Search results for " Purinergic P2X"

showing 9 items of 9 documents

Abacavir Induces Arterial Thrombosis in a Murine Model.

2018

Background The purinergic system is known to underlie prothrombotic and proinflammatory vascular programs, making the profile of experimental actions demonstrated by abacavir compatible with thrombogenesis. However, direct evidence of a prothrombotic effect by the drug has been lacking. Methods The present study appraised the effects of abacavir in a well-validated animal model of arterial thrombosis. The role of ATP-P2X7 receptors in the actions of the drug was also assessed, and the actions of recognized vascular-damaging agents and other nucleoside reverse-transcriptase inhibitors (NRTIs) were evaluated and compared to those of abacavir. Results Abacavir dose-dependently promoted thrombu…

0301 basic medicineDrugMaleAnti-HIV Agentsmedia_common.quotation_subject030204 cardiovascular system & hematologyPharmacologyProinflammatory cytokine03 medical and health sciences0302 clinical medicineimmune system diseasesAbacavirmedicineImmunology and AllergyAnimalsRofecoxibmedia_commonMice KnockoutDose-Response Relationship Drugbusiness.industryPurinergic receptorAntagonistvirus diseasesThrombosisPurinergic signallingmedicine.diseaseThrombosisDideoxynucleosidesDisease Models Animal030104 developmental biologyInfectious DiseasesReceptors Purinergic P2X7businessmedicine.drugThe Journal of infectious diseases
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Tissue factor prothrombotic activity is regulated by integrin-arf6 trafficking

2017

Objective— Coagulation initiation by tissue factor (TF) is regulated by cellular inhibitors, cell surface availability of procoagulant phosphatidylserine, and thiol-disulfide exchange. How these mechanisms contribute to keeping TF in a noncoagulant state and to generating prothrombotic TF remain incompletely understood. Approach and Results— Here, we study the activation of TF in primary macrophages by a combination of pharmacological, genetic, and biochemical approaches. We demonstrate that primed macrophages effectively control TF cell surface activity by receptor internalization. After cell injury, ATP signals through the purinergic receptor P2rx7 induce release of TF + microvesicles. T…

0301 basic medicinedynaminsIntegrin alpha4CellCardiorespiratory Medicine and Haematology030204 cardiovascular system & hematologyIntegrin alpha4beta1Inbred C57BLTransgenicMicechemistry.chemical_compound0302 clinical medicineAdenosine TriphosphateCell-Derived MicroparticlesReceptors2.1 Biological and endogenous factorsfibrinGene Knock-In TechniquesAetiologyPhospholipidsTumorbiologyChemistryADP-Ribosylation FactorsHematologyPhosphatidylserineCell biologyProtein Transportmedicine.anatomical_structurePhenotypeProteomeextracellular vesiclesCardiology and Cardiovascular MedicinePurinergic P2X7BiotechnologySignal TransductionGenotypeproteomeClinical SciencesIntegrinMice TransgenicFactor VIIaTransfectionExtracellular vesiclesFibrinArticleCell LineThromboplastin03 medical and health sciencesTissue factorCell Line TumormedicineAnimalsHumansBlood CoagulationMacrophagesThrombosisMice Inbred C57BL030104 developmental biologyCardiovascular System & HematologyADP-Ribosylation Factor 6biology.proteinReceptors Purinergic P2X7
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Complex regional pain syndrome:intradermal injection of phenylephrine evokes pain and hyperalgesia in a subgroup of patients with upregulated α1-adre…

2018

The aim of this study was to determine whether upregulated cutaneous expression of α1-adrenoceptors (α1-AR) is a source of pain in patients with complex regional pain syndrome (CRPS). Immunohistochemistry was used to identify α1-AR on nerve fibres and other targets in the affected and contralateral skin of 90 patients, and in skin samples from 38 pain-free controls. The distribution of α1-AR was compared between patients and controls, and among subgroups of patients defined by CRPS duration, limb temperature asymmetry, and diagnostic subtype (CRPS I vs CRPS II). In addition, α1-AR expression was investigated in relation to pain and pinprick hyperalgesia evoked by intradermal injection of th…

AdultMale0301 basic medicineAgonistInjections Intradermalmedicine.drug_classPainAdrenergicClonidinePhenylephrineYoung Adult03 medical and health sciences0302 clinical medicineReceptors Adrenergic alpha-1Adrenergic alpha-2 Receptor AgonistsmedicineHumansIntradermal injectionPhenylephrineAgedbusiness.industryMiddle Agedmedicine.diseaseUp-Regulation030104 developmental biologyAnesthesiology and Pain MedicineComplex regional pain syndromeNociceptionNeurologyHyperalgesiaAnesthesiaHyperalgesiaImmunohistochemistryFemaleAdrenergic alpha-1 Receptor AgonistsNeurology (clinical)medicine.symptombusinessComplex Regional Pain SyndromesReceptors Purinergic P2X3030217 neurology & neurosurgerymedicine.drug
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Evidence for the presence of P2y and P2x receptors with different functions in mouse stomach.

2005

To clarify the function of P2 receptor subtypes in mouse stomach, the motor responses to ATP, alpha,beta-methyleneATP (alpha,beta-MeATP), P2X receptor agonist, 2-methylthioATP (2-MeSATP), P2Y receptor agonist, and the effects of the desensitisation of P2X receptors with alpha,beta-MeATP and of P2Y receptors with ADPbetaS were analysed recording the endoluminal pressure from whole-organ. ATP-induced relaxation was antagonised by suramin, non-selective P2 receptor antagonist, by desensitisation of P2Y receptors with ADPbetaS, and increased by desensitisation of P2X receptors with alpha,beta-MeATP. alpha,beta-MeATP produced biphasic responses: relaxation, reduced by P2X- or P2Y desensitisation…

Agonistmedicine.medical_specialtyP2Y receptorRelaxationContraction (grammar)medicine.drug_classSuraminMuscle RelaxationTetrodotoxinP2 receptorBiologyIn Vitro TechniquesSettore BIO/09 - Fisiologiachemistry.chemical_compoundMiceAdenosine TriphosphateInternal medicinemedicineAnimalsReceptorPharmacologyContractionDose-Response Relationship DrugReceptors Purinergic P2Mouse stomachStomachAntagonistP2Y receptorThionucleotidesATPAdenosine DiphosphateMice Inbred C57BLEndocrinologychemistryP2X receptorReceptors Purinergic P2XTetrodotoxinmedicine.drugMuscle ContractionEuropean journal of pharmacology
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H89 enhances the sensitivity of cancer cells to glyceryl trinitrate through a purinergic receptor-dependent pathway

2014

// Marion Cortier 1, 2, 3 , Rahamata Boina-Ali 1, 2, 3 , Cindy Racoeur 1, 2, 3 , Catherine Paul 1, 2, 3 , Eric Solary 2, 4, 5 , Jean-Francois Jeannin 1, 2, 3 , Ali Bettaieb 1, 2, 3 1 EPHE, Tumor Immunology and Immunotherapy Laboratory, Dijon, F-21000, France 2 Inserm U866, Dijon, F-21000, France 3 EA7269, University of Burgundy, Dijon, F-21000, France 4 Inserm UMR1009, Gustave Roussy Institute, Villejuif F-94805, France 5 University Paris-Sud, Faculty of Medicine, Le Kremlin-Bicetre, F-94800, France Correspondence to: Ali Bettaieb, e-mail: ali.bettaieb@u-bourgogne.fr Keywords: H89, GTN, cancer, purinergic receptors, cGMP Received: October 08, 2014      Accepted: January 09, 2015      Publis…

H89SuraminApoptosisPharmacologyBiologyNitric OxideTransfectionNitric oxideMiceNitroglycerinReceptors Purinergic P2Y1chemistry.chemical_compoundAdenosine TriphosphateCell Line TumorNeoplasmspurinergic receptorsmedicineAnimalsHumanscancerCytotoxic T cellReceptorProtein Kinase InhibitorsMembrane Potential MitochondrialSulfonamidesReceptors Purinergic P2Gene Expression ProfilingPurinergic receptorReceptors PurinergicDrug SynergismOligonucleotides AntisenseIsoquinolinescGMPOncologychemistryApoptosisColonic NeoplasmsCancer cellcardiovascular systemSignal transductionReactive Oxygen SpeciesGTNReceptors Purinergic P2X3circulatory and respiratory physiologySignal TransductionResearch Papermedicine.drugOncotarget
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Melittin Modulates Keratinocyte Function through P2 Receptor-dependent ADAM Activation

2012

Melittin, the major component of the bee venom, is an amphipathic, cationic peptide with a wide spectrum of biological properties that is being considered as an anti-inflammatory and anti-cancer agent. It modulates multiple cellular functions but the underlying mechanisms are not clearly understood. Here, we report that melittin activates disintegrin-like metalloproteases (ADAMs) and that downstream events likely contribute to the biological effects evoked by the peptide. Melittin stimulated the proteolysis of ADAM10 and ADAM17 substrates in human neutrophil granulocytes, endothelial cells and murine fibroblasts. In human HaCaT keratinocytes, melittin induced shedding of the adhesion molecu…

KeratinocytesCell SurvivalBlotting WesternADAM17 ProteinP2 receptorBiologyModels Biologicalcomplex mixturesBiochemistryMelittinCell LineADAM10 ProteinMicechemistry.chemical_compoundTransactivationAdenosine TriphosphateAnimalsHumansPhosphorylationExtracellular Signal-Regulated MAP KinasesReceptorMolecular BiologyCells CulturedMice KnockoutDose-Response Relationship DrugReverse Transcriptase Polymerase Chain ReactionPurinergic receptorHEK 293 cellstechnology industry and agricultureMembrane ProteinsCell BiologyFibroblastsCadherinsEmbryo MammalianMelittenCell biologyErbB ReceptorsADAM ProteinsHaCaTHEK293 CellschemistryPhosphorylationlipids (amino acids peptides and proteins)Receptors Purinergic P2X7Amyloid Precursor Protein SecretasesJournal of Biological Chemistry
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Interference with purinergic signalling

2016

Objective: The association of abacavir (ABC), a guanosine analogue, with cardiovascular toxicity is a long-lasting matter of controversy engendered by the lack of a mechanism of action. Clinical data point to an acute mechanism of vascular inflammation. Previous studies have shown that ABC induces leukocyte-endothelial cell interactions, an indicator of vascular inflammation. These effects are reproduced by another purine analogue, didanosine, but not by pyrimidine or acyclic nucleotide analogues, hinting at an interference with the purinergic system. The aim of the present study was to assess the role of ATP-receptors in leukocyte accumulation induced by ABC. Design and methods: Clinical c…

Male0301 basic medicineIntravital MicroscopyAnti-HIV AgentsImmunologyMacrophage-1 AntigenLeukocyte RollingPharmacologyleukocyte-endothelium interactionsP2X7 receptors03 medical and health sciences0302 clinical medicineIn vivoCell AdhesionLeukocytesmedicineAnimalsHumansImmunology and Allergypurinergic030212 general & internal medicineCell adhesionReceptorCells CulturedMice KnockoutChemistryabacavirPurinergic receptorEndothelial CellsHIVPurinergic signallingDideoxynucleosidescardiovascular diseasesMice Inbred C57BLATP030104 developmental biologyInfectious DiseasesMechanism of actionKnockout mouseReceptors Purinergic P2X7medicine.symptomAIDS
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Involvement of the P2X7 purinergic receptor in colonic motor dysfunction associated with bowel inflammation in rats

2014

Background and Purpose Recent evidence indicates an involvement of P2X7 purinergic receptor (P2X7R) in the fine tuning of immune functions, as well as in driving enteric neuron apoptosis under intestinal inflammation. However, the participation of this receptor in the regulation of enteric neuromuscular functions remains undetermined. This study was aimed at investigating the role of P2X7Rs in the control of colonic motility in experimental colitis. Experimental Approach Colitis was induced in rats by 2,4-dinitrobenzenesulfonic acid. P2X7R distribution was examined by immunofluorescence analysis. The effects of A804598 (selective P2X7R antagonist) and BzATP (P2X7R agonist) were tested on co…

MalePurinergic P2X Receptor AntagonistsInflammatory Diseaseslcsh:MedicineInflammationGastroenterology and HepatologyBiologyInflammatory bowel diseaseSettore BIO/09 - FisiologiaGuanidinesPurinergic P2X Receptor AgonistsRats Sprague-DawleyImmune systemAdenosine TriphosphatemedicineMedicine and Health SciencesAnimalsP2X7 purinergic receptorColitisReceptorlcsh:SciencePurinergic P2X Receptor AgonistsPharmacologyNeuronsMultidisciplinaryPurinergic receptorlcsh:RBenzenesulfonatesMuscle Smoothmedicine.diseaseColitisRatsDisease Models AnimalImmunologyQuinolineslcsh:QP2X7 Purinergic Receptor Bowel Inflammation colonReceptors Purinergic P2X7medicine.symptomPurinergic P2X Receptor AntagonistsResearch Article
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Structural and Functional Basis for Understanding the Biological Significance of P2X7 Receptor

2020

The P2X7 receptor (P2X7R) possesses a unique structure associated to an as yet not fully understood mechanism of action that facilitates cell permeability to large ionic molecules through the receptor itself and/or nearby membrane proteins. High extracellular adenosine triphosphate (ATP) levels—inexistent in physiological conditions—are required for the receptor to be triggered and contribute to its role in cell damage signaling. The inconsistent data on its activation pathways and the few studies performed in natively expressed human P2X7R have led us to review the structure, activation pathways, and specific cellular location of P2X7R in order to analyze its biological relevance. The ATP-…

Models MolecularTranscription GeneticP2X7 receptor physiological rolechannel membrane proteinsAllosteric regulationReviewModels BiologicalCatalysislcsh:ChemistryInorganic ChemistryTransduction (genetics)chemistry.chemical_compoundAdenosine Triphosphateallosteric modulationsmedicineExtracellularAnimalsHumansPhysical and Theoretical ChemistryProtein Structure QuaternaryReceptorlcsh:QH301-705.5Molecular BiologySpectroscopyhuman P2X7 receptor isoformsPolymorphism GeneticCell MembraneOrganic ChemistryGeneral MedicineComputer Science ApplicationsCell biologyATPlcsh:Biology (General)lcsh:QD1-999Mechanism of actionchemistryMembrane proteinP2X7 receptorReceptors Purinergic P2X7medicine.symptomAdenosine triphosphateIntracellularSignal TransductionInternational Journal of Molecular Sciences
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