Search results for "PROTEIN KINASES"

showing 10 items of 427 documents

The stem rust resistance gene Rpg5 encodes a protein with nucleotide-binding-site, leucine-rich, and protein kinase domains

2008

We isolated the barley stem rust resistance genes Rpg5 and rpg4 by map-based cloning. These genes are colocalized on a 70-kb genomic region that was delimited by recombination. The Rpg5 gene consists of an unusual structure encoding three typical plant disease resistance protein domains: nucleotide-binding site, leucine-rich repeat, and serine threonine protein kinase. The predicted RPG5 protein has two putative transmembrane sites possibly involved in membrane binding. The gene is expressed at low but detectable levels. Posttranscriptional gene silencing using VIGS resulted in a compatible reaction with a normally incompatible stem rust pathogen. Allele sequencing also validated the candi…

LRP1BSerine threonine protein kinaseBiologyGenes PlantSYT1LeucineHSPA2SNAP23Gene SilencingCloning MolecularPlant DiseasesPlant ProteinsTAF15HSPA9GeneticsBinding SitesMultidisciplinaryPlant StemsNucleotidesFungifood and beveragesHordeumBiological SciencesPhysical Chromosome MappingProtein Structure TertiaryGPS2Protein KinasesProceedings of the National Academy of Sciences
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Fasting enhances the response of arcuate neuropeptide Y-glucose-inhibited neurons to decreased extracellular glucose

2009

0363-6143 (Print) Comparative Study In Vitro Journal Article Research Support, N.I.H., Extramural; Fasting increases neuropeptide Y (NPY) expression, peptide levels, and the excitability of NPY-expressing neurons in the hypothalamic arcuate (ARC) nucleus. A subpopulation of ARC-NPY neurons ( approximately 40%) are glucose-inhibited (GI)-type glucose-sensing neurons. Hence, they depolarize in response to decreased glucose. Because fasting enhances NPY neurotransmission, we propose that during fasting, GI neurons depolarize in response to smaller decreases in glucose. This increased excitation in response to glucose decreases would increase NPY-GI neuronal excitability and enhance NPY neurotr…

LeptinMalemedicine.medical_specialtyArcuate Nucleus/cytology/*metabolismPhysiologyGlucose/*deficiencyAMP-Activated Protein Kinases/metabolismAMP-Activated Protein KinasesIn Vitro TechniquesNeurotransmissionBiologySynaptic TransmissionEnergy homeostasisMembrane PotentialsRats Sprague-Dawley03 medical and health sciences0302 clinical medicineNeuropeptide Y/*metabolismArcuate nucleusInternal medicinemental disordersmedicineAnimalsHomeostasisNeuropeptide YNervous System Cell BiologyFasting/*metabolismNeurons/enzymology/*metabolism030304 developmental biologyNeuronsMembrane potential0303 health sciencesLeptinArcuate Nucleus of HypothalamusLeptin/metabolismNeural InhibitionFastingCell BiologyNeuropeptide Y receptorhumanitiesRatsGlucosemedicine.anatomical_structureEndocrinologyNeuronSprague-DawleyEnergy Metabolism030217 neurology & neurosurgeryHomeostasis
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Bisphenol-A impairs insulin action and up-regulates inflammatory pathways in human subcutaneous adipocytes and 3T3-L1 cells.

2013

Current evidence indicates that chemical pollutants may interfere with the homeostatic control of nutrient metabolism, thereby contributing to the increased prevalence of metabolic disorders. Bisphenol-A (BPA) is a lipophilic compound contained in plastic which is considered a candidate for impairing energy and glucose metabolism. We have investigated the impact of low doses of BPA on adipocyte metabolic functions. Human adipocytes derived from subcutaneous adipose tissue and differentiated 3T3-L1 cells were incubated with BPA, in order to evaluate the effect on glucose utilization, insulin sensitivity and cytokine secretion. Treatment with 1 nM BPA significantly inhibited insulin-stimulate…

Leptinmedicine.medical_treatmentAdipose tissuechemistry.chemical_compoundMice0302 clinical medicineAdipocyteAdipocytesInsulinPhosphorylation0303 health sciencesMultidisciplinaryPERSISTENT ORGANIC POLLUTANTS BODY-MASS INDEX METABOLIC SYNDROME ENVIRONMENTAL CONTAMINANTS CARDIOVASCULAR-DISEASE ENDOCRINE DISRUPTORS SERUM CONCENTRATIONS WIDESPREAD EXPOSURE PERINATAL EXPOSURE DIABETES-MELLITUSbiologyQRNF-kappa BCell Differentiation3. Good healthUp-RegulationAdipogenesisMedicinehormones hormone substitutes and hormone antagonistsResearch ArticleSignal TransductionSTAT3 Transcription Factormedicine.medical_specialtyendocrine systemScienceSubcutaneous FatDown-Regulation030209 endocrinology & metabolism03 medical and health sciencesDownregulation and upregulationPhenolsInternal medicine3T3-L1 CellsmedicineAnimalsHumansRNA MessengerBenzhydryl Compounds030304 developmental biologyInflammationurogenital systemInsulinJNK Mitogen-Activated Protein KinasesReceptor InsulinInsulin receptorEndocrinologyGlucosechemistry13. Climate actionbiology.proteinCytokine secretionGLUT4PloS one
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HSP27 controls GATA-1 protein level during erythroid cell differentiation.

2010

AbstractHeat shock protein 27 (HSP27) is a chaperone whose cellular expression increases in response to various stresses and protects the cell either by inhibiting apoptotic cell death or by promoting the ubiquitination and proteasomal degradation of specific proteins. Here, we show that globin transcription factor 1 (GATA-1) is a client protein of HSP27. In 2 models of erythroid differentiation; that is, in the human erythroleukemia cell line, K562 induced to differentiate into erythroid cells on hemin exposure and CD34+ human cells ex vivo driven to erythroid differentiation in liquid culture, depletion of HSP27 provokes an accumulation of GATA-1 and impairs terminal maturation. More spec…

LeupeptinsPyridines[SDV]Life Sciences [q-bio]Cellular differentiationCellHSP27 Heat-Shock ProteinsAntigens CD34Biochemistryp38 Mitogen-Activated Protein Kinases0302 clinical medicineTransforming Growth Factor betahemic and lymphatic diseasesChlorocebus aethiopsGATA1 Transcription FactorPhosphorylationComputingMilieux_MISCELLANEOUSCells CulturedHeat-Shock Proteins0303 health sciencesbiologyImidazolesCell DifferentiationHematology[SDV] Life Sciences [q-bio]medicine.anatomical_structure030220 oncology & carcinogenesisembryonic structuresCOS CellsRNA InterferenceSignal transductionProteasome InhibitorsProtein BindingProteasome Endopeptidase ComplexImmunologyImmunoblotting03 medical and health sciencesHsp27Erythroid CellsHeat shock proteinmedicineAnimalsHumansTranscription factor030304 developmental biologyCell NucleusInterleukin-6UbiquitinationCell BiologyTransforming growth factor betaMolecular biologyChaperone (protein)biology.proteinK562 CellsHeLa CellsMolecular ChaperonesBlood
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Voluntary distance running prevents TNF-mediated liver injury in mice through alterations of the intrahepatic immune milieu

2017

AbstractPhysical activity confers a broad spectrum of health benefits. Beyond the obvious role in metabolically driven diseases, the role of physical activity in acute liver injury is poorly explored. To study the role of physical activity in acute liver injury, a novel model of voluntary distance running in mice was developed and mice were subjected to acute liver injury induced by N-galactosamine (GalN) and lipopolysaccharide (LPS). Analyses included histological stains, immunoblotting, qRT-PCR and FACS analysis. Voluntary distance running increased to an average of 10.3 km/day after a learning curve. Running lead to a decrease in the absolute numbers of intrahepatic CD4+ T and B lymphocy…

Lifestyle modification0301 basic medicineLipopolysaccharidesMaleCancer ResearchChemokineApoptosisGalactosamineLiver Function TestsAlarminsLiver injurybiologymedicine.diagnostic_testChemotaxisNF-kappa Bmedicine.anatomical_structureLiverReceptors Pattern RecognitionModels AnimalCytokinesTumor necrosis factor alphaOriginal Articlemedicine.symptomChemokinesInflammation Mediatorsmedicine.medical_specialtyImmunologyInflammationCCL2Proinflammatory cytokine03 medical and health sciencesCellular and Molecular NeuroscienceInternal medicinePhysical Conditioning AnimalmedicineAnimalsLiver diseasesInflammationbusiness.industryTumor Necrosis Factor-alphaMonocyteBody WeightJNK Mitogen-Activated Protein KinasesCell BiologyLiver Failure Acutemedicine.diseaseEnzyme ActivationMice Inbred C57BL030104 developmental biologyEndocrinologyImmunologybiology.proteinLiver function testsbusinessCell Death & Disease
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2′O-galloylhyperin attenuates LPS-induced acute lung injury via up-regulation antioxidation and inhibition of inflammatory responses in vivo

2019

2'O-galloylhyperin, an active flavonol glycoside compound with remarkable anti-immune activity, was isolated from Pyrola [P. incarnata Fisch.]. However, the evidence of anti-inflammatory activity in pulmonary diseases was still not convincing. The aim of the present study was (1) to investigate the effect of 2'O-galloylhyperin on LPS-induced acute lung injury in mice, and (2) to identify the mechanisms of attenuation of inflammatory responses. The results demonstrated that 2'O-galloylhyperin significantly reduced LPS-induced inflammation damage in a dose-dependent manner. After LPS challenge, treatment with 2'O-galloylhyperin reduced the production of pro-inflammatory cytokines and chemokin…

LipopolysaccharidesMale0301 basic medicineMAPK/ERK pathwayp38 mitogen-activated protein kinasesAcute Lung InjuryMolecular ConformationInflammationPharmacologyLung injuryToxicologyAntioxidantsMiceStructure-Activity Relationship03 medical and health sciences0302 clinical medicineGallic AcidmedicineAnimalsProtein kinase AInflammationMice Inbred ICRDose-Response Relationship DrugChemistryAnti-Inflammatory Agents Non-SteroidalAMPKGeneral MedicineUp-Regulation030104 developmental biology030220 oncology & carcinogenesisPhosphorylationQuercetinmedicine.symptomSignal transductionChemico-Biological Interactions
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Quaking and miR-155 interactions in inflammation and leukemogenesis.

2015

Quaking (QKI) is a tumor-suppressor gene encoding a conserved RNA-binding protein, whose expression is downregulated in several solid tumors. Here we report that QKI plays an important role in the immune response and suppression of leukemogenesis. We show that the expression of Qki is reduced in lipopolysaccharide (LPS)-challenged macrophages, suggesting that Qki is a key regulator of LPS signaling pathway. Furthermore, LPS-induced downregulation of Qki expression is miR-155-dependent. Qki overexpression impairs LPS-induced phosphorylation of JNK and particularly p38 MAPKs, in addition to increasing the production of anti-inflammatory cytokine IL-10. In contrast, Qki ablation decreases Fas …

LipopolysaccharidesTime Factorsmedicine.medical_treatmentmedicine.disease_causeTransgenicMiceInnatePhosphorylationChronicB-LymphocytesLeukemiaRNA-Binding ProteinsU937 CellsLymphocyticCell biologyCytokineOncologyPhosphorylationCytokinesCLL; Glioblastoma; Inflammation; MiR-155; QKI; Animals; Apoptosis Regulatory Proteins; B-Lymphocytes; Case-Control Studies; Cytokines; Humans; Immunity Innate; Inflammation; Leukemia Lymphocytic Chronic B-Cell; Lipopolysaccharides; Macrophages; Mice; Mice Transgenic; MicroRNAs; Mitogen-Activated Protein Kinases; Phosphorylation; RAW 264.7 Cells; RNA-Binding Proteins; Signal Transduction; Time Factors; Transfection; U937 Cells; OncologySignal transductionMitogen-Activated Protein KinasesSignal Transductionp38 mitogen-activated protein kinasesOncology and CarcinogenesisMice TransgenicTransfectionNOmiR-155miR-155Downregulation and upregulationmicroRNAmedicineAnimalsHumansInflammationQKIbusiness.industryMacrophagesB-CellImmunityglioblastomaLeukemia Lymphocytic Chronic B-CellImmunity InnateMicroRNAsRAW 264.7 CellsCase-Control StudiesImmunologyCarcinogenesisbusinessApoptosis Regulatory ProteinsCLLPriority Research Paper
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p38 MAPK-dependent shaping of the keratin cytoskeleton in cultured cells

2007

Plasticity of the resilient keratin intermediate filament cytoskeleton is an important prerequisite for epithelial tissue homeostasis. Here, the contribution of stress-activated p38 MAPK to keratin network organization was examined in cultured cells. It was observed that phosphorylated p38 colocalized with keratin granules that were rapidly formed in response to orthovanadate. The same p38p recruitment was noted during mitosis, in various stress situations and in cells producing mutant keratins. In all these situations keratin 8 became phosphorylated on S73, a well-known p38 target site. To demonstrate that p38-dependent keratin phosphorylation determines keratin organization, p38 activity …

MAP Kinase Signaling SystemIntermediate filament cytoskeletonmacromolecular substancesBiologyp38 Mitogen-Activated Protein KinasesArticleKeratinHumansPhosphorylationCytoskeletonProtein Kinase InhibitorsMitosisResearch ArticlesCells CulturedCytoskeletonchemistry.chemical_classificationKeratin Filamentintegumentary systemCell BiologyCell biologyKeratin 5chemistryKeratin 8KeratinsPhosphorylationVanadatesJournal of Cell Biology
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Differences in the signaling pathways of α(1A)- and α(1B)-adrenoceptors are related to different endosomal targeting.

2013

AIMS: To compare the constitutive and agonist-dependent endosomal trafficking of α(1A)- and α(1B)-adrenoceptors (ARs) and to establish if the internalization pattern determines the signaling pathways of each subtype. METHODS: Using CypHer5 technology and VSV-G epitope tagged α(1A)- and α(1B)-ARs stably and transiently expressed in HEK 293 cells, we analyzed by confocal microscopy the constitutive and agonist-induced internalization of each subtype, and the temporal relationship between agonist induced internalization and the increase in intracellular calcium (determined by FLUO-3 flouorescence), or the phosphorylation of ERK1/2 and p38 MAP kinases (determined by Western blot). RESULTS AND C…

MAPK signaling cascadesEndosomemedia_common.quotation_subjecteducationIntracellular Spacelcsh:MedicineEndosomesSignal transductionERK signaling cascadeBiologyEndocytosisp38 Mitogen-Activated Protein KinasesSignaling PathwaysCell LineMolecular cell biologyReceptors Adrenergic alpha-1Calcium-Mediated Signal TransductionHumansMembrane Receptor SignalingCalcium SignalingInternalizationlcsh:ScienceBiologyCalcium signalingmedia_commonMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3MultidisciplinaryHEK 293 cellslcsh:RNeurotransmitter Receptor SignalingSignaling cascadesNeurotransmittersLipid signalingEndocytosisCell biologyTransport proteinProtein TransportHEK293 CellsCalcium signaling cascadeMembranes and Sortinglcsh:QAdrenergic alpha-1 Receptor AgonistsMolecular NeuroscienceSignal transductionResearch ArticleAdrenergic Signal TransductionNeurosciencePLoS ONE
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Oestradiol or genistein rescues neurons from amyloid beta-induced cell death by inhibiting activation of p38.

2007

Oestrogenic compounds have been postulated as neuroprotective agents. This prompted us to investigate their mechanism action in neurons in primary culture. Cells were pretreated with physiological concentrations of 17-beta estradiol (0.2 nm) or with nutritionally relevant concentrations of genistein (0.5 microm), and 48 h later treated with 5 microm of amyloid beta (Abeta) for 24 h. We found that Abeta increased oxidative stress, measured as peroxide levels or oxidized glutathione/reduced glutathione ratio, which in turn, caused phosphorylation of p38 MAP kinase. Amyloid beta subsequently induced neuronal death. Inhibiting the MAP kinase pathway prevented cell death, confirming the role of …

MAPK/ERK pathwayAgingProgrammed cell deathmedicine.medical_specialtyAmyloid betaCell Survivalp38 mitogen-activated protein kinasesGenisteinPhytoestrogensIn Vitro Techniquesmedicine.disease_causeNeuroprotectionp38 Mitogen-Activated Protein Kinaseschemistry.chemical_compoundInternal medicinemedicineAnimalsCells CulturedCerebral CortexNeuronsAmyloid beta-PeptidesbiologyCell DeathEstradiolEstrogensCell BiologyGlutathioneGenisteinMitochondriaRatsOxidative StressEndocrinologychemistrybiology.proteinOxidation-ReductionOxidative stressAging cell
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