0000000000342461

AUTHOR

Stephanie Makhoul

showing 4 related works from this author

Curcumin at Low Doses Potentiates and at High Doses Inhibits ABT-737-Induced Platelet Apoptosis

2021

Curcumin is a natural bioactive component derived from the turmeric plant Curcuma longa, which exhibits a range of beneficial activities on human cells. Previously, an inhibitory effect of curcumin on platelets was demonstrated. However, it is unknown whether this inhibitory effect is due to platelet apoptosis or procoagulant platelet formation. In this study, curcumin did not activate caspase 3-dependent apoptosis of human platelets, but rather induced the formation of procoagulant platelets. Interestingly, curcumin at low concentration (5 µM) potentiated, and at high concentration (50 µM) inhibited ABT-737-induced platelet apoptosis, which was accompanied by inhibition of ABT-737-mediated…

0301 basic medicinePharmacologyPiperazinesNitrophenolschemistry.chemical_compound0302 clinical medicinePlateletBiology (General)SpectroscopyCaspaseSulfonamidesbiologyKinaseapoptosisGeneral MedicinethrombinDrug Resistance Multipleprocoagulant activityComputer Science ApplicationsChemistry030220 oncology & carcinogenesisplateletsmedicine.drugBlood PlateletsAdenosine monophosphateautophagyCurcuminQH301-705.5ArticleCatalysisInorganic Chemistry03 medical and health sciencesCurcumaThrombinmedicineHumansATP Binding Cassette Transporter Subfamily B Member 1Physical and Theoretical ChemistryQD1-999Molecular BiologyProtein kinase BPlant ExtractsBiphenyl CompoundsOrganic ChemistryAdenosine Monophosphate030104 developmental biologychemistryApoptosisbiology.proteinCurcuminProto-Oncogene Proteins c-aktPlatelet Aggregation InhibitorsInternational Journal of Molecular Sciences
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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
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Feedback Regulation of Syk by Protein Kinase C in Human Platelets

2019

The spleen tyrosine kinase (Syk) is essential for immunoreceptor tyrosine-based activation motif (ITAM)-dependent platelet activation, and it is stimulated by Src-family kinase (SFK)-/Syk-mediated phosphorylation of Y352 (interdomain-B) and Y525/526 (kinase domain). Additional sites for Syk phosphorylation and protein interactions are known but remain elusive. Since Syk S297 phosphorylation (interdomain-B) was detected in platelets, we hypothesized that this phosphorylation site regulates Syk activity via protein kinase C (PKC)-and cyclic adenosine monophosphate (cAMP)-dependent pathways. ADP, the GPVI-agonist convulxin, and the GPIb&alpha

0301 basic medicineIndolesPlatelet AggregationSyk030204 cardiovascular system & hematologyenvironment and public healthMaleimideslcsh:Chemistrychemistry.chemical_compound0302 clinical medicinePhosphorylationlcsh:QH301-705.5SpectroscopyFeedback PhysiologicalKinaseConvulxinhemic and immune systemsGeneral MedicineComputer Science ApplicationsCell biologyAdenosine DiphosphateplateletsPhosphorylationbiological phenomena cell phenomena and immunityBlood Plateletschemical and pharmacologic phenomenaViper Venomsspleen tyrosine kinase (Syk)CatalysisArticleInorganic Chemistryglycoprotein VIglycoprotein Ibα03 medical and health sciencesCrotalid VenomsHumansSyk KinaseCyclic adenosine monophosphateLectins C-TypePlatelet activationPhysical and Theoretical ChemistryMolecular BiologyProtein kinase CPhospholipase C gammaOrganic Chemistryenzymes and coenzymes (carbohydrates)030104 developmental biologyProtein kinase domainchemistrylcsh:Biology (General)lcsh:QD1-999Calciumcyclic adenosine monophosphate (cAMP)protein kinase CInternational Journal of Molecular Sciences
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CD36-fibrin interaction propagates FXI-dependent thrombin generation of human platelets.

2019

Thrombin converts fibrinogen to fibrin and activates blood and vascular cells in thrombo-inflammatory diseases. Platelets are amplifiers of thrombin formation when activated by leukocyte- and vascular cell-derived thrombin. CD36 on platelets acts as sensitizer for molecules with damage-associated molecular patterns, thereby increasing platelet reactivity. Here, we investigated the role of CD36 in thrombin-generation on human platelets, including selected patients with advanced chronic kidney disease (CKD). Platelets deficient in CD36 or blocked by anti-CD36 antibody FA6.152 showed impaired thrombin generation triggered by thrombin in calibrated automated thrombography. Using platelets with …

0301 basic medicineBlood PlateletsCD36 AntigensCD36InflammationFibrinogenBiochemistryFibrin03 medical and health sciences0302 clinical medicineThrombinBlocking antibodyGeneticsmedicineHumansPlateletRenal Insufficiency ChronicMolecular BiologyFactor XIFibrinbiologyChemistryCell adhesion moleculeThrombinPlatelet ActivationBlood Coagulation FactorsCell biology030104 developmental biologybiology.proteinmedicine.symptom030217 neurology & neurosurgerycirculatory and respiratory physiologyBiotechnologymedicine.drugFASEB journal : official publication of the Federation of American Societies for Experimental BiologyREFERENCES
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