Loss of matriptase suppression underlies spint1 mutation-associated ichthyosis and postnatal lethality.
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HATL5: a cell surface serine protease differentially expressed in epithelial cancersMutations in CSTA, encoding Cystatin A, underlie exfoliative ichthyosis and reveal a role for this protease inhibitor in cell-cell adhesionStructure of catalytic domain of Matriptase in complex with Sunflower trypsin inhibitor-1Reduced prostasin (CAP1/PRSS8) activity eliminates HAI-1 and HAI-2 deficiency-associated developmental defects by preventing matriptase activationTMPRSS13 deficiency impairs stratum corneum formation and epidermal barrier acquisitionMatriptase activation, an early cellular response to acidosis.Membrane-anchored serine proteases in vertebrate cell and developmental biologyThe protease inhibitor HAI-2, but not HAI-1, regulates matriptase activation and shedding through prostasin.Transport via the transcytotic pathway makes prostasin available as a substrate for matriptaseIncreased matriptase zymogen activation in inflammatory skin disorders.Antithrombin regulates matriptase activity involved in plasmin generation, syndecan shedding, and HGF activation in keratinocytes.PAR2 absence completely rescues inflammation and ichthyosis caused by altered CAP1/Prss8 expression in mouse skin.Detection of active matriptase using a biotinylated chloromethyl ketone peptideFunctional analysis of a missense mutation in the serine protease inhibitor SPINT2 associated with congenital sodium diarrhea.Matriptase is inhibited by extravascular antithrombin in epithelial cells but not in most carcinoma cellsMatriptase protects against experimental colitis and promotes intestinal barrier recoveryMechanisms for the control of matriptase activity in the absence of sufficient HAI-1Selective Inhibition of Prostasin in Human Enterocytes by the Integral Membrane Kunitz-Type Serine Protease Inhibitor HAI-2Targeting matriptase in breast cancer abrogates tumour progression via impairment of stromal-epithelial growth factor signalling.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.Type II transmembrane serine proteases as potential targets for cancer therapy.Imbalanced matriptase pericellular proteolysis contributes to the pathogenesis of malignant B-cell lymphomas.The matriptase-prostasin proteolytic cascade in epithelial development and pathology.Membrane-bound serine protease inhibitor HAI-1 is required for maintenance of intestinal epithelial integrity.Hepatocyte growth factor activator inhibitor type 1 maintains the assembly of keratin into desmosomes in keratinocytes by regulating protease-activated receptor 2-dependent p38 signaling.Loss of membrane-bound serine protease inhibitor HAI-1 induces oral squamous cell carcinoma cells' invasiveness.Delineation of proteolytic and non-proteolytic functions of the membrane-anchored serine protease prostasin.Crystal Structure of a Two-domain Fragment of Hepatocyte Growth Factor Activator Inhibitor-1: FUNCTIONAL INTERACTIONS BETWEEN THE KUNITZ-TYPE INHIBITOR DOMAIN-1 AND THE NEIGHBORING POLYCYSTIC KIDNEY DISEASE-LIKE DOMAIN.Identification of the matriptase second CUB domain as the secondary site for interaction with hepatocyte growth factor activator inhibitor type-1.
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Loss of matriptase suppression underlies spint1 mutation-associated ichthyosis and postnatal lethality.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 23 April 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Loss of matriptase suppression ...... yosis and postnatal lethality.
@en
Loss of matriptase suppression ...... yosis and postnatal lethality.
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type
label
Loss of matriptase suppression ...... yosis and postnatal lethality.
@en
Loss of matriptase suppression ...... yosis and postnatal lethality.
@nl
prefLabel
Loss of matriptase suppression ...... yosis and postnatal lethality.
@en
Loss of matriptase suppression ...... yosis and postnatal lethality.
@nl
P2093
P2860
P1476
Loss of matriptase suppression ...... yosis and postnatal lethality.
@en
P2093
Karin List
Peter Kosa
Roman Szabo
P2860
P304
P356
10.2353/AJPATH.2009.090053
P407
P577
2009-04-23T00:00:00Z