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Bovine serum albumin + H2O
?
-
-
-
-
?
denatured collagen + H2O
?
-
-
-
-
?
G-protein-coupled protease-activated receptor-2 + H2O
?
-
-
-
-
?
growth factor macrophage-stimulating protein 1 + H2O
?
-
-
-
-
?
H-Glu-Gly-Arg-p-nitroanilide + H2O
H-Glu-Gly + Arg-p-nitroanilide
-
low activity
-
-
?
hemojuvelin + H2O
?
-
-
-
-
?
hepatocyte growth factor + H2O
activated hepatocyte growth factor + ?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
insulin-like growth factor binding-related protein-1 + H2O
?
-
-
-
-
?
pro-hepatocyte growth factor + H2O
?
-
-
-
-
?
pro-prostasin + H2O
prostasin + propeptide of prostasin
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
pro-urokinase-type plasminogen activator + H2O
?
-
-
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
proform acid-sensing ion channel 1 + H2O
mature acid-sensing ion channel 1 + ?
-
-
-
-
?
proform G-protein-coupled protease activated receptor-2 + H2O
mature G-protein-coupled protease activated receptor-2 + ?
-
-
-
-
?
proform hepatocyte growth factor + H2O
mature hepatocyte growth factor + ?
-
-
-
-
?
proform platelet-derived growth factor-D + H2O
mature platelet-derived growth factor-D + ?
-
-
-
-
?
proform prostasin + H2O
mature prostasin + ?
-
-
-
-
?
proform urokinase-type plasminogen activator + H2O
mature urokinase-type plasminogen activator + ?
-
-
-
-
?
prostatin + H2O
?
-
-
-
-
?
serine protease uPA + H2O
?
-
-
-
-
?
SIMA135 + H2O
?
-
-
-
-
?
Suc-Ala-Ala-Pro-Arg-p-nitroanilide + H2O
Suc-Ala-Ala-Pro + Arg-p-nitroanilide
-
low activity
-
-
?
Suc-Ala-Ala-Pro-Lys-p-nitroanilide + H2O
Suc-Ala-Ala-Pro-Lys + p-nitroaniline
-
-
-
-
?
urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
pro-uPA activation
-
-
?
Z-Phe-Val-Arg-p-nitroanilide + H2O
Z-Phe-Val + Arg-p-nitroanilide
-
-
-
-
?
additional information
?
-
collagen type IV + H2O
?
-
-
-
-
?
collagen type IV + H2O
?
-
involved in ECM degradation/remodeling
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
involved in adhesion and migration/invasiveness
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
involved in ECM degradation/remodeling
-
-
?
hepatocyte growth factor + H2O
activated hepatocyte growth factor + ?
-
-
-
-
?
hepatocyte growth factor + H2O
activated hepatocyte growth factor + ?
-
proteolytic activation of hepatocyte growth factor/scatter factor, 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 + ?
-
seven proteases are involved in the activation of HGF/SF, involved in cell proliferation and adhesion, ECM degradation/remodeling, and migration/invasiveness, overview
-
-
?
IGFBP-rP1 + H2O
?
-
-
-
-
?
IGFBP-rP1 + H2O
?
-
involved in involved in cell proliferation and adhesion
-
-
?
Laminin + H2O
?
-
-
-
-
?
Laminin + H2O
?
-
involved in adhesion and migration/invasiveness
-
-
?
PAR-2 + H2O
?
-
-
-
-
?
PAR-2 + H2O
?
-
G-protein coupled receptor
-
-
?
PAR-2 + H2O
?
-
involved in involved in cell adhesion
-
-
?
pro-prostasin + H2O
prostasin + propeptide of prostasin
-
soluble matriptase efficiently converts soluble prostasin zymogen to an active two-chain form, prostasin is exclusively found in the zymogen form in matriptase-deficient epidermis
-
-
?
pro-prostasin + H2O
prostasin + propeptide of prostasin
-
the channel activating protease prostasin/CAP1/PRSS8, a glycosylphosphatidylinositol-anchored membrane serine protease, is co-localized with matriptase
-
-
?
pro-prostasin + H2O
prostasin + propeptide of prostasin
-
activation, cleavage after Arg12 within the amino acid sequence QPR12-ITG
-
-
?
pro-prostasin + H2O
prostasin + propeptide of prostasin
-
cleavage after Arg12 within the amino acid sequence QPR12-ITG
-
-
?
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 at the cell surface, where uPA and matriptase co-localize, involved in cell proliferation and adhesion, ECM degradation/remodeling, and migration/invasiveness
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
-
-
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
-
involved in terminal epithelial cell differentiation, mechanism of enzyme access for direct cleavage in vivo, overview
-
-
?
prostasin + H2O
?
-
-
-
-
?
prostasin + H2O
?
-
a serine protease
-
-
?
VEGFR-2 + H2O
?
-
-
-
-
?
VEGFR-2 + H2O
?
-
i.e. vascular endothelial growth factor receptor 2, a growth factor receptor
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
component of the profilaggrin-processing pathway and a key regulator of terminal epidermal differentiation, involved in lipid matrix formation, cornified envelope morphogenesis and stratum corneum desquamation
-
?
additional information
?
-
-
a matriptase-prostasin zymogen activation cascade may be functionally operative in multiple epithelial tissues, but matriptase promotes epithelial carcinogenesis independent of prostasin, overview
-
-
?
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, the protease is essential for postnatal survival, matriptase has pleiotropic functions in the development of the epidermis, hair follicles, and cellular immune system, the protease is essential for postnatal survival, overview
-
-
?
additional information
?
-
-
matriptase inhibition by hepatocyte growth factor activator inhibitor-1 is essential for placental development, mechanism, overview
-
-
?
additional information
?
-
-
matriptase is a type II transmembrane serine protease, that 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, a type II transmembrane serine protease, and prostasin, a glycosylphosphatidylinositol-anchored membrane serine protease, are both required for processing of the epidermis-specific polyprotein, profilaggrin, stratum corneum formation, and acquisition of epidermal barrier function, matriptase, an autoactivating protease, acts upstream from prostasin to initiate a zymogen cascade that is essential for epidermal differentiation, overview
-
-
?
additional information
?
-
-
physiological functions, overview, MT-SP1 is critical for proper epidermal development and postnatal survival, MT-SP1 plays a role in embryologic development
-
-
?
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, spatial dysregulation of matriptase leads to the activation of the PI3K-Akt signaling pathway, and dysregulated matriptase synergizes strongly with activated ras to promote epithelial carcinogenesis
-
-
?
additional information
?
-
-
matriptase performs autoactivation
-
-
?
additional information
?
-
-
R/KXSR-/-A is the cleavage sequence of matriptase
-
-
?
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collagen type IV + H2O
?
-
involved in ECM degradation/remodeling
-
-
?
Fibronectin + H2O
?
-
involved in adhesion and migration/invasiveness
-
-
?
G-protein-coupled protease-activated receptor-2 + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
involved in ECM degradation/remodeling
-
-
?
growth factor macrophage-stimulating protein 1 + H2O
?
-
-
-
-
?
hemojuvelin + H2O
?
-
-
-
-
?
hepatocyte growth factor + H2O
activated hepatocyte growth factor + ?
-
proteolytic activation of hepatocyte growth factor/scatter factor, overview
-
-
?
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
-
-
?
IGFBP-rP1 + H2O
?
-
involved in involved in cell proliferation and adhesion
-
-
?
insulin-like growth factor binding-related protein-1 + H2O
?
-
-
-
-
?
Laminin + H2O
?
-
involved in adhesion and migration/invasiveness
-
-
?
pro-hepatocyte growth factor + H2O
?
-
-
-
-
?
pro-prostasin + H2O
prostasin + propeptide of prostasin
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-type plasminogen activator + H2O
?
-
-
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
proform hepatocyte growth factor + H2O
mature hepatocyte growth factor + ?
-
-
-
-
?
proform prostasin + H2O
mature prostasin + ?
-
-
-
-
?
prostatin + H2O
?
-
-
-
-
?
serine protease uPA + H2O
?
-
-
-
-
?
SIMA135 + H2O
?
-
-
-
-
?
urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
pro-uPA activation
-
-
?
additional information
?
-
PAR-2 + H2O
?
-
G-protein coupled receptor
-
-
?
PAR-2 + H2O
?
-
involved in involved in cell adhesion
-
-
?
pro-prostasin + H2O
prostasin + propeptide of prostasin
-
soluble matriptase efficiently converts soluble prostasin zymogen to an active two-chain form, prostasin is exclusively found in the zymogen form in matriptase-deficient epidermis
-
-
?
pro-prostasin + H2O
prostasin + propeptide of prostasin
-
the channel activating protease prostasin/CAP1/PRSS8, a glycosylphosphatidylinositol-anchored membrane serine protease, is co-localized with matriptase
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
-
-
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
-
involved in terminal epithelial cell differentiation, mechanism of enzyme access for direct cleavage in vivo, overview
-
-
?
prostasin + H2O
?
-
-
-
-
?
prostasin + H2O
?
-
a serine protease
-
-
?
VEGFR-2 + H2O
?
-
-
-
-
?
VEGFR-2 + H2O
?
-
i.e. vascular endothelial growth factor receptor 2, a growth factor receptor
-
-
?
additional information
?
-
-
component of the profilaggrin-processing pathway and a key regulator of terminal epidermal differentiation, involved in lipid matrix formation, cornified envelope morphogenesis and stratum corneum desquamation
-
?
additional information
?
-
-
a matriptase-prostasin zymogen activation cascade may be functionally operative in multiple epithelial tissues, but matriptase promotes epithelial carcinogenesis independent of prostasin, overview
-
-
?
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, the protease is essential for postnatal survival, matriptase has pleiotropic functions in the development of the epidermis, hair follicles, and cellular immune system, the protease is essential for postnatal survival, overview
-
-
?
additional information
?
-
-
matriptase inhibition by hepatocyte growth factor activator inhibitor-1 is essential for placental development, mechanism, overview
-
-
?
additional information
?
-
-
matriptase is a type II transmembrane serine protease, that 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, a type II transmembrane serine protease, and prostasin, a glycosylphosphatidylinositol-anchored membrane serine protease, are both required for processing of the epidermis-specific polyprotein, profilaggrin, stratum corneum formation, and acquisition of epidermal barrier function, matriptase, an autoactivating protease, acts upstream from prostasin to initiate a zymogen cascade that is essential for epidermal differentiation, overview
-
-
?
additional information
?
-
-
physiological functions, overview, MT-SP1 is critical for proper epidermal development and postnatal survival, MT-SP1 plays a role in embryologic development
-
-
?
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, spatial dysregulation of matriptase leads to the activation of the PI3K-Akt signaling pathway, and dysregulated matriptase synergizes strongly with activated ras to promote epithelial carcinogenesis
-
-
?
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alpha-1-antitrypsin
-
-
-
alpha-2-Antiplasmin
-
-
-
alpha1 proteinase
-
formation of a stable inhibitor complex
-
alpha2-antiplasmin
-
formation of a stable inhibitor complex
-
hepatocyte growth factor activator inhibitor I
-
-
-
hepatocyte growth factor activator inhibitor-1
-
hepatocyte growth factor activator inhibitor-2
-
HAI-2
-
plasminogen activator inhibitor-1
-
formation of a stable inhibitor complex
Protein C inhibitor
-
formation of a stable inhibitor complex
-
SFTI1
-
serine protease inhibitor can only inhibit Epi/MTP and cathepsin G. Mammary epithelial growth and morphogenesis in the presence of the latent form hepatocyte growth factor (pro-HGF) is blocked by addition of SFTI1 an inhibitor of the Epi/MTP protease activity
antithrombin III
-
-
-
antithrombin III
-
formation of a stable inhibitor complex
-
hepatocyte growth factor activator inhibitor-1
-
HAI-1
-
hepatocyte growth factor activator inhibitor-1
-
HAI-1, a Kunitz-type transmembrane serine protease inhibitor, complex formation with the enzyme, enzyme inhibition is essential for placental development, overview
-
hepatocyte growth factor activator inhibitor-1
-
HAI-1, the cognate matriptase inhibitor is able to compensate for the effect of augmented matriptase activity, providing a rationale for the inhibition of matriptase to prevent tumor growth in vivo
-
hepatocyte growth factor activator inhibitor-1
-
is required for proper development of placenta, overview
-
hepatocyte growth factor activator inhibitor-1
-
HAI-1, an extremely effective inhibitor of matriptase in vitro, that has a high affinity for matriptase binding and is typically co-expressed with matriptase in vivo. Matriptase activation appears to require physical interaction with its related inhibitor, HAI-1, which may serve to protect against aberrant matriptase proteolysis. Deletion or mutation of the LDLA domain of HAI-1 results in both a reduction in surface matriptase expression and abolishment of matriptase activity
-
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additional information
-
spatial and temporal co-expression of matriptase and prostasin
malfunction
-
hepatocyte growth factor activator inhibitor-1 knockout mice with one or two wild-type matriptase alleles die in utero. Knockout mice on the matriptase hypomorphic mouse background complete embryonic development, are viable, healthy, and display normal long-term survival. Matriptase is identified as a critical inhibitory target for hepatocyte growth factor activator inhibitor-1 in keratinized squamous epithelium and a delicate balance between matriptase and hepatocyte growth factor activator inhibitor-1 maintains homeostasis of adult mammalian tissues
malfunction
-
mammary epithelial growth and morphogenesis in the presence of the latent form hepatocyte growth factor (pro-HGF) is blocked either by addition of SFTI1 an inhibitor of the Epi/MTP protease activity or by siRNA knockdown of the Epi/MTP expression
malfunction
-
mice lacking the protease domain of matriptase-2 are crossed with mice lacking hemojuvelin in order to examine the relationship between hemojuvelin and matriptase-2 in vivo. Mice lacking functional matriptase-2 and hemojuvelin exhibit low Hamp (Hepcidin encoding gene) expression, high serum and liver iron, and high transferrin saturation. Double mutant mice also exhibit lower levels of iron in the heart compared to hemojuvelin-deficient mice, demonstrating a possible cardioprotective effect resulting from the loss of matriptase-2
malfunction
-
Tmprss6-/- mice knockout mice exhibit an iron deficiency phenotype. Tmprss6 -/- mice exhibit reduced ferroportin immunostaining and iron accumulation in intestinal enterocytes
malfunction
-
the genetic elimination of matriptase completely abolishes the aberrant caseinolytic activity that is caused by lympho-epithelial Kazal-type-related inhibitor (LEKTI) deficiency in both the lower epidermal layers as well as in the dermis. Matriptase elimination prevents spontaneous stratum corneum loss, restores keratohyalin granules, and improves the barrier function of LEKTI-deficient epidermis. Loss of matriptase restores corneodesmosome integrity to LEKTI-deficient epidermis. Matriptase ablation prevents kallikrein hyperactivity-mediated inflammation caused by LEKTI-deficiency
malfunction
-
matriptase and prostasin null mice have identical phenotypes, mice deficient for matriptase phenocopy mice deficient for epidermal prostasin and show impaired corneocyte differentiation, imparied lipid matrix formation, loss of profilaggrin processing and loss of tight junction formation and function. Matriptase-deficient mice present with a variety of epidermal defects, including a generalized disruption of the stratum corneum architecture, loss of vesicular bodies that generate intercorneocyte lipids and hypoplasia and dysgenesis of hair follicles. Together, these defects lead to a compromised epidermal barrier and result in fatal dehydration during the neonatal period. Targeted postnatal ablation of matriptase in mice perturbs the function of multiple adult tissues, indicating an ongoing requirement for matriptase proteolysis in the maintenance of diverse types of epithelia. Matriptase-deficient Caco-2 monolayers as well as matriptase hypomorphic mice are shown to express abnormally high levels of the tight junction protein claudin-2, which is associated with the formation of ion channels that decrease the cohesion between adjacent epithelial cells. Matriptase pathophysiology, overview
physiological function
-
Epi/MTP participates in mammary epithelial growth and modeling through activation of pro-hepatocyte growth factor
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
-
matriptase initiates Netherton syndrome in a lympho-epithelial Kazal-type-related inhibitor (LEKTI)-deficient mouse model by premature activation of a pro-kallikrein-related cascade. Matriptase is an efficient activator of epidermal pro-kallikreins that co-localize with LEKTI at the granular-transitional layer boundary
physiological function
-
matriptase is a potential oncogene, its expression correlates with the severity of tumors in the breast and prostate and de novo matriptase expression has been found in both ovarian and cervical carcinomas. The ratio of matriptase/HAI-1 mRNA is increased in ovarian and colorectal cancer, indicating that deregulated matriptase proteolysis may contribute to tumor formation or metastasis. In the epidermis, the glycosylphosphatidylinositol anchored membrane serine protease prostasin is activated by matriptase to initiate a proteolytic cascade that is required for the development of the stratum corneum barrier function. Matriptase in epidermal barrier and epidermal development, detailed overview. Proteolytic activity of the matriptase-prostasin cascade is regulated in the epidermis via inhibition by the Kunitz-type serine protease inhibitor hepatocyte growth factor activator inhibitor-1
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MT2MASK
-
matriptase-2 mutant lacking the serine protease domain
R599X
-
point mutation identified in zorro mice causing premature termination of matriptase-2 and an iron deficiency phenotype
W783X
-
point mutation identified in masquerade mice causing premature termination of matriptase-2 and an iron deficiency phenotype
additional information
-
construction of matriptase knockout mice
additional information
-
genetic ablation of the enzyme in hepatocyte growth factor activator inhibitor-1-deficient embryos restores the integrity of chorionic trophoblasts and enables placental labyrinth formation and development in turn, which otherwise is prevented, overview, phenotype of single enzyme knockout and double enzyme and inhibitor knockout mutant embryos, overview
additional information
-
matriptase depletion results in postnatal death of the mice due to dehydration which is caused by a lack of epithelial barrier function in the skin of newborns, these matriptase knockout mice also have abnormal hair follicle development and disturbed thymic homeostasis showing increased lymphocyte apoptosis in the thymuses and profilaggrin accumulation in epidermal tissue, transgenic mice with increased expression of matriptase in the epidermis show induction of spontaneous squamous cell carcinomas and strongly potentiated chemical skin carcinogenesis, possibly through activation of the tumor-promoting PI3K-Akt pathway, while double transgenic mice co-expressing matriptase and its cognate inhibitor HAI-1 do not develop spontaneous skin cancers and do not show increased susceptibility to chemical carcinogenesis
additional information
-
matriptase-deficient mice develop normally, but do not survive postnatally owing to an epidermal barrier defect, transgenic mice with a very modest overexpression of matriptase in the skin become remarkably susceptible to carcinogen-induced tumour formation
additional information
-
null mice show impaired development of the hair follicles and immune system and are unable to survive 48 hours past birth due to rapid dehydration through an abnormally formed epidermal barrier
additional information
-
phenotype of enzyme-deficient mice and pathogenesis of dysregulated matriptase activity, overview, early lethality of ST14 null mice, transgenic mice expressing modest levels of matriptase in basal keratinocytes display progressive epidermal hyperplasia with fibrosis and dermal inflammation, which spontaneously progresses to invasive squamous cell carcinoma
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List, K.; Szabo, R.; Wertz, P.W.; Segre, J.; Haudenschild, C.C.; Kim, S.Y.; Bugge, T.H.
Loss of proteolytically processed filaggrin caused by epidermal deletion of matriptase/MT-SP1
J. Cell. Biol.
163
901-910
2003
Mus musculus
brenda
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
-
brenda
Netzel-Arnett, S.; Currie, B.M.; Szabo, R.; Lin, C.Y.; Chen, L.M.; Chai, K.X.; Antalis, T.M.; Bugge, T.H.; List, K.
Evidence for a matriptase-prostasin proteolytic cascade regulating terminal epidermal differentiation
J. Biol. Chem.
281
32941-32945
2006
Mus musculus
brenda
List, K.; Hobson, J.P.; Molinolo, A.; Bugge, T.H.
Co-localization of the channel activating protease prostasin/(CAP1/PRSS8) with its candidate activator, matriptase
J. Cell. Physiol.
213
237-245
2007
Mus musculus
brenda
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
brenda
Uhland, K.
Matriptase and its putative role in cancer
Cell. Mol. Life Sci.
63
2968-2978
2006
Homo sapiens, Mus musculus
brenda
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
brenda
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
brenda
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)
brenda
Szabo, R.; Molinolo, A.; List, K.; Bugge, T.H.
Matriptase inhibition by hepatocyte growth factor activator inhibitor-1 is essential for placental development
Oncogene
26
1546-1556
2007
Mus musculus
brenda
Folgueras, A.R.; de Lara, F.M.; Pendas, A.M.; Garabaya, C.; Rodriguez, F.; Astudillo, A.; Bernal, T.; Cabanillas, R.; Lopez-Otin, C.; Velasco, G.
Membrane-bound serine protease matriptase-2 (Tmprss6) is an essential regulator of iron homeostasis
Blood
112
2539-2545
2008
Mus musculus
brenda
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
brenda
List, K.
Matriptase: a culprit in cancer?
Future Oncol.
5
97-104
2009
Homo sapiens, Mus musculus
brenda
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
brenda
Lee, P.
Role of matriptase-2 (TMPRSS6) in iron metabolism
Acta Haematol.
122
87-96
2009
Mus musculus, Homo sapiens (Q8IU80)
brenda
Szabo, R.; Kosa, P.; List, K.; Bugge, T.H.
Loss of matriptase suppression underlies spint1 mutation-associated ichthyosis and postnatal lethality
Am. J. Pathol.
174
2015-2022
2009
Mus musculus
brenda
Truksa, J.; Gelbart, T.; Peng, H.; Beutler, E.; Beutler, B.; Lee, P.
Suppression of the hepcidin-encoding gene Hamp permits iron overload in mice lacking both hemojuvelin and matriptase-2/TMPRSS6
Br. J. Haematol.
147
571-581
2009
Mus musculus
brenda
Lee, S.L.; Huang, P.Y.; Roller, P.; Cho, E.G.; Park, D.; Dickson, R.B.
Matriptase/epithin participates in mammary epithelial cell growth and morphogenesis through HGF activation
Mech. Dev.
127
82-95
2010
Mus musculus
brenda
Sales, K.U.; Masedunskas, A.; Bey, A.L.; Rasmussen, A.L.; Weigert, R.; List, K.; Szabo, R.; Overbeek, P.A.; Bugge, T.H.
Matriptase initiates activation of epidermal pro-kallikrein and disease onset in a mouse model of Netherton syndrome
Nat. Genet.
42
676-683
2010
Mus musculus
brenda
Miller, G.S.; List, K.
The matriptase-prostasin proteolytic cascade in epithelial development and pathology
Cell Tissue Res.
351
245-253
2013
Mus musculus
brenda
Buzza, M.S.; Johnson, T.A.; Conway, G.D.; Martin, E.W.; Mukhopadhyay, S.; Shea-Donohue, T.; Antalis, T.M.
Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis
J. Biol. Chem.
292
10801-10812
2017
Mus musculus
brenda