Search results for " Transport"

showing 10 items of 3573 documents

The Role of Osteoprotegerin and Its Ligands in Vascular Function

2019

International audience; The superfamily of tumor necrosis factor (TNF) receptors includes osteoprotegerin (OPG) and its ligands, which are receptor activators of nuclear factor kappa-B ligand (RANKL) and TNF-related apoptosis-inducing ligand (TRAIL). The OPG/RANKL/RANK system plays an active role in pathological angiogenesis and inflammation as well as cell survival. It has been demonstrated that there is crosstalk between endothelial cells and osteoblasts during osteogenesis, thus establishing a connection between angiogenesis and osteogenesis. This OPG/RANKL/RANK/TRAIL system acts on specific cell surface receptors, which are then able to transmit their signals to other intracellular comp…

0301 basic medicineAngiogenesismedicine.medical_treatmentReview030204 cardiovascular system & hematologyLigandslcsh:ChemistryTNF-Related Apoptosis-Inducing Ligand0302 clinical medicineReceptorlcsh:QH301-705.5Cellular SenescenceSpectroscopyReceptor Activator of Nuclear Factor-kappa BbiologyChemistryvascular diseaseGeneral MedicineComputer Science ApplicationsProtein Transportmedicine.anatomical_structureCytokineRANKLTumor necrosis factor alphaDisease Susceptibilitymedicine.symptomProtein BindingSignal Transductionmusculoskeletal diseasesProteasome Endopeptidase ComplexEndotheliumendotheliumNeovascularization PhysiologicInflammationCatalysisInorganic ChemistryStructure-Activity Relationship03 medical and health sciencesOsteoprotegerin[SDV.MHEP.CSC]Life Sciences [q-bio]/Human health and pathology/Cardiology and cardiovascular systemmedicineAnimalsHumansPhysical and Theoretical ChemistryMolecular BiologyMyocardiumRANK LigandOrganic ChemistryEndothelial Cells030104 developmental biologylcsh:Biology (General)lcsh:QD1-999osteoprotegerinOPG/RANKL/RANKCancer researchbiology.proteinBlood VesselsBiomarkers
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Sorting signals for PIN1 trafficking and localization

2016

PIN-FORMED (PIN) family proteins direct polar auxin transport based on their asymmetric (polar) localization at the plasma membrane. In the case of PIN1, it mainly localizes to the basal (rootward) plasma membrane domain of stele cells in root meristems. Vesicular trafficking events, such as clathrin-dependent PIN1 endocytosis and polar recycling, are probably the main determinants for PIN1 polar localization. However, very little is known about the signals which may be involved in binding the μ-adaptin subunit of clathrin adaptor complexes (APs) for sorting of PIN1 within clathrin-coated vesicles, which can determine its trafficking and localization. We have performed a systematic mutagene…

0301 basic medicineArabidopsis ProteinsVesicleClathrin adaptor complexCell MembraneMembrane Transport ProteinsPlant ScienceBiologyEndocytosisClathrinEndocytosisAdaptor Protein Complex mu SubunitsArticle AddendumCell biologyAdaptor Proteins Vesicular Transport03 medical and health sciences030104 developmental biologybiology.proteinClathrin adaptor proteinsPolar auxin transportTyrosineSecretory pathwayPlant Signaling & Behavior
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Endocytosis of the glutamate transporter 1 is regulated by laforin and malin: Implications in Lafora disease.

2020

Postprint 36 páginas, 7 figuras

0301 basic medicineArrestinsAmino Acid Transport System X-AGPhosphataseProgressive myoclonus epilepsyBiologyEndocytosisLafora diseaseArticle03 medical and health sciencesCellular and Molecular NeuroscienceMice0302 clinical medicineUbiquitinmedicineAnimalsNedd4.2Lafora diseaseGlutamate receptorUbiquitinationTransportermedicine.diseaseProtein Tyrosine Phosphatases Non-ReceptorEndocytosisCell biologyGLT-1030104 developmental biologyNeurologyLafora Diseasebiology.proteinGlutamateLaforin030217 neurology & neurosurgeryGlia
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Reversible Axonal Dystrophy by Calcium Modulation in Frataxin-Deficient Sensory Neurons of YG8R Mice

2017

15 Pages, 8 Figures. The Supplementary Material for this article can be found online at: http://journal.frontiersin.org/article/10.3389/fnmol.2017.00264/full#supplementary-material

0301 basic medicineAtaxiaNeuriteFriedreich’s ataxiarare diseaseMitochondrionlcsh:RC321-57103 medical and health sciencesCellular and Molecular Neurosciencechemistry.chemical_compound0302 clinical medicineBAPTAmedicinelcsh:Neurosciences. Biological psychiatry. NeuropsychiatryMolecular BiologyOriginal ResearchcalciumbiologyNeurodegenerationneurodegenerationFriedreich's ataxiaaxonal spheroidsmedicine.disease3. Good healthmitochondria030104 developmental biologyPeripheral neuropathychemistrynervous systemFrataxinbiology.proteinAxoplasmic transportmedicine.symptomNeuroscience030217 neurology & neurosurgeryNeuroscience
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How Glutamate Is Managed by the Blood-Brain Barrier.

2016

A facilitative transport system exists on the blood–brain barrier (BBB) that has been tacitly assumed to be a path for glutamate entry to the brain. However, glutamate is a non-essential amino acid whose brain content is much greater than plasma, and studies in vivo show that glutamate does not enter the brain in appreciable quantities except in those small regions with fenestrated capillaries (circumventricular organs). The situation became understandable when luminal (blood facing) and abluminal (brain facing) membranes were isolated and studied separately. Facilitative transport of glutamate and glutamine exists only on the luminal membranes, whereas Na+-dependent transport systems for g…

0301 basic medicineBBB (blood–brain barrier)brainglutamateReviewBiologyBlood–brain barrierGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciences0302 clinical medicineExtracellular fluidmedicinelcsh:QH301-705.5Circumventricular organsoxoprolinechemistry.chemical_classificationGeneral Immunology and Microbiologyamino acid transportGlutamate receptorAmino acidGlutamine030104 developmental biologymedicine.anatomical_structureMembranelcsh:Biology (General)BiochemistrychemistryBiophysicsglutamineGeneral Agricultural and Biological SciencesCotransporter030217 neurology & neurosurgeryBiology
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Ticket to Ride: Targeting Proteins to Exosomes for Brain Delivery.

2017

Exosomes represent an attractive vehicle for the delivery of biomolecules. However, mechanisms for loading functional molecules into exosomes are relatively unexplored. Here we report the use of the evolutionarily conserved late-domain (L-domain) pathway as a mechanism for loading exogenous proteins into exosomes. We demonstrate that labeling of a target protein, Cre recombinase, with a WW tag leads to recognition by the L-domain-containing protein Ndfip1, resulting in ubiquitination and loading into exosomes. Our results show that Ndfip1 expression acts as a molecular switch for exosomal packaging of WW-Cre that can be suppressed using the exosome inhibitor GW4869. When taken up by floxed …

0301 basic medicineBiocompatibilityRecombinant Fusion ProteinsGene ExpressionComputational biologyBiologyExosomesPermeabilityCell LineExtracellular VesiclesMice03 medical and health sciencesDrug Delivery SystemsDrug DiscoveryGeneticsAnimalsMolecular BiologyPharmacologyIntegrasesbusiness.industryImmunogenicityMembrane ProteinsRNABrainProteinsMicrovesiclesBiotechnologyProtein Transport030104 developmental biologyTargeted drug deliveryBlood-Brain BarrierCommentaryMolecular MedicineOriginal ArticleNasal AbsorptionCarrier ProteinsGenetic EngineeringbusinessMolecular therapy : the journal of the American Society of Gene Therapy
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Cationic Amino Acid Transporter-1-Mediated Arginine Uptake Is Essential for Chronic Lymphocytic Leukemia Cell Proliferation and Viability

2019

Interfering with tumor metabolism by specifically restricting the availability of extracellular nutrients is a rapidly emerging field of cancer research. A variety of tumor entities depend on the uptake of the amino acid arginine since they have lost the ability to synthesize it endogenously, that is they do not express the rate limiting enzyme for arginine synthesis, argininosuccinate synthase (ASS). Arginine transport through the plasma membrane of mammalian cells is mediated by eight different transporters that belong to two solute carrier (SLC) families. In the present study we found that the proliferation of primary as well as immortalized chronic lymphocytic leukemia (CLL) cells depen…

0301 basic medicineCancer ResearchArginineArgininosuccinate synthaseargininelcsh:RC254-282amino acid transporter03 medical and health sciences0302 clinical medicineDownregulation and upregulationhemic and lymphatic diseasesAmino acid transporterViability assayOriginal Researchchemistry.chemical_classificationnutrient restrictionArginine transportbiologylcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogensAmino acidSolute carrier familyCell biology030104 developmental biologyOncologychemistry030220 oncology & carcinogenesisbiology.proteinchronic lymphocytic leukemiatumor metabolismFrontiers in Oncology
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2-Methoxyestradiol Affects Mitochondrial Biogenesis Pathway and Succinate Dehydrogenase Complex Flavoprotein Subunit A in Osteosarcoma Cancer Cells.

2017

Background/aim Dysregulation of mitochondrial pathways is implicated in several diseases, including cancer. Notably, mitochondrial respiration and mitochondrial biogenesis are favored in some invasive cancer cells, such as osteosarcoma. Hence, the aim of the current work was to investigate the effects of 2-methoxyestradiol (2-ME), a potent anticancer agent, on the mitochondrial biogenesis of osteosarcoma cells. Materials and methods Highly metastatic osteosarcoma 143B cells were treated with 2-ME separately or in combination with L-lactate, or with the solvent (non-treated control cells). Protein levels of α-syntrophin and peroxisome proliferator-activated receptor gamma, coactivator 1 alph…

0301 basic medicineCancer ResearchSIRT3Protein subunitSDHAMuscle ProteinsAntineoplastic AgentsMolecular Dynamics SimulationBiochemistryElectron Transport Complex IV03 medical and health sciences0302 clinical medicineGeneticSettore BIO/10 - BiochimicaCell Line TumorSirtuin 3CoactivatorGeneticsHumansMolecular BiologyOsteosarcomaOrganelle BiogenesisbiologyEstradiolSettore BIO/16 - Anatomia UmanaChemistryElectron Transport Complex IICalcium-Binding ProteinsMembrane ProteinsPeroxisomeMitochondrial biogenesiPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaCell biology2-MethoxyestradiolMitochondriaSuccinate dehydrogenaseMolecular Docking Simulation030104 developmental biologyMitochondrial biogenesisSettore CHIM/03 - Chimica Generale E Inorganica030220 oncology & carcinogenesisSirtuinCancer cellbiology.proteinResearch ArticleCancer genomicsproteomics
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Lack of a peroxiredoxin suppresses the lethality of cells devoid of electron donors by channelling electrons to oxidized ribonucleotide reductase

2017

The thioredoxin and glutaredoxin pathways are responsible of recycling several enzymes which undergo intramolecular disulfide bond formation as part of their catalytic cycles such as the peroxide scavengers peroxiredoxins or the enzyme ribonucleotide reductase (RNR). RNR, the rate-limiting enzyme of deoxyribonucleotide synthesis, is an essential enzyme relying on these electron flow cascades for recycling. RNR is tightly regulated in a cell cycle-dependent manner at different levels, but little is known about the participation of electron donors in such regulation. Here, we show that cytosolic thioredoxins Trx1 and Trx3 are the primary electron donors for RNR in fission yeast. Unexpectedly,…

0301 basic medicineCancer ResearchThioredoxin reductaseSynthesis PhaseYeast and Fungal ModelsBiochemistryElectron DonorsSchizosaccharomyces PombeThioredoxinsGlutaredoxinCell Cycle and Cell DivisionGenetics (clinical)Chemical ReactionsOxidesPeroxidesNucleic acidsChemistryRibonucleotide reductaseBiochemistryExperimental Organism SystemsCell ProcessesSchizosaccharomyces pombePhysical SciencesSynthesis phaseThioredoxinOxidation-ReductionResearch ArticleDNA Replicationlcsh:QH426-470DNA transcriptionElectron donorsBiologyDNA replicationResearch and Analysis MethodsCatalysisElectron Transport03 medical and health sciencesModel OrganismsSchizosaccharomycesRibonucleotide ReductasesOxidationGeneticsMolecular BiologyEcology Evolution Behavior and SystematicsGlutaredoxinsCell growthDNA replicationChemical CompoundsOrganismsFungiBiology and Life SciencesCell BiologyDNAPeroxiredoxinsbiology.organism_classificationYeastCell cycle and cell divisionCheckpoint Kinase 2lcsh:Genetics030104 developmental biologySchizosaccharomyces pombeGene expressionSchizosaccharomyces pombe ProteinsPeroxiredoxin
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Palmitoylethanolamide Promotes a Proresolving Macrophage Phenotype and Attenuates Atherosclerotic Plaque Formation

2018

Objective— Palmitoylethanolamide is an endogenous fatty acid mediator that is synthetized from membrane phospholipids by N -acyl phosphatidylethanolamine phospholipase D. Its biological actions are primarily mediated by PPAR-α (peroxisome proliferator-activated receptors α) and the orphan receptor GPR55. Palmitoylethanolamide exerts potent anti-inflammatory actions but its physiological role and promise as a therapeutic agent in chronic arterial inflammation, such as atherosclerosis remain unexplored. Approach and Results— First, the polarization of mouse primary macrophages towards a proinflammatory phenotype was found to reduce N -acyl phosphatidylethanolamine phospholipase D expression …

0301 basic medicineCannabinoid receptorTime FactorsMice Knockout ApoECHOLESTEROL TRANSPORTAnti-Inflammatory AgentsPhospholipaseProto-Oncogene Maschemistry.chemical_compoundCannabinoid receptor type 2Receptors CannabinoidAortachemistry.chemical_classificationMARROW-DERIVED CELLSAPOPTOTIC CELL ACCUMULATIONPlaque AtheroscleroticCell biologymacrophagesDENSITY-LIPOPROTEIN RECEPTORPhenotypeREDUCES INFLAMMATIONCB2 RECEPTOREthanolaminesFemaleCardiology and Cardiovascular MedicineSCAVENGER RECEPTORAortic DiseasesPalmitic Acidsta3111fatty acidsCell Line03 medical and health sciencesMediatorPhagocytosisPhospholipase DAnimalsHumansScavenger receptorCANNABINOID RECEPTORPhosphatidylethanolaminePalmitoylethanolamidec-Mer Tyrosine KinaseFatty acidcholesterolta3121AmidesRatsMice Inbred C57BLDisease Models Animal030104 developmental biologychemistryinflammationRECEPTOR CLASS-BatherosclerosisCONTACT ALLERGIC DERMATITISArteriosclerosis Thrombosis and Vascular Biology
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