Search results for "Platelet Aggregation"

showing 10 items of 155 documents

Modulation of platelet activation and initial cytokine release by alloplastic bone substitute materials.

2010

Objectives: Platelet-derived cytokines play a crucial role in tissue regeneration. In regenerative dental medicine, bone substitute materials (BSM) are widely used. However, initial interactions of BSM and platelets are still unknown. The aim of this study was to evaluate the potential of platelet activation and subsequent initial cytokine release by different commercial alloplastic BSM. Material and methods: Eight commercial BSM of different origins and chemical compositions (tricalcium phosphate, hydroxyapatite, bioactive glass: SiO2 and mixtures) were incubated with a platelet concentrate (platelet-rich plasma, PRP) of three healthy volunteers at room temperature for 15 min. Platelet cou…

Blood PlateletsCalcium PhosphatesVascular Endothelial Growth Factor APlatelet Aggregationmedicine.medical_treatmentPharmacologyCell Degranulationlaw.inventionlawmedicineHumansPlateletPlatelet activationPlatelet-Derived Growth FactorbiologyChemistryPlatelet CountPlatelet-Rich PlasmaGrowth factorDegranulationFlow CytometryPlatelet ActivationSilicon DioxideP-SelectinCytokineDurapatiteBioactive glassPlatelet-rich plasmaImmunologyBone Substitutesbiology.proteinOral SurgeryPlatelet-derived growth factor receptorClinical oral implants research
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Conformation-specific blockade of the integrin GPIIb/IIIa: a novel antiplatelet strategy that selectively targets activated platelets.

2006

Platelet activation causes conformational changes of integrin GPIIb/IIIa (α IIb β 3 ), resulting in the exposure of its ligand-binding pocket. This provides the unique possibility to design agents that specifically block activated platelets only. We used phage display of single-chain antibody (scFv) libraries in combination with several rounds of depletion/selection to obtain human scFvs that bind specifically to the activated conformation of GPIIb/IIIa. Functional evaluation of these scFv clones revealed that fibrinogen binding to human platelets and platelet aggregation can be effectively inhibited by activation-specific scFvs. In contrast to clinically used GPIIb/IIIa blockers, which ar…

Blood PlateletsCarotid Artery DiseasesBleeding TimePhysiologyAmino Acid MotifsMolecular ConformationEptifibatidePlatelet Glycoprotein GPIIb-IIIa ComplexFerric CompoundsAntibodiesMiceChloridesFibrinolytic AgentsmedicineAbciximabAnimalsHumansPlateletPlatelet activationChemistryFibrinogen bindingFibrinogenThrombosisTirofibanPlatelet ActivationMolecular biologyComplementarity Determining RegionsMice Inbred C57BLTirofibanImmunologyEptifibatidePlatelet aggregation inhibitorTyrosineCardiology and Cardiovascular MedicineGlycoprotein IIb/IIIaPeptidesPlatelet Aggregation Inhibitorsmedicine.drugCirculation research
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Vitamin C blocks inflammatory platelet-activating factor mimetics created by cigarette smoking.

1997

Cigarette smoking within minutes induces leukocyte adhesion to the vascular wall and formation of intravascular leukocyte-platelet aggregates. We find this is inhibited by platelet-activating factor (PAF) receptor antagonists, and correlates with the accumulation of PAF-like mediators in the blood of cigarette smoke-exposed hamsters. These mediators were PAF-like lipids, formed by nonenzymatic oxidative modification of existing phospholipids, that were distinct from biosynthetic PAF. These PAF-like lipids induced isolated human monocytes and platelets to aggregate, which greatly increased their secretion of IL-8 and macrophage inflammatory protein-1alpha. Both events were blocked by a PAF r…

Blood PlateletsChemokineAntioxidantTime FactorsPlatelet Aggregationmedicine.drug_classNeutrophilsmedicine.medical_treatmentPhospholipidReceptors Cell SurfaceAscorbic AcidPlatelet Membrane GlycoproteinsPharmacologyAntioxidantsMonocytesReceptors G-Protein-Coupledchemistry.chemical_compoundReference ValuesCricetinaemedicineCell AdhesionAnimalsHumansPlateletPlatelet Activating FactorReceptorChemokine CCL4Cell AggregationLeukocyte aggregationbiologyPlatelet-activating factorChemistryInterleukin-8SmokingGeneral MedicineAzepinesMacrophage Inflammatory ProteinsTriazolesReceptor antagonistBiochemistrybiology.proteinlipids (amino acids peptides and proteins)Platelet Aggregation InhibitorsResearch Article
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Time-resolved characterization of cAMP/PKA-dependent signaling reveals that platelet inhibition is a concerted process involving multiple signaling p…

2014

One of the most important physiological platelet inhibitors is endothelium-derived prostacyclin which stimulates the platelet cyclic adenosine monophosphate/protein kinase A (cAMP/PKA)-signaling cascade and inhibits virtually all platelet-activating key mechanisms. Using quantitative mass spectrometry, we analyzed time-resolved phosphorylation patterns in human platelets after treatment with iloprost, a stable prostacyclin analog, for 0, 10, 30, and 60 seconds to characterize key mediators of platelet inhibition and activation in 3 independent biological replicates. We quantified over 2700 different phosphorylated peptides of which 360 were significantly regulated upon stimulation. This com…

Blood PlateletsImmunologyProstacyclinBiologyBiochemistrychemistry.chemical_compoundCyclic AMPmedicineHumansCyclic adenosine monophosphateIloprostProtein Interaction MapsPlatelet activationPhosphorylationProtein kinase AKinaseCell BiologyHematologyPlatelet ActivationCyclic AMP-Dependent Protein KinaseschemistryBiochemistryPlatelet aggregation inhibitorPhosphorylationSignal transductionPlatelet Aggregation InhibitorsSignal Transductionmedicine.drugBlood
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Incorporation and metabolism of dietary trans isomers of linolenic acid alter the fatty acid profile of rat tissues

2000

To study the influence on lipid metabolism and platelet aggregation of the fatty acid isomerization that occurs during heat treatment, weanling rats were fed for 8 wk a diet enriched with 5% isomerized (experimental group) or normal (control group) canola oil. Geometrical isomers of alpha-linolenic acid representing 0.2 g/100 g of the experimental diet were incorporated into liver, platelets, aorta and heart, at the expense of their cis homologue and of 18:2(n-6). The major isomer, 9c,12c,15t-18:3, was also metabolized to 5c,8c,11c,14c,17t-20:5 and to an unknown compound, found in liver, platelets and aorta, which has been identified tentatively as 7c, 10c,13c,16c,19t-22:5. The greater 20:4…

Blood PlateletsMalePlatelet Aggregation030309 nutrition & dieteticsLinolenic acidMedicine (miscellaneous)WeanlingWeaningBiologyFatty Acids Monounsaturated03 medical and health sciencesDietary Fats UnsaturatedIsomerismAnimalsPlateletRats WistarComputingMilieux_MISCELLANEOUS030304 developmental biologychemistry.chemical_classification0303 health sciencesNutrition and DieteticsMyocardiumBody WeightFatty Acidsalpha-Linolenic AcidFatty acidLipid metabolismMetabolismRats[SDV.AEN] Life Sciences [q-bio]/Food and NutritionLiverBiochemistrychemistryRATRapeseed OilCollagenIsomerization[SDV.AEN]Life Sciences [q-bio]/Food and NutritionCis–trans isomerism
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In-vitro and Ex-vivo Inhibition of Blood Platelet Aggregation by Naftazone

1996

Abstract Because of the considerable interest in the role of platelets and antiplatelet therapy in cardiovascular disease, including the aggregation of platelets to each other during arterial thrombosis and atherogenesis, we have studied the effect of naftazone (Etioven), an original vasculotropic drug on platelet aggregation. Rat and human platelets were prepared and incubated in-vitro with different concentrations of naftazone. We found that naftazone inhibited both platelet secretion and aggregation in platelet-rich plasma (PRP) and washed platelets after stimulation with thrombin or ADP. Rats were also treated intraperitoneally for five days with various naftazone doses (0.125-10 mg kg−…

Blood PlateletsMaleSerotoninPlatelet AggregationPharmaceutical ScienceStimulationIn Vitro TechniquesPharmacologyRats Sprague-DawleyThrombinmedicineAnimalsHumansPlateletTiclopidinePharmacologyAspirinChemistryThrombinBiological activityRatsAdenosine DiphosphateDipyridamoleBiochemistryPlatelet Aggregation InhibitorsEx vivoNaphthoquinonesmedicine.drugJournal of Pharmacy and Pharmacology
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PHOSPHODIESTERASE INHIBITORS PIROXIMONE AND ENOXIMONE INHIBIT PLATELET AGGREGATION IN VIVO AND IN VITRO

1997

The phosphodiesterase type III inhibitors piroximone (PIR) and enoximone (ENO) exert positive inotropic and vasodilating effects in patients with severe heart failure. PIR and ENO raise cyclic AMP levels in cardiac and vascular smooth muscle cells. Platelet activity is also regulated by intracellular levels of cyclic AMP. In this study we have investigated the effects of PIR and ENO on platelet activity in vivo and in vitro. PIR and ENO inhibited ADP induced platelet aggregation in a time- and concentration-dependent manner with IC50-values of 67 +/- 14 mumol/l and 129 +/- 6 mumol/l, respectively. Coincubation of PIR with the adenylate cyclase activator iloprost resulted in a synergistic po…

Blood PlateletsMalemedicine.medical_specialtyCardiotonic AgentsVascular smooth musclePlatelet AggregationPhosphodiesterase InhibitorsVasodilationIn vivoInternal medicineCyclic AMPmedicineAnimalsHumansEnoximonePlateletPlatelet activationRats WistarEnoximonebiologyChemistryImidazolesPhosphodiesteraseHematologyRatsEndocrinologyEnzyme inhibitorbiology.proteinCalciumPlatelet Aggregation Inhibitorsmedicine.drugThrombosis Research
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Blood flow patterns spatially associated with platelet aggregates in murine colitis.

2009

In the normal murine mucosal plexus, blood flow is generally smooth and continuous. In inflammatory conditions, such as chemically-induced murine colitis, the mucosal plexus demonstrates markedly abnormal flow patterns. The inflamed mucosal plexus is associated with widely variable blood flow velocity as well as discontinuous and even bidirectional flow. To investigate the mechanisms responsible for these blood flow patterns, we used intravital microscopic examination of blood flow within the murine mucosal plexus during dextran sodium sulphate-and trinitrobenzenesulfonic acid-induced colitis. The blood flow patterns within the mucosal plexus demonstrated flow exclusion in 18% of the vessel…

Blood PlateletsPathologymedicine.medical_specialtyHistologyPlatelet AggregationInterleukin-1betaBiologyArticleMicrocirculationchemistry.chemical_compoundMiceIntestinal mucosamedicineAnimalsPlateletColitisIntestinal MucosaEcology Evolution Behavior and SystematicsPlexusMice Inbred BALB CGene Expression ProfilingMicrocirculationDextran SulfateBlood flowmedicine.diseaseColitisMice Inbred C57BLDextranchemistryTrinitrobenzenesulfonic AcidRegional Blood FlowAcute DiseaseEndothelium VascularAnatomyChemokinesIntravital microscopyBiotechnologyAnatomical record (Hoboken, N.J. : 2007)
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The histone deacetylase sirtuin 2 is a new player in the regulation of platelet function

2015

SummaryBackground Histone deacetylases (HDACs) play a key role in signaling in many cell types. However, little is known about the participation of HDACs, particularly sirtuins (SIRTs), in platelet reactivity. Objective To investigate the role of HDACs in platelets, we examined the effects of SIRT inhibition on platelet function and protein acetylation in human platelets. Methods We used washed platelets obtained from healthy subjects. Cambinol (SIRT1 and SIRT2 inhibitor), AGK2 (specific SIRT2 inhibitor) and EX527 (specific SIRT1 inhibitor) were used as SIRT inhibitors. Platelets were stimulated with collagen, thrombin, or U46619, and platelet responses were determined according to optical …

Blood PlateletsPlatelet AggregationCytoplasmic GranulesSIRT2Glycogen Synthase Kinase 3Akt3 protein kinaseSirtuin 2sirtuinsHumansPlateletRNA MessengerPhosphorylationProtein kinase Bacetylationblood plateletGlycogen Synthase Kinase 3 betabiologySecretory VesiclesAcetylationHematologyCell biologyHistone Deacetylase InhibitorsBiochemistryAcetylationSirtuinbiology.proteinPhosphorylationPlatelet aggregation inhibitorCalciumHistone deacetylaseProtein Processing Post-TranslationalProto-Oncogene Proteins c-aktPlatelet Aggregation Inhibitorssignal transductionSignal TransductionJournal of Thrombosis and Haemostasis
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Phosphorylation of CalDAG-GEFI by protein kinase A prevents Rap1b activation.

2013

Summary Background Signaling via protein kinase A (PKA) and protein kinase G (PKG) is critical for maintaining platelets in the resting state. Both kinases down-regulate the activity of the small GTPase Rap1b, a critical signaling switch for integrin activation and platelet aggregation. However, the mechanism of Rap1b regulation by PKA and PKG is largely unknown. Objective To identify the PKA phosphorylation sites in calcium and diacylglycerol-regulated guanine nucleotide exchange factor I (CalDAG-GEFI), the main GEF for Rap1b in platelets, and the effect of CalDAG-GEFI phosphorylation in Rap1b activation. Methods The phosphorylation sites in CalDAG-GEFI were identified by radio-active phos…

Blood PlateletsPlatelet AggregationMolecular Sequence DataBiologyMass SpectrometryPhosphorylation cascadeCyclic AMPGuanine Nucleotide Exchange FactorsHumansImmunoprecipitationProtein phosphorylationAmino Acid SequenceCalcium SignalingPhosphorylationProtein kinase ACalcium signalingAlanineSequence Homology Amino AcidKinaseHematologyCyclic AMP-Dependent Protein KinasesEnzyme Activationrab1 GTP-Binding ProteinsHEK293 CellsBiochemistryMutationPhosphorylationGuanine nucleotide exchange factorGuanosine TriphosphatecGMP-dependent protein kinasePlasmidsSignal TransductionJournal of thrombosis and haemostasis : JTH
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