Search results for "Endosomes"

showing 9 items of 39 documents

Entry of Human Parechovirus 1

2001

ABSTRACT Human parechovirus 1 (HPEV-1) is a prototype member of parechoviruses, a recently established picornavirus genus. Although there is preliminary evidence that HPEV-1 recognizes α V integrins as cellular receptors, our understanding of early events during HPEV-1 infection is still very limited. The aim of this study was to clarify the entry mechanisms of HPEV-1, including the attachment of the virus onto the host cell surface and subsequent internalization. In blocking experiments with monoclonal antibodies against different receptor candidates, antibodies against α V and β 3 integrin subunits, in particular in combination, appeared to be the most efficient ones in preventing the HPE…

PicornavirusEndosomeImmunologyEndocytic cycleGolgi ApparatusHuman parechovirus 1EndosomesPicornaviridaePlatelet Membrane GlycoproteinsEndoplasmic ReticulumVirus ReplicationCaveolinsMicrobiologyClathrinEEA103 medical and health sciencessymbols.namesakeCapsidAntigens CDVirologyTumor Cells CulturedHumans030304 developmental biologyHost cell surface0303 health sciencesbiology030302 biochemistry & molecular biologyIntegrin beta3Clathrin-Coated VesiclesIntegrin alphaVGolgi apparatusbiology.organism_classificationVirologyClathrinEndocytosisVirus-Cell Interactions3. Good healthCell biologyInsect Sciencesymbolsbiology.proteinReceptors VirusJournal of Virology
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Clustering induces a lateral redistribution of α2β1 integrin from membrane rafts to caveolae and subsequent protein kinase C-dependent internalization

2004

Integrin alpha 2 beta 1 mediates the binding of several epithelial and mesenchymal cell types to collagen. The composition of the surrounding plasma membrane, especially caveolin-1- and cholesterol-containing membrane structures called caveolae, may be important to integrin signaling. On cell surface alpha 2 beta 1 integrin was located in the raft like membrane domain, rich in GPI-anchored proteins, rather than in caveolae. However, when antibodies were used to generate clusters of alpha 2 beta 1 integrin, they started to move laterally on cell surface along actin filaments. During the lateral movement small clusters fused together. Finally alpha 2 beta 1 integrin was found inside caveolae …

Protein Kinase C-alphaEndosomeintegrinkinasemedia_common.quotation_subjectCaveolin 1IntegrinCoated VesiclesEndosomesCaveolaeCaveolinsCell Membrane StructuresCD49cCollagen receptorCell membraneCaveolaemedicineHumansantibodiesMicroscopy ImmunoelectronInternalizationMolecular BiologyCells CulturedProtein Kinase Cmedia_commonbiologyCell MembraneArticlesCell BiologyIntegrin alphaVproteinsEnterovirus B HumanCell biologyActin Cytoskeletonmedicine.anatomical_structureIntegrin alphaVcaveolaebiology.proteinIntegrin alpha2beta1
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Lipid presentation by the protein C receptor links coagulation with autoimmunity.

2021

A lipid-protein autoimmunity target Several autoimmune diseases, including systemic lupus erythematosus and primary antiphospholipid syndrome, are characterized by the presence of antiphospholipid antibodies (aPLs). These molecules can activate the complement and coagulation cascades, which contributes to pathologies such as thrombosis, stroke, and pregnancy complications. Müller-Calleja et al. found that endothelial protein C receptor (EPCR) in complex with lysobisphosphatidic acid (LBPA) is the cell-surface target for aPL and mediates its internalization (see the Perspective by Kaplan). aPL binding to EPCR-LBPA resulted in the activation of tissue factor–mediated coagulation and interfero…

Receptor complexAntigen presentationAutoimmunityEndosomesmedicine.disease_causeArticleAutoimmunityMiceInterferonimmune system diseasesmedicineAnimalsHumansLupus Erythematosus SystemicneoplasmsBlood CoagulationAutoantibodiesAutoimmune diseaseEndothelial protein C receptorAntigen PresentationMultidisciplinaryInnate immune systemLupus erythematosusEndothelial Protein C ReceptorThrombosismedicine.diseaseAntiphospholipid SyndromeImmunity InnateMice Mutant StrainsDisease Models AnimalSphingomyelin PhosphodiesteraseToll-Like Receptor 7ImmunologyAntibodies AntiphospholipidEmbryo LossMonoglyceridesEndothelium VascularLysophospholipidsmedicine.drugScience (New York, N.Y.)
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Reconstitution of vesicular transport to Rab11-positive recycling endosomes in vitro.

2003

Rab GTPases are key regulators of vesicular protein transport in both the endocytic and exocytic pathways. In endocytosis and recycling, Rab11 plays a role in receptor recycling to plasma membrane via the pericentriolar recycling compartment. However, little is known about the molecular requirements and partners that promote transport through Rab11-positive recycling endosomes. Here, we report a novel approach to reconstitute transport to immunoabsorbed recycling endosomes in vitro. We show that transport is temperature-, energy-, and time-dependent and requires the presence of Rab proteins, as it is inhibited by the Rab-interacting protein Rab GDP-dissociation inhibitor that removes Rab pr…

Receptor recyclingCytochalasin DEndosomeEndocytic cycleBiophysicsVesicular Transport ProteinsCHO CellsEndosomesEndocytosisBiochemistryCricetulusCricetinaeReceptors TransferrinAnimalsVesicular Protein TransportTransport VesiclesMolecular BiologyGuanine Nucleotide Dissociation InhibitorsChemistryCell BiologyActin cytoskeletonAdaptation PhysiologicalCell biologyVesicular transport proteinProtein Transportrab GTP-Binding ProteinsRabBiochemical and biophysical research communications
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Elimination of a bacterial pore-forming toxin by sequential endocytosis and exocytosis

2008

Staphylococcus aureus alpha-toxin is the archetype of bacterial pore forming toxins and a key virulence factor secreted by the majority of clinical isolates of S. aureus. Toxin monomers bind to target cells and oligomerize to form small beta-barrel pores in the plasma membrane. Many nucleated cells are able to repair a limited number of lesions by unknown, calcium-independent mechanisms. Here we show that cells can internalize alpha-toxin, that uptake is essential for cellular survival, and that pore-complexes are not proteolytically degraded, but returned to the extracellular milieu in the context of exosome-like structures, which we term toxosomes.

Staphylococcus aureusEndosomeBacterial ToxinsBiophysicsEndosomesBiologyEndocytosisHemolysin ProteinsBiochemistryα-ToxinExocytosisVirulence factorExocytosisCell LineHemolysin ProteinsStructural BiologyNucleated cellChlorocebus aethiopsGeneticsExtracellularAnimalsHumansMolecular BiologyCell NucleusBacterial pore forming toxinPore-forming toxinInnate defence mechanismCell BiologyEndocytosisCell biologyExosomeBiochemistryCOS CellsMutationMacrolidesFEBS Letters
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A subunit of eukaryotic translation initiation factor 2α-phosphatase (CreP/PPP1R15B) regulates membrane traffic.

2012

The constitutive reverter of eIF2α phosphorylation (CReP)/PPP1r15B targets the catalytic subunit of protein phosphatase 1 (PP1c) to phosphorylated eIF2α (p-eIF2α) to promote its dephosphorylation and translation initiation. Here, we report a novel role and mode of action of CReP. We found that CReP regulates uptake of the pore-forming Staphylococcus aureus α-toxin by epithelial cells. This function was independent of PP1c and translation, although p-eIF2α was involved. The latter accumulated at sites of toxin attack and appeared conjointly with α-toxin in early endosomes. CReP localized to membranes, interacted with phosphomimetic eIF2α, and, upon overexpression, induced and decorated a pop…

Staphylococcus aureusanimal structuresEndosomePopulationPhosphataseBacterial ToxinsEukaryotic Initiation Factor-2EndosomesBiologyBiochemistryExocytosisProtein Structure SecondaryEukaryotic translationProtein Phosphatase 1Initiation factorAnimalsHumansPhosphorylationeducationPeptide Chain Initiation TranslationalMolecular Biologyeducation.field_of_studyCell MembraneTranslation (biology)Epithelial CellsCell BiologyCell biologyProtein Structure TertiaryProtein TransportPhosphorylationRabbitsK562 CellsThe Journal of biological chemistry
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Capture of extracellular zinc ions by astrocytes.

2006

Synaptic zinc ions released during synaptic transmission interact with pre- and postsynaptic neuroreceptors, thus modulating neurotransmission. It is likely that they have to be efficiently cleared from the extracellular milieu to assure subsequent synaptic events. Both neurons and glia are assumed to participate in this clearance by mechanisms that are not fully understood. In this study, electron microscopic zinc cytochemistry has shown zinc-electrondense particles associated with hippocampal astrocytic membranes frequently found accumulated in stacked lamellae. In cultured astrocytes, the use of zinc fluorochromes and endocytic markers allowed the simultaneous imaging of the capture of e…

SucroseEndosomeEndocytic cyclechemistry.chemical_elementZincEndosomesNeurotransmissionBiologyCellular and Molecular NeuroscienceGlial Fibrillary Acidic ProteinmedicineExtracellularAnimalsHomeostasisCells CulturedOrganellesDose-Response Relationship DrugImmunohistochemistryMicroscopy ElectronZincmedicine.anatomical_structureNeurologychemistryAstrocytesBiophysicsCytochemistryNeurogliaRabbitsExtracellular SpaceNeuroscienceAstrocyteGlia
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Interactions of silica nanoparticles with lung epithelial cells and the association to flotillins

2012

Amorphous silica nanoparticles (aSNPs) gain increasing popularity for industrial and therapeutic claims. The lung with its surface area of 100-140 m(2) displays an ideal target for therapeutic approaches, but it represents also a serious area of attack for harmful nanomaterials. The exact nature of the cytotoxic effects of NPs is still unknown. Furthermore, cellular pathways and the destiny of internalized NPs are still poorly understood. Therefore, we examined the cytotoxicity (MTS, LDH) and inflammatory responses (IL-8) for different-sized aSNPs (30, 70, 300 nm) on our lung epithelial cells line NCI H441 and endothelial cell line ISO-HAS-1. Additionally, colocalization studies have been c…

Time FactorsEndosomeCell SurvivalHealth Toxicology and MutagenesisEndothelial cellsCytotoxicityEndosomessilica nanoparticlesToxicologyEndocytosisTransfectionClathrinFlotillin-1siliciumFlotillin-2Alveolar-capillary barrierCell Line TumorAlveolar capillary barrierHumansInterleukin 8Inorganic CompoundsParticle SizeCytotoxicityLungbiologyDose-Response Relationship DrugL-Lactate DehydrogenaseInterleukin-8Membrane ProteinsInflammatory responseEpithelial CellsGeneral MedicineTransfectionSilicon DioxideEndocytosisCell biologyLung epithelial cellsEndothelial stem cellEndocytic vesiclebiology.proteinNanoparticlesRNA InterferenceInflammation Mediators
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Infectious Entry Pathway of Enterovirus B Species

2015

Enterovirus B species (EV-B) are responsible for a vast number of mild and serious acute infections. They are also suspected of remaining in the body, where they cause persistent infections contributing to chronic diseases such as type I diabetes. Recent studies of the infectious entry pathway of these viruses revealed remarkable similarities, including non-clathrin entry of large endosomes originating from the plasma membrane invaginations. Many cellular factors regulating the efficient entry have recently been associated with macropinocytic uptake, such as Rac1, serine/threonine p21-activated kinase (Pak1), actin, Na/H exchanger, phospholipace C (PLC) and protein kinase Cα (PKCα). Another…

coxsackievirus A9EchovirusEndosomelcsh:QR1-502Virus AttachmentEndosomesReviewCoxsackievirusEndocytosismedicine.disease_causelcsh:Microbiology03 medical and health sciencesVirologymedicineReceptorProtein kinase A030304 developmental biology0303 health sciencesbiologyKinase030302 biochemistry & molecular biologyechovirusVirus Internalizationbiology.organism_classificationVirologyEndocytosisEnterovirus B Human3. Good healthCell biologyInfectious DiseasesHost-Pathogen InteractionsEnterovirusentrycoxsackievirus B3signalingViruses
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