Search results for "Phosphatidylinositols"

showing 10 items of 20 documents

p24 Family Proteins Are Involved in Transport to the Plasma Membrane of GPI-Anchored Proteins in Plants

2020

p24 proteins are a family of type-I membrane proteins that cycle between the endoplasmic reticulum (ER) and the Golgi apparatus via Coat Protein I (COPI)- and COPII-coated vesicles. These proteins have been proposed to function as cargo receptors, but the identity of putative cargos in plants is still elusive. We previously generated an Arabidopsis (Arabidopsis thaliana) quadruple loss-of-function mutant affecting p24 genes from the δ-1 subclass of the p24 delta subfamily (p24δ3δ4δ5δ6 mutant). This mutant also had reduced protein levels of other p24 family proteins and was found to be sensitive to salt stress. Here, we used this mutant to test the possible involvement of p24 proteins in the…

0106 biological sciencesGenotypePhysiologyGlycosylphosphatidylinositolsMutantArabidopsisGolgi ApparatusPlant ScienceEndoplasmic Reticulum01 natural sciencessymbols.namesakeArabidopsisGeneticsArabidopsis thalianaResearch ArticlesbiologyChemistryArabidopsis ProteinsVesicleEndoplasmic reticulumCell MembraneGenetic VariationMembrane ProteinsCOPIGolgi apparatusbiology.organism_classificationCell biologyProtein TransportMembrane proteinMutationsymbols010606 plant biology & botany
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Identification of Candida auris and related species by multiplex PCR based on unique GPI protein‐encoding genes

2020

Background The pathogen Candida auris is rapidly gaining clinical importance because of its resistance to antifungal treatments and its persistence in hospital environments. Early and accurate diagnosis of C. auris infections is crucial, however, the fungus has often been misidentified by commercial systems. Objectives To develop conventional and real-time PCR methods for accurate and rapid identification of C. auris and its discrimination from closely related species by exploiting the uniqueness of certain glycosylphosphatidylinositol-modified protein-encoding genes. Methods Species-specific primers for two unique putative GPI protein-encoding genes per species were designed for C. auris, …

0301 basic medicineAntifungal AgentsGlycosylphosphatidylinositolsGenes Fungal030106 microbiologyDermatologyBiologyReal-Time Polymerase Chain ReactionFungal Proteins030207 dermatology & venereal diseases03 medical and health sciences0302 clinical medicineSpecies SpecificityMultiplex polymerase chain reactionHumansMultiplexMycological Typing TechniquesGenePathogenCandidaDNA PrimersGeneticsCandidiasisReproducibility of ResultsGeneral MedicineAmpliconCorpus albicansInfectious DiseasesCandida aurisIndansIdentification (biology)Multiplex Polymerase Chain ReactionMycoses
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Plasma and fibroblasts of Tangier disease patients are disturbed in transferring phospholipids onto apolipoprotein A-I

1998

Plasmas of patients with Tangier disease (TD) lack lipid-rich α-HDL which, in normal plasma, constitutes the majority of high density lipoprotein (HDL). Residual amounts of apolipoprotein (apo)A-I in TD plasma occur as lipid-poor or even lipid-free preβ-HDL. By contrast to normal plasma, TD plasma does not convert preβ-HDL into α-HDL. Moreover, fibroblasts of TD patients were found to be defective in secreting cholesterol or phospholipids in the presence of lipid-free apoA-I. We have therefore hypothesized that both defective conversion of preβ-HDL into α-HDL and defective lipid efflux from TD cells onto lipid-free apoA-I result from a disturbance in phospholipid transfer occurring in both …

AdultMaletransferring phospholipidsPhospholipidTangier diseasePhosphatidic AcidsQD415-436PhosphatidylinositolsBiochemistrychemistry.chemical_compoundEndocrinologyTangier diseasePhosphatidylcholinePhospholipid transfer proteinExtracellularmedicineHumansCells CulturedPhosphatidylethanolamineApolipoprotein A-ICholesterolPhosphatidylethanolaminesReverse cholesterol transportnutritional and metabolic diseasesBiological TransportCell BiologyFibroblastsmedicine.diseaseMolecular biologyfamilial HDL deficiencyreverse cholesterol transportLipoproteins LDLphospholipid transfer proteinsprebeta-HDLTangier disease; transferring phospholipidschemistryPhosphatidylcholinesFemalelipids (amino acids peptides and proteins)cholesterol efflux
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Identification of a mannoprotein present in the inner layer of the cell wall of Saccharomyces cerevisiae.

1997

Cell wall extracts from the double-mutant mnn1 mnn9 strain were used as the immunogen to obtain a monoclonal antibody (MAb), SAC A6, that recognizes a specific mannoprotein--which we have named Icwp--in the walls of cells of Saccharomyces cerevisiae. Icwp runs as a polydisperse band of over 180 kDa in sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of Zymolyase extracts of cell walls, although an analysis of the secretory pattern of the mannoprotein shows that at the level of secretory vesicles, it behaves like a discrete band of 140 kDa. Immunofluorescence analysis with the MAb showed that Icwp lies at the inner layer of the cell wall, being accessible to the antibody on…

Antigens FungalDNA ComplementarySaccharomyces cerevisiae ProteinsGlycosylphosphatidylinositolsSaccharomyces cerevisiaeGenes FungalMolecular Sequence DataSaccharomyces cerevisiaeCalcofluor-whiteBiologyMicrobiologySerineCell wallFungal Proteinschemistry.chemical_compoundCell WallThreonineMolecular BiologyGel electrophoresisMembrane GlycoproteinsBase SequenceAntibodies MonoclonalTunicamycinbiology.organism_classificationMolecular biologycarbohydrates (lipids)Open reading frameMutagenesis InsertionalchemistryBiochemistryResearch Article
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Interaction of Neuronal Calcium Sensor-1 (NCS-1) with Phosphatidylinositol 4-Kinase β Stimulates Lipid Kinase Activity and Affects Membrane Trafficki…

2001

Phosphatidylinositol 4-kinases (PI4K) catalyze the first step in the synthesis of phosphatidylinositol 4,5-bisphosphate, an important lipid regulator of several cellular functions. Here we show that the Ca(2+)-binding protein, neuronal calcium sensor-1 (NCS-1), can physically associate with the type III PI4Kbeta with functional consequences affecting the kinase. Recombinant PI4Kbeta, but not its glutathione S-transferase-fused form, showed enhanced PI kinase activity when incubated with recombinant NCS-1, but only if the latter was myristoylated. Similarly, in vitro translated NCS-1, but not its myristoylation-defective mutant, was found associated with recombinant- or in vitro translated P…

Cell Membrane PermeabilityLipoproteinsNeuronal Calcium-Sensor ProteinsLipid kinase activityBiologyPhosphatidylinositolsbehavioral disciplines and activitiesBiochemistrychemistry.chemical_compoundsymbols.namesakePhosphatidylinositol PhosphatesChlorocebus aethiopsmental disordersAnimalsCalcium SignalingPhosphatidylinositol1-Phosphatidylinositol 4-KinaseMolecular BiologyCellular compartmentMyristoylationKinaseCalcium-Binding ProteinsCell MembraneNeuropeptidesBiological TransportCell BiologyTransfectionGolgi apparatusCell CompartmentationRatsCell biologychemistryBiochemistryNeuronal calcium sensor-1COS Cellssymbolsbiology.proteinCattleMyristic AcidsProtein Processing Post-TranslationalProtein BindingJournal of Biological Chemistry
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Light-Dependent Translocation of Arrestin in Rod Photoreceptors is Signaled through a Phospholipase C Cascade and Requires ATP

2009

Light adaptation of rod photoreceptors induces translocation of arrestin from inner segments (IS) to outer segments (OS). Our study suggests that components of the G-protein linked phosphoinositide pathway play a role in signaling the initiating events of arrestin translocation. We show that arrestin translocation can be stimulated by activators of phospholipase C (PLC) and protein kinase C (PKC) in the absence of light. Conversely, arrestin translocation to the OS is significantly slowed by inhibitors of PLC and PKC.In the second part of this study, we investigated the mechanism by which arrestin translocates in response to light. Other investigators have suggested that arrestin translocat…

Cholera ToxinLightgenetic structuresG proteinBiophysicsXenopusChromosomal translocationBiologyPhosphatidylinositolsArticleMiceXenopus laevisAdenosine TriphosphateRetinal Rod Photoreceptor CellsArrestinAnimalsEnzyme InhibitorsPotassium CyanideCells CulturedProtein Kinase CProtein kinase CArrestinPhosphoinositide PathwayPhospholipase CChemistryCell Biologybiology.organism_classificationeye diseasesCell biologyRhodopsinType C Phospholipasesbiology.proteinPhosphorylationArrestin beta 2Arrestin beta 1sense organsSignal transductionSignal TransductionBiophysical Journal
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Cytosolic Ca2+ and Phosphoinositide Hydrolysis Linked to Constitutively Active α1d-Adrenoceptors in Vascular Smooth Muscle

2003

In the present study, we analyzed changes in intracellular Ca2+ levels and inositol phosphate accumulation related to a population of alpha 1d-adrenoceptors in rat aorta resembling constitutively active receptors. Following intracellular Ca2+ store depletion by noradrenaline in Ca2+-free medium and removal of the agonist, restoration of extracellular Ca2+ induced four signals: a biphasic (transient and sustained) increase in [Ca2+]i, inositol phosphate accumulation, and a contractile response in the aorta. The transient increase in Ca2+, the inositol phosphate accumulation, and the contractile response were not observed in aortae incubated with prazosin or BMY 7378 [8-[2-[4-(2-methoxyphenyl…

Guanethidinemedicine.medical_specialtyVascular smooth muscleInositol PhosphatesPopulationchemistry.chemical_elementCalciumBiologyPhosphatidylinositolsMuscle Smooth VascularAdrenergic AgentsReceptors Adrenergic alpha-1Internal medicinemedicinePrazosinExtracellularAnimalsRats WistarInositol phosphateeducationAortaPharmacologyCalcium metabolismchemistry.chemical_classificationeducation.field_of_studyHydrolysisCalcium Channel BlockersRatsEndocrinologychemistryBiophysicsMolecular MedicineCalciumIntracellularSignal Transductionmedicine.drugJournal of Pharmacology and Experimental Therapeutics
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Inhibitory effect of nonviable preparations from human immunodeficiency virus 1 on inositol phospholipid metabolism

1989

Previously it was established [Pahwa, S., Pahwa, R., Saxinger, C., Gallo, R. C. & Good, R. A. (1985) Proc. Natl Acad. Sci. USA 82, 8198] that nonviable preparations of human immunodeficiency virus 1 (HIV-1) abolish the proliferative response of human lymphocytes to phytohemagglutinin A. Now we describe that this effect might be, at least partially, due to an impairment of the function of phospholipase C. It was found that addition of HIV-1 preparation to lymphocytes diminished the stimulation of phosphatidylinositol phosphorylation caused by phytohemagglutinin A. Moreover, this preparation completely abolished the phytohemagglutinin-A-stimulated release of inositol trisphosphate and prevent…

Inositol PhosphatesInositol 145-TrisphosphateBiologyPhospholipasePhosphatidylinositolsBiochemistrychemistry.chemical_compoundCytosolCyclic AMPPhosphatidylinositol phosphorylationHumansInositolLymphocytesPhosphorylationPhytohemagglutininsInositol phosphateProtein kinase AProtein Kinase CProtein kinase Cchemistry.chemical_classificationCell MembraneVirionBiological TransportInositol trisphosphateMolecular biologyCytosolchemistryBiochemistryType C PhospholipasesHIV-1Sugar PhosphatesCell DivisionEuropean Journal of Biochemistry
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Pro-prion Binds Filamin A, Facilitating Its Interaction with Integrin β1, and Contributes to Melanomagenesis

2010

Filamin A (FLNA) is an integrator of cell mechanics and signaling. The spreading and migration observed in FLNA sufficient A7 melanoma cells but not in the parental FLNA deficient M2 cells have been attributed to FLNA. In A7 and M2 cells, the normal prion (PrP) exists as pro-PrP, retaining its glycosylphosphatidyl-inositol (GPI) anchor peptide signal sequence (GPI-PSS). The GPI-PSS of PrP has a FLNA binding motif and binds FLNA. Reducing PrP expression in A7 cells alters the spatial distribution of FLNA and organization of actin and diminishes cell spreading and migration. Integrin β1 also binds FLNA. In A7 cells, FLNA, PrP, and integrin β1 exist as two independent, yet functionally linked,…

Integrin beta ChainsGlycosylphosphatidylinositolsPrionsFilaminsanimal diseasesAmino Acid MotifsIntegrinPlasma protein bindingBiologyFilaminBiochemistryCell membraneContractile ProteinsCell MovementCell Line TumormedicineHumansFLNACytoskeletonMelanomaMolecular BiologyActinMicrofilament ProteinsCell Biologynervous system diseasesCell biologyGene Expression Regulation Neoplasticmedicine.anatomical_structurebiology.proteinCancer researchSignal transductionProtein BindingJournal of Biological Chemistry
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Interaction of antibodies to proteinase 3 (classic anti-neutrophil cytoplasmic antibody) with human renal tubular epithelial cells: impact on signali…

2002

Abstract Among the anti-neutrophil cytoplasmic Abs (ANCA), those targeting proteinase 3 (PR3) have a high sensitivity and specificity for Wegener’s granulomatosis (WG). A pathogenetic role for these autoantibodies has been proposed due to their capacity of activating neutrophils in vitro. Recently, PR3 was also detected in human renal tubular epithelial cells (TEC). In the present study, the effect of murine monoclonal anti-PR3 Abs (anti-PR3) and purified c-ANCA targeting PR3 from WG serum on isolated human renal tubular cell signaling and inflammatory mediator release was characterized. Priming of TEC with TNF-α resulted in surface expression of PR3, as quantified in immunofluorescence stu…

Intracellular Fluidmedicine.medical_specialtyMyeloblastinImmunologyImmunofluorescencePhosphatidylinositolsAutoantigensDinoprostoneFlow cytometryAntibodies Antineutrophil CytoplasmicAntigen-Antibody ReactionsThromboxane A2Proteinase 3SuperoxidesInternal medicinemedicineCyclic AMPImmunology and AllergyHumanscardiovascular diseasesCells CulturedArachidonic Acidmedicine.diagnostic_testbiologyHydrolysisImmune SeraCell MembraneSerine EndopeptidasesAntibodies MonoclonalEpithelial CellsLipid signalingIn vitroCell biologyEndocrinologyKidney Tubulesbiology.proteinCyclooxygenaseSignal transductionInflammation MediatorsIntracellularSignal TransductionJournal of immunology (Baltimore, Md. : 1950)
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