Search results for "Phosphorylation"

showing 10 items of 975 documents

Differential role of p38 mitogen activated protein kinase for cellular recovery from attack by pore-forming S. aureus alpha-toxin or streptolysin O.

2006

Following the observation that cells are able to recover from membrane lesions incurred by Staphylococcus aureus alpha-toxin and streptolysin O (SLO), we investigated the role of p38 in this process. p38 phosphorylation occurred in response to attack by both toxins, commencing within minutes after toxin treatment and waning after several hours. While SLO reportedly activates p38 via ASK1 and ROS, we show that this pathway does not play a major role for p38 induction in alpha-toxin-treated cells. Strikingly divergent effects of p38 blockade were noted depending on the toxin employed. In the case of alpha-toxin, inhibition of p38 within the time frame of its activation led to disruption of th…

KeratinocytesProgrammed cell deathStaphylococcus aureusCell Membrane Permeabilityp38 mitogen-activated protein kinasesBacterial ToxinsBiophysicsBiologymedicine.disease_causeMAP Kinase Kinase Kinase 5Biochemistryp38 Mitogen-Activated Protein KinasesMicrobiologyHemolysin ProteinsAdenosine TriphosphateBacterial ProteinsProto-Oncogene ProteinsmedicineHumansASK1PhosphorylationMolecular BiologyCells CulturedPore-forming toxinToxinCell MembraneCell BiologyProtein-Tyrosine KinasesBlockadeCell biologyEnzyme ActivationStreptolysinsPhosphorylationStreptolysinBiochemical and biophysical research communications
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Potential antipsoriatic effect of chondroitin sulfate through inhibition of NF-κB and STAT3 in human keratinocytes

2012

Abstract Chondroitin sulfate (CS) is a natural glycosaminoglycan, formed by the 1–3 linkage of d -glucuronic acid to N-acetylgalactosamine, present in the extracellular matrix. It is used as a slow acting disease modifying agent in the treatment of osteoarthritis, and part of its beneficial effects are due to its antiinflammatory properties that result from an inhibitory effect on NF-κB signaling pathway. This ability raises the hypothesis that CS might be effective in other chronic inflammatory processes such as psoriasis, in which a deregulation of NF-κB is a key feature. In addition, psoriasis is characterized by an upregulation of STAT3 signaling pathway that is related to the epidermal…

KeratinocytesSTAT3 Transcription FactorBlotting WesternPrimary Cell CultureAnti-Inflammatory AgentsDermoscopyElectrophoretic Mobility Shift AssayPharmacologyStat3 Signaling Pathwaychemistry.chemical_compoundDownregulation and upregulationPsoriasismedicineHumansPsoriasisChondroitin sulfateCells CulturedPharmacologyChemistryChondroitin SulfatesNF-kappa BNF-κBmedicine.diseaseMicroscopy FluorescenceImmunologyPhosphorylationTumor necrosis factor alphaSignal transductionProtein BindingPharmacological Research
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Studies of Jak/STAT3 expression and signalling in psoriasis identifies STAT3-Ser727 phosphorylation as a modulator of transcriptional activity

2013

Jak/Tyk proteins have recently aroused as possible therapeutic targets for the treatment of psoriasis. In psoriasis, these proteins signal through STAT molecules including STAT3, and STAT3 expression and activation has been shown augmented in psoriatic lesions. Here, we characterized the expression of Jak/Tyk proteins in lesional compared with non-lesional psoriatic skin. Jak1, Jak2 mRNA and protein and Tyk2 mRNA appeared to be downregulated, whereas Jak3 mRNA expression was increased. Moreover, STAT3 expression and activation was examined in psoriasis. STAT3 is activated at two phosphorylation sites: Tyr705 and Ser727. Both phosphorylation sites were phosphorylated in lesional psoriatic sk…

KeratinocytesSTAT3 Transcription FactorTranscription GeneticMAP Kinase Signaling SystemBiopsyp38 mitogen-activated protein kinasesPrimary Cell CultureGene ExpressionDermatologyBiochemistrystatInterleukin 20PsoriasisSerinemedicineHumansPsoriasisRNA MessengerPhosphorylationSTAT3Molecular BiologySkinTYK2 KinasebiologyInterleukin-6InterleukinsJanus Kinase 3Janus Kinase 1Janus Kinase 2medicine.diseaseTyrosine kinase 2biology.proteinCancer researchPhosphorylationTumor necrosis factor alphaSignal Transduction
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LS104, a Novel Kinase Inhibitor, Induces Apoptosis, Synergizes with Cytostatic Drugs and Is Targeting the Receptor Tyrosine Kinase FLT3.

2005

Abstract Fms-like tyrosine kinase 3 (FLT3), a member of the class III tyrosine kinase receptor family, is expressed in up to 90% of acute myeloid leukemia (AML). Activating mutations like internal tandem duplication (ITD) of the juxtamembrane domain and kinase domain point mutations are found in approximately 35% of AML-cases and are considered to represent an attractive therapeutic target. In this study, we report that the novel hydroxystyryl-acrylonitrile compound LS104 induces potent cytotoxic effects in FLT3 ITD-positive leukemic cells. As a cellular model to investigate FLT3-ITD specific effects we used 32D myeloid cells stably transfected with FLT3-ITD and wt-FLT3, respectively. In MT…

KinaseCell growthImmunologyTyrosine phosphorylationCell BiologyHematologyBiologymedicine.diseaseBiochemistryMolecular biologyReceptor tyrosine kinaseLeukemiachemistry.chemical_compoundchemistryAnnexinhemic and lymphatic diseasesembryonic structuresmedicinebiology.proteinKinase activityTyrosineBlood
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Control of the mutagenicity of arylamines by protein kinases and phosphatases:

1997

Treatment of rat hepatocytes with the phosphatase inhibitors okadaic acid or ortho-vanadate had led to an 80% decrease in the bacterial mutagenicity of several aromatic amines metabolically activated by these hepatocytes. This is the most dramatic change yet demonstrated in mutagenicity by phosphorylation modulation. However, incorporation of phosphate into and catalytic activity of cytochromes P450 (CYP) 1A1 and 1A2, the major catalysts for the first step in the toxication of aromatic amines, were unchanged. We therefore investigated whether changes in the phosphorylation status would influence the activities of the N-acetyltransferases NAT1 and/or NAT2, being responsible for one of the tw…

KinaseHealth Toxicology and MutagenesisPhosphataseCYP1A2Adenylate kinaseGeneral MedicineProtein phosphatase 2Okadaic acidBiologyToxicologychemistry.chemical_compoundBiochemistrychemistryPhosphorylationProtein kinase AArchives of Toxicology
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STAT1 expression and activation is increased in lesional psoriatic skin

2013

Summary Background  The JAK (Janus kinase)/STAT (signal transducer and activator of transcription) signalling pathway is known to play an important role in many cellular processes including inflammation. The activation of STAT1 is dependent on tyrosine 701 and serine 727 phosphorylation, which leads to the formation of the STAT dimer and modulation of STAT1 activity, respectively. Objective  To determine STAT1 expression and activation in psoriatic skin. Methods  Biopsies were collected from patients with psoriasis. mRNA expression was evaluated by quantitative polymerase chain reaction, whereas the protein and phosphorylation level of STAT1 were evaluated by Western blotting. STAT1 localiz…

Kinasep38 mitogen-activated protein kinasesDermatologyBiologymedicine.diseaseMolecular biologyPsoriasismedicineSTAT proteinbiology.proteinPhosphorylationSTAT1Janus kinaseProtein kinase CBritish Journal of Dermatology
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Clusterin and LRP2 are critical components of the hypothalamic feeding regulatory pathway.

2012

Hypothalamic feeding circuits are essential for the maintenance of energy balance. There have been intensive efforts to discover new biological molecules involved in these pathways. Here we report that central administration of clusterin, also called apolipoprotein J, causes anorexia, weight loss and activation of hypothalamic signal transduction-activated transcript-3 in mice. In contrast, inhibition of hypothalamic clusterin action results in increased food intake and body weight, leading to adiposity. These effects are likely mediated through the mutual actions of the low-density lipoprotein receptor-related protein-2, a potential receptor for clusterin, and the long-form leptin receptor…

LeptinMaleSTAT3 Transcription Factormedicine.medical_specialtyApolipoprotein BHypothalamusGeneral Physics and AstronomyGeneral Biochemistry Genetics and Molecular BiologyCell LineMiceInternal medicinemedicineAnimalsHumansObesityPhosphorylationReceptorInjections IntraventricularEpididymisMultidisciplinaryLeptin receptorbiologyClusterinLeptinBody WeightGeneral ChemistryFeeding BehaviorLRP2ImmunohistochemistryHedgehog signaling pathwayAnorexiaRatsLow Density Lipoprotein Receptor-Related Protein-2EndocrinologyClusterinStarvationbiology.proteinReceptors LeptinLipoproteinProtein BindingSignal TransductionNature communications
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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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Selective uptake and degradation of c-Fos and v-Fos by rat liver lysosomes

1996

AbstractThe transcription factor c-Fos is a short-lived protein and calpains and ubiquitin-dependent systems have been proposed to be involved in its degradation. In this report, we consider a lysosomal degradation pathway for c-Fos. Using a cell-free assay, we have found that freshly isolated lysosomes can take up and degrade c-Fos with high efficiency. v-Fos, the oncogenic counterpart of c-Fos, can also be taken up by lysosomes, yet the amount of incorporated protein is much lower. c-Fos uptake is independent of its phosphorylation state but it appears to be regulated by dimerization with differentially phosphorylated forms of c-Jun, while v-Fos escapes this regulation. Moreover, we show …

LeupeptinsProto-Oncogene Proteins c-junBiophysicsProtein degradationProtein degradationTransfectionBiochemistryc-FosCell Linechemistry.chemical_compoundStructural BiologyLysosomeGeneticsmedicineAnimalsHumansProtease InhibitorsTrypsinPhosphorylationMolecular BiologyTranscription factorc-FosCell-Free Systembiologyc-junLeupeptinc-Junv-FosCalpainCell BiologyLysosomeRecombinant ProteinsRatsKineticsOncogene Proteins v-fosmedicine.anatomical_structureLiverchemistryBiochemistrybiology.proteinPhosphorylationElectrophoresis Polyacrylamide GelLysosomesProto-Oncogene Proteins c-fosHeLa CellsFEBS Letters
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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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