Search results for "Tissue factor"

showing 10 items of 41 documents

Assessing the carcinogenic potential of low-dose exposures to chemical mixtures in the environment: the challenge ahead

2015

Goodson, William H. et al.

Cancer ResearchCarcinogenesis[SDV]Life Sciences [q-bio]METHOXYCHLOR-INDUCED ALTERATIONSReviewPharmacologyMESH: Carcinogens EnvironmentalCarcinogenic synergiesChemical mixturesNeoplasmsMESH: AnimalsMESH: NeoplasmsCarcinogenesiRisk assessmentCancerACTIVATED PROTEIN-KINASESMedicine (all)Low dose1. No povertyCumulative effectsBREAST-CANCER CELLSGeneral MedicineEnvironmental exposureMESH: CarcinogenesisBIO/10 - BIOCHIMICAEPITHELIAL-MESENCHYMAL TRANSITION3. Good health[SDV] Life Sciences [q-bio]Environmental CarcinogenesisESTROGEN-RECEPTOR-ALPHARisk assessmentHumanMESH: Environmental ExposureENDOCRINE-DISRUPTING CHEMICALSTARGETING TISSUE FACTOR[SDV.CAN]Life Sciences [q-bio]/CancerBiologyPrototypical chemical disruptorsExposure[SDV.CAN] Life Sciences [q-bio]/CancerEnvironmental healthmedicine[SDV.EE.SANT] Life Sciences [q-bio]/Ecology environment/HealthCarcinogenEnvironmental carcinogenesis[SDV.EE.SANT]Life Sciences [q-bio]/Ecology environment/HealthMESH: HumansAnimalPOLYBROMINATED DIPHENYL ETHERSCancerEnvironmental Exposuremedicine.diseaseMESH: Hazardous SubstancesCarcinogens EnvironmentalMIGRATION INHIBITORY FACTORVASCULAR ENDOTHELIAL-CELLSHazardous SubstanceNeoplasmCarcinogenesis
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Gpibα Engagement Induces Activation of Human Platelet TF and Association with Constitutively Platelet Surface-Bound FVIIa

2019

The membranes of activated platelets assemble clotting protein complexes and enzymatic reactions needed for hemostasis and causing pathological thrombosis. Several reports have shown that human platelets contain TF, but controversies remain on the functional contributions of platelet TF to coagulation initiation. Here, we delineate the mechanism that converts platelet-associated TF to a procoagulant molecule. By combining specific inhibitors with human platelets from normal probands or patients with Glanzmann thrombasthenia or homozygous GPVI deficiency, we analyzed the procoagulant activation of platelet TF by biochemical methods, confocal microscopy, platelet adhesion under flow on VWF an…

Glanzmann's thrombastheniaChemistryImmunologyCell BiologyHematologymedicine.diseaseBiochemistryCell biologychemistry.chemical_compoundTissue factor pathway inhibitorThrombinCoagulationmedicinePlateletPlatelet activationGPVIRistocetinmedicine.drugBlood
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CD248 enhances tissue factor procoagulant function, promoting arterial and venous thrombosis in mouse models

2021

BACKGROUND: CD248 is a pro-inflammatory, transmembrane glycoprotein expressed by vascular smooth muscle cells (VSMC), monocytes/macrophages, and other cells of mesenchymal origin. Its distribution and properties are reminiscent of those of the initiator of coagulation, tissue factor (TF). OBJECTIVE: We examined whether CD248 also participates in thrombosis. METHODS: We evaluated the role of CD248 in coagulation using mouse models of vascular injury, and by assessing its functional interaction with the TF-factor VIIa (FVIIa)-factor X (FX) complex. RESULTS: The time to ferric chloride-induced occlusion of the carotid artery in CD248 knockout (KO) mice was significantly longer than in wild-typ…

InflammationFactor VIIa030204 cardiovascular system & hematologyInferior vena cavaArticleThromboplastin03 medical and health sciencesTissue factorchemistry.chemical_compoundMice0302 clinical medicineThrombinTissue factor pathway inhibitorAntigens CDAntigens NeoplasmmedicineAnimalsHumansMice KnockoutVenous Thrombosismedicine.diagnostic_testFactor XHematologyCoagulationchemistrymedicine.veinCancer researchProthrombin Timemedicine.symptommedicine.drugPartial thromboplastin time
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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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Neuroprotective effect of Fn14 deficiency is associated with induction of the granulocyte-colony stimulating factor (G-CSF) pathway in experimental s…

2010

Using a transgenic mouse model of ischemic stroke we checked for a possible interaction of antiphospholipid antibodies (aPL) which often cause thromboses as well as central nervous system (CNS) involvement under non-thrombotic conditions and the TWEAK/Fn14 pathway known to be adversely involved in inflammatory and ischemic brain disease. After 7 days, infarct volumes were reduced in Fn14 deficient mice and were further decreased by aPL treatment. This was associated with strongest increase of the endogenous neuroprotective G-CSF/G-CSF receptor system. This unexpected beneficial action of aPL is an example for a non-thrombogenic action and the double-edged nature of aPL.

MaleGenetically modified mouseImmunologyMice TransgenicBiologyNeuroprotectionReceptors Tumor Necrosis FactorBrain IschemiaMiceRandom AllocationTissue factorimmune system diseasesAntiphospholipid syndromeGranulocyte Colony-Stimulating FactormedicineAnimalsHumansImmunology and AllergyneoplasmsStrokeLupus anticoagulantmedicine.diseaseMice Inbred C57BLDisease Models AnimalNeurologyTWEAK ReceptorReceptors Granulocyte Colony-Stimulating FactorImmunologyAntibodies AntiphospholipidTumor necrosis factor alphaNeurology (clinical)Inflammation MediatorsGranulocyte colony-stimulating factor receptorSignal TransductionJournal of Neuroimmunology
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Natural and engineered carboxy-terminal variants: decreased secretion and gain-of-function result in asymptomatic coagulation factor VII deficiency.

2012

We report 2 asymptomatic homozygotes for the nonsense p.R462X mutation affecting the carboxy-terminus of coagulation factor VII (FVII, 466 aminoacids). FVII levels of 3-5% and 2.7 ± 0.4% were found in prothrombin time-based and activated factor X (FXa) generation assays with human thromboplastins. Noticeably, FVII antigen levels were barely detectable (0.7 ± 0.2%) which suggested a gain-of-function effect. This effect was more pronounced with bovine thromboplastin (4.8 ± 0.9%) and disappeared with rabbit thromboplastin (0.7 ± 0.2%). This suggests that the mutation influences tissue factor/FVII interactions. Whereas the recombinant rFVII-462X variant confirmed an increase in specific activit…

MaleProteasesHeterozygoteFactor VII DeficiencyEnzyme-Linked Immunosorbent AssayFVIIBiologymedicine.disease_causeThromboplastinTissue factorchemistry.chemical_compoundCarboxy-terminalhemic and lymphatic diseasesmedicineFACTOR VII DEFICIENCY MOLECULAR VARIANTSThromboplastinMissense mutationAnimalsHumanscardiovascular diseasesChildBlood CoagulationProthrombin timeMutationmedicine.diagnostic_testFactor VIIHomozygoteHematologyFactor VIIMiddle AgedMolecular biologyAsymptomatic; Carboxy-terminal; FVII; Mutation;AsymptomaticchemistryCoagulationCodon NonsenseMutationMutagenesis Site-DirectedProthrombin TimeCattleFemaleRabbitsOriginal Articles and Brief Reports
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Prognostic value of plasma tissue factor and tissue factor pathway inhibitor for cardiovascular death in patients with coronary artery disease: the A…

2007

Summary. Background: Tissue factor (TF) and its specific inhibitor, tissue factor pathway inhibitor (TFPI), are important contributors to the initiation of the coagulation process. Objectives: To compare plasma levels of soluble TF (sTF) and free-TFPI (f-TFPI) between patients with stable angina pectoris (SAP) and acute coronary syndrome (ACS) and to assess the impact of the two variables on long-term prognosis. Patients/methods: Patients with SAPs (n = 1146) and acute coronary syndrome (n = 523) from the AtheroGene study were included and followed for 2.3 years. Because of the strong impact of unfractionated heparin (UFH) on f-TFPI levels, but not on sTF levels, patients having received UF…

Malemedicine.medical_specialtyAcute coronary syndromeTime FactorsLipoproteinsMyocardial InfarctionRisk AssessmentSeverity of Illness IndexAngina PectorisThromboplastinCoronary artery diseaseCohort StudiesTissue factor pathway inhibitorPredictive Value of TestsInternal medicineGermanymedicineHumansMyocardial infarctionProspective StudiesAgedProportional Hazards ModelsUnstable anginabusiness.industryHazard ratioCoronary StenosisHematologySyndromeMiddle Agedmedicine.diseasePrognosisThrombosisCardiovascular DiseasesCardiologyFemalebusinessBiomarkersBlood drawingFollow-Up StudiesJournal of thrombosis and haemostasis : JTH
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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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Plasma Kallikrein Contributes to Coagulation in the Absence of Factor XI by Activating Factor IX

2019

Objectives: FXIa (factor XIa) induces clot formation, and human congenital FXI deficiency protects against venous thromboembolism and stroke. In contrast, the role of FXI in hemostasis is rather small, especially compared with FIX deficiency. Little is known about the cause of the difference in phenotypes associated with FIX deficiency and FXI deficiency. We speculated that activation of FIX via the intrinsic coagulation is not solely dependent on FXI(a; activated FXI) and aimed at identifying an FXI-independent FIX activation pathway. Approach and Results: We observed that ellagic acid and long-chain polyphosphates activated the coagulation system in FXI-deficient plasma, as could be demo…

Malemedicine.medical_specialtyplasma kallikreinPREKALLIKREIN030204 cardiovascular system & hematologyPATHWAYMice03 medical and health sciencesTissue factor0302 clinical medicineThrombinInternal medicinemedicineAnimalsHEMOSTASIScoagulationBLOOD-COAGULATIONBlood CoagulationFactor XIFactor IXfactor IXPURIFICATIONbusiness.industryMOLECULAR-WEIGHT KININOGENThrombinPrekallikreinKallikreinfactor XIfactor XI deficiencyMice Inbred C57BLDEFICIENCYDisease Models AnimalTHROMBOSISEndocrinologyCoagulationTISSUE FACTOR030220 oncology & carcinogenesisHemostasisFemaleREDUCED INCIDENCECardiology and Cardiovascular Medicinebusinessmedicine.drug
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Further link between complement activation and blood coagulation

1977

EVIDENCE for interactions between the complement and haemostatic systems has come from two lines of research—blood platelets have been shown to interact with various complement components1–6, and more ambiguous results have been obtained with respect to the role of complement in endotoxin shock and the Shwartzman reaction7–13. We report here that the activated complement component C3b triggers a marked increase of tissue thromboplastin (factor III) activity in cultured human monocytes. Differential counting and nonspecific esterase staining14 of the final preparations regularly revealed more than 85% monocytes.

MultidisciplinaryChemistryComplement C3MonocytesThromboplastinComplement (complexity)Endotoxin shockComplement systemTissue factorCoagulationNonspecific esteraseImmunologyPlateletCycloheximideBlood CoagulationCells CulturedNature
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