Search results for "PLATELET ACTIVATION"

showing 10 items of 121 documents

The evolving role of platelets in inflammation.

2003

Platelets are small in size and simple in structure. Nevertheless, these anucleate cytoplasts utilize complex molecular systems to regulate a variety of biological functions. Here we review evolutionary paths, traditional roles, and previously unrecognized biological capacities of platelets that interface thrombosis with inflammation and potentially identify new roles in inflammatory diseases.

Blood PlateletsInflammationIntegrinsInflammationTranslation (biology)ThrombosisHematologyMolecular systemsBiologyPlatelet ActivationCell biologymedicineHumansPlateletPlatelet activationmedicine.symptomPhylogenyJournal of thrombosis and haemostasis : JTH
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Potential and limitations of PKA/ PKG inhibitors for platelet studies

2021

Cyclic nucleotides (cAMP and cGMP) and corresponding protein kinases, protein kinase A (PKA) and protein kinase G (PKG), are the main intracellular mediators of endothelium-derived platelet inhibitors. Pharmacological PKA/PKG inhibitors are often used to discriminate between these two kinase activities and to analyze their underlying mechanisms. Previously we showed that all widely used PKG inhibitors (KT5823, DT3, RP isomers) either did not inhibit PKG or inhibited and even activated platelets independently from PKG. In this study, we examined several PKA inhibitors as well as inhibitors of adenylate and guanylate cyclases to reveal their effects on platelets and establish whether they are…

Blood PlateletsKinaseIntracellular Signaling Peptides and ProteinsAdenylate kinaseHematologyGeneral MedicineKT5720Cyclic AMP-Dependent Protein Kinaseschemistry.chemical_compoundchemistryBiochemistryCyclic AMPCyclic GMP-Dependent Protein Kinasescardiovascular systemHumansPlateletPlatelet activationProtein kinase ACyclic GMPcGMP-dependent protein kinaseIntracellularPlatelets
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Cortisol, Platelet Serotonin Content, and Platelet Activity in Patients With Major Depression and Type 2 Diabetes

2015

OBJECTIVE Hypothalamic-pituitary-adrenal system dysfunction, serotonergic system alterations, and enhanced platelet activity may contribute to the increased cardiac risk in depression. This exploratory study examined associations between cortisol parameters, platelet serotonin (5-HT) content, and platelet activity markers in patients with newly diagnosed major depression (MD) and/or Type 2 diabetes (T2DM) compared with healthy controls. METHODS We compared cortisol awakening response (CAR), diurnal decrease in salivary cortisol concentrations (slope), platelet 5-HT, and platelet markers (CD40, CD40 ligand [CD40L], soluble CD40L, CD62P, β-thromboglobulin, and platelet factor-4) in 22 T2DM pa…

Blood PlateletsMaleSerotoninmedicine.medical_specialtyCortisol awakening responseHydrocortisoneCD40 LigandType 2 diabetesPlatelet Factor 4SerotonergicCoronary artery diseaseDiabetes mellitusInternal medicinemedicineHumansPlateletPlatelet activationCD40 AntigensSalivaApplied PsychologyDepressive Disorder Majorbusiness.industryCase-control studyMiddle Agedbeta-Thromboglobulinmedicine.diseaseP-SelectinPsychiatry and Mental healthEndocrinologyDiabetes Mellitus Type 2Case-Control StudiesFemalebusinessPsychosomatic Medicine
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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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Platelet-endothelial interaction in tumor angiogenesis and microcirculation

2003

Activated platelets release angiogenic growth factors and have therefore been proposed to contribute to tumor angiogenesis within a potentially prothrombotic tumor microcirculation. The aim of the study was to investigate interactions of platelets with the angiogenic microvascular endothelium of highly vascularized solid tumors during growth and in response to endothelial stimulation in comparison with normal subcutaneous tissue. Experiments were performed in the dorsal skinfold chamber preparation of C57BL/6J mice bearing the Lewis lung carcinoma (LLC-1) or methylcholanthrene-induced fibrosarcoma (BFS-1). Fluorescently labeled rolling and adherent platelets, red blood cell velocity, and ve…

Blood PlateletsMalemedicine.medical_specialtyEndotheliumAngiogenesisFibrosarcomaImmunologyBiologyBiochemistrySkin Window TechniqueNeovascularizationCarcinoma Lewis LungMicePlatelet AdhesivenessCell MovementPlatelet adhesivenessInternal medicinemedicineAnimalsPlateletPlatelet activationCalcimycinIonophoresNeovascularization PathologicMicrocirculationVideotape RecordingLewis lung carcinomaCell BiologyHematologyPlatelet ActivationMice Inbred C57BLEndothelial stem cellmedicine.anatomical_structureEndocrinologyImmunologyCalciumEndothelium Vascularmedicine.symptomBlood Flow VelocityMethylcholanthreneBlood
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A peptide from the staphylococcal protein Efb binds P‐selectin and inhibits the interaction of platelets with leukocytes

2022

AimsP-selectin is a key surface adhesion molecule for the interaction of platelets with leukocytes. We have shown previously that the N-terminal domain of S. aureus extracellular fibrinogen-binding protein (Efb) binds to P-selectin and interferes with platelet-leukocyte aggregate formation. Here, we aimed to identify the minimal Efb motif required for binding platelets and to characterise its ability to interfering with the formation of platelet-leukocyte aggregates.Methods and ResultsUsing a library of synthetic peptides, we mapped the platelet-binding site to a continuous 20 amino acid stretch. The peptide Efb68-87 was able to bind to resting and, to a greater extent, thrombin-stimulated …

Blood PlateletsP-selectinPeptide030204 cardiovascular system & hematologyFibrinogenplatelet-leukocyte aggregate03 medical and health sciences/dk/atira/pure/subjectarea/asjc/2700/27200302 clinical medicineLeukocytesExtracellularmedicineHumansPlateletPlatelet activation030304 developmental biologyplateletInflammationchemistry.chemical_classification0303 health sciencesneutrophil extracellular trapChemistryFibrinogenThrombosisHematologyNeutrophil extracellular trapsPlatelet ActivationCell biologyP-SelectinthromboinflammationP-selectinPeptidesGlycoproteinleukocytemedicine.drugJournal of Thrombosis and Haemostasis
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High-throughput elucidation of thrombus formation reveals sources of platelet function variability

2019

In combination with microspotting, whole-blood microfluidics can provide high-throughput information on multiple platelet functions in thrombus formation. Based on assessment of the inter-and intra-subject variability in parameters of microspot-based thrombus formation, we aimed to determine the platelet factors contributing to this variation. Blood samples from 94 genotyped healthy subjects were analyzed for conventional platelet phenotyping: i.e. hematologic parameters, platelet glycoprotein (GP) expression levels and activation markers (24 parameters). Furthermore, platelets were activated by ADP, CRP-XL or TRAP. Parallel samples were investigated for whole-blood thrombus formation (6 mi…

Blood PlateletsPlatelet AggregationPlatelet Function TestsDISORDERSIntegrinPlatelet Membrane GlycoproteinsADHESIONPlatelet membrane glycoproteinArticleImmunophenotypingFlow cytometry03 medical and health sciences0302 clinical medicinePlatelet Biology & Its DisordersmedicineHumansPlateletPlatelet activationThrombuschemistry.chemical_classificationmedicine.diagnostic_testbiologyPlatelet CountThrombosisHematologyFlow CytometryPlatelet Activationmedicine.diseaseDIFFERENCEHigh-Throughput Screening AssaysCell biologychemistrybiology.proteinGPVIGlycoproteinBiomarkers030215 immunologyRESPONSESHaematologica-the Hematology Journal
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Flow Cytometric Analysis of Calcium Mobilization in Whole‐Blood Platelets

2003

Flow cytometry provides a convenient method to evaluate platelet activation by following the kinetics of intracellular free Ca2+, using sensitive fluorescent indicators that can be loaded into intact cells. Moreover, in the clinical setting, whole-blood techniques have obvious advantages to avoid artifactual platelet activation and allow the maintenance of near-physiological conditions. This unit describes a fast and sensitive flow cytometric procedure using the Ca2+-sensitive dye fluo-3 AM and the platelet-specific antibody CD41-PE to determine the kinetics of intracellular Ca2+ mobilization in whole-blood platelets with minimal manipulation of the samples. The technique may be applied to …

Blood PlateletsPlatelet Membrane Glycoprotein IIbHistologyStimulation030204 cardiovascular system & hematologyBiochemistryFlow cytometry03 medical and health sciences0302 clinical medicineThrombinMethodsmedicineAnimalsHumansPlateletCalcium SignalingPlatelet activationFluorescent Dyes030304 developmental biologyWhole blood0303 health sciencesAniline Compoundsmedicine.diagnostic_testChemistryAntibodies MonoclonalGeneral MedicineFlow CytometryIn vitro3. Good healthKineticsMedical Laboratory TechnologyXanthenesBiochemistryBiophysicsCalciumIntracellularmedicine.drugCurrent Protocols in Cytometry
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Deciphering of ADP-induced, phosphotyrosine-dependent signaling networks in human platelets by Src-homology 2 region (SH2)-profiling.

2012

Tyrosine phosphorylation plays a central role in signal transduction controlling many important biological processes. In platelets, the activity of several signaling proteins is controlled by tyrosine phosphorylation ensuring proper platelet activation and aggregation essential for regulation of the delicate balance between bleeding and hemostasis. Here, we applied Src-homology 2 region (SH2)-profiling for deciphering of the phosphotyrosine state of human platelets activated by adenosine diphosphate (ADP). Applying a panel of 31 SH2-domains, rapid and complex regulation of the phosphotyrosine state of platelets was observed after ADP stimulation. Specific inhibition of platelet P2Y receptor…

Blood PlateletsProtein tyrosine phosphataseSH2 domainBiochemistryReceptor tyrosine kinasePhosphorylation cascadesrc Homology Domainschemistry.chemical_compoundReceptors Purinergic P2Y1Tandem Mass SpectrometryHumansProtease-activated receptorProtein phosphorylationIloprostPhosphorylationPhosphotyrosineMolecular BiologybiologyTyrosine phosphorylationPlatelet ActivationCyclic AMP-Dependent Protein KinasesAdenosine MonophosphateReceptors Purinergic P2Y12Cell biologyAdenosine DiphosphateEnzyme ActivationBiochemistrychemistrybiology.proteinPurinergic P2Y Receptor AntagonistsPhosphorylationProtein Processing Post-TranslationalSignal TransductionProteomics
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Molecular Proteomics and Signalling of Human Platelets in Health and Disease

2021

Platelets are small anucleate blood cells that play vital roles in haemostasis and thrombosis, besides other physiological and pathophysiological processes. These roles are tightly regulated by a complex network of signalling pathways. Mass spectrometry-based proteomic techniques are contributing not only to the identification and quantification of new platelet proteins, but also reveal post-translational modifications of these molecules, such as acetylation, glycosylation and phosphorylation. Moreover, target proteomic analysis of platelets can provide molecular biomarkers for genetic aberrations with established or non-established links to platelet dysfunctions. In this report, we review …

Blood PlateletsProteomicsADPProteomeQH301-705.5receptorsProstacyclinReviewPROTEIN-COMPOSITIONProteomicsCatalysisInorganic ChemistryThromboxane A2chemistry.chemical_compoundThrombinREVEALSGPVImedicineHumansSYKPlateletPlatelet activationPhysical and Theoretical ChemistrysignallingBiology (General)Molecular BiologyQD1-999SpectroscopyNITRIC-OXIDEChemistryOrganic ChemistryACTIVATED PLATELETSPATHWAYSGLOBAL PROTEOMEGeneral MedicinePlatelet ActivationproteinsComputer Science ApplicationsCell biologyChemistrypost-translational modificationProteomeplateletsBlood Platelet DisordersGPVIProtein Processing Post-TranslationalSignal Transductionmedicine.drugInternational Journal of Molecular Sciences
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