Search results for " PAR-2"

showing 8 items of 8 documents

High density of tryptase-positive mast cells in human colorectal cancer: a poor prognostic factor related to protease-activated receptor 2 expression

2013

Tryptase(+) mast cells (MCs), abundant in the invasive front of tumours, contribute to tissue remodelling. Indeed, protease-activated receptor- 2 (PAR-2) activation by MC-tryptase is considered an oncogenic event in colorectal cancer (CRC). Recently, we have suggested NHERF1 as a potential new marker in CRC. In this study, we aimed to determine the distribution of tryptase(+) MCs and PAR-2 and to examine the relationship between PAR-2 and NHERF1, investigating their reputed usefulness as tumour markers. We studied a cohort of 115 CRC specimens including primary cancer (C) and adjacent normal mucosa (NM) by immunohistochemical double staining, analyzing the protein expression of MC-tryptase,…

AdultMaleCytoplasmPathologymedicine.medical_specialtySodium-Hydrogen ExchangersColorectal cancerLymphovascular invasionSettore MED/06 - Oncologia MedicainvasivenesstryptasePAR-2Cell CountTryptaseModels BiologicalImmunophenotypingNHERF1Intestinal mucosamedicineHumansReceptor PAR-2Mast CellsIntestinal Mucosaprognostic factorProtease-activated receptor 2AgedAged 80 and overbiologyColorectal cancer PAR-2 mast cell tryptase NHERF1 prognostic factor invasiveness aggressivenessOriginal ArticlesCell BiologyaggressivenessMiddle AgedPhosphoproteinsPrognosismedicine.diseaseMast cellColorectal cancermedicine.anatomical_structurebiology.proteinMolecular MedicineImmunohistochemistryFemaleTryptasesmast cellColorectal Neoplasms
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Signal transduction pathways involved in the mechanical responses to protease-activated receptors in rat colon.

2002

Recording simultaneously in vitro the changes of endoluminal pressure (index of circular muscle activity) and isometric tension (index of longitudinal muscle activity), we examined the mechanisms responsible for the apamin-sensitive relaxant and contractile responses induced by protease-activated receptor (PAR)-1 and PAR-2 activating peptides, SFLLRN-NH2 and SLIGRL-NH2, respectively, in rat colon. In the circular muscle, the inhibitory effects of SFLLRN-NH2 and SLIGRL-NH2 were significantly reduced by ryanodine, an inhibitor of Ca2+ release from the sarcoplasmic reticulum, but unaffected by 1-[6-[[17beta-methoxyestra-1,3,5(10)-trien-17-yl]amino]hexyl]-1H-pyrrole-2,5-dione (U73122), a phosph…

Intracellular FluidMalemedicine.medical_specialtyColonGenisteinBiologyIn Vitro Techniqueschemistry.chemical_compoundInternal medicinemedicineAnimalsReceptor PAR-2Receptor PAR-1Rats WistarReceptorProtein kinase CPharmacologyPhospholipase CRyanodine receptorNeural InhibitionRatsEndocrinologychemistryType C PhospholipasesMolecular MedicineCalciumReceptors ThrombinSignal transductionmedicine.symptomExtracellular SpaceTyrosine kinaseMuscle contractionMuscle ContractionSignal TransductionThe Journal of pharmacology and experimental therapeutics
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Identification of the integrin-binding site on coagulation factor VIIa required for proangiogenic PAR2 signaling.

2018

The tissue factor (TF) pathway serves both hemostasis and cell signaling, but how cells control these divergent functions of TF remains incompletely understood. TF is the receptor and scaffold of coagulation proteases cleaving protease-activated receptor 2 (PAR2) that plays pivotal roles in angiogenesis and tumor development. Here we demonstrate that coagulation factor VIIa (FVIIa) elicits TF cytoplasmic domain-dependent proangiogenic cell signaling independent of the alternative PAR2 activator matriptase. We identify a Lys-Gly-Glu (KGE) integrin-binding motif in the FVIIa protease domain that is required for association of the TF-FVIIa complex with the active conformer of integrin β1. A po…

0301 basic medicineCell signalingImmunologyIntegrinNeovascularization PhysiologicFactor VIIa030204 cardiovascular system & hematologyBiochemistryThromboplastinThrombosis and Hemostasis03 medical and health sciencesTissue factorMice0302 clinical medicineAnimalsHumansReceptor PAR-2Protein Interaction Domains and MotifsProtein Interaction MapsProtein kinase ACells CulturedIntegrin bindingBinding SitesbiologyChemistryIntegrin beta1Cell BiologyHematologyCell biologyCrosstalk (biology)030104 developmental biologyADP-Ribosylation Factor 6biology.proteinNIH 3T3 CellsPhosphorylationSignal transductionProtein BindingSignal TransductionBlood
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Factor VIIa-induced interaction with integrin controls the release of tissue factor on extracellular vesicles from endothelial cells.

2019

Essentials Prothrombotic extracellular vesicles (EV) carry agonist pathway-specific proteomes Agonists for protease activated receptor (PAR) 2 signaling have distinct effects on EV composition PAR2 signaling rapidly generates prothrombotic EV and slowly EV with inactive tissue factor (TF) FVIIa integrin ligation restricts TF incorporation into EV from endothelial cells SUMMARY: Background Cell injury signal-induced activation and release of tissue factor (TF) on extracellular vesicles (EVs) from immune and vessel wall cells propagate local and systemic coagulation initiation. TF trafficking and release on EVs occurs in concert with the release of cell adhesion receptors, including integrin …

Time Factorsmedia_common.quotation_subjectIntegrinFactor VIIa030204 cardiovascular system & hematologyThromboplastin03 medical and health sciencesTissue factorchemistry.chemical_compoundExtracellular Vesicles0302 clinical medicineHumansReceptor PAR-2Protease-activated receptorintegrin traffickingInternalizationReceptorCell adhesionBlood CoagulationCells Culturedmedia_commonbiologyFactor VIIChemistryIntegrin beta1protease-activated receptorsEndothelial CellsHematologytissue factorCell biologyProtein Transportbiology.proteinOligopeptidesIntracellularSignal TransductionJournal of thrombosis and haemostasis : JTH
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Macrophage protease-activated receptor 2 regulates fetal liver erythropoiesis in mice.

2020

AbstractDeficiencies in many coagulation factors and protease-activated receptors (PARs) affect embryonic development. We describe a defect in definitive erythropoiesis in PAR2-deficient mice. Embryonic PAR2 deficiency increases embryonic death associated with variably severe anemia in comparison with PAR2-expressing embryos. PAR2-deficient fetal livers display reduced macrophage densities, erythroblastic island areas, and messenger RNA expression levels of markers for erythropoiesis and macrophages. Coagulation factor synthesis in the liver coincides with expanding fetal liver hematopoiesis during midgestation, and embryonic factor VII (FVII) deficiency impairs liver macrophage development…

0301 basic medicinemedicine.medical_specialtyBiologyThrombosis and Hemostasis03 medical and health sciencesMice0302 clinical medicineHepcidinInternal medicinemedicineMacrophageAnimalsReceptor PAR-2ErythropoiesisProtease-activated receptor 2Mice KnockoutFetusMacrophagesHematologymedicine.diseaseHemolysisHaematopoiesis030104 developmental biologyEndocrinologymedicine.anatomical_structureLiver030220 oncology & carcinogenesisbiology.proteinErythropoiesisBone marrowBlood advances
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Human neutrophil elastase induces endothelial cell apoptosis by activating the PERK‐CHOP branch of the unfolded protein response

2017

Human neutrophil elastase impacts on atherosclerotic plaque stability by inducing apoptosis in endothelial cells. Our aim was to investigate the proapoptotic mechanism of elastase on endothelial cells and to evaluate the presence of elastase in human plaque material. Human endothelial cells were treated with purified human neutrophil elastase. Apoptosis was assayed by capsase-3/7 activation, TUNEL, and sub-G1 assay. Activation of unfolded protein response (UPR) effector molecules binding Ig protein, soluble X-binding protein-1, protein kinase RNA-like ER kinase (PERK), and C/EBP-homologous protein (CHOP) was analyzed by RT-PCR, immunocytochemistry, and Western blot. Genetic silencing of CHO…

0301 basic medicineSmall interfering RNACell SurvivalApoptosisCHOPBiochemistryGene Expression Regulation EnzymologicCell LineeIF-2 Kinase03 medical and health sciencesGeneticsHumansReceptor PAR-2Receptor PAR-1Protein kinase AMolecular BiologyCaspase 7Caspase 3KinaseChemistryElastaseEndothelial CellsAtherosclerosisMolecular biologyEndothelial stem cellCarotid Arteries030104 developmental biologyApoptosisUnfolded Protein ResponseUnfolded protein responseLeukocyte ElastaseTranscription Factor CHOPBiotechnologyThe FASEB Journal
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Tissue factor at the crossroad of coagulation and cell signaling

2018

The tissue factor (TF) pathway plays a central role in hemostasis and thrombo-inflammatory diseases. Although structure-function relationships of the TF initiation complex are elucidated, new facets of the dynamic regulation of TF?s activities on cells continue to emerge. Cellular pathways that render TF non-coagulant participate in signaling of distinct TF complexes with associated proteases through the protease-activated receptor (PAR) family of G-protein coupled receptors. Additional coreceptors, including the endothelial protein C receptor (EPCR) and integrins, confer signaling specificity by directing subcellular localization and trafficking. We here review how TF is switchedbetween it…

0301 basic medicineCell signalingProteasesCIENCIAS MÉDICAS Y DE LA SALUDIntegrinInmunologíaFactor VIIaThromboplastin03 medical and health sciencesTissue factorPROTEINASE- ACTIVATED RECEPTORSNeoplasmsmedicineAnimalsHumansReceptor PAR-2Myeloid CellsHEMOSTASISProtease-activated receptorENDOTHELIAL PROTEIN C RECEPTORBlood CoagulationInflammationEndothelial protein C receptorInnate immune systembiologyChemistryEndothelial CellsThrombosisInflammasomeHematologyCell biologyTHROMBOSISMedicina Básica030104 developmental biologyFactor Xabiology.proteinPROTEIN DISULFIDE-ISOMERASESSignal Transductionmedicine.drugJournal of Thrombosis and Haemostasis
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Proteases, Protease-Activated Receptors, and Atherosclerosis

2018

Coagulation activation by the TF (tissue factor) pathway plays pivotal roles in triggering platelets and precipitating acute coronary syndromes. Although dual antiplatelet therapy is effective in secondary cardiovascular prevention, combining platelet antagonism with low-dose aspirin and the oral coagulation FXa antagonist rivaroxaban has a synergistic clinical benefit over monotherapy in preventing the composite outcome of cardiovascular death, stroke, or myocardial infarction.1 It is, therefore, of considerable interest to understand the roles of coagulation proteases and their cell signaling effects in the development of atherosclerosis and vascular inflammation. Acute thrombosis in anim…

0301 basic medicineApolipoprotein EProteasesReceptors Proteinase-Activated030204 cardiovascular system & hematologyArticleMice03 medical and health sciencesTissue factor0302 clinical medicineThrombinEndopeptidasesAnimalsReceptor PAR-2MedicinePlateletbusiness.industryArteriosclerosisAtherosclerosismedicine.diseaseThrombosis030104 developmental biologyCoagulationCancer researchCardiology and Cardiovascular MedicinebusinessPeptide Hydrolasesmedicine.drugArteriosclerosis, Thrombosis, and Vascular Biology
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