Search results for "3T"

showing 10 items of 171 documents

Immune Cell Toll-like Receptor 4 Mediates the Development of Obesity- and Endotoxemia-Associated Adipose Tissue Fibrosis

2014

International audience; Adipose tissue fibrosis development blocks adipocyte hypertrophy and favors ectopic lipid accumulation. Here, we show that adipose tissue fibrosis is associated with obesity and insulin resistance in humans and mice. Kinetic studies in C3H mice fed a high-fat diet show activation of macrophages and progression of fibrosis along with adipocyte metabolic dysfunction and death. Adipose tissue fibrosis is attenuated by macrophage depletion. Impairment of Toll-like receptor 4 signaling protects mice from obesity-induced fibrosis. The presence of a functional Toll-like receptor 4 on adipose tissue hematopoietic cells is necessary for the initiation of adipose tissue fibros…

LipopolysaccharidesMESH: Signal TransductionMESH: InflammationMESH : Toll-Like Receptor 4Adipose tissueMESH : AdipocytesMESH : LipopolysaccharidesMicechemistry.chemical_compoundFibrosisAdipocyteAdipocytes[ SDV.IMM ] Life Sciences [q-bio]/ImmunologyMESH: ObesityMESH: Animalslcsh:QH301-705.5Mice Inbred C3HToll-like receptorMESH : Diet High-FatMESH: Toll-Like Receptor 43. Good healthMESH: Insulin ResistanceAdipose TissueMESH: FibrosisMESH : Fibrosis[SDV.IMM]Life Sciences [q-bio]/ImmunologyMESH : ObesityMESH : Insulin ResistanceMESH: Adipose TissueSignal Transductionmedicine.medical_specialty[SDV.IMM] Life Sciences [q-bio]/ImmunologyAdipose tissue macrophagesBiologyDiet High-FatMESH : Adipose TissueGeneral Biochemistry Genetics and Molecular BiologyImmune systemMESH : Mice Inbred C3HInternal medicineMESH : MicemedicineAnimalsHumansObesityMESH: Mice Inbred C3HMESH: MiceMESH: AdipocytesInflammationMESH : Signal TransductionMESH : InflammationMESH: HumansMESH : EndotoxemiaMESH : Humans3T3-L1medicine.diseaseFibrosisMESH : Disease Models AnimalEndotoxemiaToll-Like Receptor 4Disease Models AnimalMESH: Diet High-FatEndocrinologylcsh:Biology (General)chemistryMESH: EndotoxemiaMESH : AnimalsInsulin ResistanceMESH: Disease Models AnimalMESH: LipopolysaccharidesAdipocyte hypertrophyCell Reports
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Cancer-associated fibroblasts do not respond to combined irradiation and kinase inhibitor treatment

2012

The emergence of radioresistance is a significant issue in the treatment of squamous cell carcinoma. We recently demonstrated that post-radiogenic extracellular signal-regulated kinase (ERK) signaling might decrease radiosensitivity in this cancer type. To further elucidate how tumor-organizing cell types respond to irradiation and ERK pathway inhibition, we analyzed one oral squamous cell carcinoma and one lung cancer cell line (HNSCCUM-02T, A549), fibroblasts (NIH3T3), primary normal and cancer-associated fibroblasts (CAFs) in vitro. Irradiated cells treated with mitogen-activated protein kinase (MAPK) inhibitor U0126 were screened for pERK levels. Post-radiogenic cellular responses were …

MAPK/ERK pathwayCancer ResearchLung NeoplasmsCell SurvivalMAP Kinase Signaling SystemBiologyRadiation DosageRadiation ToleranceMiceCarcinoma Non-Small-Cell LungCell Line TumorRadioresistanceNitrilesButadienesmedicineAnimalsHumansExtracellular Signal-Regulated MAP KinasesProtein kinase AFibroblastProtein Kinase InhibitorsTumor Stem Cell AssayCell ProliferationOncogeneKinaseGeneral MedicineFibroblastsCell cycleMolecular biologymedicine.anatomical_structureOncologyCarcinoma Squamous CellNIH 3T3 CellsCancer researchCancer-Associated FibroblastsMouth NeoplasmsOncology Reports
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Regulation of ERK1/2 activity upon contact inhibition in fibroblasts.

2011

Contact inhibition is a crucial mechanism regulating proliferation in vitro and in vivo. Despite its generally accepted importance for maintaining tissue homeostasis knowledge about the underlying molecular mechanisms of contact inhibition is still scarce. Since the MAPK ERK1/2 plays a pivotal role in the control of proliferation, we investigated regulation of ERK1/2 phosphorylation which is downregulated in confluent NIH3T3 cultures. We found a decrease in upstream signaling including phosphorylation of the growth factor receptor adaptor protein ShcA and the MAPK kinase MEK1/2 in confluent compared to exponentially growing cultures whereas involvement of ERK1/2 phosphatases in ERK1/2 inact…

MAPK/ERK pathwayCell signalingBiophysicsDown-RegulationCell CommunicationBiochemistryReceptor Platelet-Derived Growth Factor betaMiceGrowth factor receptorAnimalsReceptors Platelet-Derived Growth FactorPhosphorylationMolecular BiologyTissue homeostasisCell ProliferationMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3biologySignal transducing adaptor proteinContact inhibitionCell BiologyFibroblastsMolecular biologyCell biologyErbB Receptorsbiology.proteinNIH 3T3 CellsPhosphorylationPlatelet-derived growth factor receptorBiochemical and biophysical research communications
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Involvement of the transcription factor FoxM1 in contact inhibition

2012

Contact inhibition is a crucial mechanism regulating proliferation in vitro and in vivo. Although it is generally accepted that contact inhibition plays a pivotal role in maintaining tissue homeostasis, the molecular mechanisms of contact inhibition are still not fully understood. FoxM1 is known as a proliferation-associated transcription factor and is upregulated in many cancer types. Vice versa, anti-proliferative signals, such as TGF-β and differentiation signals decrease FoxM1 expression. Here we investigated the role of FoxM1 in contact inhibition in fibroblasts. We show that protein expression of FoxM1 is severely and rapidly downregulated upon contact inhibition, probably by inhibiti…

MAPK/ERK pathwayCyclin ABiophysicsDown-RegulationCell Cycle ProteinsCyclin AProtein Serine-Threonine KinasesBiochemistryMiceDownregulation and upregulationProto-Oncogene ProteinsAnimalsPhosphorylationRNA Small InterferingExtracellular Signal-Regulated MAP KinasesMolecular BiologyTranscription factorTissue homeostasisbiologyContact InhibitionKinaseForkhead Box Protein M1Contact inhibitionForkhead Transcription FactorsCell BiologyG1 Phase Cell Cycle CheckpointsCell biologyNIH 3T3 Cellsbiology.proteinEctopic expressionBiochemical and Biophysical Research Communications
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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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Disulfide-crosslinked hyaluronan-gelatin hydrogel films: a covalent mimic of the extracellular matrix for in vitro cell growth

2003

A new disulfide crosslinking method was developed for the preparation of blended hyaluronan (HA)-gelatin hydrogels to form a synthetic, covalently linked mimic of the extracellular matrix (ECM). The HA and gelatin were chemically modified using 3,3′-dithiobis(propionic hydrazide) (DTP). After reduction with dithiothreitol (DTT), the thiol derivatives of HA (HA-DTPH) and gelatin (gelatin-DTPH) were obtained and characterized. To minimize interference with biological function, the degree of substitution of HA-DTPH and gelatin-DTPH was kept below 50%. Solutions of HA-DTPH and gelatin-DTPH in varying blends (20%, 40%, 60%, 80% gelatin) were prepared in 1% w/v NaCl and crosslinked by disulfide b…

Magnetic Resonance SpectroscopyTime FactorsBiocompatible MaterialsSodium ChlorideGelatinHydrogel Polyethylene Glycol DimethacrylateDithiothreitolCell growthMicechemistry.chemical_compoundHyaluronic acidDisulfidesHyaluronic Acidchemistry.chemical_classificationMice Inbred BALB CBiomaterialHydrogels3T3 CellsMethylgalactosidesExtracellular MatrixCross-Linking ReagentsMechanics of MaterialsCovalent bondSelf-healing hydrogelsThiolCell DivisionBiotechnologyfood.ingredientMaterials scienceCell SurvivalBiomedical EngineeringBiophysicsHyaluronoglucosaminidaseBioengineeringmacromolecular substancesIn Vitro TechniquesHydrazideBiomaterialsDisulfidefoodPolymer chemistryCell AdhesionAnimalsSulfhydryl Compoundstechnology industry and agricultureFibroblastsBiomaterialDithiothreitolModels ChemicalchemistryCeramics and CompositesGelatinPolystyrenesBiomaterials
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The nucleotide excision repair protein XPC is essential for bulky DNA adducts to promote interleukin-6 expression via the activation of p38-SAPK

2016

Polycyclic aromatic hydrocarbons (PAHs) are environmental pollutants, and many are potent carcinogens. Benzo[a]pyrene (B[a]P), one of the best-studied PAHs, is metabolized ultimately to the genotoxin anti-B[a]P-7,8-dihydrodiol-9,10-epoxide (BPDE). BPDE triggers stress responses linked to gene expression, cell death and survival. So far, the underlying mechanisms that initiate these signal transduction cascades are unknown. Here we show that BPDE-induced DNA damage is recognized by DNA damage sensor proteins to induce activation of the stress-activated protein kinase (SAPK) p38. Surprisingly, the classical DNA damage response, which involves the kinases ATM and ATR, is not involved in p38-SA…

Male0301 basic medicineCancer ResearchDNA RepairCarcinogenesisDNA damagep38 mitogen-activated protein kinases78-Dihydro-78-dihydroxybenzo(a)pyrene 910-oxideBlotting WesternEnzyme-Linked Immunosorbent AssayBiologyReal-Time Polymerase Chain ReactionTransfectionp38 Mitogen-Activated Protein KinasesDNA AdductsMice03 medical and health scienceschemistry.chemical_compoundGeneticsmedicinepolycyclic compoundsAnimalsHumansRNA Small InterferingMolecular BiologyCarcinogenMice KnockoutCisplatinInterleukin-6KinaseFibroblastsCell biologyDNA-Binding ProteinsMice Inbred C57BL030104 developmental biologychemistryCarcinogensNIH 3T3 CellsCancer researchComet AssaySignal transductionDNADNA DamageHeLa CellsMutagensSignal Transductionmedicine.drugNucleotide excision repairOncogene
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The interaction of Fe(III), adriamycin and daunomycin with nucleotides and DNA and their effects on cell growth of fibroblasts (NIH-3T3)

1996

The interactions of the iron complexes of the anthracycline antitumour drugs daunomycin (DN) and adriamycin (ADM) with the mononucleotide AMP, herring sperm DNA, plasmic pBR322 and immortalized 3T3 fibroblasts were studied. By means of Mössbauer spectroscopy it was demonstrated that DNA is a powerful ferric iron chelator as compared with AMP, which is not able to compete with DN or acetohydroxamic acid for ferric iron. The difference between AMP and DNA is postulated to be based on the chelate effect. The Mössbauer spectra of the ternary Fe-anthracycline-DNA systems differ from Fe-anthracycline binary complexes, indicating rearrangement reactions. Dialysis experiments clearly disclose the f…

MaleBase pairStereochemistryIronIntercalation (chemistry)General Biochemistry Genetics and Molecular BiologyBiomaterialsMiceSpectroscopy Mossbauerchemistry.chemical_compoundmedicineAnimalsNucleotideCytotoxicitychemistry.chemical_classificationChemistryCell growthAcetohydroxamic acidDaunorubicinFishesMetals and AlloysBiological Transport3T3 CellsDNASpermatozoaAdenosine MonophosphateDoxorubicinFerricGeneral Agricultural and Biological SciencesCell DivisionDNAPlasmidsmedicine.drugBiometals
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4-Epidoxycycline: an alternative to doxycycline to control gene expression in conditional mouse models

2004

Since the pioneering work by Gossen and Bujard in 1992 demonstrating the usefulness of the Escherichia coli derived tet resistance operon for regulating gene expression a large collection of doxycycline-controlled transgenic mice has been established. Gene switching in eukaryotic tissue culture cells or mice requires administration of tetracycline, anhydrotetracycline or doxycycline to efficiently inactivate the transactivator protein tTA (TET-OFF system) or alternatively to activate the reverse transactivator protein rtTA (TET-ON system). However, the antibiotic activity of doxycycline can create an imbalance of the intestinal flora, resulting in diarrhoea and in a smaller number of animal…

MaleGenetically modified mouseReceptor ErbB-2TransgeneBiophysicsAdministration OralMice NudeAntineoplastic AgentsBreast NeoplasmsMice TransgenicBiologyPharmacologyBiochemistryMiceTransactivationCell Line TumorGene expressionmedicineAnimalsMolecular BiologyDoxycyclineRegulation of gene expressionDose-Response Relationship DrugOncogeneStereoisomerismCell BiologyRatsGene Expression Regulation NeoplasticDisease Models AnimalTreatment OutcomeTetracyclinesCell cultureDoxycyclineImmunologyNIH 3T3 Cellsmedicine.drugBiochemical and Biophysical Research Communications
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Cancer cells induce immune escape via glycocalyx changes controlled by the telomeric protein TRF2

2019

International audience; Myeloid-derived suppressor cells (MDSCs) are immature myeloid cells with strong immunosuppressive activity that promote tumor growth. In this study, we describe a mechanism by which cancer cells control MDSCs in human cancers by upregulating TRF2, a protein required for telomere stability. Specifically, we showed that the TRF2 upregulation in cancer cells has extratelomeric roles in activating the expression of a network of genes involved in the biosynthesis of heparan sulfate proteoglycan, leading to profound changes in glycocalyx length and stiffness, as revealed by atomic force microscopy. This TRF2-dependent regulation facilitated the recruitment of MDSCs, their …

MaleHSPG;immunosurveillance;MDSC;NK cells;TRF2Mice NudeBiologyGlycocalyxGeneral Biochemistry Genetics and Molecular BiologyMetastasisGlycocalyx03 medical and health sciencesMice0302 clinical medicineDownregulation and upregulationNeoplasmsmedicineAnimalsHumansTelomeric Repeat Binding Protein 2STAT3Molecular BiologyCells Cultured030304 developmental biology0303 health sciencesGeneral Immunology and MicrobiologyGeneral NeuroscienceMyeloid-Derived Suppressor CellsArticlesTelomeremedicine.disease3. Good healthImmunosurveillanceGene Expression Regulation NeoplasticMice Inbred C57BLTLR2HEK293 CellsTumor progressionCancer cellCancer researchbiology.proteinNIH 3T3 Cells[SDV.IMM]Life Sciences [q-bio]/ImmunologyFemaleTumor Escape030217 neurology & neurosurgery
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