N-terminal processing is essential for release of epithin, a mouse type II membrane serine protease
about
Matriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivityBikunin target genes in ovarian cancer cells identified by microarray analysisInhibition of tumor invasion by genomic down-regulation of matriptase through suppression of activation of receptor-bound pro-urokinaseHuman cancer cells retain modest levels of enzymatically active matriptase only in extracellular milieu following induction of zymogen activationEvidence for the occurrence of membrane-type serine protease 1/matriptase on the basolateral sides of enterocytesSerase-1B, a new splice variant of polyserase-1/TMPRSS9, activates urokinase-type plasminogen activator and the proteolytic activation is negatively regulated by glycosaminoglycansMouse matriptase-2: identification, characterization and comparative mRNA expression analysis with mouse hepsin in adult and embryonic tissuesMatriptase zymogen supports epithelial development, homeostasis and regenerationDeregulated matriptase causes ras-independent multistage carcinogenesis and promotes ras-mediated malignant transformation.Targeting zymogen activation to control the matriptase-prostasin proteolytic cascade.The protease inhibitor HAI-2, but not HAI-1, regulates matriptase activation and shedding through prostasin.A novel TMPRSS6 mutation that prevents protease auto-activation causes IRIDA.Functional analysis of the transmembrane domain and activation cleavage of human corin: design and characterization of a soluble corin.Filamin is essential for shedding of the transmembrane serine protease, epithin.Endogenous expression of matriptase in neural progenitor cells promotes cell migration and neuron differentiation.Matriptase: potent proteolysis on the cell surface.Detection of active matriptase using a biotinylated chloromethyl ketone peptidePossible role of matriptase in the diagnosis of ovarian cancer.Differential subcellular localization renders HAI-2 a matriptase inhibitor in breast cancer cells but not in mammary epithelial cellsPolyserase-I, a human polyprotease with the ability to generate independent serine protease domains from a single translation product.Autosomal recessive ichthyosis with hypotrichosis caused by a mutation in ST14, encoding type II transmembrane serine protease matriptase.The cutting edge: membrane-anchored serine protease activities in the pericellular microenvironment.A matriptase-prostasin reciprocal zymogen activation complex with unique features: prostasin as a non-enzymatic co-factor for matriptase activation.Matriptase-2 (TMPRSS6): a proteolytic regulator of iron homeostasisImpact of suppression of tumorigenicity 14 (ST14)/serine protease 14 (Prss14) expression analysis on the prognosis and management of estrogen receptor negative breast cancer.Overexpression of matriptase correlates with poor prognosis in esophageal squamous cell carcinoma.The structural requirements of matriptase in its ectodomain release in polarized epithelial cells.Mutation G827R in matriptase causing autosomal recessive ichthyosis with hypotrichosis yields an inactive protease.Matriptase shedding is closely coupled with matriptase zymogen activation and requires de novo proteolytic cleavage likely involving its own activity.Identification of the matriptase second CUB domain as the secondary site for interaction with hepatocyte growth factor activator inhibitor type-1.Matriptase-2 mutations in iron-refractory iron deficiency anemia patients provide new insights into protease activation mechanisms.Matriptase activation and shedding with HAI-1 is induced by steroid sex hormones in human prostate cancer cells, but not in breast cancer cells.Expansion of divergent SEA domains in cell surface proteins and nucleoporin 54.Morpholino knockdown of the ubiquitously expressed transmembrane serine protease TMPRSS4a in zebrafish embryos exhibits severe defects in organogenesis and cell adhesion.HAI-2 stabilizes, inhibits and regulates SEA-cleavage-dependent secretory transport of matriptase.
P2860
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P2860
N-terminal processing is essential for release of epithin, a mouse type II membrane serine protease
description
2001 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2001
@ast
im November 2001 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2001/11/30)
@sk
vědecký článek publikovaný v roce 2001
@cs
wetenschappelijk artikel (gepubliceerd op 2001/11/30)
@nl
наукова стаття, опублікована в листопаді 2001
@uk
name
N-terminal processing is essen ...... pe II membrane serine protease
@ast
N-terminal processing is essen ...... pe II membrane serine protease
@en
N-terminal processing is essen ...... pe II membrane serine protease
@nl
type
label
N-terminal processing is essen ...... pe II membrane serine protease
@ast
N-terminal processing is essen ...... pe II membrane serine protease
@en
N-terminal processing is essen ...... pe II membrane serine protease
@nl
prefLabel
N-terminal processing is essen ...... pe II membrane serine protease
@ast
N-terminal processing is essen ...... pe II membrane serine protease
@en
N-terminal processing is essen ...... pe II membrane serine protease
@nl
P2093
P2860
P3181
P356
P1476
N-terminal processing is essen ...... pe II membrane serine protease
@en
P2093
I. S. Seong
R. H. Schwartz
P2860
P304
44581–44589
P3181
P356
10.1074/JBC.M107059200
P407
P577
2001-11-30T00:00:00Z