Search results for "protein phosphorylation"

showing 10 items of 43 documents

PPARβ activation restores the high glucose-induced impairment of insulin signalling in endothelial cells

2014

Background and Purpose PPARβ enhances insulin sensitivity in adipocytes and skeletal muscle cells, but its effects on insulin signalling in endothelial cells are not known. We analysed the effects of the PPARβ/δ (PPARβ) agonists, GW0742 and L165041, on impaired insulin signalling induced by high glucose in HUVECs and aortic and mesenteric arteries from diabetic rats. Experimental Approach Insulin-stimulated NO production, Akt-Ser 473 and eNOS-Ser 1177 phosphorylation, and reactive oxygen species (ROS) production were studied in HUVECs incubated in low- or high-glucose medium. Insulin-stimulated relaxations and protein phosphorylation in vessels from streptozotocin (STZ)-induced diabetic rat…

2. Zero hungerPharmacologymedicine.medical_specialtyPyruvate dehydrogenase kinaseInsulinmedicine.medical_treatmentPDK4Oxidative phosphorylationBiologyStreptozotocinmedicine.diseaseInsulin resistanceEndocrinologyInternal medicinemedicinePhosphorylationProtein phosphorylationmedicine.drugBritish Journal of Pharmacology
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Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors

1997

AbstractThe electron-transport chains of Escherichia coli are composed of many different dehydrogenases and terminal reductases (or oxidases) which are linked by quinones (ubiquinone, menaquinone and demethylmenaquinone). Quinol:cytochrome c oxido-reductase (`bc1 complex') is not present. For various electron acceptors (O2, nitrate) and donors (formate, H2, NADH, glycerol-3-P) isoenzymes are present. The enzymes show great variability in membrane topology and energy conservation. Energy is conserved by conformational proton pumps, or by arrangement of substrate sites on opposite sides of the membrane resulting in charge separation. Depending on the enzymes and isoenzymes used, the H+/e− rat…

Anaerobic respirationTranscription GeneticCellular respirationFNRBiophysicsBiochemistryElectron TransportOxygen sensorOxygen ConsumptionBacterial Proteins(Escherichia coli)Escherichia coliProtein phosphorylationAnaerobiosischemistry.chemical_classificationbiologyCytochrome cQuinonesArcAGene Expression Regulation BacterialCell BiologyElectron acceptorElectron transport chainAerobiosisAerobic electron transportResponse regulatorAnaerobic electron transportBiochemistrychemistrybiology.proteinCarrier ProteinsEnergy MetabolismOxidoreductasesFlux (metabolism)RegulationBiochimica et Biophysica Acta (BBA) - Bioenergetics
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Phosphorylation of CalDAG-GEFI by protein kinase A prevents Rap1b activation.

2013

Summary Background Signaling via protein kinase A (PKA) and protein kinase G (PKG) is critical for maintaining platelets in the resting state. Both kinases down-regulate the activity of the small GTPase Rap1b, a critical signaling switch for integrin activation and platelet aggregation. However, the mechanism of Rap1b regulation by PKA and PKG is largely unknown. Objective To identify the PKA phosphorylation sites in calcium and diacylglycerol-regulated guanine nucleotide exchange factor I (CalDAG-GEFI), the main GEF for Rap1b in platelets, and the effect of CalDAG-GEFI phosphorylation in Rap1b activation. Methods The phosphorylation sites in CalDAG-GEFI were identified by radio-active phos…

Blood PlateletsPlatelet AggregationMolecular Sequence DataBiologyMass SpectrometryPhosphorylation cascadeCyclic AMPGuanine Nucleotide Exchange FactorsHumansImmunoprecipitationProtein phosphorylationAmino Acid SequenceCalcium SignalingPhosphorylationProtein kinase ACalcium signalingAlanineSequence Homology Amino AcidKinaseHematologyCyclic AMP-Dependent Protein KinasesEnzyme Activationrab1 GTP-Binding ProteinsHEK293 CellsBiochemistryMutationPhosphorylationGuanine nucleotide exchange factorGuanosine TriphosphatecGMP-dependent protein kinasePlasmidsSignal TransductionJournal of thrombosis and haemostasis : JTH
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Deciphering of ADP-induced, phosphotyrosine-dependent signaling networks in human platelets by Src-homology 2 region (SH2)-profiling.

2012

Tyrosine phosphorylation plays a central role in signal transduction controlling many important biological processes. In platelets, the activity of several signaling proteins is controlled by tyrosine phosphorylation ensuring proper platelet activation and aggregation essential for regulation of the delicate balance between bleeding and hemostasis. Here, we applied Src-homology 2 region (SH2)-profiling for deciphering of the phosphotyrosine state of human platelets activated by adenosine diphosphate (ADP). Applying a panel of 31 SH2-domains, rapid and complex regulation of the phosphotyrosine state of platelets was observed after ADP stimulation. Specific inhibition of platelet P2Y receptor…

Blood PlateletsProtein tyrosine phosphataseSH2 domainBiochemistryReceptor tyrosine kinasePhosphorylation cascadesrc Homology Domainschemistry.chemical_compoundReceptors Purinergic P2Y1Tandem Mass SpectrometryHumansProtease-activated receptorProtein phosphorylationIloprostPhosphorylationPhosphotyrosineMolecular BiologybiologyTyrosine phosphorylationPlatelet ActivationCyclic AMP-Dependent Protein KinasesAdenosine MonophosphateReceptors Purinergic P2Y12Cell biologyAdenosine DiphosphateEnzyme ActivationBiochemistrychemistrybiology.proteinPurinergic P2Y Receptor AntagonistsPhosphorylationProtein Processing Post-TranslationalSignal TransductionProteomics
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New Insights into Platelet Signalling Pathways by Functional and Proteomic Approaches

2018

As circulating sentinels of vascular integrity, platelets act as crucial haemostatic cells as well as important inflammatory and immune cells, whereas under pathological conditions platelets drive thrombotic as well as non-thrombotic diseases related to chronic inflammation. In addition, platelets serve as an important cellular model to study the biology and pharmacology of signal transduction pathways. Platelet inhibition and activation responses are mediated by multiple signalling networks, which are tightly regulated by balanced catalysis of protein phosphorylation and dephosphorylation through protein kinases and protein phosphatases, respectively. However, we are only at the beginning …

Blood PlateletsProteomicsKinaseInflammationHematology030204 cardiovascular system & hematologyBiologyPhosphoproteinsPlatelet ActivationProteomicsCell biology03 medical and health sciences0302 clinical medicinemedicineHumansKinomePlateletProtein phosphorylationPlatelet activationSignal transductionmedicine.symptomProtein KinasesSignal Transduction030215 immunologyHämostaseologie
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A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase

1999

Protein tyrosine phosphatase PTP-SL retains mitogen-activated protein (MAP) kinases in the cytoplasm in an inactive form by association through a kinase interaction motif (KIM) and tyrosine dephosphorylation. The related tyrosine phosphatases PTP-SL and STEP were phosphorylated by the cAMP-dependent protein kinase A (PKA). The PKA phosphorylation site on PTP-SL was identified as the Ser231 residue, located within the KIM. Upon phosphorylation of Ser231, PTP-SL binding and tyrosine dephosphorylation of the MAP kinases extracellular signal–regulated kinase (ERK)1/2 and p38α were impaired. Furthermore, treatment of COS-7 cells with PKA activators, or overexpression of the Cα catalytic subunit …

Cytoplasmanimal structuresRecombinant Fusion ProteinsCèl·lulesAmino Acid MotifsNerve Tissue ProteinsProtein tyrosine phosphataseSH2 domainTransfectionenvironment and public healthModels Biologicalp38 Mitogen-Activated Protein KinasesReceptor tyrosine kinaseSH3 domainCell LinePhosphoserinetyrosine phosphatasesAnimalsHumansProtein phosphorylationPKAReceptor-Like Protein Tyrosine Phosphatases Class 7PhosphorylationPTP-SLCell NucleusMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3biologyBrief ReportIntracellular Signaling Peptides and ProteinsBiological TransportCell BiologyProtein Tyrosine Phosphatases Non-ReceptorCyclic AMP-Dependent Protein KinasesEnzyme Activationenzymes and coenzymes (carbohydrates)MAP kinasesBiochemistryMitogen-activated protein kinaseCOS CellsMutationbiology.proteinPhosphorylationMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesEnzimssignal transductionProto-oncogene tyrosine-protein kinase Src
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The Elicitor Cryptogein Blocks Glucose Transport in Tobacco Cells

2002

Abstract Cryptogein is a 10-kD protein secreted by the oomycetePhytophthora cryptogea that induces a hypersensitive response on tobacco (Nicotiana tabacum var. Xanthi) plants and a systemic acquired resistance against various pathogens. The mode of action of this elicitor has been studied using tobacco cell suspensions. Our previous data indicated that within minutes, cryptogein signaling involves various events including changes in ion fluxes, protein phosphorylation, sugar metabolism, and, eventually, cell death. These results suggested that transport of sugars could be affected and, thus, involved in the complex relationships between plant and microorganisms via elicitors. This led us to…

Hypersensitive responsebiologyPhysiologyNicotiana tabacumGlucose transporterfood and beveragesDepolarizationPlant ScienceMitochondrionbiology.organism_classificationElicitorBiochemistryGeneticsProtein phosphorylationSystemic acquired resistancePlant Physiology
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Emerging MEK inhibitors

2010

IMPORTANCE OF THE FIELD: The Ras/Raf/MEK/ERK pathway is often activated by genetic alterations in upstream signaling molecules. Integral components of this pathway such as Ras and B-Raf are also activated by mutation. The Ras/Raf/MEK/ERK pathway has profound effects on proliferative, apoptotic and differentiation pathways. This pathway can often be effectively silenced by MEK inhibitors. AREAS COVERED BY THIS REVIEW: This review will discuss targeting of MEK which could lead to novel methods to control abnormal proliferation which arises in cancer and other proliferative diseases. This review will cover the scientific literature from 1980 to present and is a follow on from a review which fo…

MAPK/ERK pathwayCell signalingAntineoplastic Agentsmedicine.disease_causemekerkEnzyme activatorNeoplasmsAntineoplastic Combined Chemotherapy ProtocolsmedicineAnimalsHumansPharmacology (medical)Protein phosphorylationProtein Kinase InhibitorsMEK inhibitorsCell ProliferationCancerPharmacologyapoptosis; cancer; erk; kinases; mek; mek inhibitors; proliferative disorders; protein phosphorylation; signal transductionproliferative disordersMutationKinasebusiness.industryapoptosisApoptosiCancerDrugs InvestigationalMAP Kinase Kinase Kinasesmedicine.diseaseprotein phosphorylationCell biologyEnzyme ActivationTreatment OutcomekinasesChemotherapy AdjuvantRadiotherapy AdjuvantSignal transductionbusinesssignal transductionExpert Opinion on Emerging Drugs
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Emerging Raf inhibitors

2009

The Raf/MAPK kinase/extracellular-signal-regulated kinase pathway is often activated by genetic alterations in upstream signaling molecules. An integral component of this pathway, BRAF, is also activated by mutation, especially in melanoma and thyroid cancers. The Raf/MAPK kinase/extracellular-signal-regulated kinase pathway has profound effects on proliferative, apoptotic and differentiation pathways as well as the sensitivity and resistance to chemotherapeutic drugs.This review discusses targeting of Raf which could control abnormal proliferation in cancer and other proliferative diseases. The important roles that genetics plays in the response of patients to Raf inhibitors is also evalua…

MAPK/ERK pathwayProto-Oncogene Proteins B-rafCell signalingMAP Kinase Signaling SystemSignal transductionrafmedicine.disease_causemekerkmedicineHumanscancerPharmacology (medical)raf inhibitorsExtracellular Signal-Regulated MAP KinasesMelanomaProtein Kinase InhibitorsPharmacologyapoptosis cancer ERK proliferative disorderssignal transductionMitogen-Activated Protein Kinase KinasesApoptosis; Cancer; ERK; Kinases; MEK; Proliferative disorders; Protein phosphorylation; Raf; Raf inhibitors; Signal transductionMutationproliferative disordersapoptosis; cancer; erk; kinases; mek; proliferative disorders; protein phosphorylation; raf; raf inhibitors; signal transduction read more: http://informahealthcare.com/doi/abs/10.1517/14728210903232633business.industryKinaseMelanomaapoptosisCancermedicine.diseaseXenograft Model Antitumor Assaysprotein phosphorylationCell Transformation Neoplastickinasessignal transduction read more: http://informahealthcare.com/doi/abs/10.1517/14728210903232633ApoptosisDrug Resistance NeoplasmCancer researchSignal transductionMitogen-Activated Protein Kinasesbusiness
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Impact of diet-induced obesity on the mouse brain phosphoproteome

2018

Obesity is closely associated to several diseases such as type 2 diabetes, cardiovascular disease, hepatic steatosis, airway disease, neurodegeneration, biliary diseases and certain cancers. It is, therefore, of importance to assess the role of nutrition in disease prevention as well as its effect in the course of such pathologies. In the present study, we addressed the impact of the exposure to different obesogenic diets in the mice brains phosphoproteome. To analyze if the obesity could be able to modify the protein pattern expression of brain neurons, obesity was induced in two different groups of mice. One group of mice was fed with hyperglycemic diet (HGD) and the other one was fed wit…

Male0301 basic medicinemedicine.medical_specialtyPhosphoproteomicsEndocrinology Diabetes and MetabolismClinical BiochemistryHyperglycemic dietType 2 diabetesDiseaseBiologyDiet High-FatBiochemistry03 medical and health sciences0302 clinical medicineInternal medicinemedicineAnimalsProtein phosphorylationObesityPhosphorylationMolecular BiologyGSK3BNutritionNeuronal impairmentNutrition and DieteticsNeurodegenerationta1182BrainObesity; Nutrition; High-fat diet; Hyperglycemic diet; Neuronal impairment; PhosphoproteomicsPhosphoproteinsmedicine.diseaseObesityMice Inbred C57BLHigh-fat dietGene Ontology030104 developmental biologyEndocrinologyHyperglycemiaPhosphorylationCalcium ChannelsSteatosis030217 neurology & neurosurgeryThe Journal of Nutritional Biochemistry
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