Search results for "Cell Movement"

showing 10 items of 396 documents

The impact of conventional and heavy ion irradiation on tumor cell migration in vitro.

2007

The influence of X-ray and (12)C heavy ion irradiation on tumor cell migration and of beta(3) and beta(1) integrin expression was investigated.Two different tumor cell lines (U87 glioma and HCT116 colon carcinoma cells) were irradiated with 1, 3, or 10 Gy X-rays or (12)C heavy ions. 24 h after irradiation a standardized Boyden Chamber assay for migration analysis was performed and cells were lysed for Western blotting.Radiation-induced influences were cell line- and radiation type-dependent. X-rays decreased HCT116 migration at higher doses and appear to increase U87 migration after 3 Gy. Heavy ions decreased migration of both cell lines dose-dependently. A trend of increased beta(3) and be…

LysisHeavy Ion RadiotherapyCell MovementGliomaCell Line TumorNeoplasmsmedicineTumor Cell MigrationHumansRadiology Nuclear Medicine and imagingIrradiationNeoplasm MetastasisneoplasmsRadiological and Ultrasound TechnologyChemistryIntegrin beta1RadiochemistryIntegrin beta3Dose-Response Relationship RadiationGliomaHeavy Ion Radiotherapymedicine.diseaseMolecular biologyIn vitroDose–response relationshipCell cultureColonic NeoplasmsInternational journal of radiation biology
researchProduct

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
researchProduct

IAPs and cell migration.

2015

Inhibitors of apoptosis (IAPs) constitute a family of cell signaling regulators controlling several fundamental biological processes such as innate immunity, inflammation, cell death, cell proliferation, and cell differentiation. Increasing evidence from in vivo and in vitro studies indicate a function for IAPs in the modulation of invasive and migratory properties of cells. Here, we present and discuss the mechanisms whereby IAPs can control cell migration.

MAPK/ERK pathwayCell signalingProgrammed cell deathInnate immune systemCell growthCellular differentiationCell migrationCell BiologyBiologyCell biologyInhibitor of Apoptosis Proteinsbody regionsApoptosisCell MovementCancer researchCell AdhesionAnimalsHumansCytoskeletonDevelopmental BiologySignal TransductionSeminars in celldevelopmental biology
researchProduct

The Late Endosomal Adaptor Molecule p14 (LAMTOR2) Regulates TGFβ1-Mediated Homeostasis of Langerhans Cells

2014

Langerhans cells (LCs), a sub-population of dendritic cells (DCs) in the skin, participate in the regulation of immunity and peripheral tolerance. The adaptor molecule p14 is part of the late endosomal/lysosomal adaptor and mitogen-activated protein kinase and mammalian target of rapamycin (mTOR) activator/regulator (LAMTOR) complex, which mediates the activation of lysosome-associated extracellular signaling regulated kinase (ERK) and the mTOR cascade. In previous work, we demonstrated that CD11c-specific deficiency of p14 disrupts LC homeostasis by affecting the LAMTOR-mediated ERK and mTOR signaling. In this study, we extended our analysis on p14 deficiency specifically in LCs. Langerin-…

MAPK/ERK pathwayMaleMAP Kinase Signaling SystemReceptor Transforming Growth Factor-beta Type IDown-Regulationchemical and pharmacologic phenomenaEndosomesDermatologyBiologyProtein Serine-Threonine KinasesDermatitis ContactBiochemistryArticleImmune toleranceImmunophenotypingTransforming Growth Factor beta103 medical and health sciences0302 clinical medicineDownregulation and upregulationCell MovementImmune ToleranceAnimalsHomeostasisProtein kinase AMolecular BiologyPI3K/AKT/mTOR pathway030304 developmental biologySkin0303 health sciencesintegumentary systemKinaseReceptor Transforming Growth Factor-beta Type IIPeripheral toleranceProteinshemic and immune systemsCell BiologyMice Mutant StrainsCell biologyCD11c AntigenLangerhans CellsFemaleReceptors Transforming Growth Factor beta030215 immunologyTransforming growth factorJournal of Investigative Dermatology
researchProduct

Erythropoietin activates cell survival pathways in breast cancer stem-like cells to protect them from chemotherapy

2013

Abstract Recombinant erythropoietin (EPO) analogs [erythropoiesis-stimulating agents (ESA)] are clinically used to treat anemia in patients with cancer receiving chemotherapy. After clinical trials reporting increased adverse events and/or reduced survival in ESA-treated patients, concerns have been raised about the potential role of ESAs in promoting tumor progression, possibly through tumor cell stimulation. However, evidence is lacking on the ability of EPO to directly affect cancer stem–like cells, which are thought to be responsible for tumor progression and relapse. We found that breast cancer stem–like cells (BCSC) isolated from patient tumors express the EPO receptor and respond to …

MAPK/ERK pathwayOncologyCancer Researchmedicine.medical_treatmentFluorescent Antibody TechniqueApoptosisMice SCIDImmunoenzyme TechniquesMiceCell MovementMice Inbred NODhemic and lymphatic diseasesTumor Cells CulturedCulturedBlottingAnemiaFlow CytometryTumor CellsTRIALSOncologyDisease ProgressionNeoplastic Stem CellsFemaleWesternSignal Transductionmedicine.drugSTIMULATING AGENTSEXPRESSIONmedicine.medical_specialtyBlotting WesternAntineoplastic AgentsBreast NeoplasmsSCIDRECOMBINANT-HUMAN-ERYTHROPOIETIN STIMULATING AGENTS EXPRESSION MORTALITY TRIALS ANEMIA ALPHA ALDH1Breast cancerIn vivoInternal medicinemedicineAnimalsHumansBreast cancer Cancer stem cellsALDH1ErythropoietinProtein kinase BCell ProliferationSettore MED/04 - Patologia GeneraleChemotherapybusiness.industryMORTALITYCancerRECOMBINANT-HUMAN-ERYTHROPOIETINmedicine.diseaseALPHAErythropoietinTumor progressionInbred NODAnemia; Animals; Antineoplastic Agents; Apoptosis; Blotting Western; Breast Neoplasms; Cell Movement; Cell Proliferation; Disease Progression; Erythropoietin; Female; Flow Cytometry; Fluorescent Antibody Technique; Humans; Immunoenzyme Techniques; Mice; Mice Inbred NOD; Mice SCID; Neoplastic Stem Cells; Signal Transduction; Tumor Cells Cultured; Cancer Research; Oncologybusiness
researchProduct

Dimerization of the kinase ARAF promotes MAPK pathway activation and cell migration.

2014

The RAF family of kinases mediates RAS signaling, and RAF inhibitors can be effective for treating tumors with BRAF V600E mutant protein. However, RAF inhibitors paradoxically accelerate metastasis in RAS -mutant tumors and become ineffective in BRAF V600E tumors because of reactivation of downstream mitogen-activated protein kinase (MAPK) signaling. We found that the RAF isoform ARAF has an obligatory role in promoting MAPK activity and cell migration in a cell type–dependent manner. Knocking down ARAF prevented the activation of MAPK kinase 1 (MEK1) and extracellular signal–regulated kinase 1 and 2 (ERK1/2) and decreased the number of protrusions from tumor cell spheroids in three-dimensi…

MAPK/ERK pathwayScaffold proteinModels MolecularNiacinamideProto-Oncogene Proteins B-rafMAP Kinase Signaling SystemBlotting WesternMAP Kinase Kinase 1MAPK cascadeBiologyKSR1BiochemistryBinding CompetitiveProto-Oncogene Proteins A-rafTime-Lapse ImagingMutant proteinCell MovementTumor Cells CulturedHumansNeoplasm InvasivenessRNA Small InterferingProtein kinase AMolecular BiologyAnalysis of VarianceKinasePhenylurea CompoundsCell BiologySorafenibCell biologyEnzyme ActivationProto-Oncogene Proteins c-rafHEK293 CellsIndenesGene Knockdown TechniquesCancer researchPyrazolesElectrophoresis Polyacrylamide GelARAFDimerizationScience signaling
researchProduct

3-Deazaneplanocin A (DZNep), an Inhibitor of the Histone Methyltransferase EZH2, Induces Apoptosis and Reduces Cell Migration in Chondrosarcoma Cells

2014

Objective Growing evidences indicate that the histone methyltransferase EZH2 (enhancer of zeste homolog 2) may be an appropriate therapeutic target in some tumors. Indeed, a high expression of EZH2 is correlated with poor prognosis and metastasis in many cancers. In addition, 3-Deazaneplanocin A (DZNep), an S-adenosyl-L homocysteine hydrolase inhibitor which induces EZH2 protein depletion, leads to cell death in several cancers and tumors. The aim of this study was to determine whether an epigenetic therapy targeting EZH2 with DZNep may be also efficient to treat chondrosarcomas. Methods EZH2 expression was determined by immunohistochemistry and western-blot. Chondrosarcoma cell line CH2879…

MESH: Cell DeathAdenosine[SDV]Life Sciences [q-bio]Cancer Treatmentlcsh:MedicineMESH: Flow CytometryApoptosischemistry.chemical_compoundSpectrum Analysis Techniques0302 clinical medicineCell MovementMolecular Cell BiologyMedicine and Health Sciences3-Deazaneplanocin AMESH: Epigenesis GeneticEnzyme Inhibitorslcsh:Science0303 health sciencesMultidisciplinaryCell DeathbiologyReverse Transcriptase Polymerase Chain ReactionEZH2Polycomb Repressive Complex 2DrugsCell migrationMESH: ChondrosarcomaFlow Cytometry3. Good healthHistone[SDV.MHEP.RSOA]Life Sciences [q-bio]/Human health and pathology/Rhumatology and musculoskeletal systemOncologyConnective TissueCell ProcessesSpectrophotometry030220 oncology & carcinogenesisHistone methyltransferaseHistone MethyltransferasesMESH: 3-deazaneplanocinCytophotometryAnatomyMESH: Polycomb Repressive Complex 2Epigenetic therapyMESH: Histone methyltransferaseResearch ArticleProgrammed cell deathHistologyChondrosarcoma[SDV.CAN]Life Sciences [q-bio]/Cancer[SDV.BC]Life Sciences [q-bio]/Cellular Biologymacromolecular substancesResearch and Analysis MethodsCell GrowthEpigenetic Therapy03 medical and health sciencesRheumatologyCell Line TumorMESH: Blotting WesternHumans[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyEZH2Tumors030304 developmental biologyMESH: Apoptosislcsh:RMESH: Histone-Lysine N-MethyltransferaseBiology and Life SciencesMESH: ImmunohistochemistryHistone-Lysine N-MethyltransferaseCell BiologyBiological TissueCartilageHistone methyltransferasechemistryApoptosisbiology.proteinCancer researchMESH: EZH2 protein humanlcsh:QCytometry
researchProduct

IL-33/ST2 pathway regulates neutrophil migration and predicts outcome in patients with severe alcoholic hepatitis.

2020

Background & Aims Severe alcoholic hepatitis (SAH) is associated with a high risk of infection. The IL-33/ST2 pathway is involved in sepsis control but data regarding its role in alcohol-related liver disease (ALD) are lacking. We aimed to characterize the role of IL-33/ST2 in the polymorphonuclear neutrophils (PMNs) of patients with ALD and SAH. Methods Serum and circulating neutrophils were collected from patients with SAH, alcoholic cirrhosis and healthy controls. We quantified IL-33/ST2 pathway activity and CXCR2 at baseline and after exposure to IL-33. We also determined the migration capacity of PMNs. Results The decoy receptor of IL-33 (soluble ST2 [sST2]) was increased in SAH vs. ci…

Male0301 basic medicineAlcoholic liver diseaseCirrhosisPolymorphonuclear neutrophilsNeutrophils[SDV.MHEP.PHY] Life Sciences [q-bio]/Human health and pathology/Tissues and Organs [q-bio.TO]ApoptosisGastroenterologyReceptors Interleukin-8BLiver disease0302 clinical medicineCell MovementLiver Cirrhosis AlcoholicProspective StudiesCXC chemokine receptorsReceptorCells CulturedMigrationMiddle AgedPrognosisRecombinant Proteins3. Good healthCirrhosisAlcoholic hepatitis;Cirrhosis;Infection;Interleukin-33;Migration;Polymorphonuclear neutrophilsFemale030211 gastroenterology & hepatologyAlcoholic hepatitisInfectionSignal TransductionAdultmedicine.medical_specialtyAlcoholic hepatitisSepsis03 medical and health sciencesInternal medicinemedicine[SDV.MHEP.PHY]Life Sciences [q-bio]/Human health and pathology/Tissues and Organs [q-bio.TO]Humanscardiovascular diseasesAgedHepatologyHepatitis Alcoholicbusiness.industrymedicine.diseaseInterleukin-33Interleukin-1 Receptor-Like 1 Proteinnervous system diseasesInterleukin 33030104 developmental biologyCase-Control StudiesbusinessFollow-Up Studies
researchProduct

Elevated levels of 2-arachidonoylglycerol promote atherogenesis in ApoE-/- mice.

2018

Background The endocannabinoid (eCB) 2-arachidonoylglycerol (2-AG) is a known modulator of inflammation and ligand to both, pro-inflammatory cannabinoid receptor 1 (CB1) and anti-inflammatory CB2. While the role of both receptors in atherogenesis has been studied extensively, the significance of 2-AG for atherogenesis is less well characterized. Methods The impact of 2-AG on atherogenesis was studied in two treatment groups of ApoE-/- mice. One group received the monoacylglycerol lipase (MAGL)-inhibitor JZL184 [5 mg/kg i.p.], which impairs 2-AG degradation and thus causes elevated 2-AG levels, the other group received vehicle for four weeks. Simultaneously, both groups were fed a high-chole…

Male0301 basic medicineCCR1Chemokinelcsh:MedicineSmooth Muscle Cells030204 cardiovascular system & hematologyPathology and Laboratory MedicineBiochemistryMonocytesWhite Blood CellsMicechemistry.chemical_compoundChemokine receptorSpectrum Analysis Techniques0302 clinical medicinePiperidinesAnimal CellsCell MovementMedicine and Health SciencesReceptorlcsh:ScienceImmune ResponseJZL184MultidisciplinarybiologyNeurochemistryFlow CytometryLipidsCholesterolSpectrophotometryCytophotometryCellular TypesNeurochemicalsAnatomymedicine.symptomResearch Articlemedicine.medical_specialtyImmune CellsImmunologyMuscle TissueAntigens Differentiation MyelomonocyticInflammationArachidonic AcidsResearch and Analysis MethodsDiet High-FatCell LineGlycerides03 medical and health sciencesSigns and SymptomsApolipoproteins EDiagnostic MedicineAntigens CDInternal medicinemedicineAnimalsOil Red OBenzodioxolesInflammationMuscle CellsBlood CellsMacrophageslcsh:RBiology and Life SciencesCell BiologyAtherosclerosisMonoacylglycerol lipaseBiological Tissue030104 developmental biologyEndocrinologychemistrybiology.proteinlcsh:QEndocannabinoidsNeurosciencePLoS ONE
researchProduct

β1 integrin signaling promotes neuronal migration along vascular scaffolds in the post-stroke brain

2017

Cerebral ischemic stroke is a main cause of chronic disability. However, there is currently no effective treatment to promote recovery from stroke-induced neurological symptoms. Recent studies suggest that after stroke, immature neurons, referred to as neuroblasts, generated in a neurogenic niche, the ventricular-subventricular zone, migrate toward the injured area, where they differentiate into mature neurons. Interventions that increase the number of neuroblasts distributed at and around the lesion facilitate neuronal repair in rodent models for ischemic stroke, suggesting that promoting neuroblast migration in the post-stroke brain could improve efficient neuronal regeneration. To move t…

Male0301 basic medicineChain migrationlcsh:MedicineExtracellular matrixNeural Stem CellsCell MovementLamininCells CulturedMice KnockoutNeuronslcsh:R5-920Mice Inbred ICRMicroscopy ConfocalTissue ScaffoldsbiologyIntegrin beta1BrainCell migrationGeneral MedicineCell biologyStrokeVasculature-guided migrationFemaleBlood vesselmedicine.symptomlcsh:Medicine (General)Signal TransductionResearch Paperanimal structuresIntegrinMice TransgenicGeneral Biochemistry Genetics and Molecular BiologyLesion03 medical and health sciencesNeuroblastβ1 integrinNeuroblast migrationmedicineAnimalsRegeneration (biology)lcsh:RCoculture TechniquesMicroscopy Electron030104 developmental biologynervous systemAstrocytesImmunologybiology.proteinBlood VesselsLamininEBioMedicine
researchProduct