Search results for "Transport"

showing 10 items of 4457 documents

Biological and biophysics aspects of metformin-induced effects: cortex mitochondrial dysfunction and promotion of toxic amyloid pre-fibrillar aggrega…

2016

The onset of Alzheimer disease (AD) is influenced by several risk factors comprising diabetes. Within this context, antidiabetic drugs, including metformin, are investigated for their effect on AD. We report that in the C57B6/J mice, metformin is delivered to the brain where activates AMP-activated kinase (AMPK), its molecular target. This drug affects the levels of β- secretase (BACE1) and β-amyloid precursor protein (APP), promoting processing and aggregation of β-amyloid (Aβ), mainly in the cortex region. Moreover, metformin induces mitochondrial dysfunction and cell death by affecting the level and conformation of Translocase of the Outer Membrane 40 (TOM40), voltage-dependent anion-sel…

0301 basic medicineAgingmedicine.medical_specialtyMitochondrial poreAmyloidTranslocase of the outer membraneContext (language use)AMP-Activated Protein KinasesBiologyAmyloid beta-Protein PrecursorMice03 medical and health sciences0302 clinical medicineβ-amyloid aggregationAlzheimer DiseaseHexokinaseInternal medicine?-amyloid aggregationmitochondrial dysfunctionmedicineAnimalsHypoglycemic Agentsmitochondrial poresMitochondrial transportAmyloid beta-PeptidesVoltage-Dependent Anion Channel 1BrainAMPKcell degenerationCell BiologyAlzheimer's diseasemedicine.diseaseMitochondriaMetformin030104 developmental biologyEndocrinologyAmyloid Precursor Protein SecretasesAlzheimer's diseasemetforminVDAC1030217 neurology & neurosurgeryResearch Papermedicine.drug
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Subchronic vortioxetine treatment -but not escitalopram- enhances pyramidal neuron activity in the rat prefrontal cortex.

2017

Abstract Vortioxetine (VOR) is a multimodal antidepressant drug. VOR is a 5-HT 3 -R, 5-HT 7 -R and 5-HT 1D -R antagonist, 5-HT 1B -R partial agonist, 5-HT 1A -R agonist, and serotonin transporter (SERT) inhibitor. VOR shows pro-cognitive activity in animal models and beneficial effects on cognitive dysfunction in major depressive patients. Here we compared the effects of 14-day treatments with VOR and escitalopram (ESC, selective serotonin reuptake inhibitor) on neuronal activity in the medial prefrontal cortex (mPFC). Ten groups of rats (5 standard, 5 depleted of 5-HT with p -chlorophenylalanine -pCPA-, used as model of cognitive impairment) were fed with control food or with two doses of …

0301 basic medicineAgonistMalegenetic structuresmedicine.drug_classSerotonin reuptake inhibitorAction PotentialsPrefrontal CortexPharmacologyCitalopramSulfidesPartial agonistPiperazines03 medical and health sciencesCellular and Molecular Neuroscience0302 clinical medicinemedicinePremovement neuronal activityAnimalsRats WistarSerotonin transporterPharmacologyVortioxetinebiologyPyramidal CellsAntagonistAntidepressive AgentsRats030104 developmental biologybiology.proteinAntidepressantVortioxetinesense organsPsychologyNeuroscience030217 neurology & neurosurgerySelective Serotonin Reuptake InhibitorsNeuropharmacology
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Palmitoylation is a post-translational modification of Alix regulating the membrane organization of exosome-like small extracellular vesicles.

2018

Abstract Background Virtually all cell types have the capacity to secrete nanometer-sized extracellular vesicles, which have emerged in recent years as potent signal transducers and cell-cell communicators. The multifunctional protein Alix is a bona fide exosomal regulator and skeletal muscle cells can release Alix-positive nano-sized extracellular vesicles, offering a new paradigm for understanding how myofibers communicate within skeletal muscle and with other organs. S-palmitoylation is a reversible lipid post-translational modification, involved in different biological processes, such as the trafficking of membrane proteins, achievement of stable protein conformations, and stabilization…

0301 basic medicineAlix (also known as PDCD6IP)Protein ConformationLipoylationLipid BilayersBiophysicsSkeletal muscle cellsCell Cycle ProteinsExosomesBiochemistryExosomeTetraspanin 29Cell Line03 medical and health sciencesExtracellular VesiclesPalmitoylationTetraspaninExtracellularHumansLipid bilayerMuscle SkeletalMolecular BiologyCells CulturedEndosomal Sorting Complexes Required for TransportChemistryVesicleCalcium-Binding ProteinsCell MembraneExtracellular vesicleTetraspaninSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Cell biologyExosomeProtein Transport030104 developmental biologyS-palmitoylationMembrane proteinextracellular vesicles (EVs)Skeletal muscle cellProtein Processing Post-TranslationalProtein BindingSignal TransductionBiochimica et biophysica acta. General subjects
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Direct Sensing of Nutrients via a LAT1-like Transporter in Drosophila Insulin-Producing Cells

2016

Summary Dietary leucine has been suspected to play an important role in insulin release, a hormone that controls satiety and metabolism. The mechanism by which insulin-producing cells (IPCs) sense leucine and regulate insulin secretion is still poorly understood. In Drosophila, insulin-like peptides (DILP2 and DILP5) are produced by brain IPCs and are released in the hemolymph after leucine ingestion. Using Ca2+-imaging and ex vivo cultured larval brains, we demonstrate that IPCs can directly sense extracellular leucine levels via minidiscs (MND), a leucine transporter. MND knockdown in IPCs abolished leucine-dependent changes, including loss of DILP2 and DILP5 in IPC bodies, consistent wit…

0301 basic medicineAmino Acid Transport Systemsheavy-chainmedicine.medical_treatmentInsulinsamino acid transporter0302 clinical medicinegenetics [Drosophila Proteins]cytology [Drosophila melanogaster]Glutamate DehydrogenaseHemolymphInsulin-Secreting Cellsmetabolism [Drosophila melanogaster]HemolymphDrosophila;Drosophila insulin-like peptides;amino acid transporter;food;glutamate dehydrogenase;glycemia;growth;insulin-producing cells;minidiscs;starvationDrosophila ProteinsProtein Isoformsmetabolism [Calcium]genetics [Insulins]genetics [Amino Acid Transport Systems]lcsh:QH301-705.5minidiscsGene knockdowncytology [Larva]pancreatic beta-cellglutamate dehydrogenaseBrainmetabolism [Hemolymph]secretionDrosophila melanogasterBiochemistryLarvaAlimentation et NutritionDrosophilaLeucineSignal Transductionglucose-transportgenetics [Glutamate Dehydrogenase]genetics [Protein Isoforms]growthamino-acidsmetabolism [Drosophila Proteins][SDV.BC]Life Sciences [q-bio]/Cellular BiologyNutrient sensingmetabolism [Larva]Biologyinsulin-producing cellsArticleGeneral Biochemistry Genetics and Molecular Biologymetabolism [Amino Acid Transport Systems]metabolism [Insulins]03 medical and health sciencesLeucineparasitic diseasesmedicineFood and NutritionAnimalsddc:610cytology [Insulin-Secreting Cells]cardiovascular diseasesAmino acid transporterMnd protein Drosophilaadministration & dosage [Leucine]metabolism [Protein Isoforms]Ilp5 protein Drosophilacytology [Brain]foodGlutamate dehydrogenaseInsulinNeurosciencesstarvationGlucose transportermetabolism [Insulin-Secreting Cells]glutamate-dehydrogenasel-leucineglycemia030104 developmental biologyGene Expression Regulationlcsh:Biology (General)metabolism [Brain]metabolism [Glutamate Dehydrogenase]Neurons and Cognitionmetabolism [Leucine]CalciumDrosophila insulin-like peptidesmetabolismfat-cells030217 neurology & neurosurgeryCell Reports
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The Blood-Brain Barrier in Alzheimer’s Disease

2020

The accumulation of neurotoxic amyloid-beta (Aβ) in the brain is one of the characteristic hallmarks of Alzheimer's disease (AD). Aβ-peptide brain homeostasis is governed by its production and various clearance mechanisms. The blood-brain barrier provides a large surface area for influx and efflux mechanisms into and out of the brain. Different transporters and receptors have been implicated to play crucial roles in Aβ clearance from brain. Besides Aβ transport, the blood-brain barrier tightly regulates the brain's microenvironment; however, vascular alterations have been shown in patients with AD. Here, we summarize how the blood-brain barrier changes during aging and in disease and focus …

0301 basic medicineAmyloid beta-PeptidesChemistryBrainATP-binding cassette transporterTransporterBlood–brain barrierLRP1ArticlePeptide Fragments03 medical and health sciences030104 developmental biology0302 clinical medicinemedicine.anatomical_structureReceptors LDLAlzheimer DiseaseBlood-Brain BarriermedicineHumansEffluxReceptorNeuroscience030217 neurology & neurosurgeryHomeostasisLipoprotein
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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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