3.4.21.109: matriptase
This is an abbreviated version!
For detailed information about matriptase, go to the full flat file.
Word Map on EC 3.4.21.109
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3.4.21.109
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hepatocyte
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hepcidin
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hai-1
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anemia
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metastasis
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prostate
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hepsin
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zymogen
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transferrin
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prostasin
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overload
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trypsin-like
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irida
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plasminogen
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hemojuvelin
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iron-refractory
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kunitz-type
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inhibitor-1
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kunitz
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ttsps
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hemochromatosis
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erythropoiesis
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microcytic
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membrane-anchored
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urokinase-type
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ferroportin
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iron-deficiency
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pro-hgf
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pericellular
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upa
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autoactivation
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two-chain
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hypochromic
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medicine
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protease-activated
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tmprss4
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spint2
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corpuscular
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erythroferrone
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profilaggrin
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camostat
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corin
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epithelial-derived
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par-2
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hypotrichosis
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drug development
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diagnostics
- 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
Reaction
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
Epi/MTP, epithin, epithin/matriptase, influenza virus-activating protease, matriptase, matriptase-1, matriptase-2, matriptase-3, matriptase1, matriptase1a, membrane-type serine protease 1, membrane-type serine protease 1/matripase, membrane-type serine protease-1, membrane-type serine protease1, membrane-type serine proteinase matripase, membrane-type serine proteinase matriptase, More, MT-2, MT-SP-1, MT-SP1, MT-SP1/matripase, MT2, notopleural, prostamin, PRSS14, r-matripase, serine protease matriptase-2, serine protease SNC19/matripase, SNC19, ST-14, ST14, suppression of tumorigenecity 14, suppressor of tumorigenicity 14, suppressor of tumorigenicity 14 protein, suppressor of tumorigenicity-14, TADG-15, TADG15, TMPRSS6, transmembrane serine protease 6, tumor-associated differentially expressed gene-15, tumor-associated type II transmembrane serine protease, type 2 transmembrane serine protease, type II transmembrane protease, type II transmembrane serine protease
ECTree
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
diagnostics
drug development
medicine
additional information
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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
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the enzyme might be a good biomarker in treatment of malignant breast tumors
drug development
matriptase-2 represents a target for the development of inhibitors, potentially useful in the treatment of hemochromatosis or beneficial as pharmacological tools
medicine
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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
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matripase mediates cell invasion through activation of receptor-bound pro-urokinase-type plasminogen activator
medicine
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multiple roles for hepatocyte growth factor activator inhibitor-1 to regulate matripase, including its proper expression, intracellular trafficking, activation and inhibition
medicine
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possibly controlls epithelial-cell turnover by regulating cell-cell and/or cell-substratum adhesions
medicine
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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
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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
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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
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matriptase may play an important role in the metastasis of prostate cancer
medicine
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matriptase-2 plays a putative role as a tumor suppressor enzyme in human breast cancer
medicine
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upregulation of matriptase-2 reduces the aggressiveness of prostate cancer cells in vitro and in vivo
medicine
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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
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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
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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
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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
medicine
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mRNA and protein expression of both matriptase and prostasin are rapidly down-regulated in the initiating inflammatory phases of dextran sulfate sodium-induced experimental colitis, and the loss of these proteases precedes the appearance of clinical symptoms. Barrier disruption by the colitis-associated Th2-type cytokines, IL-4 and IL-13, down-regulates matriptase as well as prostasin through phosphorylation of the transcriptional regulator STAT6
