Search results for "Suramin"

showing 9 items of 9 documents

Pharmacological characterization of uracil nucleotide-preferring P2Y receptors modulating intestinal motility: a study on mouse ileum.

2011

We investigated the possible modulation of the intestinal contractility by uracil nucleotides (UTP and UDP), using as model the murine small intestine. Contractile activity of a mouse ileum longitudinal muscle was examined in vitro as changes in isometric tension. Transcripts encoding for uracil-sensitive receptors was investigated by RT-PCR. UDP induced muscular contractions, sensitive to PPADS, suramin, or MRS 2578, P2Y(6) receptor antagonist, and mimicked by PSB 0474, P2Y(6)-receptor agonist. UTP induced biphasic effects characterized by an early inhibition of the spontaneous contractile activity followed by muscular contraction. UTP excitatory effects were antagonized by PPADS, suramin,…

AgonistMalemedicine.medical_specialtyP2Y receptormedicine.drug_classSuraminUDP UTP P2Y2 receptors P2Y4 receptors P2Y6 receptors Intestinal motilityUridine TriphosphateBiologySettore BIO/09 - FisiologiaUridine DiphosphateCellular and Molecular Neurosciencechemistry.chemical_compoundMiceOrgan Culture TechniquesIleumInternal medicinemedicineAnimalsPPADSheterocyclic compoundsReceptorMolecular BiologyPhospholipase CDose-Response Relationship DrugReceptors Purinergic P2Cell BiologyReceptor antagonistMice Inbred C57BLEndocrinologychemistryOriginal ArticleGastrointestinal MotilityUracil nucleotidemedicine.drug
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ATP and endogenous agonists inhibit evoked [3H]-noradrenaline release in rat iris via A1 and P2y-like purinoceptors.

1993

Effects of ATP, adenosine and purinoceptor antagonists on field stimulation-evoked (3 Hz, 2 min) [3H]-noradrenaline overflow were investigated in the rat isolated iris. ATP and adenosine inhibited the evoked overflow of [3H]-noradrenaline. 1,3-Dipropyl-8-cyclopentylxanthine (DPCPX) shifted the concentration-response curve of ATP to the right in a concentration-dependent manner, but with a potency (-log KB = 7.88) much lower than expected for an A1 adenosine receptor. In the continuous presence of DPCPX, the ATP-induced prejunctional inhibition was unaffected by suramin (100 mumol/l) and DIDS (4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid, 50 mumol/l) but was antagonized by the P2Y-rece…

Agonistmedicine.medical_specialtyAdenosinemedicine.drug_classSuraminIrisSuraminBiologyP2 receptor44'-Diisothiocyanostilbene-22'-Disulfonic AcidIn Vitro TechniquesSynaptic Transmissionchemistry.chemical_compoundNorepinephrineAdenosine TriphosphateInternal medicinemedicinePurinergic P2 Receptor AntagonistsAnimalsRats WistarPharmacologyProtein Synthesis InhibitorsReceptors Purinergic P2TriazinesPurinergic receptorReceptors Purinergic P1General MedicineAdenosine receptorAdenosineElectric StimulationRatsEndocrinologychemistryPurinergic P1 Receptor AntagonistsDIDSXanthinesAutoreceptormedicine.drugNaunyn-Schmiedeberg's archives of pharmacology
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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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Apoptotic effects of different drugs on cultured retinoblastoma Y79 cells

1998

This paper deals with the apoptotic effect exerted in human retinoblastoma Y79 cells by a number of compounds. A remarkable effect was observed after treatment with DNA-damaging agents, such as camptothecin, etoposide, cisplatin and carboplatin; camptothecin was found to be the most efficacious. Treatment with these compounds induced the appearance of morphological features of apoptosis in the cells together with the distinct fragmentation of DNA, as shown by agarose gel electrophoresis. These effects were also accompanied by a remarkable increase in the level of p53. Many other compounds, which are not DNA-damaging agents, induced the morphological features of apoptosis but none of them we…

AmsacrinePaclitaxelDNA damageAntineoplastic AgentsApoptosisSuraminDNA ladderingBiologyretinoblastomaCarboplatinchemistry.chemical_compoundTumor Cells CulturedmedicineHumansFragmentation (cell biology)EtoposideCisplatinSodium butyrateGeneral MedicineAntineoplastic Agents PhytogenicMolecular biologyButyrateschemistryApoptosisAgarose gel electrophoresisImmunologyButyric AcidCamptothecinCisplatinDrug Screening Assays AntitumorCamptothecinDNA Damagemedicine.drug
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Displacement of phenprocoumon (Marcumar) from albumin by sulfonylurea compounds, suramin, and ioglycamic acid.

1972

The technique of Sephadex gel filtration was employed to characterize the effect of some sulfonylurea compounds, ioglycamic acid, and suramin on the binding of phenprocoumon to bovine serum albumin.

ChlorpropamideChlorpropamideSuraminTolbutamideSerum albuminSuraminIn Vitro TechniquesBenzoatesPhenprocoumonCoumarinsBenzyl CompoundsmedicineAnimalsBovine serum albuminPharmacologyChromatographyBinding SitesbiologyChemistryAlbuminAnticoagulantsDextransSerum Albumin BovineGeneral MedicineCarbutamideGlycolatesCarbutamideSulfonylurea CompoundsSephadexbiology.proteinChromatography GelIodobenzoatesCattlemedicine.drugProtein BindingNaunyn-Schmiedeberg's archives of pharmacology
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Distribution of chlorpromazine in a simplified blood influenced by various drugs

1973

The binding of chlorpromazine to erythrocytes and to albumin as influenced by other drugs was studied in a simplified blood (31.5±0.3% bovine erythrocytes, 4 g-% bovine serum albumin in 0.02 M phosphate buffer solution containing 0.15 M NaCl). the total concentration of chlorpromazine in the simplified blood was 10−4 M, the concentration of the displacing drugs was 10−3 M. After an incubation period of 3 h at 22° C the chlorpromazine concentration was determined in the albumin solution after centrifugation of the blood at 3000×g and in the aqueous phase after ultracentrifugation at 150000×g. Under control conditions 68.1±0.9% of chlorpromazine was bound to the erythrocytes, 28.5±0.9% was bo…

ErythrocytesChlorpromazineIndomethacinSuraminBenzoatesBinding CompetitiveIncubation periodCoumarinsmedicineAnimalsDistribution (pharmacology)CentrifugationThiopentalBovine serum albuminChlorpromazinePharmacologySulfonamidesBinding SitesChromatographyQuininebiologyProbenecidChemistryFatty AcidsAqueous two-phase systemAlbuminSerum Albumin BovineGeneral MedicineChlorothiazideTetracyclineAntidepressive AgentsSalicylatesAcetazolamidePhenylbutazoneSolubilityPhenytoinbiology.proteinCattleUltracentrifugeDeoxycholic AcidProtein Bindingmedicine.drugNaunyn-Schmiedeberg's Archives 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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Neurotransmitters involved in the fast inhibitory junction potentials in mouse distal colon

2003

We investigated, in murine colon circular muscle, the role of adenosine 5′-triphosphate (ATP) and pituitary adenylate cyclase activating peptide (PACAP) as inhibitory neurotransmitters of the fast component of nerve-evoked inhibitory junction potential (fast IJP). Fast IJP was antagonised by apamin or suramin, abolished by desensitisation with the P2Y receptor agonist, adenosine 5′-O-2-thiodiphosphate (ADPβS), unaffected by desensitisation with P2X receptor agonist, α,β-methylene ATP (α,β-meATP), and reduced by PACAP-(6-38), a PACAP receptor antagonist. ATP induced membrane hyperpolarization resistant to tetrodotoxin, Nω-nitro-L-arginine methyl ester (L-NAME) or PACAP-(6-38), but antagonise…

MaleAgonistendocrine systemmedicine.medical_specialtyP2Y receptorColonmedicine.drug_classPurinoceptorNeuromuscular JunctionSuraminTetrodotoxinBiologyApaminSettore BIO/09 - FisiologiaMembrane PotentialsCellular and Molecular NeuroscienceMicechemistry.chemical_compoundAdenosine TriphosphateInternal medicinemedicineAnimalsMurinePharmacologyNeurotransmitter AgentsDose-Response Relationship Drugmusculoskeletal neural and ocular physiologyNeuropeptidesMembrane hyperpolarizationThionucleotidesHyperpolarization (biology)Receptor antagonistAdenosinePeptide FragmentsATPAdenosine DiphosphatePituitary adenylate cyclase-activating peptideNG-Nitroarginine Methyl EsterEndocrinologyApaminchemistryPituitary Adenylate Cyclase-Activating PolypeptideFast inhibitory junction potentialPACAP (pituitary adenylate cyclase activating peptide)hormones hormone substitutes and hormone antagonistsmedicine.drugEuropean Journal of Pharmacology
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Inhibitory purinergic transmission in mouse caecum: Role for P2Y1 receptors as prejunctional modulators of ATP release

2007

Using conventional microelectrode recording techniques, we investigated, in the circular muscle of the mouse caecum, the neurotransmitter(s) involved in the neurally-evoked inhibitory junction potentials (IJPs) and the existence of possible prejunctional mechanisms controlling neurotransmitter release. Electrical field stimulation with single pulses elicited IJPs, consisting only of a "fast" hyperpolarization, while using train stimuli (30-50 Hz) the initial fast hyperpolarization was followed by a slower hyperpolarization. The fast and the slow component were selectively antagonized by apamin, a blocker of calcium-activated potassium channels, and N(omega)-nitro-l-arginine methyl ester (l-…

MaleP2Y receptormedicine.medical_specialtyAntineoplastic AgentsSuraminNitric OxideApaminSettore BIO/09 - FisiologiaSynaptic TransmissionEnteric Nervous SystemMembrane PotentialsMiceReceptors Purinergic P2Y1chemistry.chemical_compoundAdenosine TriphosphateInternal medicinePurinergic P2 Receptor AntagonistsmedicineAnimalsPPADSReceptorCecumMembrane potentialReceptors Purinergic P2General NeurosciencePurinergic receptorMembrane ProteinsHyperpolarization (biology)Electric StimulationReceptors Purinergic P2Y12Potassium channelMice Inbred C57BLEndocrinologyApaminchemistryBiophysicsenteric nerves intestinal muscle ATP purinergic receptors inhibitory junction potentialsNeuroscience
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