Search results for "lipid raft"

showing 10 items of 65 documents

Actin Filaments Are Involved in the Coupling of V0-V1 Domains of Vacuolar H+-ATPase at the Golgi Complex*

2016

We previously reported that actin-depolymerizing agents promote the alkalization of the Golgi stack and the trans-Golgi network. The main determinant of acidic pH at the Golgi is the vacuolar-type H+-translocating ATPase (V-ATPase), whose V1 domain subunits B and C bind actin. We have generated a GFP-tagged subunit B2 construct (GFP-B2) that is incorporated into the V1 domain, which in turn is coupled to the V0 sector. GFP-B2 subunit is enriched at distal Golgi compartments in HeLa cells. Subcellular fractionation, immunoprecipitation, and inversal FRAP experiments show that the actin depolymerization promotes the dissociation of V1-V0 domains, which entails subunit B2 translocation from Go…

0301 basic medicineVacuolar Proton-Translocating ATPasesGolgi ApparatusBiologyMicrofilamentBiochemistry03 medical and health sciencessymbols.namesakeCytosolHumansActin-binding proteinMolecular BiologyLipid raftActinGolgi membraneCell BiologyIntracellular MembranesGolgi apparatusHydrogen-Ion ConcentrationActin cytoskeletonCell biologyProtein Structure TertiaryCytosolActin Cytoskeleton030104 developmental biologysymbolsbiology.proteinHeLa Cells
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Pantethine Alters Lipid Composition and Cholesterol Content of Membrane Rafts, With Down-Regulation of CXCL12-Induced T Cell Migration

2015

Pantethine, a natural low-molecular-weight thiol, shows broad activity in a large range of essential cellular pathways. It has been long known as a hypolipidemic and hypocholesterolemic agent. We showed recently that it exerts a neuroprotective action in mouse models of cerebral malaria and Parkinson's disease through multiple mechanisms. In the present study we looked at its effects on membrane lipid rafts that serve as platforms for molecules engaged in cell activity, therefore providing a target against inappropriate cell response leading to chronic inflammation. We found that pantethine-treated cells showed a significant change in raft fatty acid composition and cholesterol content, wit…

0303 health sciencesCell signalingPhysiologyT cellPantethineClinical BiochemistryCellLinker for Activation of T cellsCell BiologyBiologyJurkat cells3. Good healthCell biology03 medical and health scienceschemistry.chemical_compound0302 clinical medicinemedicine.anatomical_structurechemistrymedicineCell adhesionLipid raft030217 neurology & neurosurgery030304 developmental biologyJournal of Cellular Physiology
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Viral entry, lipid rafts and caveosomes.

2005

Lipid rafts and caveolae are detergent-insoluble plasma membrane microdomains, involved in cellular endocytic processes and signalling. Several viruses, including a human pathogen, echovirus 1, and an extensively studied simian virus 40 utilize these domains for internalization into the host cells. Interaction of viruses with receptors on the cell surface triggers specific conformational changes of the virus particle and can give rise to signalling events, which determine the mechanisms of virus entry. After internalization via cell surface lipid rafts or caveolae, virus-containing vesicles can fuse with caveosomes, pre-existing cytoplasmic organelles, or dock on other intracellular organel…

0303 health sciencesvirusesmedia_common.quotation_subject030302 biochemistry & molecular biologyEndocytic cycleGeneral MedicineSimian virus 40BiologyEndocytosisEndocytosis3. Good healthCell biologyEnterovirus B Human03 medical and health sciencesMembrane MicrodomainsViral replicationCytoplasmViral entryCaveolaeInternalizationLipid raft030304 developmental biologymedia_commonAnnals of medicine
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Statins and the squalene synthase inhibitor zaragozic acid stimulate the non-amyloidogenic pathway of amyloid-beta protein precursor processing by su…

2010

Cholesterol-lowering drugs such as statins influence the proteolytic processing of the amyloid-beta protein precursor (AbetaPP) and are reported to stimulate the activity of alpha-secretase, the major preventive secretase of Alzheimer's disease. Statins can increase the alpha-secretase activity by their cholesterol-lowering properties as well as by impairment of isoprenoids synthesis. In the present study, we elucidate the contribution of these pathways in alpha-secretase activation. We demonstrate that zaragozic acid, a potent inhibitor of squalene synthase which blocks cholesterol synthesis but allows synthesis of isoprenoids, also stimulates alpha-secretase activity. Treatment of human n…

ADAM10Blotting Westernchemistry.chemical_compoundSqualeneADAM10 ProteinAmyloid beta-Protein PrecursorCell Line TumormedicineHumansLovastatinRNA Small InterferingProtein precursorLuciferasesLipid raftNeuronsbiologyATP synthaseChemistryReverse Transcriptase Polymerase Chain ReactionTerpenesGeneral NeuroscienceAnticholesteremic AgentsCell MembraneMembrane ProteinsTricarboxylic AcidsZaragozic acidGeneral MedicineBridged Bicyclo Compounds HeterocyclicEnzyme ActivationPsychiatry and Mental healthClinical PsychologyADAM ProteinsCholesterolFarnesyl-Diphosphate FarnesyltransferaseBiochemistrybiology.proteinlipids (amino acids peptides and proteins)LovastatinGeriatrics and GerontologyAmyloid Precursor Protein SecretasesHydroxymethylglutaryl-CoA Reductase InhibitorsAmyloid precursor protein secretasemedicine.drugJournal of Alzheimer's disease : JAD
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Pravastatin reverses the membrane cholesterol reorganization induced by myocardial infarction within lipid rafts in CD14(+)/CD16(-) circulating monoc…

2012

International audience; Large numbers of monocytes are recruited in the infarcted myocardium. Their cell membranes contain cholesterol-rich microdomains called lipids rafts, which participate in numerous signaling cascades. In addition to its cholesterol-lowering effect, pravastatin has several pleiotropic effects and is widely used as secondary prevention treatment after myocardial infarction (MI). The aim of this study was to investigate the effects of pravastatin on the organization of cholesterol within monocyte membrane rafts from patients who had suffered myocardial infarction. Monocytes from healthy donors and acute MI patients were cultured with or without 4μM pravastatin. Lipid raf…

AdultMalemedicine.medical_specialtyStatinmedicine.drug_classCD14[ SDV.AEN ] Life Sciences [q-bio]/Food and NutritionCaveolin 1Lipopolysaccharide Receptors030204 cardiovascular system & hematologyCD16GPI-Linked ProteinsMonocytes03 medical and health scienceschemistry.chemical_compound0302 clinical medicineCaveolaeInternal medicinemedicineHumansMolecular BiologyLipid raftCells Cultured030304 developmental biologyPravastatin0303 health sciencesCholesterolMonocyteAnticholesteremic AgentsReceptors IgGstatinCell BiologyMiddle Aged3. Good healthlipid raftEndocrinologymedicine.anatomical_structureCholesterolmyocardial infarctionchemistryGene Expression RegulationImmunologycaveolaemonocyteFemalelipids (amino acids peptides and proteins)[SDV.AEN]Life Sciences [q-bio]/Food and NutritionPravastatinmedicine.drug
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Duck Hepatitis B Virus Requires Cholesterol for Endosomal Escape during Virus Entry

2008

ABSTRACT The identity and functionality of biological membranes are determined by cooperative interaction between their lipid and protein constituents. Cholesterol is an important structural lipid that modulates fluidity of biological membranes favoring the formation of detergent-resistant microdomains. In the present study, we evaluated the functional role of cholesterol and lipid rafts for entry of hepatitis B viruses into hepatocytes. We show that the duck hepatitis B virus (DHBV) attaches predominantly to detergent-soluble domains on the plasma membrane. Cholesterol depletion from host membranes and thus disruption of rafts does not affect DHBV infection. In contrast, depletion of chole…

AvihepadnavirusbiologyvirusesImmunologyDuck hepatitis B virusBiological membraneEndosomesVirus Internalizationbiology.organism_classificationMicrobiologyVirologyVirusHepatitis B Virus DuckVirus-Cell InteractionsCholesterolViral envelopeHepadnaviridaeViral entryCell Line TumorVirologyInsect ScienceHepatocytesHumanslipids (amino acids peptides and proteins)Lipid raftJournal of Virology
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Comparative lipidomics and proteomics analysis of platelet lipid rafts using different detergents

2016

Lipid rafts play a pivotal role in physiological functions of platelets. Their isolation using nonionic mild detergents is considered as the gold standard method, but there is no consensual detergent for lipid raft studies. We aimed to investigate which detergent is the most suitable for lipid raft isolation from platelet membrane, based on lipidomics and proteomics analysis. Platelets were obtained from healthy donors. Twelve sucrose fractions were extracted by three different detergents, namely Brij 35, Lubrol WX, and Triton X100, at 0.05% and 1%. After lipidomics analysis and determination of fractions enriched in cholesterol (Ch) and sphingomyelin (SM), proteomics analysis was performed…

Blood Platelets0301 basic medicineProteome[SDV]Life Sciences [q-bio]Detergents030204 cardiovascular system & hematologyProteomics03 medical and health scienceschemistry.chemical_compoundMembrane Microdomains0302 clinical medicineproteomicsLipidomicsCentrifugation Density GradientHumansLipid raftlipid rafts[ SDV ] Life Sciences [q-bio]ChemistryCholesterolMembrane ProteinsHematologyGeneral MedicineLipids6. Clean water030104 developmental biologyMembraneBiochemistryMembrane proteinProteomeplateletslipidomicslipids (amino acids peptides and proteins)Sphingomyelin
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Impact of ticagrelor on P2Y1 and P2Y12 localization and on cholesterol levels in platelet plasma membrane

2017

Ticagrelor is an antiplatelet agent that inhibits platelet activation via P2Y12 antagonism. There are several studies showing that P2Y12 needs lipid rafts to be activated, but there are few data about how ticagrelor impacts lipid raft organization. Therefore, we aimed to investigate how ticagrelor could impact the distribution of cholesterol and consequently alter the organization of lipid rafts on platelet plasma membranes. We identified cholesterol-enriched raft fractions in platelet membranes by quantification of their cholesterol levels. Modifications in cholesterol and protein profiles (Flotillin 1, Flotillin 2, CD36, P2Y1, and P2Y12) were studied in platelets stimulated by ADP, treate…

Blood Platelets0301 basic medicineTicagrelorAdenosineCD36030204 cardiovascular system & hematologyPharmacologyReceptors Purinergic P2Y103 medical and health scienceschemistry.chemical_compoundMembrane Microdomains0302 clinical medicineP2Y12medicineHumansPlateletPlatelet activationLipid raftbiologyChemistryCholesterolCell MembraneHematologyGeneral MedicineReceptors Purinergic P2Y12Cholesterol030104 developmental biologyMembraneBiochemistryPurinergic P2Y Receptor Antagonistsbiology.proteinlipids (amino acids peptides and proteins)Ticagrelormedicine.drugPlatelets
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Plasma membrane and lysosomal localization of CB1 cannabinoid receptor are dependent on lipid rafts and regulated by anandamide in human breast cance…

2005

AbstractIn this report we show, by confocal analysis of indirect immunofluorescence, that the type-1 cannabinoid receptor (CB1R), which belongs to the family of G-protein-coupled receptors, is expressed on the plasma membrane in human breast cancer MDA-MB-231 cells. However, a substantial proportion of the receptor is present in lysosomes. We found that CB1R is associated with cholesterol- and sphyngolipid-enriched membrane domains (rafts). Cholesterol depletion by methyl-β-cyclodextrin (MCD) treatment strongly reduces the flotation of the protein on the raft-fractions (DRM) of sucrose density gradients suggesting that CB1 raft-association is cholesterol dependent. Interestingly binding of …

CB1 receptorCannabinoid receptorMESH: Membrane MicrodomainsMESH: Receptor Cannabinoid CB1Biochemistrychemistry.chemical_compoundRaftsMESH: Cholesterol0302 clinical medicineReceptor Cannabinoid CB1Structural BiologyReceptorLipid raft0303 health sciencesChemistrybeta-CyclodextrinsAnandamideEndocannabinoid system3. Good healthCell biologyCholesterollipids (amino acids peptides and proteins)AgonistMESH: beta-CyclodextrinsMESH: Cell Line TumorPolyunsaturated Alkamidesmedicine.drug_classBiophysicsBreast NeoplasmsArachidonic Acids03 medical and health sciencesMembrane MicrodomainsCell Line TumorGeneticsmedicineMESH: Arachidonic AcidsHumansMolecular Biology030304 developmental biologyG protein-coupled receptorMESH: HumansMESH: Polyunsaturated AlkamidesCell Membrane[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyAnandamideCell BiologyCaveolin 1LysosomesIntracellular traffickingMESH: Breast Neoplasms030217 neurology & neurosurgeryMESH: Cell MembraneMESH: LysosomesEndocannabinoids
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CD95 DISC formation and internalizzation occur in lipid rafts of typeI and typeII cells

2004

We investigated the membrane localization of CD95 in type I and type II cells, which differ in their ability to recruit and activate caspase-8. We found that CD95 was preferentially located in lipid rafts of type I cells, while it was present both in raft and non-raft plasma membrane sub-domains of type II cells. After stimulation, CD95 located in phospholipid-rich plasma membrane was recruited to lipid rafts in both types of cells. Similarly, CD95 cross-linking resulted in caspase-independent translocation of FADD/MORT1 and caspase-8 to the lipid rafts, which was prevented by a death domain-defective receptor. CD95 internalization was then rapid in type I and delayed in type II cells and s…

CD95Caspase-8Lipid rafts
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