Search results for "Acellular"

showing 10 items of 1986 documents

<p>Isolation and Functions of Extracellular Vesicles Derived from Parasites: The Promise of a New Era in Immunotherapy, Vaccination, and Diagno…

2020

Experimental and epidemiological evidence shows that parasites, particularly helminths, play a central role in balancing the host immunity. It was demonstrated that parasites can modulate immune responses via their excretory/secretory (ES) and some specific proteins. Extracellular vesicles (EVs) are nano-scale particles that are released from eukaryotic and prokaryotic cells. EVs in parasitological studies have been mostly employed for immunotherapy of autoimmune diseases, vaccination, and diagnosis. EVs can carry virulence factors and play a central role in the development of parasites in host cells. These molecules can manipulate the immune responses through transcriptional changes. Moreo…

Isolation (health care)medicine.medical_treatmentBiophysicsPharmaceutical ScienceVirulenceBioengineering02 engineering and technologyBiology010402 general chemistry01 natural sciencesExtracellular vesiclesBiomaterialsImmune systemImmunityDrug DiscoverymedicineOrganic ChemistryGeneral MedicineImmunotherapy021001 nanoscience & nanotechnologybiology.organism_classification0104 chemical sciencesVaccinationImmunologyProtozoa0210 nano-technologyInternational Journal of Nanomedicine
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Correction: Oncogenic extracellular HSP70 disrupts the gap-junctional coupling between capillary cells

2021

High levels of circulating heat shock protein 70 (HSP70) are detected in many cancers. In order to explore the effects of extracellular HSP70 on human microvascular endothelial cells (HMEC), we initially used gap-FRAP technique. Extracellular human HSP70 (rhHSP70), but not rhHSP27, blocks the gap-junction intercellular communication (GJIC) between HMEC, disrupts the structural integrity of HMEC junction plaques, and decreases connexin43 (Cx43) expression, which correlates with the phosphorylation of Cx43 serine residues. Further exploration of these effects identified a rapid transactivation of the Epidermal Growth Factor Receptor in a Toll-Like Receptor 4-dependent manner, preceding its in…

Junctional couplingChemistryCapillary actionCorrectionEndothelial CellsGap JunctionsCell CommunicationRecombinant ProteinsHsp70OncologyConnexin 43BiophysicsExtracellularHumansHSP70 Heat-Shock ProteinsPhosphorylationOncotarget
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Melittin Modulates Keratinocyte Function through P2 Receptor-dependent ADAM Activation

2012

Melittin, the major component of the bee venom, is an amphipathic, cationic peptide with a wide spectrum of biological properties that is being considered as an anti-inflammatory and anti-cancer agent. It modulates multiple cellular functions but the underlying mechanisms are not clearly understood. Here, we report that melittin activates disintegrin-like metalloproteases (ADAMs) and that downstream events likely contribute to the biological effects evoked by the peptide. Melittin stimulated the proteolysis of ADAM10 and ADAM17 substrates in human neutrophil granulocytes, endothelial cells and murine fibroblasts. In human HaCaT keratinocytes, melittin induced shedding of the adhesion molecu…

KeratinocytesCell SurvivalBlotting WesternADAM17 ProteinP2 receptorBiologyModels Biologicalcomplex mixturesBiochemistryMelittinCell LineADAM10 ProteinMicechemistry.chemical_compoundTransactivationAdenosine TriphosphateAnimalsHumansPhosphorylationExtracellular Signal-Regulated MAP KinasesReceptorMolecular BiologyCells CulturedMice KnockoutDose-Response Relationship DrugReverse Transcriptase Polymerase Chain ReactionPurinergic receptorHEK 293 cellstechnology industry and agricultureMembrane ProteinsCell BiologyFibroblastsCadherinsEmbryo MammalianMelittenCell biologyErbB ReceptorsADAM ProteinsHaCaTHEK293 CellschemistryPhosphorylationlipids (amino acids peptides and proteins)Receptors Purinergic P2X7Amyloid Precursor Protein SecretasesJournal of Biological Chemistry
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Dystroglycan in Skin and Cutaneous Cells: β-Subunit Is Shed from the Cell Surface

2004

In skin, hemidesmosomal protein complexes attach the epidermis to the dermis and are critical for stable connection of the basal epithelial cell cytoskeleton with the basement membrane (BM). In muscle, a similar supramolecular aggregate, the dystrophin glycoprotein complex links the inside of muscle cells with the BM. A component of the muscle complex, dystroglycan (DG), also occurs in epithelia. In this study, we characterized the expression and biochemical properties of authentic and recombinant DG in human skin and cutaneous cells in vitro. We show that DG is present at the epidermal BM zone, and it is produced by both keratinocytes and fibroblasts in vitro. The biosynthetic precursor is…

KeratinocytesCellHuman skinPerlecanDermatologyTransfectionBiochemistryCell LineDystroglycanmedicineExtracellularMyocyteHumansCytoskeletonDystroglycansMolecular BiologyBasement membraneMembrane GlycoproteinsbiologyMembrane ProteinsDermisCell BiologyCell biologyCulture MediaProtein Structure TertiaryCytoskeletal Proteinsmedicine.anatomical_structureBiochemistrybiology.proteinProtein BindingJournal of Investigative Dermatology
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cFLIPL Inhibits Tumor Necrosis Factor-related Apoptosis-inducing Ligand-mediated NF-κB Activation at the Death-inducing Signaling Complex in Human Ke…

2004

Human keratinocytes undergo apoptosis following treatment with tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) via surface-expressed TRAIL receptors 1 and 2. In addition, TRAIL triggers nonapoptotic signaling pathways including activation of the transcription factor NF-kappaB, in particular when TRAIL-induced apoptosis is blocked. The intracellular protein cFLIP(L) interferes with TRAIL-induced apoptosis at the death-inducing signaling complex (DISC) in many cell types. To study the role of cFLIP(L) in TRAIL signaling, we established stable HaCaT keratinocyte cell lines expressing varying levels of cFLIP(L). Functional analysis revealed that relative cFLIP(L) levels correlat…

KeratinocytesCytoplasmReceptor complexCell SurvivalCASP8 and FADD-Like Apoptosis Regulating ProteinApoptosisCell SeparationBiologyCaspase 8Sensitivity and SpecificityBiochemistryProinflammatory cytokineTNF-Related Apoptosis-Inducing LigandRibonucleasesCell Line TumorHumansEnzyme InhibitorsMolecular BiologyTranscription factorSkinInflammationCaspase 8Membrane GlycoproteinsTumor Necrosis Factor-alphaIntracellular Signaling Peptides and ProteinsNF-kappa BCell BiologyFlow CytometryRecombinant ProteinsCell biologyRetroviridaeApoptosisCaspasesDeath-inducing signaling complexRNATumor necrosis factor alphaSignal transductionApoptosis Regulatory ProteinsPropidiumProtein BindingSignal TransductionJournal of Biological Chemistry
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α-parvin is required for epidermal morphogenesis, hair follicle development and basal keratinocyte polarity

2020

Epidermal morphogenesis and hair follicle (HF) development depend on the ability of keratinocytes to adhere to the basement membrane (BM) and migrate along the extracellular matrix. Integrins are cell-matrix receptors that control keratinocyte adhesion and migration, and are recognized as major regulators of epidermal homeostasis. How integrins regulate the behavior of keratinocytes during epidermal morphogenesis remains insufficiently understood. Here, we show that alpha-parvin (alpha-pv), a focal adhesion protein that couples integrins to actin cytoskeleton, is indispensable for epidermal morphogenesis and HF development. Inactivation of the murine alpha-pv gene in basal keratinocytes res…

KeratinocytesIntegrinsEpitheliumBasement MembraneExtracellular matrixMiceAnimal CellsCell MovementMedicine and Health SciencesMorphogenesisCells CulturedSkinMultidisciplinarybiologyintegumentary systemChemistryQMicrofilament ProteinsMorfogènesiRCell DifferentiationDermisCell biologyExtracellular Matrixmedicine.anatomical_structureMedicineCellular TypesAnatomyCellular Structures and OrganellesIntegumentary SystemKeratinocyteHair FollicleResearch ArticleCèl·lulesCellsScienceIntegrinMorphogenesisMice TransgenicActin cytoskeleton organizationFocal adhesionHair FolliclesmedicineCell AdhesionAnimalsFocal AdhesionsBiology and Life SciencesEpithelial CellsCell BiologyActin cytoskeletonActinsBiological Tissuebiology.proteinEpidermisEpidermal thickeningDevelopmental BiologyHairPLoS ONE
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The Ras/Raf-1/MEK1/ERK Signaling Pathway Coupled to Integrin Expression Mediates Cholinergic Regulation of Keratinocyte Directional Migration

2005

The physiologic mechanisms that determine directionality of lateral migration are a subject of intense research. Galvanotropism in a direct current (DC) electric field represents a natural model of cell re-orientation toward the direction of future migration. Keratinocyte migration is regulated through both the nicotinic and muscarinic classes of acetylcholine (ACh) receptors. We sought to identify the signaling pathway mediating the cholinergic regulation of chemotaxis and galvanotropism. The pharmacologic and molecular modifiers of the Ras/Raf-1/MEK1/ERK signaling pathway altered both chemotaxis toward choline and galvanotropism toward the cathode in a similar way, indicating that the sam…

KeratinocytesMAPK/ERK pathwayIntegrinsalpha7 Nicotinic Acetylcholine ReceptorMAP Kinase Signaling SystemIntegrinMAP Kinase Kinase 1Receptors NicotinicBiologyTransfectionBiochemistryMuscarinic acetylcholine receptormedicineHumansRNA Small InterferingKeratinocyte migrationExtracellular Signal-Regulated MAP KinasesMolecular BiologyCells CulturedChemotaxisReceptor Muscarinic M1ChemotaxisCell BiologyAcetylcholineUp-RegulationCell biologyElectrophysiologyras Proteinsbiology.proteinraf KinasesLamellipodiumSignal transductionAcetylcholineSignal Transductionmedicine.drugJournal of Biological Chemistry
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Medium-term Culture of Normal Human Oral Mucosa: A Novel Three-dimensional Model to Study the Effectiveness of Drugs Administration

2012

Tissue-engineered oral mucosal equivalents have been developed for in vitro studies for a few years now. However, the usefulness of currently available models is still limited by many factors, mainly the lack of a physiological extracellular matrix (ECM) and the use of cell populations that do not reflect the properly differentiated cytotypes of the mucosa of the oral cavity. For this reason, we have developed a novel three-dimensional culture model reflecting the normal architecture of the human oral mucosa, with the main aim of creating a better in vitro model where to test cellular responses to drugs administration. This novel 3D cell culture model (3D outgrowth) was set up using an arti…

KeratinocytesPathologymedicine.medical_specialtyCell Culture TechniquesModels BiologicalExtracellular matrix3D cell cultureMatrigelMicroscopy Electron TransmissionSettore MED/28 - Malattie OdontostomatologicheIn vivoLamininDrug DiscoverymedicineHumansOral mucosaPharmacologyLamina propriaMicroscopy Confocal3d Outgrowths; Human Oral Mucosa; Matrigel; Drugs administrationTissue EngineeringbiologySettore BIO/16 - Anatomia UmanaMouth MucosaFibroblastsIn vitroHuman Oral MucosaExtracellular MatrixCell biologyFibronectinDrug Combinationsmedicine.anatomical_structureSettore CHIM/09 - Farmaceutico Tecnologico Applicativobiology.proteinProteoglycansCollagenLaminin3d OutgrowthDrugs administrationCurrent Pharmaceutical Design
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Exosomes released by keratinocytes modulate melanocyte pigmentation

2015

Cells secrete extracellular vesicles (EVs), exosomes and microvesicles, which transfer proteins, lipids and RNAs to regulate recipient cell functions. Skin pigmentation relies on a tight dialogue between keratinocytes and melanocytes in the epidermis. Here we report that exosomes secreted by keratinocytes enhance melanin synthesis by increasing both the expression and activity of melanosomal proteins. Furthermore, we show that the function of keratinocyte-derived exosomes is phototype-dependent and is modulated by ultraviolet B. In sum, this study uncovers an important physiological function for exosomes in human pigmentation and opens new avenues in our understanding of how pigmentation is…

KeratinocytesProteomicsUltraviolet RaysGeneral Physics and AstronomyBiologyMelanocyteProteomicsExosomesReal-Time Polymerase Chain ReactionGeneral Biochemistry Genetics and Molecular BiologyArticleTandem Mass SpectrometrymedicineHumansSecretionRNA MessengerCells CulturedMelanosomeRegulation of gene expressionMelaninsMultidisciplinaryMelanosomesEpidermis (botany)PigmentationGeneral ChemistryMicrovesiclesCell biologyMicroscopy Electronmedicine.anatomical_structureGene Expression RegulationMicroscopy FluorescenceMelanocytesEpidermisIntracellularChromatography LiquidNature Communications
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Staphylococcal alpha-toxin kills human keratinocytes by permeabilizing the plasma membrane for monovalent ions

1993

Incubation of human keratinocytes with nanomolar concentrations of Staphylococcus aureus alpha-toxin leads to irreversible depletion of cellular ATP. The toxin forms hexamers in the target cell membranes, and rapid transmembrane flux of K+, Na+, and 86Rb+ is observed. Unexpectedly, pores formed in keratinocytes through application of low but lethal doses of alpha-toxin appeared to be considerably smaller than those formed in erythrocyte membranes. They permitted neither rapid influx of Ca2+ or propidium iodide, nor efflux of carboxyfluorescein. Larger pores allowing flux of all three markers did form when the toxin was applied at high concentrations. Flux of monovalent ions and reduction in…

KeratinocytesStaphylococcus aureusCell Membrane PermeabilityBacterial ToxinsImmunologyMolecular ConformationBiologymedicine.disease_causeMicrobiologyCell membraneHemolysin Proteinschemistry.chemical_compoundOxygen ConsumptionNucleated cellmedicineExtracellularHumansPropidium iodideCells CulturedCell DeathToxinCell MembraneCations MonovalentCulture MediaMolecular WeightKineticsCytolysisInfectious Diseasesmedicine.anatomical_structureMembraneBiochemistrychemistryPotassiumBiophysicsCalciumParasitologyFlux (metabolism)Research ArticleInfection and Immunity
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