Search results for "Inositols"

showing 10 items of 21 documents

Glucose-induced loss of glycosyl-phosphatidylinositol-anchored membrane regulators of complement activation (CD59, CD55) by in vitro cultured human u…

2000

Aims/hypothesis. This study examines whether increased glucose concentrations are responsible for a decreased expression of membrane regulators of complement activation molecules. The effect of high glucose in determining an increase in membrane attack complex deposition on endothelial cells was also investigated. Methods. Endothelial cells were isolated from umbilical cord tissue, cultured in the presence of increased concentrations of glucose, and the expression of CD46, CD55, and CD59 was detected by ELISA (enzyme-linked immunosorbent assay) and by flow cytometry. Glucose-treated endothelial cells were also incubated with antiendothelial cell antibodies and fresh complement to assess the…

medicine.medical_specialtyUmbilical VeinsEndotheliumGlycosylphosphatidylinositolsEndocrinology Diabetes and MetabolismCellCD59 AntigensCD59Complement Membrane Attack ComplexBiologyUmbilical veinMembrane Cofactor ProteinAntigens CDPregnancyInternal medicineInternal MedicinemedicineHumansComplement ActivationCells CulturedMembrane GlycoproteinsCD55 AntigensCD46Cell biologyComplement systemEndothelial stem cellEndocrinologymedicine.anatomical_structureGlucoseFemaleEndothelium VascularComplement membrane attack complexDiabetologia
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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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The Host Response toListeria monocytogenesMutants Defective in Genes Encoding Phospholipases C(plcA, plcB)and Actin Assembly(actA)

1997

Several genes involved in the determination of Listeria monocytogenes pathogenesis have been identified. Among them, plcA gene encodes phosphatidylinositol-specific phospholipase C (PI-PLC), plcB gene encodes a broad-range phospholipase C (PC-PLC), and actA encodes a protein contributing to actin assembly in infected cells. The interaction of L. monocytogenes wild type (LO 28) strain and two derivative mutants, plcA- (BUG 206) and actA-/plcB- (LUT 12), with macrophages and T lymphocytes was investigated in a mouse model of listeriosis. Both mutants showed evidence of attenuation. The plcA- mutant, but not the plcB- mutant, expressed an increase in susceptibility to the anti-listerial activi…

LipopolysaccharidesCellular immunityT-LymphocytesImmunologyMutantDose-Response Relationship ImmunologicBiologyLymphocyte ActivationPhosphatidylinositolsmedicine.disease_causeMicrobiologyMicrobiologyMicePhagocytosisListeria monocytogenesVirologyEscherichia colimedicineAnimalsListeriosisGeneEscherichia coliCells CulturedMice Inbred BALB CPhospholipase CWild typeInterleukin-12Listeria monocytogenesActinsGenes BacterialType C PhospholipasesMutationMacrophages PeritonealInterleukin 12FemaleSpleenMicrobiology and Immunology
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Chronic consumption of an inositol-enriched carob extract improves postprandial glycaemia and insulin sensitivity in healthy subjects: A randomized c…

2016

Background & aims: Inositols are thought to be mediators of the insulin signalling pathway. We assessed the effects of inositols on glycaemic control in fasting and postprandial states and evaluated lipoprotein profile and LDL particle size in healthy population. Methods: A 12-week double-blind clinical trial was performed with forty healthy subjects administered either an inositol-enriched beverage (IEB) -containing 2.23 g of inositols in 250 ml- or a sucrose-sweetened beverage (SB) twice a day. Anthropometric measurements, fasting glucose levels, insulin and HOMA-IR index, lipoprotein profile and postprandial glucose concentrations (measured using the continuous glucose monitoring system …

Blood GlucoseMaleApolipoprotein Bmedicine.medical_treatment030204 cardiovascular system & hematologyCritical Care and Intensive Care Medicinelaw.inventionchemistry.chemical_compound0302 clinical medicineRandomized controlled triallawContinuous glucose monitoring systemHealthy subjects030212 general & internal medicineHypolipidemic AgentsNutrition and DieteticsbiologyArea under the curveFabaceaePostprandial PeriodPostprandialLDL particle sizeSeedsFemaleInositolsAdultmedicine.medical_specialtyCarob pod extractMonitoring AmbulatoryHyperlipidemias03 medical and health sciencesDouble-Blind MethodInternal medicinemedicineHumansHypoglycemic AgentsParticle SizePinitolPlant Extractsbusiness.industryPinitolInsulinMetabolismEndocrinologyLipoproteins IDLchemistrySpainFruitHyperglycemiaDietary Supplementsbiology.proteinInsulin ResistancebusinessInositolLipoproteinClinical Nutrition
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The MBOAT7-TMC4 Variant rs641738 Increases Risk of Nonalcoholic Fatty Liver Disease in Individuals of European Descent

2016

Background & Aims Nonalcoholic fatty liver disease (NAFLD) is a leading cause of liver damage and is characterized by steatosis. Genetic factors increase risk for progressive NAFLD. A genome-wide association study showed that the rs641738 C>T variant in the locus that contains the membrane bound O-acyltransferase domain-containing 7 gene (MBOAT7, also called LPIAT1) and transmembrane channel-like 4 gene (TMC4) increased the risk for cirrhosis in alcohol abusers. We investigated whether the MBOAT7-TMC4 is a susceptibility locus for the development and progression of NAFLD. Methods We genotyped rs641738 in DNA collected from 3854 participants from the Dallas Heart Study (a multi-ethnic…

Liver CirrhosisMale0301 basic medicineCirrhosisBiopsyProton Magnetic Resonance SpectroscopyPhosphatidylinositolsTriglycerideSeverity of Illness IndexGastroenterologyLiver disease0302 clinical medicineNon-alcoholic Fatty Liver DiseaseRisk FactorsNonalcoholic fatty liver diseaseMembrane Proteineducation.field_of_studyArachidonic Acidmedicine.diagnostic_testNASHGastroenterologyTexasEuropePhenotypeLiverLiver biopsyFemale030211 gastroenterology & hepatologyTexaCase-Control StudiePhosphatidylinositolHumanmedicine.medical_specialtyAcyltransferaseLiver CirrhosiEuropean Continental Ancestry GroupPopulationTM6SF2White PeopleArticle03 medical and health sciencesArachidonic Acid; NASH; PNPLA3; TM6SF2; Acetyltransferases; Acyltransferases; Biopsy; Case-Control Studies; Cross-Sectional Studies; Europe; European Continental Ancestry Group; Female; Genetic Predisposition to Disease; Genome-Wide Association Study; Humans; Liver; Liver Cirrhosis; Male; Membrane Proteins; Non-alcoholic Fatty Liver Disease; Phenotype; Phosphatidylinositols; Proton Magnetic Resonance Spectroscopy; Risk Factors; Severity of Illness Index; Texas; Triglycerides; Polymorphism GeneticGeneticAcetyltransferasesInternal medicineAcetyltransferasemedicineHumansGenetic Predisposition to DiseasePolymorphismeducationPNPLA3TriglyceridesCross-Sectional StudiePolymorphism GeneticHepatologybusiness.industryRisk FactorCase-control studyMembrane Proteinsmedicine.diseaseCross-Sectional Studies030104 developmental biologyEndocrinologyCase-Control StudiesSteatosisbusinessAcyltransferasesGenome-Wide Association StudyTM6SF2Gastroenterology
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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 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 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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AtPGAP1 functions as a GPI inositol-deacylase required for efficient transport of GPI-anchored proteins

2021

Abstract Glycosylphosphatidylinositol (GPI)-anchored proteins (GPI-APs) play an important role in a variety of plant biological processes including growth, stress response, morphogenesis, signaling, and cell wall biosynthesis. The GPI anchor contains a lipid-linked glycan backbone that is synthesized in the endoplasmic reticulum (ER) where it is subsequently transferred to the C-terminus of proteins containing a GPI signal peptide by a GPI transamidase. Once the GPI anchor is attached to the protein, the glycan and lipid moieties are remodeled. In mammals and yeast, this remodeling is required for GPI-APs to be included in Coat Protein II-coated vesicles for their ER export and subsequent t…

Signal peptideGlycanGenotypePhysiologyGlycosylphosphatidylinositolsPlant ScienceGenes Plantchemistry.chemical_compoundGene Expression Regulation PlantArabidopsisGeneticsArabidopsis thalianaInositolbiologyChemistryArabidopsis ProteinsEndoplasmic reticulumGenetic VariationMembrane Proteinsbiology.organism_classificationYeastPhosphoric Monoester HydrolasesCell biologyFocus Issue on Transport and Signalingcarbohydrates (lipids)Protein Transportbiology.proteinlipids (amino acids peptides and proteins)Function (biology)
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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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