Search results for "Tissue Factor"

showing 10 items of 41 documents

Tissue factor pathway inhibitor primes monocytes for antiphospholipid antibody-induced thrombosis

2019

Antiphospholipid antibodies (aPLs) with complex lipid and/or protein reactivities cause complement-dependent thrombosis and pregnancy complications. Although cross-reactivities with coagulation regulatory proteins contribute to the risk for developing thrombosis in patients with antiphospholipid syndrome, the majority of pathogenic aPLs retain reactivity with membrane lipid components and rapidly induce reactive oxygen species-dependent proinflammatory signaling and tissue factor (TF) procoagulant activation. Here, we show that lipid-reactive aPLs activate a common species-conserved TF signaling pathway. aPLs dissociate an inhibited TF coagulation initiation complex on the cell surface of m…

Male0301 basic medicineLipoproteinsImmunologyPlenary Paper030204 cardiovascular system & hematologyBiochemistryMonocytesThromboplastinProinflammatory cytokine03 medical and health sciencesTissue factor0302 clinical medicineTissue factor pathway inhibitorThrombinimmune system diseasesmedicineAnimalsHumansThromboplastinBlood CoagulationneoplasmsCells CulturedNADPH oxidasebiologyChemistryThrombosisCell BiologyHematologyComplement systemMice Inbred C57BL030104 developmental biologyAntibodies Antiphospholipidbiology.proteinCancer researchFemaleSignal transductionSignal Transductionmedicine.drugBlood
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GAS6

2017

Venous thrombosis is determined by the recruitment of monocytes and neutrophils to the inflamed endothelium and is primarily influenced by the plasmatic coagulation system.1 Monocyte tissue factor (TF) was identified as the causative trigger for intraluminal fibrin formation and thrombus load in the inferior vena cava (IVC) stenosis model, resembling human deep vein thrombosis.1 Although monocyte TF is prothrombotic, the TF expressed by activated endothelial cells triggers proinflammatory protease-activated receptor signaling pathways.2,3 See accompanying article on page 1315 In the past years, GAS6 (growth arrest–specific gene-6) was described as a major regulatory protein of prothrombotic…

0301 basic medicineEndotheliumVena Cava Inferior030204 cardiovascular system & hematologyFibrinogenInferior vena cavaMonocytes03 medical and health sciencesTissue factor0302 clinical medicinemedicineHumansPlateletThrombusVenous ThrombosisGAS6business.industryImpaired platelet aggregationmedicine.disease030104 developmental biologymedicine.anatomical_structuremedicine.veinAnesthesiaCancer researchCardiology and Cardiovascular MedicinebusinessGasolinemedicine.drugArteriosclerosis, Thrombosis, and Vascular Biology
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Platelet-localized FXI promotes a vascular coagulation-inflammatory circuit in arterial hypertension

2017

Multicellular interactions of platelets, leukocytes, and the blood vessel wall support coagulation and precipitate arterial and venous thrombosis. High levels of angiotensin II cause arterial hypertension by a complex vascular inflammatory pathway that requires leukocyte recruitment and reactive oxygen species production and is followed by vascular dysfunction. We delineate a previously undescribed, proinflammatory coagulation-vascular circuit that is a major regulator of vascular tone, blood pressure, and endothelial function. In mice with angiotensin II-induced hypertension, tissue factor was up-regulated, as was thrombin-dependent endothelial cell vascular cellular adhesion molecule 1 ex…

Blood PlateletsMale0301 basic medicinemedicine.medical_specialtyMacrophage-1 AntigenVascular Cell Adhesion Molecule-1Blood Pressure030204 cardiovascular system & hematologyThromboplastinMice03 medical and health sciencesTissue factor0302 clinical medicineThrombinInternal medicinemedicineAnimalsHumansPlateletRats WistarEndothelial dysfunctionBlood CoagulationFactor XIAgedMice Knockoutbusiness.industryAngiotensin IIThrombinGeneral MedicineMiddle AgedOligonucleotides Antisensemedicine.diseaseAngiotensin IIMice Inbred C57BL030104 developmental biologyEndocrinologyBlood pressuremedicine.anatomical_structurePlatelet Glycoprotein GPIb-IX ComplexPathophysiology of hypertensionHypertensionFemalebusinessmedicine.drugBlood vesselScience Translational Medicine
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Murine tissue factor disulfide mutation causes a bleeding phenotype with sex specific organ pathology and lethality.

2019

Tissue factor is highly expressed in sub-endothelial tissue. The extracellular allosteric disulfide bond Cys186-Cys209 of human tissue factor shows high evolutionary conservation and in vitro evidence suggests that it significantly contributes to tissue factor procoagulant activity. To investigate the role of this allosteric disulfide bond in vivo, we generated a C213G mutant tissue factor mouse by replacing Cys213 of the corresponding disulfide Cys190-Cys213 in murine tissue factor. A bleeding phenotype was prominent in homozygous C213G tissue factor mice. Pre-natal lethality of 1/3rd of homozygous offspring was observed between E9.5 and E14.5 associated with placental hemorrhages. After b…

Malemedicine.medical_specialtyOffspring610 Medicine & healthHemorrhage030204 cardiovascular system & hematologyBiologymedicine.disease_causeArticleThromboplastin11459 Center for Molecular Cardiology03 medical and health sciencesTissue factorArterial Thrombosis; Blood Coagulation and Fibrinolysis; Disorders of Coagulation and FibrinolysisMice0302 clinical medicineIn vivoPregnancyInternal medicinemedicineExtracellularAnimalsDisulfidesMutationHematologyPhenotypeIn vitroEndocrinologyPhenotype10036 Medical Clinic10076 Center for Integrative Human PhysiologyHemostasisMutation10209 Clinic for CardiologyFemale030215 immunologyHaematologica
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Protease‐activated receptor signaling in intestinal permeability regulation

2019

Protease-activated receptors (PARs) are a unique class of G-protein-coupled transmembrane receptors, which revolutionized the perception of proteases from degradative enzymes to context-specific signaling factors. Although PARs are traditionally known to affect several vascular responses, recent investigations have started to pinpoint the functional role of PAR signaling in the gastrointestinal (GI) tract. This organ is exposed to the highest number of proteases, either from the gut lumen or from the mucosa. Luminal proteases include the host's digestive enzymes and the proteases released by the commensal microbiota, while mucosal proteases entail extravascular clotting factors and the enzy…

0301 basic medicineProteasesCell typeProtease-activated receptorReceptors Proteinase-ActivatedBiologyBiochemistryPermeabilityEpitheliumInflammatory bowel disease03 medical and health sciencesGastrointestinal cancer0302 clinical medicineImmune systemmedicineAnimalsHumansProtease-activated receptorIntestinal MucosaSymbiosisReceptorMolecular BiologyMicrobial proteasesGastrointestinal NeoplasmsClotting factorIntestinal permeabilityCoagulationMicrobiotaEpithelial barrier functionCell BiologyInflammatory Bowel Diseasesmedicine.diseaseIntestinal epitheliumTissue factorGastrointestinal MicrobiomeCell biologyIntestineGastrointestinal TractDisease Models Animal030104 developmental biologyGene Expression RegulationBacterial Translocation030220 oncology & carcinogenesisPeptide HydrolasesSignal Transduction
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INFLAMMATORY CYTOKINES IN ACUTE ISCHEMIC STROKE.

2008

Three major cytokines, namely, tumor necrosis factor (TNF-alpha), interleukin (IL)-1, and IL-6 are produced by cultured brain cells after various stimuli such as ischemia. Neurones, astrocytes, microglia and oligodendrocytes can produce inflammatory mediators, and cytokine receptors are expressed constitutionally throughout the Central Nervous System (CNS), albeit at low levels. Cytokines are involved in virtually every facet of stroke and they have numerous pro-inflammatory and pro-coagulant effects on endothelium. TNF-alpha expression after stroke stimulates expression of tissue factor and adhesion molecules for leukocytes, release of interleukin-1 (IL-1), nitric oxide, factor VIII/von Wi…

medicine.medical_treatmentInflammationProinflammatory cytokineBrain IschemiaBrain ischemiaTissue factorDrug DiscoverymedicineHumansStrokePharmacologyInflammationMicrogliabusiness.industrymedicine.diseasePrognosisStrokeCytokinemedicine.anatomical_structureImmunologyAcute DiseaseCytokinesTumor necrosis factor alphamedicine.symptomStroke cytokinesbusinessBiomarkers
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Complement C5 but not C3 is expendable for tissue factor activation by cofactor-independent antiphospholipid antibodies

2018

The complement and coagulation cascades interact at multiple levels in thrombosis and inflammatory diseases. In venous thrombosis, complement factor 3 (C3) is crucial for platelet and tissue factor (TF) procoagulant activation dependent on protein disulfide isomerase (PDI). Furthermore, C5 selectively contributes to the exposure of leukocyte procoagulant phosphatidylserine (PS), which is a prerequisite for rapid activation of monocyte TF and fibrin formation in thrombosis. Here, we show that monoclonal cofactor-independent antiphospholipid antibodies (aPLs) rapidly activate TF on myelomonocytic cells. TF activation is blocked by PDI inhibitor and an anti-TF antibody interfering with PDI bin…

inorganic chemicals0301 basic medicineComplement factor I030204 cardiovascular system & hematologyMonocytesImmunoglobulin GThromboplastinThrombosis and HemostasisMice03 medical and health sciencesTissue factor0302 clinical medicineimmune system diseasesmedicineAnimalsPlateletneoplasmsBlood CoagulationMice KnockoutVenous ThrombosisComplement component 5biologyChemistryMonocyteComplement C5Complement C3Hematologynervous system diseasesbody regions030104 developmental biologymedicine.anatomical_structureCoagulationAntibodies Antiphospholipidbiology.proteinCancer researchAntibodyBlood Advances
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Acute methionine load‐induced hyperhomocysteinemia enhances platelet aggregation, thromboxane biosynthesis, and macrophage‐derived tissue factor acti…

1997

A moderate elevation of plasma homocysteine is a risk factor for atherosclerosis and arterial and veinous thrombosis. However, the mechanisms leading to vascular disorders are poorly understood because studies that have investigated the potential atherothrombogenicity of hyperhomocysteinemia in vivo are scarce. Using a rat model, we were the first to show that dietary folic acid deficiency, a major cause of basal hyperhomocysteinemia, is associated with enhanced macrophage-derived tissue factor and platelet activities. We proposed that an homocysteine-induced oxidative stress may account for this hypercoagulable state. To determine the true thrombogenicity of moderate hyperhomocysteinemia a…

medicine.medical_specialtyHyperhomocysteinemiaMethioninebiologybusiness.industryThromboxanemedicine.disease_causemedicine.diseaseBiochemistryLipid peroxidationchemistry.chemical_compoundTissue factorEndocrinologychemistryInternal medicineGeneticsbiology.proteinmedicinePlateletThromboxane-A synthasebusinessMolecular BiologyOxidative stressBiotechnologyThe FASEB Journal
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Inflammation and the coagulation system in tuberculosis: Tissue Factor leads the dance

2016

Mycobacterium tuberculosis, the causative agent of tuberculosis, drives the formation of granulomas, structures in which both immune cells and the bacterial pathogen cohabit. The most abundant cells in granulomas are macrophages, which contribute as both cells with bactericidal activity and as targets for M. tuberculosis infection and proliferation during the entire course of infection. The mechanisms and factors involved in the regulation and control of macrophage microenvironment-specific polarization and plasticity are not well understood, as some granulomas are able to control bacteria growth and others fail to do so, permitting bacterial spread. In this issue of the European Journal of…

0301 basic medicineTuberculosisMacrophageTuberculosiImmunologyInflammationMacrophages; Mycobacterium tuberculosis; Tissue Factor; Tuberculosis; Animals; Bacteremia; Cell Differentiation; Fibrin; Host-Pathogen Interactions; Humans; Immunity Innate; Lung; Macrophages; Mice; Mice Knockout; Mycobacterium tuberculosis; Pneumonia; Thromboplastin; Tuberculoma; Tuberculosis Pulmonary; Blood Coagulation; Immunology; Immunology and Allergy; Medicine (all)BacteremiaMycobacterium tuberculosiThromboplastinMycobacterium tuberculosis03 medical and health sciencesTissue factorMiceImmune systemImmunitymedicineMacrophageImmunology and AllergyAnimalsHumansTuberculomaBlood CoagulationLungTuberculosis PulmonaryMice KnockoutFibrinCord factorbiologyAnimalMedicine (all)MacrophagesCell DifferentiationMycobacterium tuberculosisPneumoniabiology.organism_classificationmedicine.diseaseImmunity Innate3. Good healthTissue FactorHost-Pathogen Interaction030104 developmental biologyImmunologyHost-Pathogen Interactionsmedicine.symptomHumanEuropean Journal of Immunology
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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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