A matriptase-prostasin reciprocal zymogen activation complex with unique features: prostasin as a non-enzymatic co-factor for matriptase activation.
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Regulation of feto-maternal barrier by matriptase- and PAR-2-mediated signaling is required for placental morphogenesis and mouse embryonic survivalSequence and conformational specificity in substrate recognition: several human Kunitz protease inhibitor domains are specific substrates of mesotrypsin.Molecular constituents of the extracellular matrix in rat liver mounting a hepatic progenitor cell response for tissue repair.The membrane-anchored serine protease prostasin (CAP1/PRSS8) supports epidermal development and postnatal homeostasis independent of its enzymatic activity.Matriptase zymogen supports epithelial development, homeostasis and regenerationNon-hematopoietic PAR-2 is essential for matriptase-driven pre-malignant progression and potentiation of ras-mediated squamous cell carcinogenesisThe protease inhibitor HAI-2, but not HAI-1, regulates matriptase activation and shedding through prostasin.Prostasin interacts with the epithelial Na+ channel and facilitates cleavage of the γ-subunit by a second proteaseDetection of active matriptase using a biotinylated chloromethyl ketone peptideProteolytic activation of the protease-activated receptor (PAR)-2 by the glycosylphosphatidylinositol-anchored serine protease testisin.Divergent Inhibitor Susceptibility among Airway Lumen-Accessible Tryptic ProteasesMatriptase Complexes and Prostasin Complexes with HAI-1 and HAI-2 in Human Milk: Significant Proteolysis in LactationNatural Endogenous Human Matriptase and Prostasin Undergo Zymogen Activation via Independent Mechanisms in an Uncoupled Manner.Selective Inhibition of Prostasin in Human Enterocytes by the Integral Membrane Kunitz-Type Serine Protease Inhibitor HAI-2Targeting the membrane-anchored serine protease testisin with a novel engineered anthrax toxin prodrug to kill tumor cells and reduce tumor burden.Distinct Developmental Functions of Prostasin (CAP1/PRSS8) Zymogen and Activated ProstasinTargeting matriptase in breast cancer abrogates tumour progression via impairment of stromal-epithelial growth factor signalling.Membrane-anchored proteases in endothelial cell biology.Matriptase activation connects tissue factor-dependent coagulation initiation to epithelial proteolysis and signalingMatriptase and prostasin are expressed in human skin in an inverse trend over the course of differentiation and are targeted to different regions of the plasma membrane.Function and clinical relevance of kallikrein-related peptidases and other serine proteases in gynecological cancers.Epidermal barrier disorders and corneodesmosome defects.The basal chorionic trophoblast cell layer: An emerging coordinator of placenta development.The serine protease-mediated increase in intestinal epithelial barrier function is dependent on occludin and requires an intact tight junction.The role of type II transmembrane serine protease-mediated signaling in cancer.Delineation of proteolytic and non-proteolytic functions of the membrane-anchored serine protease prostasin.The Kunitz Domain I of Hepatocyte Growth Factor Activator Inhibitor-2 Inhibits Matriptase Activity and Invasive Ability of Human Prostate Cancer Cells.Tissue distribution and subcellular localizations determine in vivo functional relationship among prostasin, matriptase, HAI-1, and HAI-2 in human skin.Inflammatory cytokines down-regulate the barrier-protective prostasin-matriptase proteolytic cascade early in experimental colitis.Deregulated hepsin protease activity confers oncogenicity by concomitantly augmenting HGF/MET signalling and disrupting epithelial cohesion.HAI-2 stabilizes, inhibits and regulates SEA-cleavage-dependent secretory transport of matriptase.Loss of HAI-2 in mice with decreased prostasin activity leads to an early-onset intestinal failure resembling congenital tufting enteropathy.Hepatocyte growth factor activator inhibitor type-2 (HAI-2)/SPINT2 contributes to invasive growth of oral squamous cell carcinoma cells.
P2860
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P2860
A matriptase-prostasin reciprocal zymogen activation complex with unique features: prostasin as a non-enzymatic co-factor for matriptase activation.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
A matriptase-prostasin recipro ...... tor for matriptase activation.
@en
type
label
A matriptase-prostasin recipro ...... tor for matriptase activation.
@en
prefLabel
A matriptase-prostasin recipro ...... tor for matriptase activation.
@en
P2093
P2860
P356
P1476
A matriptase-prostasin recipro ...... tor for matriptase activation.
@en
P2093
Chen-Yong Lin
Diane E Peters
Katiuchia Uzzun Sales
Lotte K Vogel
Sine Godiksen
Stine Friis
P2860
P304
19028-19039
P356
10.1074/JBC.M113.469932
P407
P577
2013-05-14T00:00:00Z