Search results for "Cell Surface"

showing 10 items of 201 documents

Expression pattern of Notch1, 2 and 3 and Jagged1 and 2 in lymphoid and stromal thymus components: distinct ligand–receptor interactions in intrathym…

1999

The suggested role of Notch1 or its mutants in thymocyte differentiation and T cell tumorigenesis raises the question of how the different members of the Notch family influence distinct steps in T cell development and the role played by Notch ligands in the thymus. We report here that different Notch receptor-ligand partnerships may occur inside the thymus, as we observed differential expression of Notch1, 2 and 3 receptors, their ligands Jagged1 and 2, and downstream intracellular effectors hairy and Enhancer of Split homolog 1 (HES-1) and hairy and Enhancer of Split homolog 5 (HES-5), depending on ontogenetic stage and thymic cell populations. Indeed, while Jagged2 is expressed in both st…

MaleT-LymphocytesLigandsMiceNotch FamilyCell–cell interactionT-Lymphocyte SubsetsBasic Helix-Loop-Helix Transcription FactorsImmunology and AllergySerrate-Jagged ProteinsReceptor Notch2Receptor Notch1Receptor Notch4Receptor Notch3Receptors NotchHelix-Loop-Helix Motifscell-cell interaction; thymic stromal cells; thymocyteCell DifferentiationGeneral MedicineCell biologyDNA-Binding ProteinsThymocytemedicine.anatomical_structureIntercellular Signaling Peptides and ProteinsJagged-2 ProteinSignal TransductionStromal cellLymphoid TissueT cellImmunologyNotch signaling pathwayReceptors Cell SurfaceThymus GlandBiologySerrate-Jagged ProteinsProto-Oncogene ProteinsmedicineAnimalsRNA MessengerHomeodomain ProteinsCalcium-Binding ProteinsMembrane ProteinsProteinsMice Inbred C57BLRepressor ProteinsProtein BiosynthesisTranscription Factor HES-1Jagged-1 ProteinStromal CellsCarrier ProteinsJagged-1 ProteinTranscription FactorsInternational Immunology
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Association of soluble endothelial protein C receptor plasma levels and PROCR rs867186 with cardiovascular risk factors and cardiovascular events in …

2012

Abstract Background Blood coagulation is an essential determinant of coronary artery disease (CAD). Soluble Endothelial Protein C Receptor (sEPCR) may be a biomarker of a hypercoagulable state. We prospectively investigated the relationship between plasma sEPCR levels and the risk of cardiovascular events (CVE). Methods We measured baseline sEPCR levels in 1673 individuals with CAD (521 with acute coronary syndrome [ACS] and 1152 with stable angina pectoris [SAP]) from the AtheroGene cohort. During a median follow up of 3.7 years, 136 individuals had a CVE. In addition, 891 of these CAD patients were genotyped for the PROCR rs867186 (Ser219Gly) variant. Results At baseline, sEPCR levels wer…

Malelcsh:Internal medicinemedicine.medical_specialtyAcute coronary syndromelcsh:QH426-470Cardiovascular risk factorsReceptors Cell Surface[SDV.GEN] Life Sciences [q-bio]/Genetics030204 cardiovascular system & hematologyBiology[SDV.GEN.GH] Life Sciences [q-bio]/Genetics/Human geneticsPolymorphism Single NucleotideCoronary artery diseaseEndothelial protein C receptorAngina PectorisCoronary artery disease03 medical and health sciences0302 clinical medicineAntigens CDRisk FactorsInternal medicineGeneticsmedicineHumansGenetics(clinical)Acute Coronary Syndromelcsh:RC31-1245GeneGenetics (clinical)030304 developmental biology0303 health sciencesEndothelial protein C receptor[SDV.GEN]Life Sciences [q-bio]/Geneticsmedicine.diseaselcsh:GeneticsCoagulation[SDV.GEN.GH]Life Sciences [q-bio]/Genetics/Human geneticsCardiovascular DiseasesImmunologyCardiologyBiomarker (medicine)Female\BiomarkersProtein CResearch Articlemedicine.drugHaemostasisProtein C
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Effects of endotoxin on neurally-mediated gastric acid secretion in the rat.

1998

Abstract The effects of a peripheral administration of E. coli endotoxin on neurally-mediated gastric acid secretion and the role of endogenous opioids or PAF receptors in endotoxin effects have been evaluated in the continuously perfused stomach of the anaesthetized rat. Gastric acid secretion stimulated by distension (20 cm H2O) was reduced dose-dependently by single intravenous bolus injection of endotoxin (0.1–10 μg kg−1). Doses of 5 μg kg−1 induced a peak reduction of distension-stimulated acid output and significantly reduced the secretory response induced by an intravenous bolus of 2-deoxy-d-glucose (150 mg kg−1). This dose of endotoxin did not significantly modify mean systemic arte…

Malemedicine.medical_specialtymedicine.drug_classNarcotic AntagonistsPharmaceutical ScienceBlood PressureReceptors Cell Surface(+)-NaloxonePlatelet Membrane GlycoproteinsDistensionDeoxyglucoseReceptors G-Protein-CoupledGastric AcidOpioid receptorInternal medicinemedicineEscherichia coliAnimalsRats WistarEndogenous opioidPharmacologyDose-Response Relationship Drugbusiness.industryNaloxoneGastric distensionStomachAntagonistAzepinesTriazolesReceptor antagonistRatsEndotoxinsEndocrinologyOpioid PeptidesReceptors OpioidGastric acidFemalemedicine.symptombusinessPlatelet Aggregation InhibitorsThe Journal of pharmacy and pharmacology
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UNC-52/perlecan affects gonadal leader cell migrations in C. elegans hermaphrodites through alterations in growth factor signaling.

2003

0012-1606 doi: DOI: 10.1016/S0012-1606(03)00014-9; The unc-52 gene of Claenorhabditis elegans encodes a homologue of the basement membrane heparan sulfate proteoglycan perlecan. Viable alleles reduce the abundance of UNC-52 in late larval stages and increase the frequency of distal tip cell (DTC) migration defects caused by mutations disrupting the UNC-6/netrin guidance system. These unc-52 alleles do not cause circumferential DTC migration defects in an otherwise wild-type genetic background. The effects of unc-52 mutations on DTC migrations are distinct from effects on myofilament organization and can be partially suppressed by mutations in several genes encoding growth factor-like molecu…

Malemedicine.medical_treatmentOrganogenesisCellDisorders of Sex DevelopmentReceptor-Like Protein Tyrosine PhosphatasesFibroblast growth factorAnimals Genetically ModifiedCell MovementNetrinGrowth SubstancesGenes HelminthGeneticsMusclesCell migrationsWnt signaling pathwayHelminth Proteinsmedicine.anatomical_structurePhenotypeLarvaC. elegansFemaleNetrinsProteoglycansSignal transductionSignal TransductionUNC-52Nerve Tissue ProteinsReceptors Cell SurfacePerlecanmacromolecular substancesBiologymedicineAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsGonadsGeneMolecular BiologyGrowth factorfungiMembrane ProteinsCell BiologyPerlecanReceptors Fibroblast Growth Factornervous systemMutationbiology.proteinProtein Tyrosine PhosphatasesDevelopmental BiologyDevelopmental biology
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Toll-like receptor 2 mediates prostaglandin E2 production in murine peritoneal macrophages and splenocytes in response to Candida albicans

2004

The involvement of Toll-like receptor 2 (TLR2) and TLR4 in triggering signal transduction pathways leading to prostaglandin E(2) (PGE(2)) production in response to Candida albicans has been studied in cells from wild-type, TLR2-/- and TLR4-/- knockout mice. In vitro PGE(2) production by macrophages challenged with zymosan, yeast or hypha cells was strongly inhibited in TLR2-deficient cells, but not in TLR4-/- cells, as compared to macrophages from wild-type mice. PGE(2) production was dependent on de novo cyclooxygenase-2 (Cox2) synthesis, since unchallenged cells failed to produce PGE(2) and specific Cox2 inhibition during challenge totally blocked PGE(2) production. Similar results were o…

Malemedicine.medical_treatmentReceptors Cell SurfaceBiologyMicrobiologyDinoprostoneMicechemistry.chemical_compoundCandida albicansmedicineAnimalsProstaglandin E2Candida albicansMolecular BiologyCells CulturedMice KnockoutToll-like receptorZymosanGeneral Medicinebiology.organism_classificationMolecular biologyToll-Like Receptor 2Corpus albicansToll-Like Receptor 4TLR2chemistryCyclooxygenase 2Prostaglandin-Endoperoxide SynthasesImmunologyMacrophages PeritonealTLR4Femalelipids (amino acids peptides and proteins)Signal Transductionmedicine.drugProstaglandin EResearch in Microbiology
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Role of membrane dynamics processes and exogenous molecules in cellular resveratrol uptake: consequences in bioavailability and activities.

2011

In the fields of nutrition prevention and therapy treatment, numerous studies have reported interesting properties of trans-resveratrol (RSV), a natural polyphenol against pathologies such as vascular diseases, cancers, viral infections and neurodegenerative processes. These beneficial effects are supported by more studies showing the pleiotropic actions of RSV. Nevertheless, a crucial question concerning these effects is how the polyphenol, when applied to an organism, gains access to its targets. In this review, we focus on the biochemical and biological parameters involved in RSV transport, particularly the role of the phospholipid bilayer in RSV uptake (passive diffusion, carrier-mediat…

Membrane FluidityvirusesLipoproteinsIntegrinEstrogen receptorBiological AvailabilityResveratrolEndocytosischemistry.chemical_compoundMembrane LipidsMembrane MicrodomainsCell surface receptorStilbenesAnimalsHumansReceptorLipid raftbiologyCell MembraneFatty Acidsvirus diseasesBiological TransportSerum Albumin Bovinerespiratory systemIntegrin alphaVbeta3EndocytosisCell biologyBiochemistrychemistryResveratrolbiology.proteinIntracellularFood ScienceBiotechnologyMolecular nutritionfood research
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Fluorescent Small Molecule Probe to Modulate and Explore α2β1 Integrin Function

2011

Collagen binding integrins are an important family of cell surface receptors that mediate bidirectionally signals between the interior of the cell and the extracellular matrix. The protein-protein interactions between cells and collagen are necessary for many physiological functions, but also promote diseases. For example, the interaction of α2β1 integrin and collagen has been shown to have an important role in thrombus formation and cancer spread. The fact that the discovery of small molecules that can block such protein-protein interactions is highly challenging has significantly hindered the discovery of pharmaceutical agents to treat these diseases. Here, we present a rationally designe…

Models MolecularCellIntegrinBiochemistryCatalysisExtracellular matrixColloid and Surface ChemistryCell surface receptormedicineHumansta116Fluorescent DyesBinding SitesbiologyChemistryta1182General ChemistryFluorescenceSmall moleculeSpectrometry Fluorescencemedicine.anatomical_structureBiochemistryBiophysicsbiology.proteinCollagenα2β1 integrinIntegrin alpha2beta1Function (biology)Protein BindingJournal of the American Chemical Society
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Mediation of Elicitin Activity on Tobacco Is Assumed by Elicitin-Sterol Complexes

2001

Elicitins secreted by phytopathogenic Phytophthora spp. are proteinaceous elicitors of plant defense mechanisms and were demonstrated to load, carry, and transfer sterols between membranes. The link between elicitor and sterol-loading properties was assessed with the use of site-directed mutagenesis of the 47 and 87 cryptogein tyrosine residues, postulated to be involved in sterol binding. Mutated cryptogeins were tested for their ability to load sterols, bind to plasma membrane putative receptors, and trigger biological responses. For each mutated elicitin, the chemical characterization of the corresponding complexes with stigmasterol (1:1 stoichiometry) demonstrated their full functionali…

Models MolecularPhytophthora0106 biological sciencesTime FactorsProtein Conformation[SDV]Life Sciences [q-bio]Receptors Cell SurfaceBiologyModels Biological01 natural sciencesArticleHost-Parasite InteractionsFungal Proteins03 medical and health sciencesTobaccoProtein IsoformsBinding siteReceptorMolecular BiologyComputingMilieux_MISCELLANEOUSCells CulturedPlant DiseasesPlant Proteins030304 developmental biology0303 health sciencesBinding SitesAlgal ProteinsCell MembraneProteinsElicitinCell BiologyHydrogen-Ion ConcentrationLigand (biochemistry)Receptor–ligand kineticsSterolElicitor[SDV] Life Sciences [q-bio]SterolsBiochemistryTyrosineCalciumSterol bindingProtein Binding010606 plant biology & botanyMolecular Biology of the Cell
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The NMR structure of the sensory domain of the membranous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli

2003

The structure of the water-soluble, periplasmic domain of the fumarate sensor DcuS (DcuS-pd) has been determined by NMR spectroscopy in solution. DcuS is a prototype for a sensory histidine kinase with transmembrane signal transfer. DcuS belongs to the CitA family of sensors that are specific for sensing di- and tricarboxylates. The periplasmic domain is folded autonomously and shows helices at the N and the C terminus, suggesting direct linking or connection to helices in the two transmembrane regions. The structure constitutes a novel fold. The nearest structural neighbor is the Per-Arnt-Sim domain of the photoactive yellow protein that binds small molecules covalently. Residues Arg107, H…

Models MolecularProtein FoldingMagnetic Resonance SpectroscopyProtein ConformationStereochemistryMolecular Sequence DataReceptors Cell SurfaceBiologyArginineBiochemistryProtein Structure SecondaryBacterial ProteinsFumaratesEscherichia coliTransferaseHistidineAmino Acid SequenceProtein kinase AMolecular BiologyHistidineBinding SitesEscherichia coli ProteinsC-terminusCell MembraneHistidine kinaseCell BiologyNuclear magnetic resonance spectroscopyPeriplasmic spaceChemoreceptor CellsTransmembrane proteinProtein Structure TertiaryCrystallographyMutationPeriplasmProtein KinasesSignal Transduction
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Killer-toxin-resistant kre12 mutants of Saccharomyces cerevisiae: genetic and biochemical evidence for a secondary K1 membrane receptor.

1995

The Saccharomyces cerevisiae killer toxin K1 is a secreted alpha/beta-heterodimeric protein toxin that kills sensitive yeast cells in a receptor-mediated two-stage process. The first step involves toxin binding to beta-1,6-D-glucan-components of the outer yeast cell surface; this step is blocked in yeast mutants bearing nuclear mutations in any of the KRE genes whose products are involved in synthesis and/or assembly of cell wall beta-D-glucans. After binding to the yeast cell wall, the killer toxin is transferred to the cytoplasmic membrane, subsequently leading to cell death by forming lethal ion channels. In an attempt to identify a secondary K1 toxin receptor at the plasma membrane leve…

MutantSaccharomyces cerevisiaeGenes FungalReceptors Cell SurfaceSaccharomyces cerevisiaeSpheroplastsBiologymedicine.disease_causeBiochemistryMicrobiologyModels BiologicalIon ChannelsFungal ProteinsCell surface receptorCell WallGeneticsmedicineMolecular BiologyDiphtheria toxinToxinMembrane ProteinsDrug Resistance MicrobialGeneral MedicineSpheroplastMycotoxinsbiology.organism_classificationYeastKiller Factors YeastBiochemistryMembrane proteinMutationArchives of microbiology
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