Search results for "Gene expression."

showing 10 items of 4076 documents

VEGF receptor signaling links inflammation and tumorigenesis in colitis-associated cancer.

2010

Inflammation drives expression of VEGFR2, which is expressed on and drives growth of tumor cells in colitis-associated cancer.

Vascular Endothelial Growth Factor AColorectal cancerGene Expressionmedicine.disease_causechemistry.chemical_compoundMice0302 clinical medicineImmunology and AllergyDecoy receptorsCells CulturedMice Knockout0303 health sciencesMicroscopy ConfocalReverse Transcriptase Polymerase Chain ReactionDextran Sulfaterespiratory systemColitisImmunohistochemistry3. Good healthUp-RegulationVascular endothelial growth factorVascular endothelial growth factor A030220 oncology & carcinogenesisColonic Neoplasmscardiovascular systemcirculatory and respiratory physiologySignal TransductionSTAT3 Transcription FactorImmunologyBlotting WesternMice TransgenicBiologyArticle03 medical and health sciencesmedicineAnimalsHumans030304 developmental biologyCell ProliferationVascular Endothelial Growth Factor Receptor-1CancerEndothelial CellsKinase insert domain receptorEpithelial CellsCell Biologymedicine.diseaseInflammatory Bowel DiseasesVascular Endothelial Growth Factor Receptor-2Mice Inbred C57BLHIF1AchemistryCancer researchCarcinogenesis030215 immunologyThe Journal of experimental medicine
researchProduct

Extracellular HSP27 mediates angiogenesis through Toll-like receptor 3.

2013

The heat-shock protein 27 (HSP27) is up-regulated in tumor cells and released in their microenvironment. Here, we show that extracellular HSP27 has a proangiogenic effect evidenced on chick chorioallantoic membrane. To explore this effect, we test the recombinant human protein (rhHSP27) at physiopathological doses (0.1-10 μg/ml) onto human microvascular endothelial cells (HMECs) grown as monolayers or spheroids. When added onto HMECs, rhHSP27 dose-dependently accelerates cell migration (with a peak at 5 μg/ml) and favors spheroid sprouting within 12-24 h. rhHSP27 increases VEGF gene transcription and promotes secretion of VEGF-activating VEGF receptor type 2. Increased VEGF transcription is…

Vascular Endothelial Growth Factor AImmunoprecipitationAngiogenesisHSP27 Heat-Shock ProteinsNeovascularization PhysiologicBiochemistry03 medical and health sciences0302 clinical medicineHsp27GeneticsExtracellularAnimalsSecretionReceptorMolecular BiologyCells Cultured030304 developmental biology0303 health sciencesbiologyNF-kappa BEndothelial CellsCell migrationMolecular biologyToll-Like Receptor 3Chorioallantoic membraneGene Expression Regulation030220 oncology & carcinogenesisbiology.proteinCalciumBiotechnologyFASEB journal : official publication of the Federation of American Societies for Experimental Biology
researchProduct

The impact of tumor nitric oxide production on VEGFA expression and tumor growth in a zebrafish rat glioma xenograft model.

2015

International audience; To investigate the effect of nitric oxide on tumor development, we established a rat tumor xenograft model in zebrafish embryos. The injected tumor cells formed masses in which nitric oxide production could be detected by the use of the cell-permeant DAF-FM-DA (diaminofluorophore 4-amino-5-methylamino-2'-7'-difluorofluorescein diacetate) and DAR-4M-AM (diaminorhodamine-4M). This method revealed that nitric oxide production could be co-localized with the tumor xenograft in 46% of the embryos. In 85% of these embryos, tumors were vascularized and blood vessels were observed on day 4 post injection. Furthermore, we demonstrated by qRT-PCR that the transplanted glioma ce…

Vascular Endothelial Growth Factor AMESH: Cyclin D1lcsh:MedicineMESH : Analysis of VarianceMESH: Flow Cytometry[ SDV.IMM.IA ] Life Sciences [q-bio]/Immunology/Adaptive immunologyBenzoates[SDV.IMM.II]Life Sciences [q-bio]/Immunology/Innate immunity[ SDV.CAN ] Life Sciences [q-bio]/CancerMESH: GliomaMESH: Reverse Transcriptase Polymerase Chain ReactionCyclin D1MESH: Animalslcsh:ScienceZebrafishMESH : RatsReverse Transcriptase Polymerase Chain ReactionMESH: Real-Time Polymerase Chain ReactionHistological TechniquesMESH : Reverse Transcriptase Polymerase Chain ReactionImidazolesGliomaMESH: Gene Expression Regulation NeoplasticFlow CytometryMESH : Cyclin D1Gene Expression Regulation NeoplasticMESH : Nitric Oxide[SDV.IMM.IA]Life Sciences [q-bio]/Immunology/Adaptive immunologyMESH : Vascular Endothelial Growth Factor AHeterograftsMESH : Histological TechniquesMESH: ImidazolesResearch ArticleMESH : BenzoatesMESH: RatsMESH : Flow CytometryMESH : Gene Expression Regulation NeoplasticMESH : Real-Time Polymerase Chain ReactionMESH : Zebrafish[SDV.CAN]Life Sciences [q-bio]/CancerMESH: Histological TechniquesMESH : HeterograftsNitric OxideReal-Time Polymerase Chain ReactionMESH : ImidazolesMESH: Analysis of VarianceAnimalsMESH: Zebrafish[ SDV.IMM.II ] Life Sciences [q-bio]/Immunology/Innate immunityAnalysis of VarianceMESH: Vascular Endothelial Growth Factor Alcsh:RMESH: BenzoatesRatsMESH : GliomaMESH: Nitric Oxidelcsh:QMESH: HeterograftsMESH : Animals
researchProduct

Hypoxia-stimulated expression of angiogenic growth factors in cervical cancer cells and cervical cancer-derived fibroblasts

2001

It is generally accepted that local growth of solid tumors and their ability to establish distant metastases are dependent on the formation of new blood vessels arising from preexisting ones (angiogenesis). The angiogenic response of the host is mediated by angiogenic molecules that are released from cancer and normal stroma cells, especially fibroblasts. The goal of the present study was to quantitatively compare the expression of the two most important angiogenic growth factors (VEGF, angiogenin) of cervical cancer cells (HeLa and Me-180) with that of cervical cancer-derived fibroblasts (from one tumor/patient) under defined normoxic and hypoxic conditions in vitro. The growth kinetics of…

Vascular Endothelial Growth Factor APathologymedicine.medical_specialtyStromal cellAngiogeninAngiogenesismedicine.medical_treatmentCellUterine Cervical NeoplasmsEnzyme-Linked Immunosorbent AssayEndothelial Growth FactorsHeLamedicineHumansHypoxiaLymphokinesNeovascularization PathologicbiologyVascular Endothelial Growth FactorsGrowth factorObstetrics and GynecologyRibonuclease PancreaticFibroblastsbiology.organism_classificationIn vitroGene Expression Regulation NeoplasticKineticsmedicine.anatomical_structureOncologyCell cultureCancer researchFemaleCell DivisionHeLa CellsInternational Journal of Gynecological Cancer
researchProduct

Tbx1 regulates Vegfr3 and is required for lymphatic vessel development

2010

Defects in lymphangiogenesis are added to the broad clinical manifestations of DiGeorge syndrome, caused by deletion of the T box transcription factor Tbx1.

Vascular Endothelial Growth Factor ATBX1Cellular differentiationBiologyMice03 medical and health sciences0302 clinical medicinestomatognathic systemReportLymphatic vesselmedicineAnimalsHumansLymphangiogenesisEnhancerCells CulturedResearch ArticlesLymphatic Vessels030304 developmental biology0303 health sciencesABNORMAL CAROTID ARTERIES; TRANSGENIC MICE; VELOCARDIOFACIAL SYNDROME; CARDIOVASCULAR DEFECTS; LYMPHANGIOGENESIS; LYMPHEDEMA; MOUSE; RECEPTOR-3; MUTATION; SYSTEMEndothelial CellsGene Expression Regulation DevelopmentalCell DifferentiationCell BiologyEmbryo Mammalian3. Good healthLymphangiogenesisCell biologyVascular endothelial growth factor ALymphatic systemmedicine.anatomical_structureVascular endothelial growth factor Cembryonic structuresImmunologyT-Box Domain Proteins030217 neurology & neurosurgeryJournal of Cell Biology
researchProduct

Dopamine agonist administration causes a reduction in endometrial implants through modulation of angiogenesis in experimentally induced endometriosis

2009

Survival of newly implanted retrograde-shed endometrial tissue during menstruation in an ectopic location requires an adequate blood supply. This suggests that angiogenesis is a prerequisite for the development of endometriosis and that its inhibition may be a target for preventing development. Previous studies have shown that vascular endothelial growth factor (VEGF), a heparin-binding glycoprotein, has an essential role in angiogenesis. The main regulatory factor for angiogenesis appears to be binding of VEGF to its type-2 receptor (VEGFR-2). Cabergoline (Cb2) and other dopamine agonists promote endocytosis of the VEGF receptor-2 (VEGFR-2) in endothelial cells, thereby preventing VEGF-VEG…

Vascular Endothelial Growth Factor Amedicine.medical_specialtyCabergolineProliferation indexAngiogenesisEndometriosisEndometriosisBiologyEndometriumDopamine agonistMicechemistry.chemical_compoundPeritoneumCabergolineInternal medicinemedicineAnimalsHumansErgolinesPhosphorylationReceptorCell ProliferationNeovascularization Pathologicbusiness.industryRehabilitationObstetrics and GynecologyKinase insert domain receptorGeneral Medicinemedicine.diseaseVascular Endothelial Growth Factor Receptor-2Vascular endothelial growth factorDisease Models AnimalVascular endothelial growth factor AEndocrinologymedicine.anatomical_structureGene Expression RegulationReproductive MedicinechemistryDopamine AgonistsFemalelipids (amino acids peptides and proteins)businessmedicine.drugHuman Reproduction
researchProduct

Tyrosine Phosphorylation Modulates the Vascular Responses of Mesenteric Arteries from Human Colorectal Tumors

2013

The aim of this study was to analyze whether tyrosine phosphorylation in tumoral arteries may modulate their vascular response. To do this, mesenteric arteries supplying blood flow to colorectal tumors or to normal intestine were obtained during surgery and prepared for isometric tension recording in an organ bath. Increasing tyrosine phosphorylation with the phosphatase inhibitor, sodium orthovanadate produced arterial contraction which was lower in tumoral than in control arteries, whereas it reduced the contraction to noradrenaline in tumoral but not in control arteries and reduced the relaxation to bradykinin in control but not in tumoral arteries. Protein expression of VEGF-A and of th…

Vascular Endothelial Growth Factor Amedicine.medical_specialtyContraction (grammar)Article SubjectMedicinaBradykininlcsh:MedicineBiologyGeneral Biochemistry Genetics and Molecular BiologyTyrosine phosphorylationchemistry.chemical_compoundOrgan Culture TechniquesInternal medicinemedicineHumansPhosphorylationTyrosineSodium orthovanadateMesenteric arteriesVascular Endothelial Growth Factor Receptor-1Neovascularization PathologicGeneral Immunology and Microbiologylcsh:RTyrosine phosphorylationGeneral MedicineMesenteric ArteriesGene Expression Regulation NeoplasticVascular endothelial growth factor AEndocrinologymedicine.anatomical_structurechemistryTyrosinePhosphorylationVanadatesColorectal NeoplasmsResearch ArticleBioMed Research International
researchProduct

Regulation of NOS expression in vascular diseases

2020

Nitric oxide synthases (NOS) are the major sources of nitric oxide (NO), a small bioactive molecule involved in the regulation of many cellular processes. One of the most prominent functions of NO is regulation of vasodilatation and thereby control of blood pressure. Most important for vascular tone is NOS3. Endothelial NOS3-generated NO diffuses into the vascular smooth muscle cells, activates the soluble guanylate cyclase resulting in enhanced cGMP concentrations and smooth muscle cell relaxation. However, more and more evidence exist that also NOS1 and NOS2 contribute to vascular function. We summarize the current knowledge about the regulation of NOS expression in the vasculature by tra…

Vascular smooth muscleNitric Oxide Synthase Type IIINOS1CellNitric Oxide Synthase Type IIBlood PressureVasodilationInflammationNitric Oxide Synthase Type INitric OxideMuscle Smooth VascularNitric oxidechemistry.chemical_compoundmedicineAnimalsHumansProtein IsoformsVascular DiseasesRNA Processing Post-TranscriptionalInflammationRegulation of gene expressionInnate immune systemAtherosclerosisImmunity InnateCell biologyGene Expression Regulation Neoplasticmedicine.anatomical_structurechemistryNitric Oxide Synthasemedicine.symptomProtein Processing Post-TranslationalFrontiers in Bioscience-Landmark
researchProduct

Enzymatically modified nonoxidized low-density lipoprotein induces interleukin-8 in human endothelial cells: role of free fatty acids.

2002

Background— Treatment of low-density lipoprotein (LDL) with a protease and cholesterolesterase transforms the lipoprotein to an entity that resembles lipoprotein particles in atherosclerotic lesions, which have a high content of free cholesterol, reflecting extensive de-esterification in the intima. Because de-esterification would occur beneath the endothelium, we examined the effects of enzymatically modified LDL (E-LDL) on cultured endothelial cells. Methods and Results— Incubation of endothelial cells with E-LDL provoked selective accumulation of interleukin (IL)-8 mRNA and production of the cytokine. Chemical analyses and depletion experiments indicated that the effect was caused by th…

Very low-density lipoproteinLow-density lipoprotein receptor-related protein 8EndotheliumNuclease Protection AssaysBiologychemistry.chemical_compoundPhysiology (medical)medicineHumansTrypsinInterleukin 8RNA MessengerCells CulturedIntermediate-density lipoproteinFatty AcidsInterleukin-8InterleukinBiological TransportSterol EsteraseMolecular biologyLipoproteins LDLmedicine.anatomical_structureBiochemistrychemistryGene Expression RegulationLow-density lipoproteinlipids (amino acids peptides and proteins)Cholesterol EstersEndothelium VascularCardiology and Cardiovascular MedicineOxidation-ReductionLipoproteinCirculation
researchProduct

Membrane topology and post-translational modification of the Saccharomyces cerevisiae essential protein Rot1.

2007

ROT1 is an essential gene that has been related to cell wall biosynthesis, the actin cytoskeleton and protein folding. In order to help to understand its molecular function, we carried out a characterization of the Rot1 protein. It is primarily located at the endoplasmic reticulum-nuclear membrane facing the lumen. Rot1 migrates more slowly than expected, which might suggest post-translational modification. Our results indicate that Rot1 is a protein that is neither GPI-anchored nor O-glycosylated. In contrast, it is N-glycosylated. By a directed mutagenesis of several Asn residues, we identified that the protein is simultaneously glycosylated at N103, N107 and N139. Although the mutation o…

Vesicle-associated membrane protein 8Saccharomyces cerevisiae ProteinsMolecular Sequence DataBioengineeringmacromolecular substancesSaccharomyces cerevisiaeBiologyEndoplasmic ReticulumApplied Microbiology and BiotechnologyBiochemistryProtein structureSEC62Gene Expression Regulation FungalGeneticsAmino Acid SequenceCell MembraneMembrane ProteinsActin cytoskeletonCell biologyTransport proteinProtein Structure TertiaryTransmembrane domainProtein TransportBiochemistryMembrane topologyProtein foldingProtein Processing Post-TranslationalBiotechnologyMolecular ChaperonesYeast (Chichester, England)
researchProduct