Search results for "Intracellular"

showing 10 items of 821 documents

Can PBDEs affect the pathophysiologic complex of epithelium in lung diseases?

2020

Brominated flame-retardant (BFRs) exposure promotes multiple adverse health outcomes involved in oxidative stress, inflammation, and tissues damage. We investigated BFR effects, known as polybrominated diphenyl ethers (PBDEs) (47, 99 and 209) in an air-liquid-interface (ALI) airway tissue derived from A549 cell line, and compared with ALI culture of primary human bronchial epithelial cells (pHBEC). The cells, exposed to PBDEs (47, 99 and 209) (0.01-1 mu M) for 24 h, were studied for IL-8, Muc5AC and Muc5B (mRNAs and proteins) production, as well as NOX-4 (mRNA) expression. Furthermore, we evaluated tight junction (TJ) integrity by Trans-Epithelial Electrical Resistance (TEER) measurements, …

Lung DiseasesHealth Toxicology and Mutagenesis0208 environmental biotechnology02 engineering and technology010501 environmental sciencesMucin 5ACBROMINATED FLAME RETARDANTSmedicine.disease_cause01 natural sciencesPolybrominated diphenyl ethersPARTICULATE MATTERElectric ImpedanceHalogenated Diphenyl EthersFlame RetardantsInhalationTight junctionAIRWAY MUCUSChemistryGeneral Medicinerespiratory systemPollutionMucin-5BINTRACELLULAR GLUTATHIONEPolybrominated diphenyl ethers; Inflammation; Oxidative stress; Mucins; Epithelial barrier integrity; Rheological propertiesmedicine.anatomical_structureNADPH Oxidase 4medicine.symptomEnvironmental EngineeringInflammationBronchiEXPOSURE SYSTEMTight JunctionsAndrologymedicineEnvironmental ChemistryHumansRheological propertiesPolybrominated diphenyl ether0105 earth and related environmental sciencesAgedInflammationEpithelial barrier integrityPOLYBROMINATED DIPHENYL ETHERSMucinInterleukin-8MucinsPublic Health Environmental and Occupational HealthEpithelial CellsGeneral ChemistryN-ACETYLCYSTEINEEpithelium020801 environmental engineeringrespiratory tract diseasesOxidative StressA549 CellsMucinEX-VIVO MODELOxidative streRespiratory epitheliumAEROSOL-PARTICLESOxidative stressChemosphere
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Synthetic (glyco-)peptides of the homophilic recognition domain of E-cadherin lead to increased E-cadherin mRNA synthesis and are inductors of cell d…

2010

E-cadherin is one of the critical molecules involved in the metastatic process in many types of cancer. Once combined, E-cadherin exceeds the amount of membranous E-cadherin on the cellular surface by activation of intracellular signaling cascades. Studies on transformed keratinocytes of the HaCat cell line showed induction of differentiation by synthetical partial structures of the homophilic binding region of E-cadherin. The knowledge of effects in lung cancer cells is sparse. Therefore, the effects in primary lung cancer cell lines were investigated. Four primary lung cancer cell lines were incubated for 3, 6, 12, 15, 18, and 24h with synthetic partial structures (peptide and glycopeptid…

Lung NeoplasmsCell SurvivalCellular differentiationCellBiologyPathology and Forensic Medicinechemistry.chemical_compoundCell Line TumorExtracellularmedicineHumansRNA MessengerReverse Transcriptase Polymerase Chain ReactionCadherinGlycopeptidesCell DifferentiationSodium butyrateCell BiologyCadherinsImmunohistochemistryMolecular biologyProtein Structure TertiaryCell biologymedicine.anatomical_structurechemistryTumor progressionCell cultureIntracellularPathology - Research and Practice
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pp32/PHAPI determines the apoptosis response of non-small-cell lung cancer

2007

During malignant transformation, cancer cells have to evade cell-intrinsic tumor suppressor mechanisms including apoptosis, thus acquiring a phenotype that is relatively resistant to clinically applied anticancer therapies. Molecular characterization of apoptotic signal transduction defects may help to identify prognostic markers and to develop novel therapeutic strategies. To this end we have undertaken functional analyses of drug-induced apoptosis in human non-small cell-lung cancer (NSCLC) cells. We found that primary drug resistance correlated with defects in apoptosome-dependent caspase activation in vitro. While cytochrome c-induced apoptosome formation was maintained, the subsequent …

Lung NeoplasmsTransplantation HeterologousAntineoplastic AgentsApoptosisMice SCIDBiologyMalignant transformationMiceProstate cancerIn vivoCarcinoma Non-Small-Cell LungmedicineAnimalsHumansLung cancerMolecular BiologyIntracellular Signaling Peptides and ProteinsNuclear ProteinsRNA-Binding ProteinsCancerCell Biologymedicine.diseaseCell biologyEnzyme ActivationApoptosisCaspasesCancer cellCancer researchSignal transductionNeoplasm TransplantationCell Death & Differentiation
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Metabolic fluxes and l-lysine synthesis by Corynebacterium glutamicum in relation to cellular total reducing activity

2001

Abstract The total reducing activity (TRA) of cells was used to estimate the physiological activity of Corynebacterium glutamicum under conditions of l -lysine synthesis. This was estimated as the rate of reduction of 2,3,5- triphenyltetrazolium chloride by intact cells. TRA of cells was linearly correlated with the intracellular concentrations of RNA and the bacterial growth rate. It was concluded that this activity reflected the rate of energy generation in cells. A decrease in TRA of growing cells was related to an increase in bacterial lysine synthesis activity. Alteration in metabolic pathway functioning and an increase in the intracellular concentrations of lysine precursors favoured …

LysineRNABioengineeringBacterial growthBiologycomplex mixturesApplied Microbiology and BiotechnologyBiochemistryCorynebacterium glutamicumMetabolic pathwayBiochemistrybacteriaLysine synthesisreproductive and urinary physiologyIntracellularTriphenyltetrazolium chlorideProcess Biochemistry
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The synthesis of SNAT2 transporters is required for the hypertonic stimulation of system A transport activity

2004

AbstractIn cultured human fibroblasts incubated under hypertonic conditions, the stimulation of system A for neutral amino acid transport, associated to the increased expression of the mRNA for SNAT2 transporter, leads to an expanded intracellular amino acid pool and to the recovery of cell volume. A protein of nearly 60 kDa, recognized by an antiserum against SNAT2, is increased both in the pool of biotinylated membrane proteins and in the total cell lysate of hypertonically stressed cells. The increased level of SNAT2 transporters in hypertonically stressed cells is confirmed by immunocytochemistry. DRB, an inhibitor of transcription, substantially inhibits the increase of SNAT2 proteins …

LysisAmino Acid Transport System AProlineTranscription GeneticGlutamineBlotting WesternHypertonic SolutionsBiophysicsStimulationBiologyHuman fibroblastBiochemistrySubstrate SpecificityAmino acid starvationHypertonic stressCell volumeNeutral amino acid transportHumansBiotinylationRNA MessengerCells CulturedCell Sizechemistry.chemical_classificationRadioisotopesCell MembraneBiological TransportPhosphorusCell BiologyFibroblastsImmunohistochemistryAmino acidGlutamineMolecular WeightKineticschemistryBiochemistryMembrane proteinHypertonic StressIntracellularDichlororibofuranosylbenzimidazoleBiochimica et Biophysica Acta (BBA) - Biomembranes
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Differences in the signaling pathways of α(1A)- and α(1B)-adrenoceptors are related to different endosomal targeting.

2013

AIMS: To compare the constitutive and agonist-dependent endosomal trafficking of α(1A)- and α(1B)-adrenoceptors (ARs) and to establish if the internalization pattern determines the signaling pathways of each subtype. METHODS: Using CypHer5 technology and VSV-G epitope tagged α(1A)- and α(1B)-ARs stably and transiently expressed in HEK 293 cells, we analyzed by confocal microscopy the constitutive and agonist-induced internalization of each subtype, and the temporal relationship between agonist induced internalization and the increase in intracellular calcium (determined by FLUO-3 flouorescence), or the phosphorylation of ERK1/2 and p38 MAP kinases (determined by Western blot). RESULTS AND C…

MAPK signaling cascadesEndosomemedia_common.quotation_subjecteducationIntracellular Spacelcsh:MedicineEndosomesSignal transductionERK signaling cascadeBiologyEndocytosisp38 Mitogen-Activated Protein KinasesSignaling PathwaysCell LineMolecular cell biologyReceptors Adrenergic alpha-1Calcium-Mediated Signal TransductionHumansMembrane Receptor SignalingCalcium SignalingInternalizationlcsh:ScienceBiologyCalcium signalingmedia_commonMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3MultidisciplinaryHEK 293 cellslcsh:RNeurotransmitter Receptor SignalingSignaling cascadesNeurotransmittersLipid signalingEndocytosisCell biologyTransport proteinProtein TransportHEK293 CellsCalcium signaling cascadeMembranes and Sortinglcsh:QAdrenergic alpha-1 Receptor AgonistsMolecular NeuroscienceSignal transductionResearch ArticleAdrenergic Signal TransductionNeurosciencePLoS ONE
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Three-dimensional invasion of human glioblastoma cells remains unchanged by X-ray and carbon ion irradiation in vitro.

2012

Purpose Cell invasion represents one of the major determinants that treatment has failed for patients suffering from glioblastoma. Contrary findings have been reported for cell migration upon exposure to ionizing radiation. Here, the migration and invasion capability of glioblastoma cells on and in collagen type I were evaluated upon irradiation with X-rays or carbon ions. Methods and Materials Migration on and invasion in collagen type I were evaluated in four established human glioblastoma cell lines exposed to either X-rays or carbon ions. Furthermore, clonogenic radiation survival, proliferation (5-bromo-2-deoxyuridine positivity), DNA double-strand breaks (γH2AX/53BP1-positive foci), a…

MAPK/ERK pathwayCancer ResearchCell signalingMMP2MAP Kinase Kinase 4p38 Mitogen-Activated Protein KinasesCollagen Type IExtracellular matrixHistonesPhosphatidylinositol 3-KinasesCell MovementMedicineHumansRadiology Nuclear Medicine and imagingDNA Breaks Double-StrandedNeoplasm InvasivenessClonogenic assayPI3K/AKT/mTOR pathwayCell ProliferationRadiationbusiness.industryCell growthBrain NeoplasmsIntegrin beta1Intracellular Signaling Peptides and ProteinsCell migrationCarbonOncologyBromodeoxyuridineImmunologyCancer researchbusinessCell Migration AssaysGlioblastomaTumor Suppressor p53-Binding Protein 1International journal of radiation oncology, biology, physics
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Activity-dependent survival of developing neocortical neurons depends on PI3K signalling

2011

J. Neurochem. (2012) 120, 495–501. Abstract Spontaneous electrical network activity plays a major role in the control of cell survival in the developing brain. Several intracellular pathways are implicated in transducing electrical activity into gene expression dependent and independent survival signals. These include activation of phosphatidylinositol 3-kinase (PI3K) and its downstream effector Akt, activation of Ras and subsequently MAPK/extracellular signal-regulated kinase (MEK) and extracellular signal-regulated kinase and signalling via calcium/calmodulin-dependent protein kinase (CaMK). In the present study, we analyzed the role of these pathways for the control of neuronal survival …

MAPK/ERK pathwayCellular and Molecular NeuroscienceKinaseExtracellularBiologyProtein kinase ABiochemistryProtein kinase BCAMKPI3K/AKT/mTOR pathwayIntracellularCell biologyJournal of Neurochemistry
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Dissecting the different biological effects of oncogenic Ras isoforms in cancer cell lines: Could stimulation of oxidative stress be the one more wea…

2012

Abstract Ras proteins are small GTPase functioning as molecular switches that, in response to particular extracellular signalling, as growth factors, activate a diverse array of intracellular effector cascades regulating cell proliferation, differentiation and apoptosis. Human tumours frequently express Ras proteins (Ha-, Ki-, N-Ras) activated by point mutations which contribute to malignant phenotype, including invasiveness and angiogenesis. Despite the common signalling pathways leading to similar cellular responses, studies clearly demonstrate unique roles of the Ras family members in normal and pathological conditions and the lack of functional redundancy seems to be explainable, at lea…

MAPK/ERK pathwayEffectorAnti-apoptotic Ras signalling cascadeCancer cellmedicineSmall GTPaseGeneral MedicineBiologyCell adhesionmedicine.disease_causeOxidative stressIntracellularCell biologyMedical Hypotheses
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p42 MAPK phosphorylates 80 kDa MARCKS at Ser-113.

1996

Abstract It is demonstrated here that p42 MAPKinase (p42 MAPK) phosphorylates the M yristoylated A lanine- R ich C - K inase S ubstrate (MARCKS) at Ser-113. In permeabilised Swiss 3T3 cells activation of protein kinase C (PKC) leads to p42 MAPK activation, but only the protein kinase C sites in MARCKS become phosphorylated and not Ser-113. The mitogen platelet-derived growth factor (PDGF) elicits the same response. These results demonstrate that while Ser-113 is a substrate for p42 MAPK in vitro and can be phosphorylated in vivo as shown by Taniguchi et al. [(1994) J. Biol. Chem. 269, 18299–18302], its phosphorylation is not subject to acute regulation by p42 MAPK in Swiss 3T3 cells.

MAPK/ERK pathwayMARCKSmedicine.medical_treatmentMitogen-activated protein kinase kinaseBiochemistryenvironment and public healthSubstrate SpecificityMiceStructural BiologySerinep42MAPKinasePhosphorylationMyristoylated Alanine-Rich C Kinase SubstrateCells CulturedProtein Kinase CMitogen-Activated Protein Kinase 1Platelet-Derived Growth FactorbiologyChemistryIntracellular Signaling Peptides and Proteins3T3 CellsProtein-Tyrosine KinasesCell biologyBiochemistryMitogen-activated protein kinasePhosphorylationTetradecanoylphorbol Acetatebiological phenomena cell phenomena and immunityPlatelet-derived growth factor receptorhormones hormone substitutes and hormone antagonistsendocrine systemRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsGeneticsmedicineAnimalsAmino Acid SequenceMARCKSMolecular BiologyProtein kinase CGrowth factorMembrane ProteinsProteinsCell BiologyPeptide FragmentsEnzyme ActivationMolecular Weightenzymes and coenzymes (carbohydrates)Calcium-Calmodulin-Dependent Protein Kinasesbiology.proteinMutagenesis Site-DirectedMitogensFEBS letters
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