Regulation of the activity of matriptase on epithelial cell surfaces by a blood-derived factor.
about
HATL5: a cell surface serine protease differentially expressed in epithelial cancersMatriptase and HAI-1 are expressed by normal and malignant epithelial cells in vitro and in vivoCatalytic domain structures of MT-SP1/matriptase, a matrix-degrading transmembrane serine proteinaseTissue expression, protease specificity, and Kunitz domain functions of hepatocyte growth factor activator inhibitor-1B (HAI-1B), a new splice variant of HAI-1The activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitorSphingosine 1-phosphate, present in serum-derived lipoproteins, activates matriptaseAssembly of adherens junctions is required for sphingosine 1-phosphate-induced matriptase accumulation and activation at mammary epithelial cell-cell contactsHuman cancer cells retain modest levels of enzymatically active matriptase only in extracellular milieu following induction of zymogen activationRoles of functional and structural domains of hepatocyte growth factor activator inhibitor type 1 in the inhibition of matriptaseProtein interaction analysis of ST14 domains and their point and deletion mutants.Local protease signaling contributes to neural tube closure in the mouse embryoMatriptase activation, an early cellular response to acidosis.Targeting zymogen activation to control the matriptase-prostasin proteolytic cascade.Proteolysis-induced N-terminal ectodomain shedding of the integral membrane glycoprotein CUB domain-containing protein 1 (CDCP1) is accompanied by tyrosine phosphorylation of its C-terminal domain and recruitment of Src and PKCdelta.Regulation of the matriptase-prostasin cell surface proteolytic cascade by hepatocyte growth factor activator inhibitor-1 during epidermal differentiationFilamin is essential for shedding of the transmembrane serine protease, epithin.Transmodulation of cell surface regulatory molecules via ectodomain shedding.Increased matriptase zymogen activation in inflammatory skin disorders.Antithrombin regulates matriptase activity involved in plasmin generation, syndecan shedding, and HGF activation in keratinocytes.Regulation of hepatocyte activator inhibitor-1 expression by androgen and oncogenic transformation in the prostate.Differential subcellular localization renders HAI-2 a matriptase inhibitor in breast cancer cells but not in mammary epithelial cellsMatriptase is inhibited by extravascular antithrombin in epithelial cells but not in most carcinoma cellsN-Glycan Branching Affects the Subcellular Distribution of and Inhibition of Matriptase by HAI-2/Placental BikuninMechanisms for the control of matriptase activity in the absence of sufficient HAI-1Matriptase Complexes and Prostasin Complexes with HAI-1 and HAI-2 in Human Milk: Significant Proteolysis in LactationEnergetic and structural basis for activation of the epithelial sodium channel by matriptaseNatural 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-2SheddomeDB: the ectodomain shedding database for membrane-bound shed markers.The molecular and clinical impact of hepatocyte growth factor, its receptor, activators, and inhibitors in wound healing.Reinforced Epithelial Barrier Integrity via Matriptase Induction with Sphingosine-1-Phosphate Did Not Result in Disturbances in Physiological Redox Status.Targeting matriptase in breast cancer abrogates tumour progression via impairment of stromal-epithelial growth factor signalling.Purification from human milk of matriptase complexes with secreted serpins: mechanism for inhibition of matriptase other than HAI-1.The cutting edge: membrane-anchored serine protease activities in the pericellular microenvironment.Matriptase activation connects tissue factor-dependent coagulation initiation to epithelial proteolysis and signalingImbalanced matriptase pericellular proteolysis contributes to the pathogenesis of malignant B-cell lymphomas.Polarized epithelial cells secrete matriptase as a consequence of zymogen activation and HAI-1-mediated inhibition.Matriptase 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.Matriptase expression and zymogen activation in human pilosebaceous unit.Matriptase regulates proliferation and early, but not terminal, differentiation of human keratinocytes
P2860
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P2860
Regulation of the activity of matriptase on epithelial cell surfaces by a blood-derived factor.
description
2001 nî lūn-bûn
@nan
2001 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի մարտին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
name
Regulation of the activity of ...... ces by a blood-derived factor.
@ast
Regulation of the activity of ...... ces by a blood-derived factor.
@en
type
label
Regulation of the activity of ...... ces by a blood-derived factor.
@ast
Regulation of the activity of ...... ces by a blood-derived factor.
@en
prefLabel
Regulation of the activity of ...... ces by a blood-derived factor.
@ast
Regulation of the activity of ...... ces by a blood-derived factor.
@en
P2093
P2860
P1433
P1476
Regulation of the activity of ...... ces by a blood-derived factor.
@en
P2093
P2860
P304
P356
10.1046/J.1432-1327.2001.02016.X
P407
P577
2001-03-01T00:00:00Z