Search results for "3T3 Cells"

showing 10 items of 138 documents

Phytochemical profiles, phototoxic and antioxidant properties of eleven Hypericum species - A comparative study

2018

Hypericum is one out of the nine genera belonging to the botanical family Clusiaceae Lindl (syn. Hypericaceae Juss.; APG III, 2009). The genus contains 484 species spread worldwide, one of which, Hypericum perforatum, is largely used in folk medicine. The aim of this study was to evaluate the chemical composition, along with the antioxidant and phototoxic activity, of 11 Hypericum species grown in Sicily (H. perforatum L., H. aegypticum L., H. androsaemum L., H. calycinum L., H. hircinum L., H. hirsutum L., H. montanum L., H. patulum Thunb., H. perfoliatum L., H. pubescens Boiss., H. tetrapterum Fr.). Samples of flowering tops collected from these Hypericum species were extracted and analys…

0106 biological sciencesDPPHHyperforinAntioxidants Hyperforin Hypericin Hypericum species (Clusiaceae Lindl.) Phototoxicity; PolyphenolsPhytochemicalsHypericinFlowersPlant ScienceHorticultureHypericaceae01 natural sciencesBiochemistryAntioxidantsMass SpectrometryPhototoxicityMicechemistry.chemical_compoundPicratesSpecies SpecificityHypericum species (Clusiaceae Lindl.) Phototoxicity Polyphenols Hypericin Hyperforin AntioxidantsAnimalsHypericum species (Clusiaceae Lindl.)Molecular BiologyChromatography High Pressure LiquidbiologyTraditional medicine010405 organic chemistryChemistryBiphenyl CompoundsPolyphenolsHypericum perforatumGeneral MedicineFibroblastsbiology.organism_classificationSettore AGR/02 - Agronomia E Coltivazioni Erbacee0104 chemical sciencesHypericinHyperforinPhotochemotherapyPhytochemicalPolyphenolNIH 3T3 CellsAntioxidantReactive Oxygen SpeciesHypericumHypericumDermatitis Phototoxic010606 plant biology & botany
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A novel ultradeformable liposomes of Naringin for anti-inflammatory therapy

2018

[EN] Ultradeformable liposomes were formulated using naringin (NA), a flavanone glycoside, at different concentrations (3, 6 and 9 mg/mL). Nanovesicles were small size (similar to 100 nm), regardless of the NA concentration used, and monodisperse (PI<0.30). All formulations showed a high entrapment efficiency (similar to 88%) and a highly negative zeta potential (around -30 mV). The selected formulations were highly biocompatible as confirmed by in vitro studies using 3T3 fibroblasts. In vitro assay showed that the amounts (%) of NA accumulated in the epidermis (similar to 10%) could explain the anti-inflammatory properties of ultradeformable liposomes. In vivo studies confirmed the higher …

0301 basic medicineAnti-Inflammatory AgentsDermatitis02 engineering and technologyPharmacologyMicechemistry.chemical_compoundColloid and Surface ChemistryZeta potentialSkinLiposomeTransdermal penetrationPellSurfaces and InterfacesGeneral Medicine021001 nanoscience & nanotechnologyFlavanonesPhosphatidylcholinesTetradecanoylphorbol AcetateBetamethasoneFemale0210 nano-technologyFlavanoneBiotechnologymedicine.drugAntiinflamatorisCell Survivalmedicine.drug_classDrug CompoundingSkin AbsorptionAdministration CutaneousIn vivo studiesAnti-inflammatory03 medical and health sciencesIn vivomedicineAnimalsPhysical and Theoretical ChemistryNaringinUltradeformable liposomesPhosphatidylethanolaminesLysophosphatidylcholinesFibroblastsIn vitro030104 developmental biologychemistryLiposomesNIH 3T3 CellsAnti-inflammatoryNaringin
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Dextran-based therapeutic nanoparticles for hepatic drug delivery.

2016

Aim: Evaluation of dextran-based nanoparticles (DNP) as a drug delivery system to target myeloid cells of the liver. Materials &amp; methods: DNP were synthesized and optionally PEGylated. Their toxicity and cellular uptake were studied in vitro. Empty and siRNA-carrying DNP were tested in vivo with regard to biodistribution and cellular uptake. Results: In vitro, DNP were taken up by cells of the myeloid lineage without compromising their viability. In vivo, empty and siRNA-carrying DNP distributed to the liver where a single treatment addressed approximately 70% of macrophages and dendritic cells. Serum parameters indicated no in vivo toxicity. Conclusion: DNP are multifunctional liver-s…

0301 basic medicineBiodistributionMaterials scienceCell SurvivalSurface PropertiesBiomedical EngineeringMedicine (miscellaneous)Antigens Differentiation Myelomonocyticchemical and pharmacologic phenomenaBioengineering02 engineering and technologyDevelopmentPharmacologyPolyethylene Glycols03 medical and health scienceschemistry.chemical_compoundMiceIn vivoAntigens CDAnimalsHumansGeneral Materials ScienceTissue DistributionParticle SizeRNA Small InterferingDrug CarriersMice Inbred BALB Corganic chemicalsMacrophageshemic and immune systemsDextransDendritic cell3T3 CellsDendritic Cells021001 nanoscience & nanotechnology030104 developmental biologyDextranRAW 264.7 CellschemistryLiverDrug deliveryToxicityPEGylationNanoparticles0210 nano-technologyDrug carrierNanomedicine (London, England)
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Morphogenetically-Active Barrier Membrane for Guided Bone Regeneration, Based on Amorphous Polyphosphate

2017

We describe a novel regeneratively-active barrier membrane which consists of a durable electrospun poly(ε-caprolactone) (PCL) net covered with a morphogenetically-active biohybrid material composed of collagen and inorganic polyphosphate (polyP). The patch-like fibrous collagen structures are decorated with small amorphous polyP nanoparticles (50 nm) formed by precipitation of this energy-rich and enzyme-degradable (alkaline phosphatase) polymer in the presence of calcium ions. The fabricated PCL-polyP/collagen hybrid mats are characterized by advantageous biomechanical properties, such as enhanced flexibility and stretchability with almost unaltered tensile strength of the PCL net. The pol…

0301 basic medicineBone Regenerationcollagen-inducingBarrier membranePolymersPharmaceutical Science02 engineering and technologyMatrix (biology)chemistry.chemical_compoundMiceOsteogenesisPolyphosphatesDrug Discoverystromal cell-derived factor-1Pharmacology Toxicology and Pharmaceutics (miscellaneous)MC3T3-E1 cellsChemistrybiologizationAnatomy3T3 Cells021001 nanoscience & nanotechnology3. Good healthMembranetensile strength/resistanceAlkaline phosphataseCollagen0210 nano-technologyinorganic polyphosphateSurface PropertiesPolyestersArticleAngiopoietin-203 medical and health sciencesCalcification PhysiologicAnimalsHumansBone regenerationTissue EngineeringPolyphosphateMesenchymal stem cellMembrane ProteinsMembranes ArtificialMesenchymal Stem Cellspolypropylene mesh030104 developmental biologyGene Expression RegulationBiophysicsbiologization; hernia repair; inorganic polyphosphate; collagen-inducing; polypropylene mesh; tensile strength/resistance; stromal cell-derived factor-1; MC3T3-E1 cellsNanoparticlesWound healinghernia repairMarine Drugs
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Identification of the integrin-binding site on coagulation factor VIIa required for proangiogenic PAR2 signaling.

2018

The tissue factor (TF) pathway serves both hemostasis and cell signaling, but how cells control these divergent functions of TF remains incompletely understood. TF is the receptor and scaffold of coagulation proteases cleaving protease-activated receptor 2 (PAR2) that plays pivotal roles in angiogenesis and tumor development. Here we demonstrate that coagulation factor VIIa (FVIIa) elicits TF cytoplasmic domain-dependent proangiogenic cell signaling independent of the alternative PAR2 activator matriptase. We identify a Lys-Gly-Glu (KGE) integrin-binding motif in the FVIIa protease domain that is required for association of the TF-FVIIa complex with the active conformer of integrin β1. A po…

0301 basic medicineCell signalingImmunologyIntegrinNeovascularization PhysiologicFactor VIIa030204 cardiovascular system & hematologyBiochemistryThromboplastinThrombosis and Hemostasis03 medical and health sciencesTissue factorMice0302 clinical medicineAnimalsHumansReceptor PAR-2Protein Interaction Domains and MotifsProtein Interaction MapsProtein kinase ACells CulturedIntegrin bindingBinding SitesbiologyChemistryIntegrin beta1Cell BiologyHematologyCell biologyCrosstalk (biology)030104 developmental biologyADP-Ribosylation Factor 6biology.proteinNIH 3T3 CellsPhosphorylationSignal transductionProtein BindingSignal TransductionBlood
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Targeting Bacterial Sortase A with Covalent Inhibitors: 27 New Starting Points for Structure-Based Hit-to-Lead Optimization.

2019

Because of its essential role as a bacterial virulence factor, enzyme sortase A (SrtA) has become an attractive target for the development of new antivirulence drugs against Gram-positive infections. Here we describe 27 compounds identified as covalent inhibitors of

0301 basic medicineStaphylococcus aureusMagnetic Resonance SpectroscopyAntivirulenceVirulence Factors030106 microbiologySmall Molecule Libraries03 medical and health sciencesMiceBacterial ProteinsCatalytic DomainDrug DiscoveryAnimalschemistry.chemical_classificationBinding SitesChemistryHit to leadFibroblastsAminoacyltransferasesAnti-Bacterial AgentsMolecular Docking SimulationCysteine Endopeptidases030104 developmental biologyInfectious DiseasesEnzymeBiochemistryCovalent bondSortase ABacterial virulenceNIH 3T3 CellsStructure basedACS infectious diseases
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Enzymatic Activity of HPGD in Treg Cells Suppresses Tconv Cells to Maintain Adipose Tissue Homeostasis and Prevent Metabolic Dysfunction.

2019

Summary Regulatory T cells (Treg cells) are important for preventing autoimmunity and maintaining tissue homeostasis, but whether Treg cells can adopt tissue- or immune-context-specific suppressive mechanisms is unclear. Here, we found that the enzyme hydroxyprostaglandin dehydrogenase (HPGD), which catabolizes prostaglandin E2 (PGE2) into the metabolite 15-keto PGE2, was highly expressed in Treg cells, particularly those in visceral adipose tissue (VAT). Nuclear receptor peroxisome proliferator-activated receptor-γ (PPARγ)-induced HPGD expression in VAT Treg cells, and consequential Treg-cell-mediated generation of 15-keto PGE2 suppressed conventional T cell activation and proliferation. C…

0301 basic medicineanalogs & derivatives [Dinoprostone]Malemetabolism [Diabetes Mellitus Type 2]Adipose tissueLymphocyte Activation15-ketoprostaglandin E2T-Lymphocytes RegulatoryJurkat cellsJurkat CellsMice0302 clinical medicineimmunology [Lymphocyte Activation]genetics [Insulin Resistance]STAT5 Transcription FactorHomeostasisImmunology and AllergyTissue homeostasisgenetics [Hydroxyprostaglandin Dehydrogenases]Mice Knockoutcytology [Intra-Abdominal Fat]enzymology [T-Lymphocytes Regulatory]FOXP3hemic and immune systems3T3 CellsCell biologyInfectious Diseases030220 oncology & carcinogenesisHydroxyprostaglandin Dehydrogenasesmedicine.symptomimmunology [T-Lymphocytes Regulatory]metabolism [STAT5 Transcription Factor]Immunologymetabolism [Dinoprostone]chemical and pharmacologic phenomenaInflammationIntra-Abdominal FatBiologyDinoprostoneCell Line03 medical and health sciencesmetabolism [Hydroxyprostaglandin Dehydrogenases]immunology [Homeostasis]medicineAnimalsHumansddc:610immunology [Intra-Abdominal Fat]HEK 293 cells030104 developmental biologyHEK293 CellsDiabetes Mellitus Type 2Cell cultureInsulin ResistanceHomeostasis
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Recombinant mussel protein Pvfp-5β: A potential tissue bioadhesive

2019

During their lifecycle, many marine organisms rely on natural adhesives to attach to wet surfaces for movement and self-defence in aqueous tidal environments. Adhesive proteins from mussels are biocompatible and elicit only minimal immune responses in humans. Therefore these proteins have received increased attention for their potential applications in medicine, biomaterials and biotechnology. The Asian green mussel Perna viridis secretes several byssal plaque proteins, molecules that help anchor the mussel to surfaces. Among these proteins, protein-5β (Pvfp-5β) initiates interactions with the substrate, displacing interfacial water molecules before binding to the surface. Here, we establis…

0301 basic medicinemedicine.disease_causeBiochemistryepidermal growth factor (EGF)law.inventionMiceCell Movementlawbiophysicsstructural biologyrecombinantCells CulturedbiologyChemistryMarine proteinsAdhesionRecombinant ProteinsadhesionProtein Structure and FoldingRecombinant DNAadhesion proteinsbiomaterialsPernaCell SurvivalSurface PropertiesBioadhesivemussel03 medical and health sciencesmedicineAnimalsHumansMolecular BiologyEscherichia coliCell ProliferationTissue Engineering030102 biochemistry & molecular biologyProteinsCell BiologyMusselbiology.organism_classificationEGF-like motifs; Marine proteins; adhesion; adhesion proteins; biomaterials; biophysics; epidermal growth factor (EGF); structural biologyEGF-like motifs030104 developmental biologyStructural biologyCell cultureNIH 3T3 CellsBiophysicsTissue AdhesivesHeLa CellsPerna viridisJournal of Biological Chemistry
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Genomic organization and promoter characterization of the gene encoding a putative endoplasmic reticulum chaperone, ERp29

2002

Abstract ERp29 is a soluble protein localized in the endoplasmic reticulum (ER) of eukaryotic cells, which is conserved in all mammalian species. The N-terminal domain of ERp29 displays sequence and structural similarity to the protein disulfide isomerase despite the lack of the characteristic double cysteine motif. Although the exact function of ERp29 is not yet known, it was hypothesized that it may facilitate folding and/or export of secretory proteins in/from the ER. ERp29 is induced by ER stress, i.e. accumulation of unfolded proteins in the ER. To gain an insight into the mechanisms regulating ERp29 expression we have cloned and characterized the rat ERp29 gene and studied in details …

5' Flanking RegionRecombinant Fusion ProteinsMolecular Sequence DataCHO CellsBiologyCell LineMiceCricetinaeSequence Homology Nucleic AcidGene expressionTumor Cells CulturedGeneticsAnimalsHumansRNA MessengerLuciferasesPromoter Regions GeneticProtein disulfide-isomeraseGeneHeat-Shock ProteinsPhylogenyBase SequenceGene Expression ProfilingEndoplasmic reticulumPromoter3T3 CellsDNAExonsSequence Analysis DNAGeneral MedicineMolecular biologyIntronsRatsHousekeeping geneSecretory proteinGenesUnfolded protein responseFemaleTranscription Initiation SiteSequence AlignmentHeLa CellsGene
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Novel mutations of the MET proto-oncogene in papillary renal carcinomas.

1999

Hereditary papillary renal carcinoma (HPRC) is characterized by multiple, bilateral papillary renal carcinomas. Previously, we demonstrated missense mutations in the tyrosine kinase domain of the MET proto-oncogene in HPRC and a subset of sporadic papillary renal carcinomas. In this study, we screened a large panel of sporadic papillary renal carcinomas and various solid tumors for mutations in the MET proto-oncogene. Summarizing these and previous results, mutations of the MET proto-oncogene were detected in 17/129 sporadic papillary renal carcinomas but not in other solid tumors. We detected five novel missense mutations; three of five mutations were located in the ATP-binding region of t…

AdenomaModels MolecularCancer ResearchProtein ConformationDNA Mutational AnalysisMolecular Sequence DataHereditary Papillary Renal Cell CarcinomaBiologymedicine.disease_causeTransfectionProto-Oncogene MasReceptor tyrosine kinaseMiceAdenosine TriphosphateNeoplastic Syndromes HereditaryProto-OncogenesGeneticsCarcinomamedicineMissense mutationAnimalsHumansPoint MutationAmino Acid SequencePhosphorylationCodonMolecular BiologyKidneyMutationBinding SitesSequence Homology Amino AcidPoint mutation3T3 CellsDNA NeoplasmProto-Oncogene Proteins c-metmedicine.diseaseCarcinoma PapillaryKidney NeoplasmsNeoplasm Proteinsmedicine.anatomical_structureCell Transformation NeoplasticCancer researchbiology.proteinMutagenesis Site-DirectedTyrosine kinaseProtein Processing Post-TranslationalSequence AlignmentOncogene
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