Search results for "Proteolipids"

showing 10 items of 10 documents

Pulmonary surfactant protein C containing lipid films at the air-water interface as a model for the surface of lung alveoli.

1995

The pulmonary surfactant lines as a complex monolayer of lipids and proteins the alveolar epithelial surface. The monolayer dynamically adapts the surface tension of this interface to the varying surface areas during inhalation and exhalation. Its presence in the alveoli is thus a prerequisite for a proper lung function. The lipid moiety represents about 90% of the surfactant and contains mainly dipalmitoylphosphatidylcholine (DPPC) and phosphatidylglycerol (PG). The surfactant proteins involved in the surface tension adaption are called SP-A, SP-B and SP-C. The aim of the present investigation is to analyse the properties of monolayer films made from pure SP-C and from mixtures of DPPC, DP…

LangmuirChemical PhenomenaSurface PropertiesProteolipidsLipid BilayersMolecular Sequence DataBiophysicsPalmitic AcidsBiophysical PhenomenaSurface tensionchemistry.chemical_compoundPulmonary surfactantEllipsometryMonolayerHumansPulmonary surfactant-associated protein CAmino Acid SequenceMolecular BiologyPhospholipidsPhosphatidylglycerolChemistryChemistry PhysicalAirtechnology industry and agricultureWaterMembranes ArtificialPulmonary SurfactantsCell BiologyLipid MetabolismLipidsPulmonary AlveoliCrystallographyChemical engineeringDipalmitoylphosphatidylcholinelipids (amino acids peptides and proteins)Protein BindingMolecular membrane biology
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Generation of proteoliposomes from subcellular fractions.

1998

Intracellular membranes are highly dynamic, yet they retain their identity and functional characteristics. Integral membrane proteins, which must confer this specific membrane identity, remain poorly characterized at the biochemical level, largely because detergent-mediated solubilization is required for purification and analysis, and several properties of integral membrane proteins can only be investigated when the molecule is properly embedded in a lipid bilayer. We present a method for the efficient reconstitution into proteoliposomes of integral membrane proteins from subcellular fractions. Integral membrane proteins were identified on high-resolution two-dimensional gels after selectiv…

ProteolipidsClinical BiochemistryPeripheral membrane proteinMembrane ProteinsBiological membraneIntracellular MembranesBiologyBiochemistryTransmembrane proteinAnalytical ChemistryCell LineMembrane proteinBiochemistryCricetinaeLiposomesMembrane fluidityAnimalsProtein–lipid interactionLipid bilayerIntegral membrane proteinSubcellular FractionsElectrophoresis
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Function of DcuS from Escherichia coli as a Fumarate-stimulated Histidine Protein Kinase in Vitro

2002

The two-component regulatory system DcuSR of Escherichia coli controls the expression of genes of C(4)-dicarboxylate metabolism in response to extracellular C(4)- dicarboxylates such as fumarate or succinate. DcuS is a membrane-integral sensor kinase, and the sensory and kinase domains are located on opposite sides of the cytoplasmic membrane. The intact DcuS protein (His(6)-DcuS) was overproduced and isolated in detergent containing buffer. His(6)-DcuS was reconstituted into liposomes made from E. coli phospholipids. Reconstituted His(6)-DcuS catalyzed, in contrast to the detergent-solubilized sensor, autophosphorylation by [gamma-(33)P]ATP with an approximate K(D) of 0.16 mm for ATP. Up t…

Time FactorsHistidine KinaseProteolipidsDetergentsBiologymedicine.disease_causeModels BiologicalBiochemistryAdenosine TriphosphateFumaratesEscherichia colimedicinePhosphorylationPromoter Regions GeneticProtein kinase AMolecular BiologyEscherichia coliDose-Response Relationship DrugKinaseEscherichia coli ProteinsCell MembraneAutophosphorylationDNACell BiologyTransmembrane proteinDNA-Binding ProteinsKineticsResponse regulatorBiochemistryLiposomesPhosphorylationSignal transductionProtein KinasesProtein BindingSignal TransductionTranscription FactorsJournal of Biological Chemistry
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Oligomeric Sensor Kinase DcuS in the Membrane of Escherichia coli and in Proteoliposomes: Chemical Cross-linking and FRET Spectroscopy

2010

The DcuSR (dicarboxylate uptake sensor and regulator) system of Escherichia coli is a typical two-component system consisting of a membranous sensor kinase (DcuS) and a cytoplasmic response regulator (DcuR) (11, 26, 48). DcuS responds to C4-dicarboxylates like fumarate, malate, or succinate (19). In the presence of the C4-dicarboxlates, the expression of the genes of anaerobic fumarate respiration (dcuB, fumB, and frdABCD) and of aerobic C4-dicarboxylate uptake (dctA) is activated. DcuS is a histidine protein kinase composed of two transmembrane helices with an intermittent sensory PAS domain in the periplasm (PASP) that was also termed the PDC domain (for PhoQ/DcuS/DctB/CitA domain or fold…

Escherichia coli ProteinsProteolipidsCell MembraneGreen Fluorescent ProteinsHistidine kinaseAutophosphorylationBiologyMicrobiologyLuminescent ProteinsResponse regulatorTransmembrane domainSpectrometry FluorescenceProtein kinase domainBiochemistryPAS domainEscherichia coliFluorescence Resonance Energy TransferKinase activityProtein kinase AProtein KinasesMolecular BiologySignal TransductionJournal of Bacteriology
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Neuroinflammation by cytotoxic T-lymphocytes impairs retrograde axonal transport in an oligodendrocyte mutant mouse.

2012

Mice overexpressing proteolipid protein (PLP) develop a leukodystrophy-like disease involving cytotoxic, CD8+ T-lymphocytes. Here we show that these cytotoxic T-lymphocytes perturb retrograde axonal transport. Using fluorogold stereotactically injected into the colliculus superior, we found that PLP overexpression in oligodendrocytes led to significantly reduced retrograde axonal transport in retina ganglion cell axons. We also observed an accumulation of mitochondria in the juxtaparanodal axonal swellings, indicative for a disturbed axonal transport. PLP overexpression in the absence of T-lymphocytes rescued retrograde axonal transport defects and abolished axonal swellings. Bone marrow tr…

Retinal Ganglion CellsProteolipid protein 1MouseCD8-Positive T-LymphocytesGranzymesMyelinMiceBone Marrow TransplantationNeuronsddc:616MultidisciplinarybiologyQRNeurodegenerative DiseasesAnimal ModelsCell biologyOligodendrogliamedicine.anatomical_structureNeurologyMedicineResearch ArticleHeterozygoteMultiple SclerosisProteolipidsScienceImmunologyMice Transgenicchemical and pharmacologic phenomenaAutoimmune DiseasesModel OrganismsmedicineAnimalsBiologyNeuroinflammationInflammationImmunityDemyelinating DisordersOligodendrocyteAxonsGranzyme BPerforinGranzymenervous systemImmune SystemImmunologyMutationAxoplasmic transportbiology.proteinClinical ImmunologyMolecular NeuroscienceT-Lymphocytes CytotoxicNeurosciencePLoS ONE
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Bax inhibitor-1 is likely a pH-sensitive calcium leak channel, not a H+/Ca2+ exchanger.

2014

The endoplasmic reticulum (ER) plays a key role in the synthesis, folding, and sorting of proteins, and disturbances of this delicate system can cause cell death. The ER also serves as the major intracellular calcium (Ca(2+)) store, and release of Ca(2+) from this store controls diverse cellular functions. At the interface of both these functions of the ER is Bax inhibitor-1 (BI-1), an evolutionarily conserved multifunctional protein that mediates Ca(2+) efflux from the ER and protects against ER stress. Several mechanisms have been proposed to explain how BI-1 might mediate Ca(2+) efflux from the ER. Chang et al. present structural evidence that a bacterial homolog of BI-1, BsYetJ, is a pH…

Programmed cell deathProtein familyProteolipidschemistry.chemical_elementCalciumBiologyEndoplasmic ReticulumBiochemistryModels BiologicalCalcium in biologySpecies SpecificityHumansMolecular BiologyBAX inhibitor 1Endoplasmic reticulumCell MembraneMembrane ProteinsCell BiologyHydrogen-Ion ConcentrationCell biologychemistryUnfolded protein responseCalciumEffluxCalcium ChannelsApoptosis Regulatory ProteinsBacillus subtilisScience signaling
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The stability and functional properties of proteoliposomes mixed with dextran derivatives bearing hydrophobic anchor groups

1992

Liposomes composed of Escherichia coli phospholipid were coated with polysaccharides bearing hydrophobic palmitoyl anchors. The effect on the stability of liposomes without or with integral membrane proteins was investigated. A high concentration of hydrophobized dextrans protected the liposomes against detergent degradation, decreased the fluidity of the membranes, prevented fusion of the liposomes and enhanced their stability. Proteoliposomes containing beef heart cytochrome-c oxidase and the lactose transport carrier of E. coli were similarly affected by coating with the dextrans. Under these conditions both membrane proteins were still active. Long-term stability of the coated liposomes…

PROTEINMembrane FusionBiochemistryMembrane Potentialschemistry.chemical_compoundFUSIONINTEGRAL MEMBRANE PROTEINBINDINGIntegral membrane proteinLiposomeSymportersEscherichia coli ProteinsVesiclePROTEOLIPOSOMEDextransDEXTRAN DERIVATIVEBIOLOGICAL-MEMBRANESFluoresceinsMembraneCarbohydrate SequenceESCHERICHIA-COLIMonosaccharide Transport ProteinsCations DivalentMembrane FluidityProteolipidsMolecular Sequence DataBiophysicsPhospholipidFluorescence PolarizationLactose transportOXIDASECYTOCHROME-CVESICLESElectron Transport Complex IVHYDROPHOBIC ANCHOR GROUPEscherichia coliAnimalsKINETICSChromatographyMyocardiumMembrane ProteinsMembrane Transport ProteinsBiological membraneCell BiologyPROTON-MOTIVE FORCEMembrane proteinchemistryLiposomesCalciumCattleBiochimica et Biophysica Acta (BBA) - Biomembranes
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Humoral autoreactivity directed against surfactant protein-A (SP-A) in rheumatoid arthritis synovial fluids.

2000

SUMMARY SP-A is found principally in the lung, and has been associated with lamellar bodies also found in the synovial joint. Both SP-A and C1q contain collagen-like regions, and SP-A and C1q have some structural similarities, both having a globular head region and a collagen-like tail. Here we are able to show that (i) autoreactivity to SP-A, as expressed by IgG and IgM autoantibodies, is present in synovial fluid (SF) isolated from patients with rheumatoid arthritis (RA); (ii) in absorption experiments only a limited degree of cross-reactivity between autoantibodies reactive with C1q and SP-A is observed; (iii) there is no cross-reactivity between autoantibodies reactive with type II coll…

Pulmonary Surfactant-Associated ProteinsKnee JointProteolipidsImmunologyType II collagenchemical and pharmacologic phenomenamedicine.disease_causeAutoantigensImmunoglobulin GAutoimmunityArthritis RheumatoidRheumatic DiseaseAntigenSynovial jointSynovial FluidmedicineImmunology and AllergySynovial fluidAnimalsHumansskin and connective tissue diseasesAutoantibodiesbiologyPulmonary Surfactant-Associated Protein AChemistryComplement C1qAutoantibodyPulmonary Surfactantsmedicine.anatomical_structureImmunoglobulin MImmunoglobulin MImmunoglobulin GImmunologybiology.proteinBinding Sites AntibodyCollagenPeptidesChickensDimerizationClinical and experimental immunology
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A critical role for the cholesterol-associated proteolipids PLP and M6B in myelination of the central nervous system.

2012

The formation of central nervous system myelin by oligodendrocytes requires sterol synthesis and is associated with a significant enrichment of cholesterol in the myelin membrane. However, it is unknown how oligodendrocytes concentrate cholesterol above the level found in nonmyelin membranes. Here, we demonstrate a critical role for proteolipids in cholesterol accumulation. Mice lacking the most abundant myelin protein, proteolipid protein (PLP), are fully myelinated, but PLP-deficient myelin exhibits a reduced cholesterol content. We therefore hypothesized that "high cholesterol" is not essential in the myelin sheath itself but is required for an earlier step of myelin biogenesis that is f…

Central Nervous SystemProteolipid protein 1Nerve Tissue ProteinsBiologyCell Line03 medical and health sciencesCellular and Molecular Neurosciencechemistry.chemical_compoundMyelinMice0302 clinical medicineimmune system diseasesmedicineEvoked Potentials Auditory Brain StemAnimalsMyelin Proteolipid ProteinMyelin Sheath030304 developmental biology0303 health sciencesMembrane GlycoproteinsCholesterolProteolipidsLeukodystrophyPelizaeus–Merzbacher diseasemedicine.diseaseOligodendrocytenervous system diseasesMyelin proteolipid proteinmedicine.anatomical_structureCholesterolnervous systemNeurologychemistryBiochemistryEvoked Potentials Visuallipids (amino acids peptides and proteins)Vomeronasal Organ030217 neurology & neurosurgeryGlia
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Effect of transfection with PLP2 antisense oligonucleotides on gene expression of cadmium-treated MDA-MB231 breast cancer cells

2012

Emerging evidence indicates that cadmium (Cd) is able to regulate gene expression, drastically affecting the pattern of transcriptional activity in human normal and pathological cells. We have already shown that exposure of MDA-MB231 breast cancer cells to 5 μM CdCl(2) for 96 h, apart from significantly affecting mitochondrial metabolism, induces modifications of the expression level of genes coding for members of stress response-, mitochondrial respiration-, MAP kinase-, NF-κB-, and apoptosis-related pathways. In the present study, we have expanded the knowledge on the biological effects of Cd-breast cancer cell interactions, indicating PLP2 (proteolipid protein-2) as a novel member of the…

ProteolipidsApoptosisBreast NeoplasmsTransfectionBiochemistryAnalytical ChemistryCadmium ChlorideStress PhysiologicalCell Line TumorGene expressionHumansRNA MessengerSettore BIO/06 - Anatomia Comparata E Citologiaskin and connective tissue diseasesGeneCaspaseHeat-Shock ProteinsMARVEL Domain-Containing Proteinsbiologycadmium PLP2 breast cancer differential display-PCR caspase gene expressionTransfectionSuicide geneOligonucleotides AntisenseMolecular biologyGene Expression Regulation NeoplasticApoptosisMitogen-activated protein kinaseCaspasesCancer cellbiology.proteinNucleic Acid ConformationFemale
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