells, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
0.0041
leupeptin
-
purified matriptase-2, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C
additional information
additional information
-
inhibition kinetics with antobodies E2 and S4 and point mutants thereof, overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5
CJ-730
Homo sapiens
-
3-amidinophenylalanine-based inhibitor CJ-730: although CJ-730 completely inhibits pro-HGF activation in PC3 cells, the IC50 value is determined to be 100fold above the Ki value. This discrepancy suggests that the inhibitory effect is possibly due to non-specific inhibition of proteases other than matriptase
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
quantitative expression analysis of matriptase-1 in breast cancer samples, overview
additional information
quantitative expression analysis of matriptase-1 in breast cancer samples, overview
additional information
-
quantitative expression analysis of matriptase-2 in breast cancer samples, overview
additional information
quantitative expression analysis of matriptase-2 in breast cancer samples, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
8.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
of ductal carcinomas in situ, and grade I-III invasive ductal carcinomas
-
RT-PCR analysis reveal a 1000fold higher matriptase expression in human pancreatic adenocarcinoma AsPC-1 cells than in the MDA-MB-435S cells
-
ovarian clear cell adenocarcinoma cells, high level expression of IGFBP-rP1-cleaving enzyme
-
using immunohistochemistry a significant overexpression of matriptase is shown in pancreatic carcinoma compared to normal pancreatic ducts
-
only matriptase-HAI-1 complexes and not latent matriptase are detected in urine and seminal fluid
-
contains only activated matriptase in complex with hepatocyte growth factor activator inhibitor-1 or antithrombin III but no latent matriptase
additional information
matriptase-2 is exclusively expressed in the liver initially under zymogen form
-
proportional increases or decreases in matripase and hepatocyte growth factor activator inhibitor-1
co-expression of matriptase and its substrate serine protease prostasin
strong expression association between matriptase and its substrate prostasin in breast cancer
-
cells target latent matriptase to the basolateral plasma membrane where activation, inhibition, and secretion of matriptase take place. A proportion of matriptase-HAI-1 complexes, but not the latent matriptase, undergoes transcytosis to the apical plasma membrane for secretion
-
latent matriptase is localized at the basolateral surface of the ductal epithelial cells of prostate and kidney
-
matriptase expression is correlated with tumor progression in epithelium-derived cancer cells
-
matriptase is up-regulated in a variety of cancers and correlates closely with disease progression
-
the secretion of matriptase from cancer cells is increased via the action of GnT-V, i.e. UDP-N-acetylglucosamine:alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase, overview
-
matriptase-dependent cell surface proteolysis in epithelial development and pathogenesis, overview
-
co-expression and co-localization of both matriptase and HAI-1 in many epithelial cells, complex formation, overview
-
tracheal, esophageal, gastric, broncheal and alveolar, of scretory duct, intestinal, a dof the urogenityl tract, overview
matriptase and prostasin display a near identical spatial expression pattern in the epithelial compartment of breast cancer tissue
-
in cancer tissue the expression of serine protease SNC19/matripase and hepatocyte growth factor activator inhibitor-1 is significantly lower than in the corresponding adjacent normal tissue, the ratio, however, shows no difference between normal and malingant tissue
-
latent matriptase is localized at the basolateral plasma membrane of the ductal epithelial cells of the prostate and kidney
-
latent matriptase is localized at the basolateral surface of the ductal epithelial cells of prostate and kidney
-
enzyme expression in normal and neoplastic mast cells, almost all different mast cells types in humans express matriptase, overview
-
gastric carcinoma cells, high level expression of IGFBP-rP1-cleaving enzyme
-
RT-PCR analysis reveal a 1000fold higher matriptase expression in human pancreatic adenocarcinoma AsPC-1 cells than in the MDA-MB-435S cells
-
expression determined by quantitative RT-PCR, highest expression among different prostate cancer cell lines
-
latent matriptase is localized at the basolateral plasma membrane of the ductal epithelial cells of the prostate and kidney
-
latent matriptase is localized at the basolateral surface of the ductal epithelial cells of prostate and kidney
-
44.1% of papillary carcinomas, 15.4% of follicular adenomas, none follicular or anaplastic carcinomas
-
co-expression of matriptase and N-acetylglucosaminyltransferase V in thyroid cancer tissues, analysis of expression of GnT-V and matriptase in thyroid neoplasm tissues, papillary carcinoma and follicular carcinoma, overview
-
contains only activated matriptase in complex with hepatocyte growth factor activator inhibitor-1 but no latent matriptase
-
only matriptase-HAI-1 complexes and not latent matriptase are detected in urine and seminal fluid
additional information
-
no activity in foreskin fibroblasts or HT-1080 fibrosacroma cells
additional information
-
stomach carcinoma cell line, low level in AZ521 cell, SCH cell, STKM-2 cell, MDA-MB cell, MMK-29 cell, YLC cell, KKI-cell, LU-65 cell and A549 cell,high level in STKM-1, RCM-1 cell, LU-99 cell and VMRC-LCP cell
additional information
-
expression profile of matriptase in cancer tissues, overview
additional information
-
matriptase-1 expression analysis, no matriptase-1 expression in cell lines: MDA-MB-157, MDA-MB-436, MDA-MB-453, MDA-MB-43S5, IRB.3.G, MIA-PACA-2, EJ-138, T-24, G-361, ECV-304, PLC-PRF-5, and in endothelial cells, overview
additional information
matriptase-1 expression analysis, no matriptase-1 expression in cell lines: MDA-MB-157, MDA-MB-436, MDA-MB-453, MDA-MB-43S5, IRB.3.G, MIA-PACA-2, EJ-138, T-24, G-361, ECV-304, PLC-PRF-5, and in endothelial cells, overview
additional information
-
matriptase-2 expression analysis, no matriptase-2 expression in cell lines: MDA-MB-157, MDA-MB-231, MDA-MB-436, MDA-MB-453, MDA-MB-43S5, BT549, PC-3, DU-145, CA-HPV-10, HT-115, HRT-18, MRC5, IRB.3.G, MIA-PACA-2, EJ-138, T-24, A-549, G-361, ECV-304, and in endothelial cells, overview
additional information
matriptase-2 expression analysis, no matriptase-2 expression in cell lines: MDA-MB-157, MDA-MB-231, MDA-MB-436, MDA-MB-453, MDA-MB-43S5, BT549, PC-3, DU-145, CA-HPV-10, HT-115, HRT-18, MRC5, IRB.3.G, MIA-PACA-2, EJ-138, T-24, A-549, G-361, ECV-304, and in endothelial cells, overview
additional information
-
no activity in chondrocytes within cartilage, in stromal fibroblasts, hepatocytes, pneumocytes, cardiac muscle, and smooth muscle of uterine myometrium
additional information
-
no endogenous expression of matriptase, prostasin or EGFR in HEK-293 cells
additional information
-
no IGFBP-rP1 processing activity in HSC-4 cells, HEK-293 cells, HLE cells, MKN-45 cells, HT-1080 cells, EJ-1 cells, and ECV-304 cells, the soluble form of active matriptase cleaves IGFBP-rP1 but HAI-1 or some other inhibitors block its activity in culture medium
additional information
-
tissue distribution, overview, postnatal expression pattern, overview
additional information
-
matriptase is expressed in prostate, breast and colorectal cancers in vitro and in vivo
additional information
-
not detected in MDA-MB-231, SUM1315, BT-549, and SUM-159 cells
additional information
not detected in MDA-MB-231, SUM1315, BT-549, and SUM-159 cells
additional information
-
expression of matriptase and prostasin in breast cancer cell lines, overview. No activity in MDA-MB-231 cells, SUM-159 cells, SUM-1315cells, and BT-549 cells
additional information
expression of matriptase and prostasin in breast cancer cell lines, overview. No activity in MDA-MB-231 cells, SUM-159 cells, SUM-1315cells, and BT-549 cells
additional information
matriptase co-localizes with hemagglutinin at the apical surface of human epithelial cells and within endosomes. No expression in A-549 cells
additional information
-
matriptase co-localizes with hemagglutinin at the apical surface of human epithelial cells and within endosomes. No expression in A-549 cells
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
a proportion of matriptase-hepatocyte growth factor activator inhibitor-1 complexes, but not the latent matriptase, undergo transcytosis to the apical plasma membrane for secretion
-
latent matriptase is localized at the basolateral surface of the ductal epithelial cells of prostate and kidney and in Caco-2 cells. The cells target latent matriptase to the basolateral plasma membrane where activation, inhibition, and secretion of matriptase take place
additional information
the cytoplasmic domain of the enzyme contains an endocytosis motif that mediates the internalization of cell surface enzyme in a dynamin-dependent manner, Iron depletion does not affect the internalization of cell surface enzyme
with a C-terminal protease domain directed to the extracellular space and a stem region with domains of different types, between the transmembrane domain near the N-terminus and the protease domain
-
matriptase translocates to the cell surface and is activated within min after exposure of breast cancer cells to sphingosine-1-phosphate requiring actin cytoskeleton remodeling
-
the catalytic domain of matriptase is located in the extracellular space
-
acid-induced matriptase activation takes place both on the cell surface and inside the cells, likely due to the parallel intracellular acidification that activates intracellular matriptase
-
acid-induced matriptase activation takes place both on the cell surface and inside the cells, likely due to the parallel intracellular acidification that activates intracellular matriptase
-
-
matriptase is a type II transmembrane trypsin-like serine protease
-
matriptase-2 is a type II transmembrane serine protease
-
lacks a classical signal peptide, and the N-terminal signal anchor, which is not removed during synthesis, functions as a single-span transmembrane domain that orients the protease in the plasma membrane as a type II integral membrane protein with a cytoplasmic N-terminus and an extracellular C-terminus
-
matriptase is a type II transmembrane trypsin-like serine protease
-
matriptase-2 is a type II transmembrane serine protease, the short intracellular domain of matriptase, residues 1-54, interact directly with the actin-associated protein filamin, and likely serves to locate matriptase to microdomains of the plasma membrane
additional information
-
no enzyme in tumor surrounding stromal cells and the extracellular matrix, overview
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
evolution
malfunction
metabolism
-
the matriptase zymogen is capable of intermolecular autoproteolytic activation, and the active enzyme is also an effective activator of the prostasin zymogen through direct proteolytic cleavage at its zymogen activation site. Prostasin is required for matriptase activation in intestinal epithelial cells to regulate closure of the paracellular pathway. 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. Matriptase and not prostasin is the primary effector protease of tight junction assembly in simple columnar epithelia
physiological function
additional information
evolution
matriptase-2 belongs to the family of type II transmembrane serine proteases
evolution
matriptase-2 belongs to the family of type II transmembrane serine proteases, representing an emerging class of cell surface proteolytic enzymes. Matriptase-2 shares high sequence similarity with matriptase, particularly in the catalytic domain which is about 45% identical
malfunction
matriptase-2 is important for iron homeostasis. Human patients with iron-refractory iron deficiency anemia show mutation in the TMPRSS6 gene
malfunction
a mutation in matriptase is implicated in autosomal recessive ichtyosis withhypotrichosis a rare skin disease
malfunction
downregulation of the enzyme stabilizes fetuin-A in the unprocessed form
malfunction
lack of the putative endocytosis motif in the cytoplasmic domain largely abolishes the sensitivity of the enzyme to iron depletion
physiological function
matriptase-2 regulates iron metabolism through proteolytic cleavage of hemojuvelin, a cell surface protein that regulates hepcidin expression through a bone morphogeneic protein/SMAD pathway
physiological function
deregulation of matriptase can lead to various pathologies. Matriptase is thought to be implicated in osteoarthritis by initiating and inducting cartilage destruction
physiological function
matriptase-2 is a regulatory protease controlling iron homeostasis
physiological function
the enzyme controls the expression of hepcidin, the key regulator of iron homeostasis. By cleaving hepcidin, the enzyme supresses bone morphogenetic protein against decapentaplegic signaling
physiological function
the enzyme suppresses the expression of hepatic hepcidin, an iron regulatory hormone, by cleaving membrane hemojuvelin into an inactive form. Hemojuvelin is a bone morphogenetic protein coreceptor. Regulation of the enzyme occurs at the level of protein degradation rather than by changes in the rate of internalization and translational or transcriptional mechanisms, the cytoplasmic enzyme domain is necessary for its regulation
physiological function
the enzyme suppresses the expression of hepcidin, the main regulator of systemic iron homeostasis, through cleavage of the bone morphogenetic protein co-receptor hemojuvelin, matriptase-2 plays an important role in iron homeostasis
evolution
matriptase shares high sequence similarity with matriptase-2, particularly in the catalytic domain which is about 45% identical
malfunction
-
matriptase expression down-regulated with matriptase-targeting siRNA effectively abolishes pro-HGF activation
malfunction
-
two novel heterozygous mutations are described within the matriptase-2 gene of monozygotic twin girls exhibiting an iron-refractory iron deficiency anemia phenotype. A frameshift mutation (P686fs) caused by the insertion of the four nucleotides CCCC in exon 16 (2172_2173insCCCC) that is predicted to terminate translation before the catalytic serine. A di-nucleotide substitution c.467C to A and c.468C to T in exon 3 that causes the missense mutation A118D in the sea urchin sperm protein, enteropeptidase, agrin (SEA) domain of the extracellular stem region of matriptase-2
malfunction
expression of matriptase is frequently dysregulated in human cancers
malfunction
siRNA knockdown of matriptase by 80.0% in human bronchial epithelial cells significantly blocks influenza virus replication in these cells
malfunction
-
siRNA silencing of matriptase expression or inhibition of matriptase activity impairs development of transepithelial electrical resistance and increases the permeability of Caco-2 epithelial barriers
physiological function
-
both matriptase and a specific peptide agonist for proteinase-activated receptor 2 are able to induce intracellular calcium mobilization and inhibition of proliferation in cultured human HaCaT keratinocytes. Results suggest that proteinase-activated receptor 2 is a substrate for matriptase in human skin in vivo. Deregulation of these proteins delineates squamous cell carcinoma progression
physiological function
-
exogenous matriptase significantly enhances cytokine-stimulated cartilage collagenolysis, while matriptase alone causes significant collagenolysis from osteoarthritis cartilage, which is metalloproteinase-dependent. Matriptase also induces metalloproteinase-1, -3, -13 gene expression. Synovial perfusion data confirm that matriptase activates proteinase activated receptor-2, and matriptase-dependent enhancement of collagenolysis from osteoarthritis cartilage is blocked by proteinase activated receptor-2 inhibition
physiological function
-
matriptase efficiently activates hepatocyte growth factor
physiological function
the matriptase-prostasin cascade plays a critical role in breast cancer
physiological function
-
TMPRSS6 controls iron homeostasis through its negative regulation of expression of hepcidin, a key hormone involved in iron metabolism
physiological function
matriptase is a regulator of the epidermal sodium channel
physiological function
matriptase is a serine protease implicated in cancer invasion and metastasis, matriptase activates latent growth factors such as hepatocyte growth factor/scatter factor, and proteases such as urokinase plasminogen activator
physiological function
matriptase is a trypsin-like serine protease with specific proteolytic activity downstream of an arginine residue at the cleavage site. Matriptase proteolytically activates influenza virus and promotes multicycle replication in the human airway epithelium. Influenza viruses do not encode any proteases and must rely on host proteases for the proteolytic activation of their surface hemagglutinin proteins in order to fuse with the infected host cells
physiological function
matriptase is involved in tumor pathogenesis
physiological function
matriptase performs cleavage activation of the human-adapted influenza virus subtypes exhibiting both subtype and strain specificities
physiological function
-
matriptase promotes intestinal epithelial barrier formation
physiological function
the type II transmembrane serine protease matriptase is a key activator of multiple signaling pathways associated with cell proliferation and modification of the extracellular matrix
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
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
physiological function
-
loss of cell surface protease inhibitor HAI-2 in intestinal epithelial cells leads to unrestrained matriptase activity and efficient cleavage of epithelial cell adhesion molecule EPCAM. Congenital tufting enteropathy-associated HAI-2 mutant proteins exhibit reduced ability to inhibit matriptase and also fail to efficiently stabilize claudin-7 in intestinal epithelial cells
additional information
in Hep-G2 cells stably expressing the coding sequence of gene TMPRSS6, encoding the enzyme, incubation with apo-transferrin or the membrane-impermeable iron chelator deferoxamine mesylate salt, increases enzyme levels. This increase does not result from the inhibition of enzyme shedding from the cells
additional information
putative substrate binding mode, molecular docking, overview
additional information
-
putative substrate binding mode, molecular docking, overview
additional information
structural differences between matriptase-2 and matriptase, the enzyme-ligand interactions of matriptase-2 involve four important amino acids, His 665, Glu 712, Ala 757, Leu785. In the active site, matriptase-2 and matriptase vary in relevant amino acids participating in the formation of the S1 and S2 pockets and the S3/S4 binding region. Location of His665, Glu712, Ala757 and Leu785 in the active site of matriptase-2, overview
additional information
structural differences between matriptase-2 and matriptase, the enzyme-ligand interactions of matriptase-2 involve four important amino acids, His 665, Glu 712, Ala 757, Leu785. In the active site, matriptase-2 and matriptase vary in relevant amino acids participating in the formation of the S1 and S2 pockets and the S3/S4 binding region. Location of His665, Glu712, Ala757 and Leu785 in the active site of matriptase-2, overview
additional information
a three-pronged model for the action of matriptase: activation of incoming viruses in the extracellular space in its shed form, upon viral attachment or exit in its membrane-bound and/or shed forms at the apical surface of epithelial cells, and within endosomes by its membrane-bound form where viral fusion takes place
additional information
-
a three-pronged model for the action of matriptase: activation of incoming viruses in the extracellular space in its shed form, upon viral attachment or exit in its membrane-bound and/or shed forms at the apical surface of epithelial cells, and within endosomes by its membrane-bound form where viral fusion takes place
additional information
comparison of trypsin and matriptase active sites, overview
additional information
structural differences between matriptase-2 and matriptase. In the active site, matriptase-2 and matriptase vary in relevant amino acids participating in the formation of the S1 and S2 pockets and the S3/S4 binding region
additional information
structural differences between matriptase-2 and matriptase. In the active site, matriptase-2 and matriptase vary in relevant amino acids participating in the formation of the S1 and S2 pockets and the S3/S4 binding region
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). TMPS6_HUMAN
811
0
90000
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
-
immunoblotting, matripase-hepatocyte growth factor activator inhibitor-1 complex
110
-
Western blot analysis using seminal fluid, seminal fluid contains only activated matriptase in complex with antithrombin III, supposed 70 kDa active matriptase and a 40 kDa antithrombin III-fragment
110000
120000
130000
-
SDS-PAGE and Western blot, reducing conditions, matriptase-hepatcyte growth factor activator inhibitor-1 complex
25000
serine protease domain, identified by SDS-PAGE, Western blot analysis and LC-MS,MS, without serpin complex
29000
30000
45000
noncatalytic domain, identified by SDS-PAGE, Western blot analysis and LC-MS,MS
60000
-
serine protease domain, dimer, determined by SDS-PAGE and Western blot analysis
70000
75000
80000
85000
95000
110000
-
gelatin zymography or immunoblotting, matripase/hepatocyte growth factor activator inhibitor complex
120000
-
immunoblotting, 70000 active matripase plus full-length hepatocyte growth factor activator inhibitor-1
120000
-
SDS-PAGE, reducing condition, and Western blot, activated form of matriptase in complex with hepatocyte growth factor activator inhibitor 1
120000
-
x * 95000, single-chain latent enzyme, SDS-PAGE, x * 120000, active enzyme in complex with inhibitor HAI-1, SDS-PAGE
30000
-
serine protease domain, determined by SDS-PAGE and Western blot analysis
30000
-
x * 70000, matriptase zymogen, SDS-PAGE, x * 30000, matriptase serine protease domain, SDS-PAGE
70000
-
SDS-PAGE, reducing condition, and Western blot, latent form of matriptase
70000
-
x * 70000, matriptase zymogen, SDS-PAGE, x * 30000, matriptase serine protease domain, SDS-PAGE
80000
serine protease domain, identified by SDS-PAGE, Western blot analysis and LC-MS,MS, including serpin complex
80000
-
x * 95000, full-length transmembrane isoform, SDS-PAGE, x * 80000, Gly149-early processed isoform, SDS-PAGE, x * 26000-29000, activated recombinant truncated wild-type catalytic domain, SDS-PAGE
85000
-
immunoblotting, full-length hepatocyte growth factor activator inhibitor-1 complexed with the serine protease domain of matripase
85000
-
SDS-PAGE and Western blot, reducing conditions, cleaved form of the enzyme
85000
-
Western blot analysis using seminal fluid, seminal fluid contains only activated matriptase in complex with hepatocyte growth factor activator inhibitor-1 (HAI-1), supposed 70 kDa active matriptase and a 15 kDa HAI-fragment
95000
complex can be converted by boiling to matriptase plus a 40000 Da protein doublet
95000
-
gelatin zymography or immunoblotting, matripase/hepatocyte growth factor activator inhibitor complex
95000
-
Western blot analysis using seminal fluid or urine, seminal fluid or urine contain only activated matriptase in complex with hepatocyte growth factor activator inhibitor-1 (HAI-1), supposed 70 kDa active matriptase and a 25 kDa HAI-fragment
95000
-
x * 95000, full-length transmembrane isoform, SDS-PAGE, x * 80000, Gly149-early processed isoform, SDS-PAGE, x * 26000-29000, activated recombinant truncated wild-type catalytic domain, SDS-PAGE
95000
-
x * 95000, single-chain latent enzyme, SDS-PAGE, x * 120000, active enzyme in complex with inhibitor HAI-1, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heteromer
noncatalytic domain 45 kDa, serine protease domain 25 kDa, serpins 55 kDa
additional information
?
-
x * 75000-80000, single-chain latent enzyme, SDS-PAGE, x * 95000-110000, active enzyme in complex with inhibitor HAI-1, SDS-PAGE
?
-
x * 95000, full-length transmembrane isoform, SDS-PAGE, x * 80000, Gly149-early processed isoform, SDS-PAGE, x * 26000-29000, activated recombinant truncated wild-type catalytic domain, SDS-PAGE
?
-
x * 95000, single-chain latent enzyme, SDS-PAGE, x * 120000, active enzyme in complex with inhibitor HAI-1, SDS-PAGE
?
-
x * 70000, matriptase zymogen, SDS-PAGE, x * 30000, matriptase serine protease domain, SDS-PAGE
additional information
the type II transmembrane protease is composed of a short cytoplasmic domain, a transmembrane domain, and a large extracellular domain, which contains a membrane-proximal stem region, a predicted activation domain, and a C-terminal catalytic domain
additional information
-
generation of the 26 kDa soluble form in matriptase expressing cells is not strictly autocatalytic and may involve other proteases, molecular modeling of wild-type and mutant G287R active site structures
additional information
-
matriptase-2 contains a short cytoplasmic amino terminal tail, a transmembrane region, a stem region containing two CUB domains and three LDL receptor class A domains, and at the carboxy terminal a trypsin-like serine protease domain, domain structure, structure-function relationship, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
sea urchin sperm protein, enteropeptidase, and agrin (SEA) domain is O-glycosylated
proteolytic modification
glycoprotein
proteolytic modification
proteolytic modification
the 811-amino-acid human protein is synthesized as an inactive zymogen and autoactivated by proteolytic cleavage
proteolytic modification
Matriptase is expressed in epithelial cells as a zymogen and needs to be activated. It undergoes spontaneous hydrolysis of a peptide bond at the Gly149 in the SEA domain. The protease is then autocatalytically processed and activated through cleavage at Arg614 within the RQAR614-VVGG activation sequence. Matriptase-2 is exclusively expressed in the liver initially under zymogen form. Matriptase-2 undergoes autocatalysis at Arg576 within the PSSR576-IVGG sequence located in the consensus activation site of its pro-domain
glycoprotein
-
matriptase contains four functional N-glycosylation sites, Asn109, 302, 485, and 772, whereas the inactivation of Asn109 and Asn485 has no effect on the activation of matriptase, glycosylation of the first CUB domain, Asn302, and the catalytic domain, Asn772, is required for zymogen activation in cultured breast cancer cells
glycoprotein
-
prolonged stabilization of matriptase by GnT-V-mediated glycosylation in vivo, thus extending its half-life and permitting it to play role in the early phases of papillary carcinoma, but not in its later phase progression, overview
proteolytic modification
-
one-chain zymogen is converted to an active two-chain protease, enzyme with mutation in its catalytic triad is unable to undergo this activational cleavage
proteolytic modification
-
activation of the matriptase zymogen requires sequential N-terminal cleavage, activation site autocleavage, and transient association with HAI-1, the mature single-chain proenzyme is first cleaved after Gly149 located in a conserved GSVIA motif in the N-terminal SEA domain by an unknown proteolytic activity or possibly by nonenzymatic hydrolysis of the dependent on SEA domain cleavage, matriptase next is converted into its active conformation by proteolytic cleavage after Arg614 within the highly conserved activation cleavage site R-VVGG in the serine protease domain
proteolytic modification
-
autocatalytic cleavage from the zymogen to the active form, autocatalytic activation cleavage at Arg614, and processing at the Gly149 site after which the enzyme remains associated with the membrane, the recombinant refolded truncated wild-type zymogen is capable to autoactivate, overview
proteolytic modification
-
matriptase is activated by cleavage at the activation sequence RQAR-/-V
proteolytic modification
-
MT-SP1 is activated by cleavage at Arg614 with the catalytic domain remaining attached to the upstream domains via a disulfide bond, the activation cleavage sequence of MT-SP1 is RXQXAXRXXV, MT-SP1 is able to autoactivate both in solution in the membrane-bound form
proteolytic modification
-
proteolytic processing during maturation, activation, and shedding, molecular mechanism of zymogen activation and autoactivation, cleavage at Gly149 within the SEA domain, overview, the level of HAI-1 expression seems to be an important factor in the regulation of matriptase zymogen activation, matriptase zymogen activation may be regulated by two independent mechanisms: a soluble, cytosolic suppressor and autonomous, lipid anchored activation machinery at the lipid bilayer biomembrane
proteolytic modification
-
matriptase is synthesized as a zymogen and undergoes autoactivation to become an active protease
proteolytic modification
-
matriptase is synthesized as a zymogen and undergoes autoactivation to become an active protease that is immediately inhibited by, and forms complexes with, hepatocyte growth factor activator inhibitor (HAI-1)
proteolytic modification
-
the matriptase zymogen performs its own activation via autoproteolysis, also mutants S805A-matriptase and G827R-matriptase are readily cleaved to the two-chain form by recombinant matriptase
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexed with benzamidine or bovine panreatic trypsin inhibitor, hanging drop vapor diffusion method
-
molecular docking of inhibitor. The P1 and P2 binding sites are occupied by the conserved Arg and then the variable second side chain, respectively. The 9-fluorenylmethyloxycarbonyl group forms pi-pi interactions with the conserved Trp in the P4 pocket
mutant N164Q/R614A/S805A, to 2.5 A resolution. The structure of zymogen matriptase reveals a classical chymotrypsin-like zymogen fold
purified recombinant refolded His-tagged matriptase catalytic domain in complex with benzamidine, 2-Nas-Phe(3-Am)-4-(2-guanidinoethyl)piperidide, and 4-([1-[(2S)-3-(3-carbamimidoylphenyl)-2-([[2,4,6-tris(1-methylethyl)phenyl]sulfonyl]amino)propanoyl]piperidin-4-yl]carbonyl)piperidine-1-carboximidamide, hanging drop vapor diffusion method, 18°C, 5 mg/mL matriptase, from 10 mM benzamidine, 0.1 M Tris-HCl, pH 8.5, 20% PEG 8000, and 200 mM MgCl2, X-ray diffraction structure determination and analysis at 2.1-2.2 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A757S
site-directed mutagenesis, the mutant shows altered sensitivity to inhibition by prototype low-molecular weight ligands compared to the wild-type enzyme
A757S/L785S
site-directed mutagenesis, the mutant shows altered sensitivity to inhibition by prototype low-molecular weight ligands compared to the wild-type enzyme
D521N
point mutations D521N and E522K located in the conserved D/NXSDE motif in the LDLa2 domain of matriptase-2 are associated with iron-refractory iron deficiency anemia in patients and affect residues predicted to bind Ca2+. In vitro, the D521N and E522K mutants show reduced cell surface localization, increased Golgi retention, impaired autoactivation of matriptase-2, impaired cleavage of hemojuvelin, and impaired ability to repress Hamp1 reporter expression but are able to bind hemojuvelin
E522K
point mutations D521N and E522K located in the conserved D/NXSDE motif in the LDLa2 domain of matriptase-2 are associated with iron-refractory iron deficiency anemia in patients and affect residues predicted to bind Ca2+. In vitro, the D521N and E522K mutants show reduced cell surface localization, increased Golgi retention, impaired autoactivation of matriptase-2, impaired cleavage of hemojuvelin, and impaired ability to repress Hamp1 reporter expression but are able to bind hemojuvelin
E712Y
site-directed mutagenesis, the mutant shows altered sensitivity to inhibition by prototype low-molecular weight ligands compared to the wild-type enzyme
E712Y/A757S/L785S
site-directed mutagenesis, the mutant shows altered sensitivity to inhibition by prototype low-molecular weight ligands compared to the wild-type enzyme
G442R
matriptase-2 containing the point mutation G442R located in the second CUB domain demonstrate impaired autoactivation, are still able to bind but demonstrate reduced cleavage of coexpressed hemojuvelin, and exhibit reduced ability to repress HAMP reporter expression
H665F
site-directed mutagenesis, the mutant shows altered sensitivity to inhibition by prototype low-molecular weight ligands compared to the wild-type enzyme
L785S
site-directed mutagenesis, the mutant shows altered sensitivity to inhibition by prototype low-molecular weight ligands compared to the wild-type enzyme
R774C
point mutation identified in an iron-refractory iron deficiency anemia patient is located in the protease domain and disrupts accurate C32/C36 or C35/C37 disulfide bonding within the protease domain
S762A
protease dead mutation is shown in vitro to be ineffective in repressing Hamp1 reporter expression
A118D
-
mutation causes an intra-molecular structural imbalance that impairs matriptase-2 activation
D217A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
D60A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
D799A
-
matripase mutant altered in the substrate binding pocket, is able to traffic in the absence of hepatocyte growth factor activator inhibitor-1
D96A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
E169A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
F94A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
F97A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
G827R
H143A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
I41A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
I60A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
K224A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
L153A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
N164Q/R614A
mutation at activation cleavage site, variant is locked in the zymogen form, about 3% of wild-type activity
N164Q/R614A/S805A
mutation at activatio, plus mutant cleavage site, variant is locked in the zymogen form, plus mutation S805A to prevent unwanted proteolytic degradation during crystallization
N302Q
N485Q
N772Q
N95A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
Q145A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
Q174A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
Q175A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
Q221A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
Q38A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
R222A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
R60A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
R87A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
S805A
T150A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
T98A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
Y146A
-
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview
additional information
G827R
a naturally occuring missense mutation in the highly conserved peptidase S1S6 domain, causing autosomal recessive ichthyosis with hypotrichosis syndrome, characterized by congenital ichthyosis associated with abnormal hair, phenotype, overview
G827R
-
naturally occurring mutation, the rare congenital human disorder, autosomal recessive ichthyosis with hypotrichosis is linked to homozygosity for a C2672GA mutation located in exon 19 of the ST14 gene, phenotype, overview
G827R
-
the mutation in the catalytic domain causes autosomal recessive Ichthyosis with hypotrichosis, the G827R mutant is catalytically inactive and does not perform autoproteolysis due to a blockade of access to the binding/catalytic cleft of the enzyme, molecular modeling, overview, elevated expression levels compared to the wild-type enzyme, the G827R substitution does not impair the ability of the protease to localize at the cell surface
N302Q
-
significant resistance to degradation in the N-acetylglucosminyltransferase V transfectants
N485Q
-
significant resistance to degradation in the N-acetylglucosminyltransferase V transfectants
N772Q
-
completely degraded in the N-acetylglucosminyltransferase V transfectants
S805A
-
matripase mutant altered in the catalytic triad, is able to traffic in the absence of hepatocyte growth factor activator inhibitor-1
S805A
-
mutation of a catalytic residue, inactive mutant, elevated expression levels compared to the wild-type enzyme
additional information
costruction of enzyme mutants with deletion of first 9 amino acids or the first 46 amino acids
additional information
-
generation of the 26 kDa soluble form in matriptase expressing cells is not strictly autocatalytic and may involve other proteases
additional information
-
mutations in any of the residues of the catalytic triad render matriptase unable to undergo activation site cleavage, inactivating mutations in the Ca2+-binding motifs of any or all of the four LDLRA domains prevents the activation of matriptase
additional information
-
pathogenesis of dysregulated matriptase activity, dysregulated matriptase potently supports epithelial transformation, overview
additional information
-
small interfering RNAs for matriptase efficiently block both the matriptase expression and the cleavage of IGBP-rP1 in OVISE cells
additional information
-
when implanting enzyme overexpressing Mat-AZ521 cells into nude mice subcutaneously or intraperitoneally, Mat-AZ521 cells grew faster and produced much larger solid tumors than the control cells, overexpression shortened the survival time of tumor-bearing mice, number and the size of blood vessels in tumor tissues are significantly higher in the Mat-AZ521 tumors than in the control cells
additional information
-
penta-alanine mutants 2-8 and 7-11 show 4 and 4.5fold enhanced proteolytic activity as compared to the wild type enzyme, respectively
additional information
-
siRNA knockdown of the enzyme in MCF-7 cells using three independent non-overlapping synthetic RNA duplexes
additional information
siRNA knockdown of the enzyme in MCF-7 cells using three independent non-overlapping synthetic RNA duplexes
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
prolonged stabilization of matriptase by GnT-V-mediated glycosylation in vivo, thus extending its half-life and permitting it to play role in the early phases of papillary carcinoma, but not in its later phase progression, overview
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant c-Myc-tagged enzyme from HEK cells by immunoaffinity chromatography
by immobilized metal-chelate affinity chromatography and ion exchange chromatography
-
from human milk using a CM-Sepharose FF column and a HAI-1 immunoaffinity column
from N-acetylglucosminyltransferase V transfectant by immunoaffinity chromatography
-
native enzyme from colon carcinoma cell line DLD-1 by gel filtration, dialysis, adsorption chromatography, abion exchange chromatography, and freeze-drying
-
recombinant His-tagged amino acids 596-855 of matriptase from Escherichia coli strain M15 by metal affinity chromatography, dialysis, and anion exchange chromatography
-
recombinant refolded His-tagged matriptase catalytic domain nickel affinity chromatography
recombinant truncated wild-type zymogen and mutant G287R from Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene TMPRSS6, expression of C-terminally c-Myc-tagged wild-type and mutant enzymes in HEK-293 cells
gene TMPRSS6, expression of C-terminally c-Myc-tagged wild-type and truncated mutant enzymes in Hep-G2 cells
amino acid residues 596 to 855 and 615 to 855, corresponding to the active sites and catalytic domains of the peptide, respectively, are expressed with a N-terminal His tag in Escherichia coli
-
DNA and amino acid sequence comparison, genetic structure, phylogenetic analysis, regulation of enzyme expression, overview
-
expression of His-tagged amino acids 596-855 of matriptase in Escherichia coli strain M15
-
expression of mutant S805A in BT549 breast cancer cells, expression of truncated wild-type zymogen and mutant G287R, comprising residues 596-855 and consisting of the C-terminal end of the fourth LDLRA domain, the activation domain, and the catalytic domain, in Escherichia coli in inclusion bodies, expression of wild-type enzyme in HEK-293 cells
-
expression of the His-tagged matriptase catalytic domain in Escherichia coli strain BL21(DE3) in inclusion bodies
gene ST14, localization at 11q24.3-q25, DNA and amino acid sequence determination and anaylsis, genotyping
into a pEF6-V5-His-TOPO plasmid vector for transfection of human PC-3 and DU-145 cells
-
overexpression in stomach cancer cell line AZ521, Mat-AZ521 cells release an active form of matriptase into culture medium
-
recombinant human matriptase protease domain is expressed in Escherichia coli and Saccharomyces cerevisiae
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in Hep-G2 cells stably expressing the coding sequence of gene TMPRSS6, encoding the enzyme, incubation with apo-transferrin or the membrane-impermeable iron chelator deferoxamine mesylate salt, increases enzyme levels. This increase does not result from the inhibition of enzyme shedding from the cells
immunoreactivity of matriptase, hepatcyte growth factor activator inhibitor-1 and proteinase-activated receptor 2 is shown to be diminished in basal cell carcinomas
-
matriptase gene expression is significantly elevated in patients with osteoarthritis cartilage compared with patients with fracture to the neck of the femur cartilage
-
RT-PACR analysis reveal a 1000fold higher matriptase expression in human pancreatic adenocarcinoma AsPC-1 cells than in the MDA-MB-435S cells
-
using immunohistochemistry a significant overexpression of matriptase is shown in pancreatic carcinoma compared to normal pancreatic ducts
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged matriptase catalytic domain from Escherichia coli strain BL21(DE3) inclusion bodies by denaturation with 6 M guanidinium hydrochloride, and refolding by dilution in 50 mM Tris-HCl, 0.5 M L-arginine, 20 mM CaCl2, 1 mM EDTA, 0,1 M NaCl, and 1 mM cysteine, pH 7.5
recombinant truncated wild-type zymogen and mutant G287R from Escherichia coli inclusion bodies
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
matriptase-2 represents a target for the development of inhibitors, potentially useful in the treatment of hemochromatosis or beneficial as pharmacological tools
diagnostics
medicine
additional information
-
resistance to degradation and stabilization of beta1-6GlcNAc matripase are specifically due to the presence of beta1-6GlcNAc branching on the sugar chains, binds strongly to leukoagglutinating phytohemagglutinin, which preferentially recognizes beta1-6 GlcNAc branches of tri- or tetraantennary sugar chains, beta1-6 GlcNAc matriptase is resistant to autodegradation, as well as trypsin digestion, compared with matriptase purified from mock-transfected cells, N-glycosidase-F treatment of beta1-6 GlcNAc matriptase greatly reduces its resistance to degradation
diagnostics
-
the enzyme might be a good biomarker in treatment of malignant breast tumors
medicine
-
expression of serine protease SNC19/matripase and hepatocyte growth factor is decreased in gastrointestinal cancer tissues compared to their normal counterparts, decreased expression may correlate with invasion and lymph node metastasis
medicine
-
matripase mediates cell invasion through activation of receptor-bound pro-urokinase-type plasminogen activator
medicine
-
multiple roles for hepatocyte growth factor activator inhibitor-1 to regulate matripase, including its proper expression, intracellular trafficking, activation and inhibition
medicine
-
prolonged stabilization of matripase is stabilized by UDP-N-acetylglucosamine: alpha-mannoside beta-1,6-N-acetylglucosminyltransferase-mediated glycosylation in vivo, thus extending its halftime and permitting it to play role in the early phases of papillary carcinoma, but not in its later progression
medicine
-
inhibition of matriptase appears to suppress both primar tumor growth and metastasis, leading to considerable interest in the development of potent matriptase inhibitors as anti-cancer drugs
medicine
-
matriptase may be considered to be a potential target for the development of anti-cancer drugs
medicine
matriptase may be considered to be a potential target for the development of anti-cancer drugs
medicine
-
matriptase may play an important role in the metastasis of prostate cancer
medicine
-
upregulation of matriptase-2 reduces the aggressiveness of prostate cancer cells in vitro and in vivo
medicine
-
time-domain near infrared fluorescence (NIRF) imaging is applied to characterize expression and activity of matriptase in vivo in an orthotopic AsPC-1 pancreatic tumor model in nude mice. Strong expression and tumor-specific binding of intravenously injected antimatriptase antibody only to primary AsPC-1 tumors and their metastases is shown. Using a synthetic substrate it is shown that matriptase is proteolytically active in vitro as well as in vivo in tumor-bearing mice, and that application of synthetic active-site inhibitors can efficiently inhibit its proteolytic activity for at least 24 h
medicine
-
coexpression of matriptase with amyloid precursor protein APP695 results in site-specific cleavagesof amyloid precursor protein. Replacement of Arg-601 (Arg-5 in Abeta1-42) by Ala in APP695 prevents matriptase cleavage at this site. Overexpression of matriptase in M17 cells results in a significant reduction of the endogenous amyloid precursor protein quantity
medicine
-
in breast cancer cells, a significant amount of the 30-40-kDa serine protease inhibitor HAI-2 can translocate to and inhibit matriptase on the cell surface, followed by shedding of the matriptase-HAI-2 complex
medicine
-
loss of cell surface protease inhibitor HAI-2 in intestinal epithelial cells leads to unrestrained matriptase activity and efficient cleavage of epithelial cell adhesion molecule EPCAM. Congenital tufting enteropathy-associated HAI-2 mutant proteins exhibit reduced ability to inhibit matriptase and also fail to efficiently stabilize claudin-7 in intestinal epithelial cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sun, J.; Pons, J.; Craik, C.S.
Potent and selective inhibition of membrane-type serine protease 1 by human single-chain antibodies
Biochemistry
42
892-900
2003
Homo sapiens
Benaud, C.; Dickson, R.B.; Lin, C.Y.
Regulation of the activity of matriptase on epithelial cell surfaces by a blood-derived factor
Eur. J. Biochem.
268
1439-1447
2001
Homo sapiens (Q9Y5Y6), Homo sapiens
Lin, C.Y.; Anders, J.; Johnson, M.; Sang, Q.A.; Dickson, R.B.
Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity
J. Biol. Chem.
274
18231-18236
1999
Homo sapiens (Q9Y5Y6), Homo sapiens
Lin, C.Y.; Anders, J.; Johnson, M.; Dickson, R.B.
Purification and characterization of a complex containing matriptase and a Kunitz-type serine protease inhibitor from human milk
J. Biol. Chem.
274
18237-18242
1999
Homo sapiens
Takeuchi, T.; Harris, J.L.; Huang, W.; Yan, K.W.; Coughlin, S.R.; Craik, C.S.
Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates
J. Biol. Chem.
275
26333-26342
2000
Homo sapiens
Lee, S.L.; Dickson, R.B.; Lin, C.Y.
Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease
J. Biol. Chem.
275
36720-36725
2000
Homo sapiens (Q9Y5Y6), Homo sapiens
Benaud, C.; Oberst, M.; Hobson, J.P.; Spiegel, S.; Dickson, R.B.; Lin, C.Y.
Sphingosine 1-phosphate, present in serum-derived lipoproteins, activates matriptase
J. Biol. Chem.
277
10539-10546
2002
Homo sapiens
Friedrich, R.; Fuentes-Prior, P.; Ong, E.; Coombs, G.; Hunter, M.; Oehler, R.; Pierson, D.; Gonzalez, R.; Huber, R.; Bode, W.; Madison, E.L.
Catalytic domain structures of MT-SP1/matriptase, a matrix-degrading transmembrane serine proteinase
J. Biol. Chem.
277
2160-2168
2002
Homo sapiens
Oberst, M.D.; Williams, C.A.; Dickson, R.B.; Johnson, M.D.; Lin, C.Y.
The activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitor
J. Biol. Chem.
278
26773-26779
2003
Homo sapiens
Enyedy, I.J.; Lee, S.L.; Kuo, A.H.; Dickson, R.B.; Lin, C.Y.; Wang, S.
Structure-based approach for the discovery of bis-benzamidines as novel inhibitors of matriptase
J. Med. Chem.
44
1349-1355
2001
Homo sapiens (Q9Y5Y6)
Szabo, R.; Netzel-Arnett, S.; Hobson, J.P.; Antalis, T.M.; Bugge, T.H.
Matriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivity
Biochem. J.
290
231-242
2005
Homo sapiens, Mus musculus
-
Oberst, M.D.; Chen, L.L.; Kiyomiya, K.; Williams, C.A.; Lee, M.; Johnson, M.D.; Dickson, R.B.; Lin, C.
HAI-1 regulates activation and expression of matriptase, a membrane-bound serine protease
Am. J. Physiol.
289
C462-C470
2005
Homo sapiens
Ahmed, S.; Jin, X.; Yagi, M.; Yasuda, C.; Sato, Y.; Higashi, S.; Lin, C.Y.; Dickson, R.B.; Miyazaki, K.
Identification of membrane-bound serine proteinase matriptase as processing enzyme of insulin-like growth factor binding protein-related protein-1 (IGFBP-rP1/angiomodulin/mac25)
FEBS J.
273
615-627
2006
Homo sapiens
Desilets, A.; Longpre, J.M.; Beaulieu, M.E.; Leduc, R.
Inhibition of human matriptase by eglin c variants
FEBS Lett.
580
2227-2232
2006
Homo sapiens
Ihara, S.; Miyoshi, E.; Nakahara, S.; Sakiyama, H.; Ihara, H.; Akinaga, A.; Honke, K.; Dickson, R.B.; Lin, C.; Taniguchi, N.
Addition of beta1-6 GlcNAc branching to the oligosaccharide attached to Asn 772 in the serine protease domain of matriptase plays a pivotal role in its stability and resistance against trypsin
Glycobiology
14
139-146
2004
Homo sapiens
Ito, Y.; Akinaga, A.; Yamanaka, K.; Nakagawa, T.; Kondo, A.; Dickson, R.B.; Lin, C.Y.; Miyauchi, A.; Taniguchi, N.; Miyoshi, E.
Co-expression of matriptase and N-acetylglucosaminyltransferase V in thyroid cancer tissues - its possible role in prolonged stability in vivo by aberrant glycosylation
Glycobiology
16
368-374
2006
Homo sapiens
Suzuki, M.; Kobayashi, H.; Kanayama, N.; Saga, Y.; Suzuki, M.; Lin, C.Y.; Dickson, R.B.; Terao, T.
Inhibition of tumor invasion by genomic down-regulation of matriptase through suppression of activation of receptor-bound pro-urokinase
J. Biol. Chem.
279
14899-14908
2004
Homo sapiens
Jin, X.; Hirosaki, T.; Lin, C.Y.; Dickson, R.B.; Higashi, S.; Kitamura, H.; Miyazaki, K.
Production of soluble matriptase by human cancer cell lines and cell surface activation of its zymogen by trypsin
J. Cell. Biochem.
95
632-647
2005
Homo sapiens
Zeng, L.; Cao, J.; Zhang, X.
Expression of serine protease SNC19/matriptase and its inhibitor hepatocyte growth factor activator inhibitor type 1 in normal and malignant tissues of gastrointestinal tract
World J. Gastroenterol.
11
6202-6207
2005
Homo sapiens
Basel-Vanagaite, L.; Attia, R.; Ishida-Yamamoto, A.; Rainshtein, L.; Ben Amitai, D.; Lurie, R.; Pasmanik-Chor, M.; Indelman, M.; Zvulunov, A.; Saban, S.; Magal, N.; Sprecher, E.; Shohat, M.
Autosomal recessive ichthyosis with hypotrichosis caused by a mutation in ST14, encoding type II transmembrane serine protease matriptase
Am. J. Hum. Genet.
80
467-477
2007
Homo sapiens (Q9Y5Y6)
Lee, M.; Tseng, I.; Wang, Y.; Kiyomiya, K.; Johnson, M.D.; Dickson, R.B.; Lin, C.
Autoactivation of matriptase in vitro: requirement for biomembrane and LDL receptor domain
Am. J. Physiol. Cell Physiol.
293
C95-C105
2007
Homo sapiens
Qiu, D.; Owen, K.; Gray, K.; Bass, R.; Ellis, V.
Roles and regulation of membrane-associated serine proteases
Biochem. Soc. Trans.
35
583-587
2007
Homo sapiens, Mus musculus
Chen, M.; Chen, L.M.; Lin, C.Y.; Chai, K.X.
The epidermal growth factor receptor (EGFR) is proteolytically modified by the Matriptase-Prostasin serine protease cascade in cultured epithelial cells
Biochim. Biophys. Acta
1783
896-903
2007
Homo sapiens
Jin, X.; Yagi, M.; Akiyama, N.; Hirosaki, T.; Higashi, S.; Lin, C.Y.; Dickson, R.B.; Kitamura, H.; Miyazaki, K.
Matriptase activates stromelysin (MMP-3) and promotes tumor growth and angiogenesis
Cancer Sci.
97
1327-1334
2006
Homo sapiens
Uhland, K.
Matriptase and its putative role in cancer
Cell. Mol. Life Sci.
63
2968-2978
2006
Homo sapiens, Mus musculus
Parr, C.; Sanders, A.J.; Davies, G.; Martin, T.; Lane, J.; Mason, M.D.; Mansel, R.E.; Jiang, W.G.
Matriptase-2 inhibits breast tumor growth and invasion and correlates with favorable prognosis for breast cancer patients
Clin. Cancer Res.
13
3568-3576
2007
Homo sapiens, Homo sapiens (Q9Y5Y6)
Cheng, M.F.; Jin, J.S.; Wu, H.W.; Chiang, P.C.; Sheu, L.F.; Lee, H.S.
Matriptase expression in the normal and neoplastic mast cells
Eur. J. Dermatol.
17
375-380
2007
Homo sapiens
Bugge, T.H.; List, K.; Szabo, R.
Matriptase-dependent cell surface proteolysis in epithelial development and pathogenesis
Front. Biosci.
12
5060-5070
2007
Homo sapiens, Mus musculus
Darragh, M.R.; Bhatt, A.S.; Craik, C.S.
MT-SP1 proteolysis and regulation of cell-microenvironment interactions
Front. Biosci.
13
528-539
2008
Homo sapiens, Mus musculus
Ramsay, A.J.; Reid, J.C.; Velasco, G.; Quigley, J.P.; Hooper, J.D.
The type II transmembrane serine protease matriptase-2 - identification, structural features, enzymology, expression pattern and potential roles
Front. Biosci.
13
569-579
2008
Bos taurus, Canis lupus familiaris, Homo sapiens, Macaca mulatta, Rattus norvegicus, Mus musculus (Q9DBI0)
Lin, C.Y.; Tseng, I.C.; Chou, F.P.; Su, S.F.; Chen, Y.W.; Johnson, M.D.; Dickson, R.B.
Zymogen activation, inhibition, and ectodomain shedding of matriptase
Front. Biosci.
13
621-635
2008
Homo sapiens
Jin, J.S.; Cheng, T.F.; Tsai, W.C.; Sheu, L.F.; Chiang, H.; Yu, C.P.
Expression of the serine protease, matriptase, in breast ductal carcinoma of Chinese women: correlation with clinicopathological parameters
Histol. Histopathol.
22
305-309
2007
Homo sapiens
Desilets, A.; Beliveau, F.; Vandal, G.; McDuff, F.O.; Lavigne, P.; Leduc, R.
Mutation G827R in matriptase causing autosomal recessive Ichthyosis with hypotrichosis yields an inactive protease
J. Biol. Chem.
283
10535-10542
2008
Homo sapiens
Steinmetzer, T.; Schweinitz, A.; Stuerzebecher, A.; Doennecke, D.; Uhland, K.; Schuster, O.; Steinmetzer, P.; Mueller, F.; Friedrich, R.; Than, M.E.; Bode, W.; Stuerzebecher, J.
Secondary amides of sulfonylated 3-amidinophenylalanine. New potent and selective inhibitors of matriptase
J. Med. Chem.
49
4116-4126
2006
Homo sapiens (Q9Y5Y6)
Li, P.; Jiang, S.; Lee, S.L.; Lin, C.Y.; Johnson, M.D.; Dickson, R.B.; Michejda, C.J.; Roller, P.P.
Design and synthesis of novel and potent inhibitors of the type II transmembrane serine protease, matriptase, based upon the sunflower trypsin inhibitor-1
J. Med. Chem.
50
5976-5983
2007
Homo sapiens
Farady, C.J.; Sun, J.; Darragh, M.R.; Miller, S.M.; Craik, C.S.
The mechanism of inhibition of antibody-based inhibitors of membrane-type serine protease 1 (MT-SP1)
J. Mol. Biol.
369
1041-1051
2007
Homo sapiens
List, K.; Bugge, T.H.; Szabo, R.
Matriptase: potent proteolysis on the cell surface
Mol. Med.
12
1-7
2006
Homo sapiens
Jiang, S.; Li, P.; Lee, S.L.; Lin, C.Y.; Long, Y.Q.; Johnson, M.D.; Dickson, R.B.; Roller, P.P.
Design and synthesis of redox stable analogues of sunflower trypsin inhibitors (SFTI-1) on solid support, potent inhibitors of matriptase
Org. Lett.
9
9-12
2007
Homo sapiens
Tsui, K.H.; Chang, P.L.; Feng, T.H.; Chung, L.C.; Sung, H.C.; Juang, H.H.
Evaluating the function of matriptase and N-acetylglucosaminyltransferase V in prostate cancer metastasis
Anticancer Res.
28
1993-1999
2008
Homo sapiens
Tseng, I.C.; Chou, F.P.; Su, S.F.; Oberst, M.; Madayiputhiya, N.; Lee, M.S.; Wang, J.K.; Sloane, D.E.; Johnson, M.; Lin, C.Y.
Purification from human milk of matriptase complexes with secreted serpins: mechanism for inhibition of matriptase other than HAI-1
Am. J. Physiol. Cell Physiol.
295
C423-C431
2008
Homo sapiens (Q9Y5Y6), Homo sapiens
Janciauskiene, S.; Nita, I.; Subramaniyam, D.; Li, Q.; Lancaster, J.R.; Matalon, S.
Alpha1-antitrypsin inhibits the activity of the matriptase catalytic domain in vitro
Am. J. Respir. Cell Mol. Biol.
39
631-637
2008
Homo sapiens
Schweinitz, A.; Doennecke, D.; Ludwig, A.; Steinmetzer, P.; Schulze, A.; Kotthaus, J.; Wein, S.; Clement, B.; Steinmetzer, T.
Incorporation of neutral C-terminal residues in 3-amidinophenylalanine-derived matriptase inhibitors
Bioorg. Med. Chem. Lett.
19
1960-1965
2009
Homo sapiens
Steinmetzer, T.; Doennecke, D.; Korsonewski, M.; Neuwirth, C.; Steinmetzer, P.; Schulze, A.; Saupe, S.M.; Schweinitz, A.
Modification of the N-terminal sulfonyl residue in 3-amidinophenylalanine-based matriptase inhibitors
Bioorg. Med. Chem. Lett.
19
67-73
2009
Homo sapiens (Q9Y5Y6)
Silvestri, L.; Pagani, A.; Nai, A.; De Domenico, I.; Kaplan, J.; Camaschella, C.
The serine protease matriptase-2 (TMPRSS6) inhibits hepcidin activation by cleaving membrane hemojuvelin
Cell Metab.
8
502-511
2008
Homo sapiens, Mus musculus
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
List, K.
Matriptase: a culprit in cancer?
Future Oncol.
5
97-104
2009
Homo sapiens, Mus musculus
Szabo, R.; Hobson, J.P.; List, K.; Molinolo, A.; Lin, C.Y.; Bugge, T.H.
Potent inhibition and global co-localization implicate the transmembrane Kunitz-type serine protease inhibitor hepatocyte growth factor activator inhibitor-2 in the regulation of epithelial matriptase activity
J. Biol. Chem.
283
29495-29504
2008
Homo sapiens, Mus musculus
Sanders, A.J.; Parr, C.; Martin, T.A.; Lane, J.; Mason, M.D.; Jiang, W.G.
Genetic upregulation of matriptase-2 reduces the aggressiveness of prostate cancer cells in vitro and in vivo and affects FAK and paxillin localisation
J. Cell. Physiol.
216
780-789
2008
Homo sapiens
Lee, P.
Role of matriptase-2 (TMPRSS6) in iron metabolism
Acta Haematol.
122
87-96
2009
Mus musculus, Homo sapiens (Q8IU80)
Wang, J.; Lee, M.; Tseng, I.; Chou, F.; Chen, Y.; Fulton, A.; Lee, H.; Chen, G.; Johnson, M.; Lin, C.
Polarized epithelial cells secrete matriptase as a consequence of zymogen activation and HAI-1-mediated inhibition
Am. J. Physiol. Cell Physiol.
297
459-470
2009
Homo sapiens
Milner, J.M.; Patel, A.; Davidson, R.K.; Swingler, T.E.; Desilets, A.; Young, D.A.; Kelso, E.B.; Donell, S.T.; Cawston, T.E.; Clark, I.M.; Ferrell, W.R.; Plevin, R.; Lockhart, J.C.; Leduc, R.; Rowan, A.D.
Matriptase is a novel initiator of cartilage matrix degradation in osteoarthritis
Arthritis Rheum.
62
1955-1966
2010
Homo sapiens
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
Ramsay, A.J.; Quesada, V.; Sanchez, M.; Garabaya, C.; Sarda, M.P.; Baiget, M.; Remacha, A.; Velasco, G.; Lopez-Otin, C.
Matriptase-2 mutations in iron-refractory iron deficiency anemia patients provide new insights into protease activation mechanisms
Hum. Mol. Genet.
18
3673-3683
2009
Homo sapiens
Napp, J.; Dullin, C.; Mueller, F.; Uhland, K.; Petri, J.B.; van de Locht, A.; Steinmetzer, T.; Alves, F.
Time-domain in vivo near infrared fluorescence imaging for evaluation of matriptase as a potential target for the development of novel, inhibitor-based tumour therapies
Int. J. Cancer
127
1958-1974
2010
Homo sapiens
Uhland, K.; Siphos, B.; Arkona, C.; Schuster, M.; Petri, B.; Steinmetzer, P.; Mueller, F.; Schweinitz, A.; Steinmetzer, T.; Van De Locht, A.
Use of IHC and newly designed matriptase inhibitors to elucidate the role of matriptase in pancreatic ductal adenocarcinoma
Int. J. Oncol.
35
347-357
2009
Homo sapiens
Tseng, I.C.; Xu, H.; Chou, F.P.; Li, G.; Vazzano, A.P.; Kao, J.P.; Johnson, M.D.; Lin, C.Y.
Matriptase activation, an early cellular response to acidosis
J. Biol. Chem.
285
3261-3270
2010
Homo sapiens
Bocheva, G.; Rattenholl, A.; Kempkes, C.; Goerge, T.; Lin, C.Y.; DAndrea, M.R.; Staender, S.; Steinhoff, M.
Role of matriptase and proteinase-activated receptor-2 in nonmelanoma skin cancer
J. Invest. Dermatol.
129
1816-1823
2009
Homo sapiens
Ganesan, R.; Eigenbrot, C.; Kirchhofer, D.
Structural and mechanistic insight into how antibodies inhibit serine proteases
Biochem. J.
430
179-189
2010
Homo sapiens
Clark, E.B.; Jovov, B.; Rooj, A.K.; Fuller, C.M.; Benos, D.J.
Proteolytic cleavage of human acid-sensing ion channel 1 by the serine protease matriptase
J. Biol. Chem.
285
27130-27143
2010
Homo sapiens
Beliveau, F.; Brule, C.; Desilets, A.; Zimmerman, B.; Laporte, S.A.; Lavoie, C.L.; Leduc, R.
Essential role of endocytosis of the type II transmembrane serine protease TMPRSS6 in regulating its functionality
J. Biol. Chem.
286
29035-29043
2011
Homo sapiens
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, Homo sapiens (Q9Y5Y6)
Sisay, M.T.; Steinmetzer, T.; Stirnberg, M.; Maurer, E.; Hammami, M.; Bajorath, J.; Guetschow, M.
Identification of the first low-molecular-weight inhibitors of matriptase-2
J. Med. Chem.
53
5523-5535
2010
Homo sapiens
Colombo, E.; Dsilets, A.; Duchne, D.; Chagnon, F.; Najmanovich, R.; Leduc, R.; Marsault E.
Design and synthesis of potent, selective inhibitors of matriptase
ACS Med. Chem. Lett.
3
530-534
2012
Homo sapiens (Q8IU80)
Wysocka, M.; Gruba, N.; Miecznikowska, A.; Popow-Stellmaszyk, J.; Guetschow, M.; Stirnberg, M.; Furtmann, N.; Bajorath, J.; Lesner, A.; Rolka, K.
Substrate specificity of human matriptase-2
Biochimie
97
121-127
2014
Homo sapiens (Q8IU80), Homo sapiens
Stirnberg, M.; Maurer, E.; Arenz, K.; Babler, A.; Jahnen-Dechent, W.; Guetschow, M.
Cell surface serine protease matriptase-2 suppresses fetuin-A/AHSG-mediated induction of hepcidin
Biol. Chem.
396
81-93
2015
Homo sapiens (Q8IU80)
Goswami, R.; Wohlfahrt, G.; Mukherjee, S.; Ghadiyaram, C.; Nagaraj, J.; Satyam, L.K.; Subbarao, K.; Gopinath, S.; Krishnamurthy, N.R.; Subramanya, H.S.; Ramachandra, M.
Discovery of O-(3-carbamimidoylphenyl)-l-serine amides as matriptase inhibitors using a fragment-linking approach
Bioorg. Med. Chem. Lett.
25
616-620
2015
Homo sapiens (Q9Y5Y6)
Goswami, R.; Mukherjee, S.; Ghadiyaram, C.; Wohlfahrt, G.; Sistla, R.K.; Nagaraj, J.; Satyam, L.K.; Subbarao, K.; Palakurthy, R.K.; Gopinath, S.; Krishnamurthy, N.R.; Ikonen, T.; Moilanen, A.; Subramanya, H.S.; Kallio, P.; Ramachandra, M.
Structure-guided discovery of 1,3,5 tri-substituted benzenes as potent and selective matriptase inhibitors exhibiting in vivo antitumor efficacy
Bioorg. Med. Chem.
22
3187-3203
2014
Homo sapiens (Q9Y5Y6), Homo sapiens
Maurer, E.; Sisay, M.; Stirnberg, M.; Steinmetzer, T.; Bajorath, J.; Guetschow, M.
Insights into matriptase-2 substrate binding and inhibition mechanisms by analyzing active-site-mutated variants
ChemMedChem
7
68-72
2012
Homo sapiens (Q8IU80), Homo sapiens (Q9Y5Y6)
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
Quimbar, P.; Malik, U.; Sommerhoff, C.P.; Kaas, Q.; Chan, L.Y.; Huang, Y.H.; Grundhuber, M.; Dunse, K.; Craik, D.J.; Anderson, M.A.; Daly, N.L.
High-affinity cyclic peptide matriptase inhibitors
J. Biol. Chem.
288
13885-13896
2013
Homo sapiens (Q9Y5Y6)
Zhao, N.; Nizzi, C.P.; Anderson, S.A.; Wang, J.; Ueno, A.; Tsukamoto, H.; Eisenstein, R.S.; Enns, C.A.; Zhang, A.S.
Low intracellular iron increases the stability of matriptase-2
J. Biol. Chem.
290
4432-4446
2015
Homo sapiens (Q8IU80)
Duchene, D.; Colombo, E.; Desilets, A.; Boudreault, P.L.; Leduc, R.; Marsault, E.; Najmanovich, R.
Analysis of subpocket selectivity and identification of potent selective inhibitors for matriptase and matriptase-2
J. Med. Chem.
57
10198-10204
2014
Homo sapiens (Q8IU80)
Hamilton, B.S.; Gludish, D.W.; Whittaker, G.R.
Cleavage activation of the human-adapted influenza virus subtypes by matriptase reveals both subtype and strain specificities
J. Virol.
86
10579-10586
2012
Homo sapiens (Q9Y5Y6)
Beaulieu, A.; Gravel, E.; Cloutier, A.; Marois, I.; Colombo, E.; Desilets, A.; Verreault, C.; Leduc, R.; Marsault, E.; Richter, M.V.
Matriptase proteolytically activates influenza virus and promotes multicycle replication in the human airway epithelium
J. Virol.
87
4237-4251
2013
Homo sapiens (Q9Y5Y6), Homo sapiens
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
Chen, L.M.; Chai, K.X.
Matriptase cleaves the amyloid-beta peptide 1-42 at Arg-5, Lys-16, and Lys-28
BMC Res. Notes
12
005
2019
Homo sapiens
Tamberg, T.; Hong, Z.; De Schepper, D.; Skovbjerg, S.; Dupont, D.M.; Vitved, L.; Schar, C.R.; Skjoedt, K.; Vogel, L.K.; Jensen, J.K.
Blocking the proteolytic activity of zymogen matriptase with antibody-based inhibitors
J. Biol. Chem.
294
314-326
2019
Homo sapiens (Q9Y5Y6), Homo sapiens
Wu, C.J.; Feng, X.; Lu, M.; Morimura, S.; Udey, M.C.
Matriptase-mediated cleavage of EpCAM destabilizes claudins and dysregulates intestinal epithelial homeostasis
J. Clin. Invest.
127
623-634
2017
Homo sapiens
Maiwald, A.; Hammami, M.; Wagner, S.; Heine, A.; Klebe, G.; Steinmetzer, T.
Changing the selectivity profile - from substrate analog inhibitors of thrombin and factor Xa to potent matriptase inhibitors
J. Enzyme Inhib. Med. Chem.
31
89-97
2016
Homo sapiens (Q9Y5Y6)
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 (Q9Y5Y6)
Lai, Y.J.; Chang, H.H.; Lai, H.; Xu, Y.; Shiao, F.; Huang, N.; Li, L.; Lee, M.S.; Johnson, M.D.; Wang, J.K.; Lin, C.Y.
N-Glycan branching affects the subcellular distribution of and inhibition of matriptase by HAI-2/placental bikunin
PLoS ONE
10
e0132163
2015
Homo sapiens
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
EXTERNAL LINKS (specific for EC-Number 3.4.21.109)
Transporter Classification Database (TCDB): 8.A.131.1.4
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