Search results for "Phosphorylation"

showing 10 items of 975 documents

Dephosphorylation of p-ERK1/2 in relation to tumor remission after HER-2 and Raf1 blocking therapy in a conditional mouse tumor model

2006

Several studies have shown that HER-2/neu (erbB-2) blocking therapy strategies can cause tumor remission. However, the responsible molecular mechanisms are not yet known. Both ERK1/2 and Akt/PKB are critical for HER-2-mediated signal transduction. Therefore, we used a mouse tumor model that allows downregulation of HER-2 in tumor tissue by administration of anhydrotetracycline (ATc). Switching-off HER-2 caused a rapid tumor remission by more than 95% within 7 d of ATc administration compared to the volume before switching-off HER-2. Interestingly, HER-2 downregulation caused a dephosphorylation of p-ERK1/2 by more than 80% already before tumor remission occurred. Levels of total ERK protein…

MaleMAPK/ERK pathwayCancer Researchmedicine.medical_specialtyReceptor ErbB-2Blotting WesternDown-RegulationMice NudeP erk1 2BiologyTransfectionDephosphorylationMiceDownregulation and upregulationInternal medicinemedicineAnimalsHumansMouse tumorPhosphorylationMolecular BiologyProtein kinase BMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Remission InductionNeoplasms ExperimentalTumor tissueGene Expression Regulation NeoplasticProto-Oncogene Proteins c-rafDisease Models AnimalEndocrinologyTetracyclinesNIH 3T3 CellsCancer researchSignal transductionSignal TransductionMolecular Carcinogenesis
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Pentoxifylline Prevents Loss of PP2A Phosphatase Activity and Recruitment of Histone Acetyltransferases to Proinflammatory Genes in Acute Pancreatitis

2009

Mitogen-activated protein kinases (MAPKs) are considered major signal transducers early during the development of acute pancreatitis. Pentoxifylline is a phosphodiesterase inhibitor with marked anti-inflammatory properties through blockade of extracellular signal regulated kinase (ERK) phosphorylation and tumor necrosis factor alpha production. Our aim was to elucidate the mechanism of action of pentoxifylline as an anti-inflammatory agent in acute pancreatitis. Necrotizing pancreatitis induced by taurocholate in rats and taurocholate-treated AR42J acinar cells were studied. Phosphorylation of ERK and ERK kinase (MEK1/2), as well as PP2A, PP2B, and PP2C serine/threonine phosphatase activiti…

MaleMAPK/ERK pathwayChromatin ImmunoprecipitationPhosphodiesterase InhibitorsBlotting WesternPhosphataseAnti-Inflammatory AgentsPharmacologyBiologyCell LinePentoxifyllineProinflammatory cytokineCyclic AMPPhosphoprotein PhosphatasesmedicineAnimalsPentoxifyllineRats WistarExtracellular Signal-Regulated MAP KinasesHistone AcetyltransferasesInflammationPharmacologyReverse Transcriptase Polymerase Chain ReactionTumor Necrosis Factor-alphaProtein phosphatase 2medicine.diseaseCyclic Nucleotide Phosphodiesterases Type 2RatsEnzyme ActivationPancreatitisBiochemistryAcute DiseaseRNAMolecular MedicinePhosphorylationPancreatitisMitogen-Activated Protein KinasesChromatin immunoprecipitationmedicine.drugJournal of Pharmacology and Experimental Therapeutics
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Phosphorylation of extracellular signal-related protein kinase is required for rapid facilitation of heat-induced currents in rat dorsal root ganglio…

2005

A subgroup of dorsal root ganglion (DRG) neurons responds to noxious heat with an influx of cations carried by specific ion channels such as the transient receptor potential channel of the vanilloid receptor type, subtype 1 (TRPV1). Application of capsaicin induces a reversible facilitation of these currents. This facilitation could be an interaction of two agonists at their common receptor or be caused by an influx of calcium ions into the cell. Calcium influx into the cell can activate protein kinases such as the extracellular signal-related protein kinase (ERK) pathway. This study explored the kinetics, calcium-dependency and intracellular signals following application of capsaicin and l…

MaleMAPK/ERK pathwayHot TemperaturePatch-Clamp TechniquesStatistics as TopicTRPV1BiologyMembrane PotentialsRats Sprague-Dawleychemistry.chemical_compoundBAPTAGanglia SpinalNitrilesButadienesAnimalsDrug InteractionsEnzyme InhibitorsPhosphorylationExtracellular Signal-Regulated MAP KinasesProtein kinase AProtein kinase CNeuronsAnalysis of VarianceDose-Response Relationship DrugGeneral NeuroscienceMEK inhibitorRatsCell biologychemistryBiochemistryCapsaicinMitogen-activated protein kinasebiology.proteinCalciumFemaleCapsaicinNeuroscience
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Inactivation of glycogen synthase kinase-3β protects against kainic acid-induced neurotoxicity in vivo

2004

Many neurodegenerative diseases involve oxidative stress and excitotoxic cell death. In an attempt to further elucidate the signal transduction pathways involved in the cell death/cell survival associated with excitotoxicity, we have used an in vivo model of excitotoxicity employing kainic acid (KA)-induced neurotoxicity. Here, we show that extracellular signal-related kinase (ERK) 2, but not ERK 1, is phosphorylated and thereby activated in the hippocampus and cerebellum of kainic acid-treated mice. Phosphorylation and hence inactivation of glycogen synthase kinase 3beta (GSK-3beta), a general survival factor, is often a downstream consequence of mitogen-activated protein kinase pathway ac…

MaleMAPK/ERK pathwayKainic acidProgrammed cell deathTime FactorsCell SurvivalBlotting WesternExcitotoxicityTetrazolium Saltsmacromolecular substancesBiologymedicine.disease_causeHippocampusGlycogen Synthase Kinase 3Micechemistry.chemical_compoundOrgan Culture TechniquesGSK-3CerebellumNitrilesButadienesSerinemedicineAnimalsEnzyme InhibitorsPhosphorylationProtein kinase AMolecular BiologyMitogen-Activated Protein Kinase 1Glycogen Synthase Kinase 3 betaKainic AcidBehavior AnimalCell DeathKinaseGeneral NeuroscienceImmunohistochemistryCell biologyEnzyme ActivationThiazolesBiochemistrychemistryTyrosineNeurotoxicity SyndromesNeurology (clinical)Signal transductionLithium ChlorideDevelopmental BiologyBrain Research
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Hormone replacement therapy enhances IGF-1 signaling in skeletal muscle by diminishing miR-182 and miR-223 expressions : a study on postmenopausal mo…

2014

MiRNAs are fine-tuning modifiers of skeletal muscle regulation, but knowledge of their hormonal control is lacking. We used a co-twin case-control study design, that is, monozygotic postmenopausal twin pairs discordant for estrogen-based hormone replacement therapy (HRT) to explore estrogen-dependent skeletal muscle regulation via miRNAs. MiRNA profiles were determined from vastus lateralis muscle of nine healthy 54-62-years-old monozygotic female twin pairs discordant for HRT (median 7 years). MCF-7 cells, human myoblast cultures and mouse muscle experiments were used to confirm estrogen's causal role on the expression of specific miRNAs, their target mRNAs and proteins and finally the act…

MaleMICRORNASMonozygotic twinmenopausePATHWAYMice0302 clinical medicineMyocyteInsulin-Like Growth Factor IIN-VIVO0303 health sciencesphosphorylationAge FactorsBREAST-CANCER CELLSWOMENMiddle Aged3142 Public health care science environmental and occupational healthPostmenopauseESTROGENmedicine.anatomical_structureMCF-7 CellsmTORGROWTHFemaleAUTOPHAGYMESSENGER-RNASignal TransductionIGF-1 receptormedicine.medical_specialtyHormone Replacement Therapymedicine.drug_classmiR-142-3pBiology03 medical and health sciencesInternal medicinemicroRNAmedicineAnimalsHumansMuscle SkeletalProtein kinase BPI3K/AKT/mTOR pathwayAged030304 developmental biologyAKTagingSkeletal muscleOriginal ArticlesTwins MonozygoticCell BiologyAKT; FOXO3A; IGF-1 signaling; IGF-1R; aging; mTOR; menopause; miR-142-3p; miR-182; miR-223; phosphorylationmiR-223EndocrinologyEstrogenCase-Control StudiesmiR-1823121 General medicine internal medicine and other clinical medicineFOXO3AIGF-1 signalingIGF-1R030217 neurology & neurosurgeryHUMAN LONGEVITYHormone
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MUC16 Is Overexpressed in Idiopathic Pulmonary Fibrosis and Induces Fibrotic Responses Mediated by Transforming Growth Factor-β1 Canonical Pathway

2021

Several transmembrane mucins have demonstrated that they contribute intracellularly to induce fibrotic processes. The extracellular domain of MUC16 is considered as a biomarker for disease progression and death in IPF patients. However, there is no evidence regarding the signalling capabilities of MUC16 that contribute to IPF development. Here, we demonstrate that MUC16 was overexpressed in the lung tissue of IPF patients (n = 20) compared with healthy subjects (n = 17) and localised in fibroblasts and hyperplastic alveolar type II cells. Repression of MUC16 expression by siRNA-MUC16 transfection inhibited the TGF-β1-induced fibrotic processes such as mesenchymal/ myofibroblast transformati…

MaleMUC16Gene ExpressionIdiopathic pulmonary fibrosis0302 clinical medicineBiology (General)PhosphorylationMyofibroblastsLungSpectroscopytransforming growth factor betabiologyChemistryGeneral MedicineTransfectionMiddle Agedrespiratory systemidiopathic pulmonary fibrosisImmunohistochemistryRespiratory Function TestsComputer Science ApplicationsChemistrymedicine.anatomical_structure030220 oncology & carcinogenesisFemaleDisease SusceptibilityMyofibroblastSignal TransductionQH301-705.5Models BiologicalArticleCatalysisCell LineTransforming Growth Factor beta1Inorganic Chemistry03 medical and health sciencesmedicineHumansPhysical and Theoretical ChemistryFibroblastQD1-999Molecular BiologyAgedCell ProliferationA549 cellOrganic ChemistryMesenchymal stem cellMembrane ProteinsTransforming growth factor betaFibroblastsmedicine.diseaserespiratory tract diseases030228 respiratory systemCA-125 AntigenCase-Control StudiesCancer researchbiology.proteinIdiopathic Pulmonary Fibrosis ; Muc16 ; Transforming Growth Factor BetaBiomarkersTransforming growth factorInternational Journal of Molecular Sciences
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The basal levels of 8-oxoG and other oxidative modifications in intact mitochondrial DNA are low even in repair-deficient (Ogg1(-/-)/Csb(-/-)) mice.

2007

Abstract Mitochondrial DNA (mtDNA) is assumed to be highly prone to damage by reactive oxygen species (ROS) because of its location in close proximity to the mitochondrial electron transport chain. Accordingly, mitochondrial oxidative DNA damage has been hypothesized to be responsible for various neurological diseases, ageing and cancer. Since 7,8-dihydro-8-oxoguanine (8-oxoG), one of the most frequent oxidative base modifications, is removed from the mitochondrial genome by the glycosylase OGG1, the basal levels of this lesion are expected to be highly elevated in Ogg1−/− mice. To investigate this hypothesis, we have used a mtDNA relaxation assay in combination with various repair enzymes …

MaleMitochondrial DNADNA RepairDNA repairHealth Toxicology and MutagenesisOxidative phosphorylationBiologyMitochondrionDNA MitochondrialDNA Glycosylaseschemistry.chemical_compoundMiceGeneticsAnimalsPoly-ADP-Ribose Binding ProteinsMolecular BiologyMice KnockoutGuanosinePlant ExtractsCorticoviridaeMolecular biologyNuclear DNAMice Inbred C57BLDNA Repair EnzymeschemistryDNA glycosylaseDNA ViralFemaleDNANucleotide excision repairDNA DamageMutation research
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Molecular oncology focus - is carcinogenesis a 'mitochondriopathy'?

2010

Abstract Mitochondria are sub-cellular organelles that produce adenosine triphosphate (ATP) through oxidative phosphorylation (OXPHOS). As suggested over 70 years ago by Otto Warburg and recently confirmed with molecular techniques, alterations in respiratory activity and in mitochondrial DNA (mtDNA) appear to be common features of malignant cells. Somatic mtDNA mutations have been reported in many types of cancer cells, and some reports document the prevalence of inherited mitochondrial DNA polymorphisms in cancer patients. Nevertheless, a careful reanalysis of methodological criteria and methodology applied in those reports has shown that numerous papers can't be used as relevant sources …

MaleMitochondrial DNAMitochondrial DiseasesEndocrinology Diabetes and MetabolismClinical BiochemistryMEDLINElcsh:MedicineComputational biologyReviewMitochondrionBiologymedicine.disease_causeMolecular oncologyDNA MitochondrialOxidative PhosphorylationNeoplasmsmedicineBiomarkers TumorHumansPharmacology (medical)Molecular BiologyBiomedicineGeneticsBiochemistry medicalbusiness.industryBiochemistry (medical)lcsh:RCancerGeneral MedicineCell BiologyDNA Neoplasmmedicine.diseaseMolecular medicineMitochondriaMutationFemaleCarcinogenesisbusinessJournal of biomedical science
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AZT induces oxidative damage to cardiac mitochondria: Protective effect of vitamins C and E

2004

Abstract AZT (zidovudine) is a potent inhibitor of HIV replication and a major antiretroviral drug used for AIDS treatment. A major limitation in the use of AZT is the occurrence of severe side effects. The aim of this work was to test whether AZT causes oxidative damage to heart mitochondria and whether this can be prevented by supranutritional doses of antioxidant vitamins. An experimental animal model was used in which mice were treated with AZT for 35 days (10 mg/kg/day) in drinking water. Animals treated with antioxidant vitamins were fed the same diet as controls but supplemented with vitamins C (ascorbic acid, 10 g/ kg diet) and E (α-dl-tocopherol, 0.6 g/kg diet) for 65 days before s…

MaleMitochondrial Diseasesmedicine.medical_treatmentAscorbic AcidOxidative phosphorylationMitochondrionPharmacologyBiologymedicine.disease_causeDNA MitochondrialMitochondria HeartGeneral Biochemistry Genetics and Molecular BiologyLipid peroxidationMiceZidovudinechemistry.chemical_compoundmedicineAnimalsVitamin Eheterocyclic compoundsGeneral Pharmacology Toxicology and PharmaceuticsVitamin CVitamin EDeoxyguanosineGeneral MedicineAscorbic acidGlutathioneBiochemistrychemistry8-Hydroxy-2'-DeoxyguanosineLipid PeroxidationZidovudineOxidative stressmedicine.drugLife Sciences
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The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase

2003

The mammalian soluble epoxide hydrolase (sEH) is an enzyme with multiple functions, being implicated in detoxification of xenobiotic epoxides as well as in regulation of physiological processes such as blood pressure. The enzyme is a homodimer, in which each subunit is composed of two domains. The 35-kDa C-terminal domain has an α/β hydrolase fold and harbors the catalytic center for the EH activity. The 25-kDa N-terminal domain has a different α/β fold and belongs to the haloacid dehalogenase superfamily of enzymes. The catalytic properties of the enzyme reported so far can all be explained by the action of the C-terminal domain alone. The function of the N-terminal domain, other than in …

MaleModels MolecularEpoxide hydrolase 2HydrolasesStereochemistryProtein subunitMolecular Sequence DataPhosphatase10050 Institute of Pharmacology and Toxicology610 Medicine & healthDephosphorylationHydrolaseAnimalsHumansAmino Acid SequenceDNA PrimersEpoxide Hydrolaseschemistry.chemical_classification1000 MultidisciplinaryMultidisciplinaryBase SequenceSequence Homology Amino AcidbiologyChemistryActive siteBiological SciencesPhosphoric Monoester HydrolasesRats Inbred F344Recombinant ProteinsRatsAmino acidEnzymeSolubilityBiochemistryMutagenesis Site-Directedbiology.protein570 Life sciences; biologyProceedings of the National Academy of Sciences
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