Search results for "signal transduction."

showing 10 items of 1278 documents

Ethanol inhibits astroglial cell proliferation by disruption of phospholipase D-mediated signaling.

2002

The activation of phospholipase D (PLD) is a common response to mitogenic stimuli in various cell types. As PLD-mediated signaling is known to be disrupted in the presence of ethanol, we tested whether PLD is involved in the ethanol-induced inhibition of cell proliferation in rat cortical primary astrocytes. Readdition of fetal calf serum (FCS) to serum-deprived astroglial cultures caused a rapid, threefold increase of PLD activity and a strong mitogenic response; both effects were dependent on tyrosine kinases but not on protein kinase C. Ethanol (0.1-2%) suppressed the FCS-induced, PLD-mediated formation of phosphatidic acid (PA) as well as astroglial cell proliferation in a concentration…

medicine.medical_specialtyPlatelet-derived growth factorIndolestert-Butyl Alcoholmedicine.medical_treatmentButanolsBecaplerminPhosphatidic AcidsNerve Tissue ProteinsBiologyBiochemistryCulture Media Serum-FreeCellular and Molecular Neurosciencechemistry.chemical_compound1-ButanolInternal medicineLysophosphatidic acidmedicinePhospholipase DAnimalsPhosphorylationProtein kinase APlatelet-Derived Growth FactorEndothelin-1EthanolPhospholipase DCell growthGrowth factorPhosphatidic acidDNAProto-Oncogene Proteins c-sisProtein-Tyrosine KinasesGenisteinGrowth InhibitorsCell biologyRatsEndocrinologychemistryFetal Alcohol Spectrum DisordersAstrocyteslipids (amino acids peptides and proteins)Signal transductionVanadatesProtein Processing Post-TranslationalCell DivisionSignal TransductionJournal of neurochemistry
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Prevention of Atherosclerosis by Interference with the Vascular Nitric Oxide System

2009

Nitric oxide (NO) produced by endothelial NO synthase (eNOS) represents an anti-atherosclerotic principle. NO bioavailability is decreased in atherosclerosis due to increased NO inactivation by reactive oxygen species and reduced NO synthesis. Various types of vascular pathophysiology are associated with oxidative stress, with NADPH oxidases as the major source of reactive oxygen species. These inactivate NO. Also, oxidative stress is likely to be the main cause for oxidation of the essential NOS cofactor, tetrahydrobiopterin (BH(4)). A lack of BH(4) leads to eNOS uncoupling (i.e., uncoupling of oxygen reduction from NO synthesis in eNOS). Based on these pathomechanisms, the therapeutic pot…

medicine.medical_specialtySepiapterinNitric Oxide Synthase Type IIImedicine.drug_classGTP cyclohydrolase INitric Oxidemedicine.disease_causeRenin inhibitorNitric oxidechemistry.chemical_compoundEnosInternal medicineDrug DiscoverymedicineAnimalsHumansHypolipidemic AgentsPharmacologybiologyArteriesTetrahydrobiopterinAtherosclerosisbiology.organism_classificationNitric oxide synthaseOxidative StressTreatment OutcomeEndocrinologychemistrybiology.proteinOxidative stressSignal Transductionmedicine.drugCurrent Pharmaceutical Design
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BDNF is essentially required for the early postnatal survival of nociceptors

2010

AbstractNeurotrophins promote the survival of specific types of neurons during development and ensure proper maintenance and function of mature responsive neurons. Significant effects of BDNF (Brain-Derived Neurotrophic Factor) on pain physiology have been reported but the contribution of this neurotrophin to the development of nociceptors has not been investigated. We present evidence that BDNF is required for the survival of a significant fraction of peptidergic and non-peptidergic nociceptors in dorsal root ganglia (DRG) postnatally. Bdnf homozygous mutant mice lose approximately half of all nociceptive neurons during the first 2 weeks of life and adult heterozygotes exhibit hypoalgesia …

medicine.medical_specialtySkin innervationCell SurvivalNeurotrophic factorMice Inbred StrainsNeuronal survivalMiceNeurotrophic factorsGanglia SpinalInternal medicineGlial cell line-derived neurotrophic factormedicineAnimalsGlial Cell Line-Derived Neurotrophic FactorNerve Growth FactorsDorsal root gangliaAutocrine signallingMolecular BiologyCells CulturedSensory neuronHypoalgesiabiologyBrain-Derived Neurotrophic FactorNociceptorsAnatomyCell BiologyBdnf knockout miceEmbryo MammalianSensory neuronmedicine.anatomical_structureEndocrinologynervous systemPeripheral nervous systembiology.proteinNociceptorNeurotrophinPeripheral nervous systemSignal TransductionNeurotrophinDevelopmental BiologyDevelopmental Biology
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Growth and differentiation factor 11 (GDF11): Functions in the regulation of erythropoiesis and cardiac regeneration

2015

International audience; Members of the TGF-β superfamily transduce their signals through type I and II receptor serine/threonine kinases. The binding of activins to activin type IIA (ActRIIA) or type IIB (ActRIIB) receptors induces the recruitment and phosphorylation of an activin type I receptor (ALK4 and/or ALK7), which then phosphorylates the Smad2 and Smad3 intracellular signaling proteins. The regulation of members of the TGF-β family is known to be complex, because many proteins able to bind the ligands and inhibit their activities have been identified. Growth and differentiation factor 11 (Gdf11) belongs to the TGF-β family. GDF11, like other members of the TGF-β superfamily, is prod…

medicine.medical_specialtySmad2 ProteinProtein Serine-Threonine Kinases030204 cardiovascular system & hematologyBiology03 medical and health sciences0302 clinical medicine[SDV.MHEP.CSC]Life Sciences [q-bio]/Human health and pathology/Cardiology and cardiovascular systemInternal medicineTGF beta signaling pathway[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologymedicineHumansRegeneration[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyPharmacology (medical)PhosphorylationCCL11Activin type 2 receptors030304 developmental biologyPharmacology0303 health sciencesR-SMADcardiac regenerationGrowth differentiation factorHeartActivins[SDV.MHEP.CSC] Life Sciences [q-bio]/Human health and pathology/Cardiology and cardiovascular systemCell biologyBMPR2Growth Differentiation FactorsEndocrinologyBone Morphogenetic ProteinsGDF11Smad2 ProteinSignal transductionActivin Receptors Type IerythropoiesisACVR2BSignal TransductionPharmacology & Therapeutics
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Combined sub-optimal doses of Rosuvastatin and Bexarotene impairs angiotensin II-induced arterial mononuclear cell adhesion through inhibition of Nox…

2015

Aim: Mononuclear cell (MC) infiltration into the arterial subendothelium is a key event in atherogenesis. Rosuvastatin (Rosu) and bexarotene (Bex) exert anti-inflammatory activity, but serious dose-related adverse effects have emerged. The need for safer and effective strategies to prevent and treat atherosclerosis led us to test the effect of combined use of both drugs on angiotensin II (Ang-II)-induced arterial MC recruitment. Results: Vehicle, Rosu (10–30 nM), Bex (0.3–1 μM), or a combination of both were administered to human umbilical arterial endothelial cells (HUAECs) 20 h before stimulation with 1 μM Ang-II (4 h). Surprisingly, a combination of Rosu (10 nM)+Bex (0.3 μM), which did n…

medicine.medical_specialtyTetrahydronaphthalenesPhysiologyPeroxisome Proliferator-Activated ReceptorsClinical BiochemistryCCL2BiologyNitric OxideBiochemistryPeripheral blood mononuclear cellCell LineInternal medicineCell AdhesionmedicineAnticarcinogenic AgentsHumansRosuvastatinInterleukin 8Rosuvastatin CalciumMolecular BiologyGeneral Environmental ScienceSistema cardiovascularBexaroteneSulfonamidesDiabetisArtèriesAngiotensin IIMembrane ProteinsNADPH OxidasesArteriesCell BiologyAngiotensin IIFluorobenzenesCXCL1Original Research CommunicationsPyrimidinesRetinoid X ReceptorsEndocrinologyNADPH Oxidase 5BexaroteneLeukocytes MononuclearGeneral Earth and Planetary SciencesSignal transductionSignal Transductionmedicine.drug
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Corticotropin-Releasing Hormone-Mediated Induction of Intracellular Signaling Pathways and Brain-Derived Neurotrophic Factor Expression Is Inhibited …

2005

CRH receptor (CRHR) 1 and the cannabinoid receptor 1 (CB1) are both G protein-coupled receptors. Activation of CRHR1 leadstoincreasesincAMPproductionandphosphorylationof the transcription factor cAMP response element-binding protein (CREB). In contrast, CB1 is negatively coupled to the cAMP signaling cascade. In this study, we analyzed a putative interaction between these two systems focusing on the regulation of the expression of brain-derived neurotrophic factor (BDNF), a CREB-regulated gene. In situ hybridization revealed coexpression of CRHR1 and CB1 receptors in the granular layer of the cerebellum. Therefore, we analyzed the effects of CRH and the CB1 agonist WIN-55,212-2 on BDNF expr…

medicine.medical_specialtyTime FactorsCorticotropin-Releasing HormoneMorpholinesmedicine.medical_treatmentImmunoblottingEnzyme-Linked Immunosorbent AssayTropomyosin receptor kinase BNaphthalenesCREBModels BiologicalRats Sprague-DawleyMiceEndocrinologyNeurotrophic factorsCerebellumInternal medicineCannabinoid Receptor ModulatorsCyclic AMPmedicineAnimalsRNA MessengerCyclic AMP Response Element-Binding ProteinReceptorEgtazic AcidCells CulturedIn Situ HybridizationNeuronsBrain-derived neurotrophic factorSulfonamidesbiologyReverse Transcriptase Polymerase Chain ReactionBrain-Derived Neurotrophic FactorCalcium Channel BlockersIsoquinolinesEndocannabinoid systemBenzoxazinesRatsMice Inbred C57BLPyrimidinesEndocrinologynervous systembiology.proteinCalciumCannabinoidSignal transductionEndocannabinoidsProtein BindingSignal TransductionEndocrinology
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Estradiol Stimulates Vasodilatory and Metabolic Pathways in Cultured Human Endothelial Cells

2009

Vascular effects of estradiol are being investigated because there are controversies among clinical and experimental studies. DNA microarrays were used to investigate global gene expression patterns in cultured human umbilical vein endothelial cells (HUVEC) exposed to 1 nmol/L estradiol for 24 hours. When compared to control, 187 genes were identified as differentially expressed with 1.9-fold change threshold. Supervised principal component analysis and hierarchical cluster analysis revealed the differences between control and estradiol-treated samples. Physiological concentrations of estradiol are sufficient to elicit significant changes in HUVEC gene expression. Notch signaling, actin cyt…

medicine.medical_specialtyUmbilical Veinsmedicine.drug_classScienceEstrogen receptorBiologyAmidohydrolasesTransforming Growth Factor beta1chemistry.chemical_compoundInternal medicinemedicineCluster AnalysisEstrogen Receptor betaHumansEstrogen receptor betaCell Biology/Gene ExpressionCells CulturedOligonucleotide Array Sequence AnalysisRegulation of gene expressionPrincipal Component AnalysisMultidisciplinaryEstradiolPhysiology/EndocrinologyReverse Transcriptase Polymerase Chain ReactionGene Expression ProfilingQPhysiology/Cardiovascular Physiology and CirculationREstrogen Receptor alphaEndothelial CellsReproducibility of ResultsActin cytoskeletonVasodilationEndocrinologychemistryGene Expression RegulationEstrogenCyclooxygenase 1MedicineSignal transductionAsymmetric dimethylarginineEstrogen receptor alphahormones hormone substitutes and hormone antagonistsMetabolic Networks and PathwaysResearch ArticleSignal TransductionPLoS ONE
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Dpp signaling inhibits proliferation in the Drosophila wing by Omb-dependent regional control of bantam

2013

The control of organ growth is a fundamental aspect of animal development but remains poorly understood. The morphogen Dpp has long been considered as a general promoter of cell proliferation during Drosophila wing development. It is an ongoing debate whether the Dpp gradient is required for the uniform cell proliferation observed in the wing imaginal disc. Here, we investigated how the Dpp signaling pathway regulates proliferation during wing development. By systematic manipulation of Dpp signaling we observed that it controls proliferation in a region-specific manner: Dpp, via omb, promoted proliferation in the lateral and repressed proliferation in the medial wing disc. Omb controlled th…

medicine.medical_specialtyanimal structuresMicroRNA GeneNerve Tissue ProteinsBiologyTranscription (biology)Internal medicinemedicineAnimalsDrosophila ProteinsWings AnimalMolecular BiologyDpp signaling pathwayBody PatterningCell ProliferationWingCell growthAnimal developmentCell biologyMicroRNAsImaginal discEndocrinologyDrosophilaT-Box Domain ProteinsSignal TransductionDevelopmental BiologyMorphogenDevelopment
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Involvement of Different networks in mammary gland involution after the pregnancy/lactation cycle: Implications in breast cancer

2015

Early pregnancy is associated with a reduction in a woman's lifetime risk for breast cancer. However, different studies have demonstrated an increase in breast cancer risk in the years immediately following pregnancy. Early and long-term risk is even higher if the mother age is above 35 years at the time of first parity. The proinflammatory microenvironment within the mammary gland after pregnancy renders an "ideal niche" for oncogenic events. Signaling pathways involved in programmed cell death and tissue remodeling during involution are also activated in breast cancer. Herein, the major signaling pathways involved in mammary gland involution, signal transducer and activator of transcripti…

medicine.medical_specialtybiologyClinical BiochemistryMammary glandCell BiologyTransforming growth factor betamedicine.disease_causemedicine.diseaseBiochemistryChromatin remodelingmedicine.anatomical_structureEndocrinologyBreast cancerInternal medicineGeneticsmedicinebiology.proteinCancer researchInvolution (medicine)Signal transductionCarcinogenesisMolecular BiologyMammary gland involutionIUBMB Life
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PEST-domain-enriched tyrosine phosphatase and glucocorticoids as regulators of anaphylaxis in mice

2011

To cite this article: Obiri DD, Flink N, Maier JV, Neeb A, Maddalo D, Thiele W, Menon A, Stassen M, Kulkarni RA, Garabedian MJ, Barrios AM, Cato ACB. PEST-domain-enriched tyrosine phosphatase and glucocorticoids as regulators of anaphylaxis in mice. Allergy 2012; 67: 175–182. Abstract Background:  PEST-domain-enriched tyrosine phosphatase (PEP) is a protein tyrosine phosphatase exclusively expressed in hematopoietic cells. It is a potent negative regulator of T-cell receptor signalling that acts on receptor-coupled protein tyrosine kinases. PEST-domain-enriched tyrosine phosphatase is also expressed in mast cell and is positively regulated by glucocorticoids, but its function is unknown. In…

medicine.medical_specialtyeducationImmunologyDegranulationProtein tyrosine phosphataseBiologyImmunoglobulin EMast cellPTPN22Endocrinologymedicine.anatomical_structureInternal medicinecardiovascular systemmedicinebiology.proteinImmunology and AllergyPhosphorylationSignal transductionGlucocorticoidcirculatory and respiratory physiologymedicine.drugAllergy
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