Search results for "Phosphorylation"

showing 10 items of 975 documents

Unraveling the evolutionary history of the phosphoryl-transfer chain of the phosphoenolpyruvate:phosphotransferase system through phylogenetic analys…

2007

[Background] The phosphoenolpyruvate phosphotransferase system (PTS) plays a major role in sugar transport and in the regulation of essential physiological processes in many bacteria. The PTS couples solute transport to its phosphorylation at the expense of phosphoenolpyruvate (PEP) and it consists of general cytoplasmic phosphoryl transfer proteins and specific enzyme II complexes which catalyze the uptake and phosphorylation of solutes. Previous studies have suggested that the evolution of the constituents of the enzyme II complexes has been driven largely by horizontal gene transfer whereas vertical inheritance has been prevalent in the general phosphoryl transfer proteins in some bacter…

FirmicutesEvolutionContext (language use)macromolecular substancesGene Expression Regulation EnzymologicEvolution MolecularPTS phosphoryl transfer chain (PTS-ptc)Genome ArchaealPhylogeneticsQH359-425DeinococcusPhosphorylationPhosphoenolpyruvate Sugar Phosphotransferase SystemGenePhylogenyEcology Evolution Behavior and SystematicsGeneticsBacteriaSequence Homology Amino AcidbiologyPhylogenetic tree:CIENCIAS DE LA VIDA::Biología celular::Citogenética [UNESCO]Phosphoenolpyruvate phosphotransferase system (PTS)Computational BiologyGene Expression Regulation BacterialPEP group translocationPhosphoenolpyruvate phosphotransferase system (PTS); Cytoplasmic phosphoryl transfer proteins; PTS phosphoryl transfer chain (PTS-ptc)biology.organism_classificationArchaeaUNESCO::CIENCIAS DE LA VIDA::Biología celular::CitogenéticaMultigene FamilyHorizontal gene transferbacteriaCytoplasmic phosphoryl transfer proteinsSequence AlignmentGenome BacterialResearch Article
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As2O3-induced oxidative stress and cycle progression in a human intestinal epithelial cell line (Caco-2)

2007

Foods and drinking water are the main routes for human exposure to inorganic arsenic, the intestinal epithelium being the first barrier against such exogenous toxicants. The present study evaluates the effect of As(III) (0.5-25 microM) upon Caco-2 cells as an intestinal epithelia model. Cell viability, intracellular formation of reactive oxygen species (ROS), mitochondrial membrane potential (Deltapsim) changes, and cell cycle distribution in exposed cultures were evaluated. The intracellular production of ROS was seen to increase in a non-dose dependent manner at all concentrations tested, with impairment of cell mitochondrial enzyme function secondary to a loss of Deltapsim. Concentration…

G2 PhaseCell SurvivalCellTetrazolium SaltsOxidative phosphorylationBiologyToxicologymedicine.disease_causeArsenicalsMembrane PotentialsArsenic TrioxidemedicineHumansViability assaychemistry.chemical_classificationReactive oxygen speciesCell CycleG1 PhaseOxidesGeneral MedicineCell cycleIntestinal epitheliumMitochondriaCell biologyOxidative StressThiazolesmedicine.anatomical_structurechemistryMitochondrial MembranesCaco-2 CellsReactive Oxygen SpeciesOxidative stressIntracellularToxicology in Vitro
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Escherichia coli cytolethal distending toxin blocks the HeLa cell cycle at the G2/M transition by preventing cdc2 protein kinase dephosphorylation an…

1997

Cytolethal distending toxins (CDT) constitute an emerging heterogeneous family of bacterial toxins whose common biological property is to inhibit the proliferation of cells in culture by blocking their cycle at G2/M phase. In this study, we investigated the molecular mechanisms underlying the block caused by CDT from Escherichia coli on synchronized HeLa cell cultures. To this end, we studied specifically the behavior of the two subunits of the complex that determines entry into mitosis, i.e., cyclin B1, the regulatory unit, and cdc2 protein kinase, the catalytic unit. We thus demonstrate that CDT causes cell accumulation in G2 and not in M, that it does not slow the progression of cells th…

G2 PhaseCytolethal distending toxinBacterial toxins[SDV]Life Sciences [q-bio]ImmunologyBacterial ToxinsMitosisBiologyMicrobiologyCDTCDC2 Protein KinaseEscherichia coliHumansKinase activityPhosphorylationMitosisCyclin-dependent kinase 1Cell growthCell CycleCell cycleG2-M DNA damage checkpointFlow CytometryMicrobiologie et ParasitologieCell biology[SDV] Life Sciences [q-bio]Enzyme ActivationInfectious DiseasesCytolethal distending toxinsParasitologyCDC2 Protein KinaseHeLa CellsResearch Article
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Type III Secretion-Dependent Cell Cycle Block Caused in HeLa Cells by Enteropathogenic Escherichia coliO103

2001

ABSTRACT Rabbit enteropathogenic Escherichia coli (EPEC) O103 induces in HeLa cells an irreversible cytopathic effect characterized by the recruitment of focal adhesions, formation of stress fibers, and inhibition of cell proliferation. We have characterized the modalities of the proliferation arrest and investigated its underlying mechanisms. We found that HeLa cells that were exposed to the rabbit EPEC O103 strain E22 progressively accumulated at 4C DNA content and did not enter mitosis. A significant proportion of the cells were able to reinitiate DNA synthesis without division, leading to 8C DNA content. This cell cycle inhibition by E22 was abrogated in mutants lacking EspA, -B, and -D…

G2 Phase[SDV]Life Sciences [q-bio]ImmunologyCyclin BMitosisReceptors Cell SurfacePATHOGENICITECyclin BMicrobiology03 medical and health sciencesBacterial ProteinsCDC2 Protein KinaseEscherichia coliHumansCyclin B1PhosphorylationCyclin B1Adhesins BacterialMitosisCytoskeleton030304 developmental biologyIntimin0303 health sciencesCyclin-dependent kinase 1Cellular Microbiology: Pathogen-Host Cell Molecular Interactionsbiology030306 microbiologyCell growthEscherichia coli ProteinsCell CycleREARRANGEMENTCell cycle[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/BacteriologyCell biology[SDV] Life Sciences [q-bio]Infectious Diseasesbiology.proteinTyrosineParasitologyCarrier ProteinsCDC2 Protein KinaseBacterial Outer Membrane ProteinsHeLa Cells
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Regulated expression and phosphorylation of the 23-26-kDa ras protein in the sponge Geodia cydonium.

1990

We have cloned, sequenced and examined the sponge Geodia cydonium cDNA encoding a protein homologous to ras proteins. The sponge ras protein has a more conserved N-terminal region and a less conserved C-terminal region, especially in comparison to Dictyostelium discoideum; the similarity to human c-Ha-ras-1 and to Saccharomyces cerevisiae is less pronounced. The sponge ras cDNA comprises five TAG triplets; at the translational level these UAG termination codons are suppressed by a Gln-tRNA. The sponge ras protein was isolated and partially purified (23-26 kDa) and found to undergo phosphorylation at a threonine moiety, when dissociated cells were incubated in the presence of a homologous ag…

GTP'Saccharomyces cerevisiaeMolecular Sequence DataGTPaseBiochemistryDictyostelium discoideumProto-Oncogene Proteins p21(ras)Complementary DNASequence Homology Nucleic AcidAnimalsInsulinNCK1Amino Acid SequenceThreonineCloning MolecularPhosphorylationGene LibrarybiologyBase SequenceDNAbiology.organism_classificationMolecular biologyPoriferaMolecular WeightKineticsBiochemistryGene Expression RegulationPhosphorylationEuropean journal of biochemistry
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Serine in plants: biosynthesis, metabolism, and functions

2014

Serine (Ser) has a fundamental role in metabolism and signaling in living organisms. In plants, the existence of different pathways of Ser biosynthesis has complicated our understanding of this amino acid homeostasis. The photorespiratory glycolate pathway has been considered to be of major importance, whereas the nonphotorespiratory phosphorylated pathway has been relatively neglected. Recent advances indicate that the phosphorylated pathway has an important function in plant metabolism and development. Plants deficient in this pathway display developmental defects in embryos, male gametophytes, and roots. We propose that the phosphorylated pathway is more important than was initially thou…

GametophyteEmbryoPlant ScienceMetabolismPlantsBiologyPlant RootsSerinechemistry.chemical_compoundBiosynthesischemistryBiochemistryAmino acid homeostasisGene Expression Regulation PlantStress PhysiologicalSeedsSerinePhosphorylationPhosphorylationPhotosynthesisGlycolysisFunction (biology)Plant ProteinsTrends in Plant Science
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Glycogen phosphorylase from flight muscle of the hawk moth, Manduca sexta: purification and properties of three interconvertible forms and the effect…

1994

Glycogen phosphorylase (EC 2.4.1.1) of Manduca sexta flight muscle was separated into three distinct peaks of activity on diethylaminoethyl-Sephacel. The three fractions of phosphorylase activity were further purified by affinity chromatography on AMP-Sepharose and shown to have the same relative molecular mass (=178000) on polyacrylamide gradient gel electrophoresis under non-denaturating conditions and to produce subunits of molecular mass =92000 on SDS gelelectrophoresis. On the basis of their kinetic properties with respect to the activator AMP and the inhibitor caffeine, the three fractions of phosphorylase activity were assigned as follows: peak 1=phosphorylase b (unphosphorylated for…

Gel electrophoresisMolecular massGlycogenPhysiologyBiologybiology.organism_classificationBiochemistryDephosphorylationGlycogen phosphorylasechemistry.chemical_compoundEndocrinologychemistryBiochemistryManduca sextaPhosphorylationAnimal Science and ZoologyPhosphorylase kinaseEcology Evolution Behavior and SystematicsJournal of Comparative Physiology B
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Determination of phosphorylation degrees in caseins by on-line gel electrophoresis coupled to ICP-SFMS

2007

The determination of the phosphorylation degree of proteins is essential in many biochemical fields. Besides mass spectrometric techniques elucidating the protein structure, ICP-MS has entered this research area as it provides excellent quantification capabilities. In this work the separation of the proteins has been carried out by gel electrophoresis on-line coupled to an ICP equipped with a double-focusing sector field-MS (ELEMENT 2). Based on the simultaneous detection of 32S+ and 31P+, this work presents an alternative approach to determining the phosphorylation degree of caseins. For the example of α- and β-casein the results obtained were in excellent agreement with the expected value…

Gel electrophoresisProtein structureChromatographyChemistryIcp sfmsPhosphorylationGel electrophoresis of proteinsPhosphorylated proteinsMass spectrometricSpectroscopyAnalytical ChemistryJournal of Analytical Atomic Spectrometry
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Oxidative stress inhibits IFN-α-induced antiviral gene expression by blocking the JAK–STAT pathway

2006

Abstract BACKGROUND/AIMS: Unresponsiveness to IFN-alpha is common in chronic hepatitis C. Since conditions associated with an increased oxidative stress (advanced age, steatosis, fibrosis, iron overload, and alcohol consumption) reduce the likelihood of response, we hypothesized that oxidative stress may affect the antiviral actions of IFN-alpha. METHODS: We examined in a human hepatocellular carcinoma cell line (Huh-7) the effect of hydrogen peroxide (H2O2), as a generator of oxidative stress, on the IFN-alpha signaling pathway. RESULTS: Pretreatment of Huh-7 cells with 0.5-1 mM H2O2 resulted in the suppression of the IFN-alpha-induced antiviral protein MxA and of IRF-9 mRNA expression. Th…

Gene Expression Regulation ViralMyxovirus Resistance ProteinsCarcinoma HepatocellularBlotting WesternAntiviral proteinProtein tyrosine phosphataseInterferon alpha-2Biologymedicine.disease_causechemistry.chemical_compoundGTP-Binding ProteinsCell Line TumormedicineHumansRNA NeoplasmHepatologyTyk-2Reverse Transcriptase Polymerase Chain ReactionSTATLiver NeoplasmsInterferon-alphaJAK-STAT signaling pathwayTyrosine phosphorylationHydrogen PeroxideJanus Kinase 1Flow CytometryInterferon-Stimulated Gene Factor 3 gamma SubunitRecombinant ProteinsIFN-aJAK-1Oxidative StressSTAT Transcription FactorsHydrogen peroxide; IFN-a; STAT; JAK-1; Tyk-2chemistryImmunologySTAT proteinCancer researchSignal transductionTyrosine kinaseOxidative stressSignal TransductionJournal of Hepatology
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Akt induces enhanced myocardial contractility and cell size in vivo in transgenic mice

2002

The serine-threonine kinase Akt seems to be central in mediating stimuli from different classes of receptors. In fact, both IGF-1 and IL6-like cytokines induce hypertrophic and antiapoptotic signals in cardiomyocytes through PI3K-dependent Akt activation. More recently, it was shown that Akt is involved also in the hypertrophic and antiapoptotic effects of β-adrenergic stimulation. Thus, to determine the effects of Akt on cardiac function in vivo, we generated a model of cardiac-specific Akt overexpression in mice. Transgenic mice were generated by using the E40K, constitutively active mutant of Akt linked to the rat α-myosin heavy chain promoter. The effects of cardiac-selective Akt overex…

Gene ExpressionTransgenicGlycogen Synthase Kinase 3MiceGSK-3Receptorsgenetics/physiologycytology/metabolismMultidisciplinaryBiological SciencesProtein-Serine-Threonine KinasesDNA-Binding Proteinsenzymology/genetics/pathologyAdrenergicPhosphorylationSignal transductionMitogen-Activated Protein KinasesSignal Transductionmedicine.medical_specialtyCardiomyopathyAnimals; Calcium-Calmodulin-Dependent Protein Kinases; metabolism; Cardiomyopathy; Hypertrophic; enzymology/genetics/pathology; Cell Size; physiology; DNA-Binding Proteins; GATA4 Transcription Factor; Gene Expression; Glycogen Synthase Kinase 3; Mice; Transgenic; Mitogen-Activated Protein Kinases; Myocardial Contraction; Myocardium; cytology/metabolism; Point Mutation; Protein-Serine-Threonine Kinases; Proto-Oncogene Proteins c-akt; Proto-Oncogene Proteins; genetics/physiology; Rats; Receptors; Adrenergic; beta; Signal Transduction; Transcription FactorsMice TransgenicBiologyProtein Serine-Threonine KinasesContractilityIn vivoInternal medicineProto-Oncogene ProteinsReceptors Adrenergic betamedicineAnimalsPoint MutationGlycogen synthaseProtein kinase BPI3K/AKT/mTOR pathwayCell SizeMyocardiumCardiomyopathy HypertrophicMyocardial ContractionGATA4 Transcription FactorRatsEndocrinologyHypertrophicphysiologyCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinbetametabolismProto-Oncogene Proteins c-aktTranscription Factors
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