Search results for "ACTIVATION"

showing 10 items of 2079 documents

The Serine/Threonine Protein Phosphatase 2A (PP2A) Regulates Syk Activity in Human Platelets

2020

Distinct membrane receptors activate platelets by Src-family-kinase (SFK)-, immunoreceptor-tyrosine-based-activation-motif (ITAM)-dependent stimulation of spleen tyrosine kinase (Syk). Recently, we reported that platelet activation via glycoprotein (GP) VI or GPIb&alpha

Blood Platelets0301 basic medicinePlatelet AggregationPhosphataseSykchemical and pharmacologic phenomena030204 cardiovascular system & hematologyenvironment and public healthspleen tyrosine kinase (Syk)ArticleCatalysisInorganic ChemistryDephosphorylationglycoprotein VIglycoprotein Ibα03 medical and health sciences0302 clinical medicineHumansSyk KinaseProtein Phosphatase 2Platelet activationPhosphorylationPhysical and Theoretical ChemistryMolecular BiologySpectroscopyProtein kinase CChemistryKinaseprotein phosphatase 2AOrganic Chemistryhemic and immune systemsGeneral MedicineProtein phosphatase 2Protein-Tyrosine KinasesPlatelet Activation3. Good healthComputer Science ApplicationsCell biologyenzymes and coenzymes (carbohydrates)030104 developmental biologyplateletsPhosphorylationbiological phenomena cell phenomena and immunitySignal TransductionInternational Journal of Molecular Sciences
researchProduct

The Neutrophil Secretome as a Crucial Link between Inflammation and Thrombosis

2021

Cardiovascular diseases are a leading cause of death. Blood–cell interactions and endothelial dysfunction are fundamental in thrombus formation, and so further knowledge of the pathways involved in such cellular crosstalk could lead to new therapeutical approaches. Neutrophils are secretory cells that release well-known soluble inflammatory signaling mediators and other complex cellular structures whose role is not fully understood. Studies have reported that neutrophil extracellular vesicles (EVs) and neutrophil extracellular traps (NETs) contribute to thrombosis. The objective of this review is to study the role of EVs and NETs as key factors in the transition from inflammation to thrombo…

Blood Platelets0301 basic medicineQH301-705.5Neutrophilsneutrophil extracellular trapsInflammationContext (language use)Review030204 cardiovascular system & hematologyExosomesExtracellular TrapsCatalysisInorganic Chemistry03 medical and health sciences0302 clinical medicinemedicineAnimalsHumansPlateletPlatelet activationBiology (General)Physical and Theoretical ChemistryThrombusEndothelial dysfunctionQD1-999Molecular BiologySpectroscopythrombosisbusiness.industryOrganic ChemistryneutrophilGeneral MedicineNeutrophil extracellular trapsmedicine.diseaseComputer Science ApplicationsCell biologyChemistryCrosstalk (biology)secretome030104 developmental biologyinflammationplateletsmedicine.symptombusinessextracellular vesiclesSignal TransductionInternational Journal of Molecular Sciences
researchProduct

Impact of ticagrelor on P2Y1 and P2Y12 localization and on cholesterol levels in platelet plasma membrane

2017

Ticagrelor is an antiplatelet agent that inhibits platelet activation via P2Y12 antagonism. There are several studies showing that P2Y12 needs lipid rafts to be activated, but there are few data about how ticagrelor impacts lipid raft organization. Therefore, we aimed to investigate how ticagrelor could impact the distribution of cholesterol and consequently alter the organization of lipid rafts on platelet plasma membranes. We identified cholesterol-enriched raft fractions in platelet membranes by quantification of their cholesterol levels. Modifications in cholesterol and protein profiles (Flotillin 1, Flotillin 2, CD36, P2Y1, and P2Y12) were studied in platelets stimulated by ADP, treate…

Blood Platelets0301 basic medicineTicagrelorAdenosineCD36030204 cardiovascular system & hematologyPharmacologyReceptors Purinergic P2Y103 medical and health scienceschemistry.chemical_compoundMembrane Microdomains0302 clinical medicineP2Y12medicineHumansPlateletPlatelet activationLipid raftbiologyChemistryCholesterolCell MembraneHematologyGeneral MedicineReceptors Purinergic P2Y12Cholesterol030104 developmental biologyMembraneBiochemistryPurinergic P2Y Receptor Antagonistsbiology.proteinlipids (amino acids peptides and proteins)Ticagrelormedicine.drugPlatelets
researchProduct

Native, Intact Glucagon-Like Peptide 1 Is a Natural Suppressor of Thrombus Growth Under Physiological Flow Conditions

2020

Objective: In patients with diabetes mellitus, increased platelet reactivity predicts cardiac events. Limited evidence suggests that DPP-4 (dipeptidyl peptidase 4) influences platelets via GLP-1 (glucagon-like peptide 1)-dependent effects. Because DPP-4 inhibitors are frequently used in diabetes mellitus to improve the GLP-1-regulated glucose metabolism, we characterized the role of DPP-4 inhibition and of native intact versus DPP-4-cleaved GLP-1 on flow-dependent thrombus formation in mouse and human blood. Approach and Results: An ex vivo whole blood microfluidics model was applied to approach in vivo thrombosis and study collagen-dependent platelet adhesion, activation, and thrombus for…

Blood Platelets0301 basic medicineendocrine systemmedicine.medical_specialtyPlatelet AggregationPLATELET ACTIVATIONLinagliptin030204 cardiovascular system & hematologyDPP4Glucagon-Like Peptide-1 Receptorlaw.invention03 medical and health sciences0302 clinical medicinedipeptidyl peptidase 4Fibrinolytic AgentslawInternal medicineDiabetes mellitusmedicineAnimalsHumansPlateletIn patientThrombusglucose610 Medicine & healthDipeptidyl peptidase-4Mice KnockoutDipeptidyl-Peptidase IV InhibitorsChemistryPharmacology. TherapySitagliptin Phosphatedigestive oral and skin physiologyThrombosismedicine.diseaseGlucagon-like peptide-1Peptide Fragmentsglucagon-like peptide 1Mice Inbred C57BLMICE030104 developmental biologyEndocrinologyPhysiological flowdiabetes mellitusplateletsSuppressorHuman medicineCardiology and Cardiovascular MedicineSignal Transduction
researchProduct

Platelet Activation: a New Biological Activity of Guinea-pig C3a Anaphylatoxin

1978

3H-serotonin-release from labelled gp-platelets is established as a sensitive method for testing a new biological activity of gp-C3a anaphylatoxin in an autologous situation. Time-, dose- and temperature-dependent release reactions as well as specific inhibition by carboxypeptidase B and anti-C3a antibodies show that C3a is a potent and specific inducer of platelet activation. Inactive C3a does not induce 3H-serotonin-release but specifically inhibits the action of C3a on platelets.

Blood PlateletsAnaphylatoxinsSerotoninTime FactorsGuinea PigsImmunologychemical and pharmacologic phenomenaTritiumGuinea pigComplement Inactivator ProteinsAnimalsPlateletAnaphylatoxinInducerPlatelet activationComplement Inactivator ProteinsbiologyChemistryTemperatureBiological activityComplement C3General MedicineChromium RadioisotopesBiochemistrybiology.proteinAntibodyPeptidesScandinavian Journal of Immunology
researchProduct

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
researchProduct

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
researchProduct

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
researchProduct

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
researchProduct

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
researchProduct