Search results for "DNA-BINDING PROTEIN"

showing 10 items of 449 documents

Tristetraprolin Regulates the Expression of the Human Inducible Nitric-Oxide Synthase Gene

2005

The expression of human inducible NO synthase (iNOS) is regulated both by transcriptional and post-transcriptional mechanisms. Stabilization of mRNAs often depends on activation of p38 mitogen-activated protein kinase (p38 MAPK). In human DLD-1 cells, inhibition of p38 MAPK by the compound 4-(4-fluorophenyl)-2-(4-methylsulfinylphenyl)-5-(4-pyridyl)1H-imidazole (SB203580) or by overexpression of a dominant-negative p38 MAPKalpha protein resulted in a reduction of human iNOS mRNA and protein expression, whereas human iNOS promoter activity was not affected. An important RNA binding protein regulated by the p38 MAPK pathway and involved in the regulation of the stability of several mRNAs is tr…

ImmunoprecipitationRNA Stabilityp38 mitogen-activated protein kinasesTristetraprolinNitric Oxide Synthase Type IIRNA-binding proteinGene Expression Regulation EnzymologicCell LineImmediate-Early ProteinsTristetraprolinEnzyme StabilityHumansRNA MessengerProtein kinase APharmacologyRegulation of gene expressionbiologyChemistryZinc FingersTransfectionMolecular biologyDNA-Binding ProteinsNitric oxide synthasebiology.proteinMolecular MedicineNitric Oxide SynthaseMolecular Pharmacology
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Diacylglycerols containing Omega 3 and Omega 6 fatty acids bind to RasGRP and modulate MAP kinase activation.

2003

We elucidated the effects of different diacylglycerols (DAGs), i.e. 1-stearoyl-2-arachidonoyl-sn-glycerol (SAG), 1-stearoyl-2-docosahexaenoyl-sn-glycerol (SDG), and 1-stearoyl-2-eicosapentaenoyl-sn-glycerol (SEG), on [3H]PDBu binding to RasGRP. The competition studies with these DAGs on [3H]PDBu binding to RasGRP revealed different Ki values for these DAG molecular species. Furthermore, we transfected human Jurkat T cells by a plasmid containing RasGRP and assessed the implication of endogenous DAGs on activation of MAP kinases ERK1/ERK2, induced by phorbol-12-myristate-13-acetate (PMA). In control cells, GF109203X, a protein kinase C inhibitor, inhibited ERK1/ERK2 activation. However, this…

IndolesTime FactorsBiochemistryJurkat cellsMaleimideschemistry.chemical_compoundJurkat CellsGuanine Nucleotide Exchange FactorsEnzyme InhibitorsMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3KinaseFatty AcidsBrainTransfectionCell biologyDNA-Binding ProteinsBiochemistryEicosapentaenoic AcidDocosahexaenoic acidMitogen-activated protein kinasePhosphorylationTetradecanoylphorbol Acetatelipids (amino acids peptides and proteins)Arachidonic acidMitogen-Activated Protein KinasesPlasmidsProtein BindingDNA ComplementaryDocosahexaenoic AcidsMAP Kinase Signaling SystemImmunoblottingBiologyTransfectionBinding CompetitiveDiglyceridesInhibitory Concentration 50Fatty Acids Omega-6Fatty Acids Omega-3Escherichia coliAnimalsHumansCalphostinMolecular BiologyDose-Response Relationship Drugurogenital systemCell BiologyRatsEnzyme ActivationKineticschemistrybiology.proteinThe Journal of biological chemistry
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The Drosophila ACP65A cuticle gene: deletion scanning analysis of cis-regulatory sequences and regulation by DHR38

2005

1526-954X (Print) Journal Article Research Support, Non-U.S. Gov't; The regulatory sequences of the Drosophila ACP65A cuticle gene were analyzed in vivo in transgenic flies, using both fusion genes constructs and transposase-mediated deletions within a P element containing ACP65A regulatory sequences fused to the lacZ gene (deletion scanning). The sequences located between -594 and +161 are sufficient to confer both temporal and spatial expression specificities, indicating the presence of tissue-specific enhancers and response elements to hormone-induced factors. In addition, timing of expression and tissue-specificity appear to be controlled by distinct cis-regulatory elements, which sugge…

Insect Proteins/*genetics/metabolismMaleBase SequenceGene Expression Regulation/*physiologyTranscription Factors/*physiologyGenetically ModifiedCytoplasmic and Nuclear/*physiologyCrossesDrosophila/*geneticsGeneticDrosophila Proteins/*genetics/metabolism/physiologyDNA-Binding Proteins/*physiologyPupa/geneticsReceptorsAnimalsFemaleSteroid/physiologyTranscriptionSequence Deletion
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Transcriptional regulation of the proton translocating NADH dehydrogenase genes (nuoA-N) of Escherichia coli by electron acceptors, electron donors a…

1995

The promoter region and transcriptional regulation of the nuoA-N gene locus encoding the proton-translocating NADH:quinone oxidoreductase was analysed. A 560 bp intergenic region upstream of the nuo locus was followed by a gene (designated lrhA for LysR homologue A) coding for a gene regulator similar to those of the LysR family. Disruption of lrhA did not affect growth (respiratory or non-respiratory) or expression of nuo significantly. Transcriptional regulation of nuo by electron acceptors, electron donors and the transcriptional regulators ArcA, FNR, NarL and NarP, and by IHF (integration host factor) was studied with protein and operon fusions containing the promoter region up to base …

Integration Host FactorsIron-Sulfur ProteinsTranscription GeneticOperonMolecular Sequence DataRepressorLocus (genetics)medicine.disease_causeMicrobiologyElectron TransportBacterial ProteinsOperonmedicineTranscriptional regulationEscherichia coliAmino Acid SequencePromoter Regions GeneticMolecular BiologyEscherichia coliGenebiologyBase SequenceSequence Homology Amino AcidEscherichia coli ProteinsNADH dehydrogenasePromoterNADH DehydrogenaseGene Expression Regulation BacterialMolecular biologyAerobiosisDNA-Binding ProteinsRepressor ProteinsBiochemistrybiology.proteinbacteriaProtonsSequence AlignmentBacterial Outer Membrane ProteinsTranscription FactorsMolecular microbiology
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Induction of interferon regulatory factors, 2′‐5′ oligoadenylate synthetase, P68 kinase and RNase L in chronic myelogenous leukaemia cells and its re…

1996

The genes crucially determining the therapeutic response of chronic myelogenous leukaemia (CML) to interferon-alpha (IFN-alpha) are unknown. Recently, two independent IFN-alpha signalling pathways were identified: the classic pathway mediates induction of 2'-5' oligoadenylate synthetase (2-5 OAS), p68 kinase and IFN regulatory factor-2 (IRF-2), whereas the alternate pathway leads to activation of IFN regulatory factor-1 (IRF-1). We investigated whether deficient or imbalanced expression of components of these two pathways is associated with resistance of CML cells to antiproliferative action of IFN alpha/beta. Constitutive and IFN-induced transcript levels of IFN-dependent genes in mononucl…

Interferon Regulatory Factor 2T-LymphocytesCellular differentiationmedicine.medical_treatmentProtein Serine-Threonine KinaseseIF-2 KinaseLeukemia Myelogenous Chronic BCR-ABL PositiveEndoribonucleases2'5'-Oligoadenylate SynthetasemedicineHumansRNA MessengerTreatment FailureInterferon alfaEIF-2 kinasebiology2'-5'-OligoadenylateInterferon-alphaHematologyBlotting NorthernHematopoietic Stem CellsPhosphoproteinsDNA-Binding ProteinsGene Expression Regulation NeoplasticRepressor ProteinsCytokineIRF1Cancer researchbiology.proteinInterferon Regulatory Factor-2GranulocytesInterferon Regulatory Factor-1Transcription Factorsmedicine.drugInterferon regulatory factorsBritish Journal of Haematology
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Study of the cytolethal distending toxin (CDT)-activated cell cycle checkpoint. Involvement of the CHK2 kinase.

2001

AbstractThe bacterial cytolethal distending toxin (CDT) triggers a G2/M cell cycle arrest in eukaryotic cells by inhibiting the CDC25C phosphatase-dependent CDK1 dephosphorylation and activation. We report that upon CDT treatment CDC25C is fully sequestered in the cytoplasmic compartment, an effect that is reminiscent of DNA damage-dependent checkpoint activation. We show that the checkpoint kinase CHK2, an upstream regulator of CDC25C, is phosphorylated and activated after CDT treatment. In contrast to what is observed with other DNA damaging agents, we demonstrate that the activation of CHK2 can only take place during S-phase. Use of wortmannin and caffeine suggests that this effect is no…

Intracellular FluidCell cycle checkpointCytolethal distending toxinCell Cycle ProteinsAtaxia Telangiectasia Mutated ProteinsBiochemistryS PhaseWortmanninchemistry.chemical_compoundStructural BiologyPhosphorylation0303 health sciences030302 biochemistry & molecular biologyCell CycleCell cycleProtein-Tyrosine Kinases3. Good healthCell biologyDNA-Binding Proteinsbiological phenomena cell phenomena and immunityWortmanninG2 PhaseCytolethal distending toxinBacterial ToxinsProto-Oncogene Proteins pp60(c-src)Biophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyProtein Serine-Threonine KinasesCell Line03 medical and health sciencesCaffeineGeneticsHumanscdc25 PhosphatasesCHEK1Molecular Biology[SDV.BC] Life Sciences [q-bio]/Cellular Biology030304 developmental biologyCheckpoint 2 kinaseCyclin-dependent kinase 1Cell growthTumor Suppressor ProteinsCell BiologyG2-M DNA damage checkpointCDC25CAndrostadienesGenes cdcchemistryCancer researchHeLa CellsFEBS letters
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A genome-wide transcriptional study reveals that iron deficiency inhibits the yeast TORC1 pathway

2019

Iron is an essential micronutrient that participates as a cofactor in a broad range of metabolic processes including mitochondrial respiration, DNA replication, protein translation and lipid biosynthesis. Adaptation to iron deficiency requires the global reorganization of cellular metabolism directed to optimize iron utilization. The budding yeast Saccharomyces cerevisiae has been widely used to characterize the responses of eukaryotic microorganisms to iron depletion. In this report, we used a genomic approach to investigate the contribution of transcription rates to the modulation of mRNA levels during adaptation of yeast cells to iron starvation. We reveal that a decrease in the activity…

IronSaccharomyces cerevisiaeBiophysicsRibosome biogenesisSaccharomyces cerevisiaeMechanistic Target of Rapamycin Complex 1Biochemistry03 medical and health sciencesStructural BiologyRibosomal proteinTranscription (biology)Gene Expression Regulation FungalLipid biosynthesisGeneticsHumansRNA MessengerPhosphorylationMolecular BiologyGene030304 developmental biology0303 health sciencesAnemia Iron-Deficiencybiology030306 microbiologyChemistryIron deficiencyRNA polymerasesRNATORbiology.organism_classificationAdaptation PhysiologicalYeastCell biologyDNA-Binding ProteinsGene Expression RegulationProtein BiosynthesisSignal transductionTranscription
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Yeast Dun1 Kinase Regulates Ribonucleotide Reductase Inhibitor Sml1 in Response to Iron Deficiency

2014

Iron is an essential micronutrient for all eukaryotic organisms because it participates as a redox-active cofactor in many biological processes, including DNA replication and repair. Eukaryotic ribonucleotide reductases (RNRs) are Fe-dependent enzymes that catalyze deoxyribonucleoside diphosphate (dNDP) synthesis. We show here that the levels of the Sml1 protein, a yeast RNR large-subunit inhibitor, specifically decrease in response to both nutritional and genetic Fe deficiencies in a Dun1-dependent but Mec1/Rad53- and Aft1-independent manner. The decline of Sml1 protein levels upon Fe starvation depends on Dun1 forkhead-associated and kinase domains, the 26S proteasome, and the vacuolar pr…

Iron-Sulfur ProteinsProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsDeoxyribonucleoside triphosphateRibonucleotideIronDeoxyribonucleotidesGenes FungalSaccharomyces cerevisiaeCell Cycle ProteinsSaccharomyces cerevisiaeRibonucleotide reductase inhibitorProtein Serine-Threonine KinasesBiologyProtein degradationchemistry.chemical_compoundTristetraprolinRibonucleotide ReductasesAspartic Acid EndopeptidasesPhosphorylationMolecular BiologyCheckpoint Kinase 2Binding SitesKinaseIntracellular Signaling Peptides and ProteinsArticlesCell Biologybiology.organism_classificationDNA-Binding ProteinsDeoxyribonucleosideCheckpoint Kinase 2chemistryBiochemistryProteolysisGene DeletionTranscription FactorsMolecular and Cellular Biology
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Resistance of keratinocytes to TGFbeta-mediated growth restriction and apoptosis induction accelerates re-epithelialization in skin wounds.

2002

The pleiotropic growth factor TGFβ plays an important role in regulating responses to skin injury. TGFβ targets many different cell types and is involved in all aspects of wound healing entailing inflammation,re-epithelialization, matrix formation and remodeling. To elucidate the role of TGFβ signal transduction in keratinocytes during cutaneous wound healing, we have used transgenic mice expressing a dominant negative type II TGFβ receptor exclusively in keratinocytes. We could demonstrate that this loss of TGFβ signaling in keratinocytes led to an accelerated re-epithelialization of full thickness excisional wounds accompanied by an increased proliferation in keratinocytes at the wound ed…

Keratinocytesmedicine.medical_treatmentEGR1InflammationApoptosisMice TransgenicBiologyImmediate early proteinCell LineImmediate-Early ProteinsMiceDownregulation and upregulationTransforming Growth Factor betamedicineAnimalsTranscription factorEarly Growth Response Protein 1Wound Healingintegumentary systemGrowth factorGene Expression ProfilingCell BiologyCell biologyDNA-Binding ProteinsEpidermal CellsImmunologymedicine.symptomSignal transductionEpidermisWound healingCell DivisionTranscription FactorsJournal of cell science
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Leptin: A pivotal mediator of intestinal inflammation in mice

2002

Abstract Background & Aims: In addition to acting as a regulator of food intake and energy expenditure, leptin can also modulate immune and inflammatory responses. The role of leptin in intestinal inflammation is the focus of the present study. Methods: Acute and chronic colitis were induced in leptin-deficient ob/ob or wild-type (WT) mice using dextran sulfate sodium (DSS) or trinitrobenzene sulfonic acid (TNBS). The severity of colitis was evaluated, and possible mechanisms were studied. Results: Leptin directly stimulates intraepithelial lymphocytes (IELs) and lamina propria mononuclear cells (LPMCs). In the DSS acute model, ob/ob mice exhibited a 72% reduction of colitis severity and sp…

LeptinSTAT3 Transcription Factormedicine.medical_specialtyColonanimal diseasesdigestive systemMonocytesProinflammatory cytokineMiceReference ValuesInternal medicinemedicineAnimalsInterferon gammaLymphocytesObesityIntestinal MucosaColitisMacrophage inflammatory proteinCells CulturedLeptin DeficiencyHepatologybusiness.industryLeptinDextran SulfateGastroenterologyColitismedicine.diseasedigestive system diseasesDNA-Binding ProteinsIsoenzymesMice Inbred C57BLEndocrinologyTrinitrobenzenesulfonic AcidCyclooxygenase 2Prostaglandin-Endoperoxide SynthasesEnzyme InductionChronic DiseaseImmunologyTrans-ActivatorsCytokinesIntraepithelial lymphocyteFemaleTumor necrosis factor alphaDisease SusceptibilityChemokinesbusinessmedicine.drugGastroenterology
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