Search results for "Phosphor"

showing 10 items of 1952 documents

In Situ Detection of Phosphorylated Platelet-derived Growth Factor Receptor β Using a Generalized Proximity Ligation Method

2007

Improved methods are needed for in situ characterization of post-translational modifications in cell lines and tissues. For example, it is desirable to monitor the phosphorylation status of individual receptor tyrosine kinases in samples from human tumors treated with inhibitors to evaluate therapeutic responses. Unfortunately the leading methods for observing the dynamics of tissue post-translational modifications in situ, immunohistochemistry and immunofluorescence, exhibit limited sensitivity and selectivity. Proximity ligation assay is a novel method that offers improved selectivity through the requirement of dual recognition and increased sensitivity by including DNA amplification as a…

ProteomicsImmunoglobulinsProximity ligation assayKidneyBiochemistryReceptor tyrosine kinaseCell LineAnalytical ChemistryReceptor Platelet-Derived Growth Factor betaGrowth factor receptorPlatelet-Derived Growth Factor Receptor BetaHumansPhosphorylationMolecular BiologyWound HealingbiologyEndothelial CellsTransfectionFibroblastsImmunohistochemistryPrimary and secondary antibodiesMolecular biologyActinsCell culturebiology.proteinTyrosinePhosphorylationProtein Processing Post-TranslationalSignal TransductionMolecular & Cellular Proteomics
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Proteomic analysis of tyrosine phosphorylation induced by exogenous expression of oncogenic kinase fusions identified in lung adenocarcinoma.

2021

Kinase fusions are considered oncogenic drivers in numerous types of cancer. In lung adenocarcinoma 5-10% of patients harbor kinase fusions. The most frequently detected kinase fusion involves the Anaplastic Lymphoma Kinase (ALK) and Echinoderm Microtubule-associated protein-Like 4 (EML4). In addition, oncogenic kinase fusions involving the tyrosine kinases RET and ROS1 are found in smaller subsets of patients. In this study, we employed quantitative mass spectrometry-based phosphoproteomics to define the cellular tyrosine phosphorylation patterns induced by different oncogenic kinase fusions identified in patients with lung adenocarcinoma. We show that exogenous expression of the kinase fu…

ProteomicsLung NeoplasmsOncogene Proteins FusionAdenocarcinoma of LungBiologyBiochemistry03 medical and health scienceschemistry.chemical_compoundProto-Oncogene ProteinsmedicineROS1Anaplastic lymphoma kinaseHumansddc:610PhosphorylationLung cancerMolecular Biology030304 developmental biology0303 health sciencesKinase030302 biochemistry & molecular biologyProto-Oncogene Proteins c-retPhosphoproteomicsTyrosine phosphorylationProtein-Tyrosine Kinasesmedicine.diseasechemistryCancer researchPhosphorylationTyrosineTyrosine kinaseProteomicsREFERENCES
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Plant protein phosphorylation monitored by capillary liquid chromatography–element mass spectrometry

2007

Abstract Many essential cellular functions such as growth rate, motility, and metabolic activity are linked to reversible protein phosphorylation, since they are controlled by signaling cascades based mainly on phosphorylation/dephosphorylation events. Quantification of global or site-specific protein phosphorylation is not straightforward with standard proteomic techniques. The coupling of capillary liquid chromatography (μLC) with ICP-MS (inductively coupled plasma-mass spectrometry) is a method which allows a quantitative screening of protein extracts for their phosphorus and sulfur content, and thus provides access to the protein phosphorylation degree. In extension of a recent pilot st…

ProteomicsPhosphataseArabidopsisProtozoan ProteinsBiophysicsChlamydomonas reinhardtiimacromolecular substancesBiologyProteomicsBiochemistryMass SpectrometryDephosphorylationMiceAnimalsProtein phosphorylationPhosphorylationMolecular BiologyCells CulturedPlant ProteinsChromatographyArabidopsis ProteinsPhosphorusCell BiologyPhosphoproteinsbiology.organism_classificationPeptide FragmentsBiochemistryPlant proteinPhosphoproteinPhosphorylationChlamydomonas reinhardtiiSulfurChromatography LiquidBiochemical and Biophysical Research Communications
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Saccharomyces cerevisiae Cytosolic Thioredoxins Control Glycolysis, Lipid Metabolism, and Protein Biosynthesis under Wine-Making Conditions.

2019

Thioredoxins are small proteins that regulate the cellular redox state, prevent oxidative damage, and play an active role in cell repair. Oxidative stress has proven to be of much relevance in biotechnological processes when the metabolism of Saccharomyces cerevisiae is mainly respiratory. During wine yeast starter production, active dry yeast cytosolic thioredoxin Trx2p is a key player in protecting metabolic enzymes from being oxidized by carbonylation. Less is known about the role of redox control during grape juice fermentation. A mutant strain that lacked both cytosolic thioredoxins, Trx1p and Trx2p, was tested for grape juice fermentation. Its growth and sugar consumption were greatly…

ProteomicsSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaethioredoxin-thioredoxin reductase systemsyeastsWineOxidative phosphorylationSaccharomyces cerevisiaeApplied Microbiology and Biotechnology03 medical and health sciencesCytosolThioredoxinsYeastsMetabolomicsVitis030304 developmental biology0303 health sciencesEcologybiology030306 microbiologyChemistryfood and beveragesMembrane ProteinsLipid metabolismMetabolismPeroxiredoxinsglycolysisbiology.organism_classificationLipid MetabolismmetabolomicsYeastYeast in winemakingOxidative StressBiochemistryProtein BiosynthesisFermentationFood MicrobiologyFermentationThioredoxinThioredoxin-thioredoxin reductase systemsGlycolysisOxidation-ReductionGene DeletionFood ScienceBiotechnology
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Phosphorylation of Elp1 by Hrr25 is required for elongator-dependent tRNA modification in yeast.

2014

Elongator is a conserved protein complex comprising six different polypeptides that has been ascribed a wide range of functions, but which is now known to be required for modification of uridine residues in the wobble position of a subset of tRNAs in yeast, plants, worms and mammals. In previous work, we showed that Elongator's largest subunit (Elp1; also known as Iki3) was phosphorylated and implicated the yeast casein kinase I Hrr25 in Elongator function. Here we report identification of nine in vivo phosphorylation sites within Elp1 and show that four of these, clustered close to the Elp1 C-terminus and adjacent to a region that binds tRNA, are important for Elongator's tRNA modification…

ProteomicsSaccharomyces cerevisiae Proteinslcsh:QH426-470Saccharomyces cerevisiaeBiochemistryMolecular GeneticsRNA TransferGene Expression Regulation FungalMolecular Cell BiologyGeneticsFungal GeneticsPhosphorylationPost-Translational ModificationUridineMolecular BiologyAdaptor Proteins Signal TransducingHistone AcetyltransferasesAlanineSpectrometric Identification of ProteinsBiology and life sciencesCasein Kinase INucleotidesMicrobial GeneticsProteinsCell BiologyPeptide Elongation Factorslcsh:GeneticsPhenotypeMultiprotein ComplexesRNAMolecular ComplexesTransfer RNAAnticodonsResearch ArticlePLoS genetics
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SIK2 orchestrates actin-dependent host response upon Salmonella infection

2021

Significance Through conducting quantitative proteomics upon Salmonella infection, we identified a SIK2 signaling network, implementing the kinase into a so far concealed biological function. Our data exposed SIK2 as a central orchestrator of an actin regulatory network, coordinating the stability of Salmonella-containing vacuole (SCV) and cellular actin assembly, in order to limit the acute phase of the infection. Most strikingly, SIK2 is not exclusively acting locally on actin assembly associated with the SCV but impacts the actin cytoskeleton architecture in its entirety upon Salmonella infection. Our work provides a mechanistic framework for how the actin cytoskeleton is regulated and h…

ProteomicsSalmonellaactin cytoskeletonImmunoblottingArp2/3 complexSalmonella infectionmacromolecular substancesProtein Serine-Threonine Kinasesmedicine.disease_causeBiochemistry03 medical and health sciencesMice0302 clinical medicineSalmonellamedicineXenophagyAnimalsHumansArp2/3 complexProtein Interaction MapsPhosphorylationActinCells Cultured030304 developmental biologyActin nucleation0303 health sciencesMultidisciplinarybiologyEpithelial CellsBiological Sciencesmedicine.diseaseActin cytoskeletonHCT116 CellsPhosphoproteinsActinsCell biologySalmonella-containing vacuoleHEK293 CellsFormins407Host-Pathogen Interactionsbiology.proteinRNA Interference030217 neurology & neurosurgeryhost–pathogen interactionsHeLa CellsSignal TransductionProceedings of the National Academy of Sciences of the United States of America
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Mitochondrial proteomics profile points oxidative phosphorylation as main target for beauvericin and enniatin B mixture

2020

Abstract Beauvericin (BEA) and enniatin B (EN B) are non-legislated Fusarium mycotoxins usually found in cereal and cereal-based products all around the world. By the proteomic analysis of mitochondria enriched extracts from Jurkat cells exposed for 24 h to three concentrations of BEA:EN B (0.01–0.1–0.5 μM), a number of 1821 proteins (202 mitochondrial) were identified and relatively quantified. 340 proteins (59 mitochondrial) were statistically significant altered in our samples (Anova p-value ≤ 0.05 and fold change (FC) ≥1.5). The protein mitochondrial translational release factor 1 like (MTRF1L) was the most abundant protein in the three mycotoxin exposures studied. The mycotoxins mixtur…

ProteomicsTranscription GeneticOxidative phosphorylationMitochondrionToxicologyProteomicsRibosomeJurkat cellsOxidative PhosphorylationElectron TransportMitochondrial ProteinsJurkat Cells03 medical and health scienceschemistry.chemical_compound0404 agricultural biotechnologyDepsipeptidesHumans030304 developmental biology0303 health sciencesfood and beverages04 agricultural and veterinary sciencesGeneral Medicine040401 food scienceBeauvericinFold changeMitochondriachemistryBiochemistryBacterial outer membraneFood ScienceFood and Chemical Toxicology
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Multi-laboratory experiment PME11 for the standardization of phosphoproteome analysis

2022

6 p.-2 fig.-2 tab.

ProteomicsenrichmentStandardizationProteomeComputer scienceCellbiologiMass-spectrometryBiophysics610 Medicine & healthComputational biologyBioinformatik och systembiologiProteòmicaProteomics:Chemical Phenomena::Biochemical Phenomena::Phosphorylation [PHENOMENA AND PROCESSES]BiochemistryExperimentFosforilació:Natural Science Disciplines::Biological Science Disciplines::Biochemistry::Proteomics [DISCIPLINES AND OCCUPATIONS]:Investigative Techniques::Epidemiologic Methods::Epidemiologic Research Design::Reproducibility of Results [ANALYTICAL DIAGNOSTIC AND THERAPEUTIC TECHNIQUES AND EQUIPMENT]Inter-laboratoryPhosphorylationquality controlEpidemiologia610 Medicine & healthBioinformatics and Systems BiologyFosfoproteïnes:fenómenos químicos::fenómenos bioquímicos::fosforilación [FENÓMENOS Y PROCESOS]:disciplinas de las ciencias naturales::disciplinas de las ciencias biológicas::bioquímica::proteómica [DISCIPLINAS Y OCUPACIONES]PhosphoproteomicsBiochemistry and Molecular BiologyReproducibility of ResultsCell BiologyReference Standards:técnicas de investigación::métodos epidemiológicos::diseño de la investigación epidemiológica::reproducibilidad de los resultados [TÉCNICAS Y EQUIPOS ANALÍTICOS DIAGNÓSTICOS Y TERAPÉUTICOS]NormalitzacióPhosphoproteinsStandardizationReference samplePhosphoproteomeProteomeLaboratory experimentLaboratoriesBiokemi och molekylärbiologi
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B-Raf Acts via the ROCKII/LIMK/Cofilin Pathway To Maintain Actin Stress Fibers in Fibroblasts

2004

Members of the Raf family of serine/threonine protein kinases have been well studied in a variety of organisms ranging from Drosophila to humans. Three raf homologues (raf-1, B-raf, and A-raf) exist in mammals, while a single prototypic homologue exists in lower organisms. A wealth of genetic and biochemical data have indicated that Raf family members are signaling kinases that are integral components of the conserved Ras/Raf/MEK/ERK signaling cascade. Following activation by Ras-dependent mechanisms, Raf protein kinases act as mitogen-activated protein (MAP) kinase kinase kinases, which phosphorylate and activate the type 1/2 MAP kinase kinases, also known as MEK1/2. These dual-specificity…

Proto-Oncogene Proteins B-rafMAPK/ERK pathwaymacromolecular substancesProtein Serine-Threonine KinasesTransfectionCell LineProto-Oncogene Proteins B-rafLim kinaseMiceCell MovementStress FibersAnimalsHumansPhosphorylationKinase activityCell Growth and DevelopmentMolecular BiologyRho-associated protein kinaseCytoskeletonrho-Associated KinasesbiologyKinaseMicrofilament ProteinsIntracellular Signaling Peptides and ProteinsLim KinasesCell BiologyFibroblastsMolecular biologyActinsCell biologyProto-Oncogene Proteins c-rafActin Depolymerizing FactorsMitogen-activated protein kinasebiology.proteinProto-Oncogene Proteins c-rafMitogen-Activated Protein KinasesProtein KinasesSignal TransductionMolecular and Cellular Biology
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Piclamilast inhibits the pro-apoptotic and anti-proliferative responses of A549 cells exposed to H(2)O(2) via mechanisms involving AP-1 activation.

2012

Reactive oxygen species (ROS) are involved in the pathogenesis of many inflammatory diseases such as chronic obstructive pulmonary disease (COPD). They can alter the expression of genes involved in cellular damage by activating transcription factors, including the NF-κB and the activator protein 1 (AP-1). Phosphodiesterase type 4 (PDE4) inhibitors have anti-inflammatory and antioxidant effects, as described in in vivo and in vitro COPD models. This study analysed the effects of piclamilast, a selective PDE4 inhibitor, on modulating the global gene expression profile in A549 cells exposed to H(2)O(2).Changes in gene expression were analysed using high-density Affymetrix microarrays and valid…

Proto-Oncogene Proteins c-junPyridinesActivating transcription factorApoptosisBiologymedicine.disease_causeBiochemistryAntioxidantschemistry.chemical_compoundPulmonary Disease Chronic ObstructiveIn vivoAnnexinCell Line TumorGene expressionmedicineHumansRNA MessengerPhosphorylationCell ProliferationOligonucleotide Array Sequence AnalysisA549 cellGene Expression ProfilingNF-kappa BGeneral MedicineCell Cycle CheckpointsHydrogen PeroxideMolecular biologyTranscription Factor AP-1chemistryGene Expression RegulationAlveolar Epithelial CellsBenzamidesPhosphodiesterase 4 InhibitorsSignal transductionReactive Oxygen SpeciesPiclamilastOxidative stressSignal TransductionFree radical research
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