Search results for "carrier protein"

showing 10 items of 361 documents

Identification of enolase as a plasminogen-binding protein in excretory-secretory products ofFasciola hepatica

2004

AbstractWe have followed a combined proteomic approach to identify proteins of Fasciola hepatica that could be involved in host–parasite interactions. Using two-dimensional gel electrophoresis, far Western immunoblot and mass spectrometry analyses, we have identified the enolase enzyme, present in the excretory/secretory materials of F. hepatica, as a human plasminogen-binding protein. This enzyme has an apparent molecular weight of 47 kDa with pI ranging from 6.2 to 7.2. These results suggest that enolase could act as a plasminogen receptor.

ProteomicsAmino Acid MotifsBlotting WesternMolecular Sequence DataEnolaseEnolaseBiophysicsProteomicsBiochemistryMass SpectrometryHost-Parasite InteractionsStructural BiologyHepaticaparasitic diseasesGeneticsAnimalsFasciola hepaticaElectrophoresis Gel Two-DimensionalAmino Acid SequenceIsoelectric PointPlasminogen bindingMolecular BiologyConserved Sequencechemistry.chemical_classificationGel electrophoresisSheepbiologyExcretory–secretoryPlasminogenHelminth ProteinsCell BiologyFasciola hepaticaHydrogen-Ion Concentrationbiology.organism_classificationMolecular biologyMolecular WeightBlotEnzymeLiverchemistryBiochemistryExcretory systemAntigens HelminthPhosphopyruvate HydrataseCarrier ProteinsFEBS Letters
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Cellular effects of bacterial N-3-Oxo-dodecanoyl-L-Homoserine lactone on the sponge Suberites domuncula (Olivi, 1792): insights into an intimate inte…

2014

International audience; Sponges and bacteria have lived together in complex consortia for 700 million years. As filter feeders, sponges prey on bacteria. Nevertheless, some bacteria are associated with sponges in symbiotic relationships. To enable this association, sponges and bacteria are likely to have developed molecular communication systems. These may include molecules such as N-acyl-L-homoserine lactones, produced by Gram-negative bacteria also within sponges. In this study, we examined the role of N-3-oxododecanoyl-L-homoserine lactone (3-oxo-C12-HSL) on the expression of immune and apoptotic genes of the host sponge Suberites domuncula. This molecule seemed to inhibit the sponge inn…

ProteomicsApoptosisPathogenesisPathology and Laboratory MedicineBiochemistrycaspase 74-Butyrolactonecaspase 3lcsh:ScienceCytoskeletoncaspase like 7 gene0303 health sciencesToll-like receptorMarine Ecologytoll like receptorGenomicsproto oncogeneEndocytosisCell biologySuberites domunculaCellular Structures and Organellesalpha actininCell signalingtoll like receptor associated factor 6Gram negative bacteriumparacrine signalingMicrobiology03 medical and health sciencesGeneticsRNA Messengerhost pathogen interactionprotein expressiontwo dimensional electrophoresisBacteria030306 microbiologyEcology and Environmental Scienceslcsh:RBiology and Life SciencesComputational BiologyImmunity Innatecarrier proteinSpongebacterial membranelcsh:Qimmunological toleranceSuberitesProtein AbundanceSuberitessuberites domuncula[SDV]Life Sciences [q-bio]lcsh:MedicineMolecular Cell BiologyMedicine and Health Sciencesinnate immunityperforinMultidisciplinaryEcologybiologymessenger RNAarticlecell communicationAnimal Modelsmatrix assisted laser desorption ionization time of flight mass spectrometryunclassified drugPoriferaHost-Pathogen InteractionscytotoxicityactinTranscriptome Analysishormone actionResearch ArticleSymbiotic bacteriaprotein bcl 2Marine BiologycofilinResearch and Analysis Methodsn (3 oxododecanoyl)homoserine lactoneMicrobial EcologycogninModel OrganismsHomoserineAnimalscontrolled study14. Life underwatergeneSymbiosiscell viabilityadenosine triphosphatase030304 developmental biologynonhumanChemical EcologyMembrane ProteinsCell Biologytumor necrosis factor receptor associated factor 6Genome Analysisbiology.organism_classificationalpha tubulinGene Expression RegulationMembrane proteingene expressioncaspase like 3 geneGenome Expression AnalysisBacteriaPLoS ONE
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Exploration of the Sea Urchin Coelomic Fluid via Combinatorial Peptide Ligand Libraries

2012

The urchin Paracentrotus lividus has been characterized via previous capture and enhancement of low-abundance proteins with combinatorial peptide ligand libraries (CPLL, ProteoMiner). Whereas in the control only 26 unique gene products could be identified, 82 species could be detected after CPLL treatment. Due to the overwhelming presence of two major proteins-the toposome (a highly glycosylated, modified calcium-binding, iron-less transferrin) and the major yolk proteins, belonging to the class of cell adhesion proteins-which constituted about 70% of the proteome of this biological fluid and strongly interfered with the capture of the minority proteome, no additional proteins could be dete…

Proteomicsfood.ingredientLigandsProteomicsParacentrotus lividusfoodSpecies SpecificityPeptide Librarybiology.animalParacentrotusAnimalsCombinatorial Chemistry TechniquesPeptide librarySea urchinchemistry.chemical_classificationbiologyCell adhesion moleculebiology.organism_classificationMolecular biologyBody FluidsBiochemistrychemistryTransferrinProteomeParacentrotusCarrier ProteinsGeneral Agricultural and Biological SciencesCell Adhesion MoleculesThe Biological Bulletin
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Divergent effects of biolistic gene transfer in a mouse model of allergic airway inflammation.

2007

Particle-mediated epidermal delivery (PMED) of allergen genes efficiently prevents systemic sensitization and suppresses specific immunoglobulin E synthesis. We investigated in a mouse model of allergic airway disease the effect of PMED on the elicitation of local inflammatory reactions in the lung. BALB/c mice were biolistically transfected with plasmids encoding beta-galactosidase (betaGal) as model allergen under control of the DC-targeting fascin promoter and the ubiquitously active cytomegalovirus promoter, respectively. Mice were challenged intranasally with betaGal-protein with or without intermediate sensitization with betaGal adsorbed to aluminiumhydroxide. Subsequently, local cyto…

Pulmonary and Respiratory Medicinemedicine.medical_treatmentClinical BiochemistryCytomegalovirusBiologymedicine.disease_causeDNA vaccinationInterferon-gammaMiceAllergenTh2 CellsmedicineRespiratory HypersensitivityAnimalsHumansPromoter Regions GeneticMolecular BiologyLungSensitizationCells CulturedInflammationMice Inbred BALB Cmedicine.diagnostic_testMicrofilament ProteinsGene Transfer TechniquesCell BiologyTransfectionDendritic Cellsrespiratory systemImmunoglobulin ETh1 Cellsmedicine.diseasebeta-Galactosidaserespiratory tract diseasesCellular infiltrationDisease Models Animalmedicine.anatomical_structureBronchoalveolar lavageCytokineNeutrophil InfiltrationImmunologyAntibody FormationFemaleEpidermisCarrier ProteinsBronchoalveolar Lavage FluidCD8T-Lymphocytes CytotoxicAmerican journal of respiratory cell and molecular biology
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Rho protein inactivation induced apoptosis of cultured human endothelial cells.

2002

Small GTP-binding Rho GTPases regulate important signaling pathways in endothelial cells, but little is known about their role in endothelial cell apoptosis. Clostridial cytotoxins specifically inactivate GTPases by glucosylation [ Clostridium difficile toxin B-10463 (TcdB-10463), C. difficile toxin B-1470 (TcdB-1470)] or ADP ribosylation ( C. botulinum C3 toxin). Exposure of human umbilical cord vein endothelial cells (HUVEC) to TcdB-10463, which inhibits RhoA/Rac1/Cdc42, or to C3 toxin, which inhibits RhoA, -B, -C, resulted in apoptosis, whereas inactivation of Rac1/Cdc42 with TcdB-1470 was without effect, suggesting that Rho inhibition was responsible for endothelial apoptosis. Disruptio…

Pulmonary and Respiratory Medicinerac1 GTP-Binding Proteinrho GTP-Binding ProteinsProgrammed cell deathUmbilical VeinsEndotheliumPhysiologyBacterial ToxinsCASP8 and FADD-Like Apoptosis Regulating ProteinApoptosisBcl-2-associated X proteinBacterial ProteinsPhysiology (medical)Proto-Oncogene ProteinsmedicineCyclic AMPIn Situ Nick-End LabelingHumanscdc42 GTP-Binding ProteinCells Culturedbcl-2-Associated X ProteinAdenosine Diphosphate RibosebiologyCaspase 3Intracellular Signaling Peptides and ProteinsCell BiologyCaspase 9Cell biologyNeoplasm ProteinsEndothelial stem cellmedicine.anatomical_structureCdc42 GTP-Binding ProteinProto-Oncogene Proteins c-bcl-2Cell cultureApoptosisCaspasesbiology.proteinMyeloid Cell Leukemia Sequence 1 ProteinEndothelium VascularSignal transductionCarrier ProteinsrhoA GTP-Binding ProteinBH3 Interacting Domain Death Agonist ProteinSignal TransductionAmerican journal of physiology. Lung cellular and molecular physiology
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Molecular determinants of large cargo transport into the nucleus

2020

Nucleocytoplasmic transport is tightly regulated by the nuclear pore complex (NPC). Among the thousands of molecules that cross the NPC, even very large (>15 nm) cargoes such as pathogens, mRNAs and pre-ribosomes can pass the NPC intact. For these cargoes, there is little quantitative understanding of the requirements for their nuclear import, especially the role of multivalent binding to transport receptors via nuclear localisation sequences (NLSs) and the effect of size on import efficiency. Here, we assayed nuclear import kinetics of 30 large cargo models based on four capsid-like particles in the size range of 17–36 nm, with tuneable numbers of up to 240 NLSs. We show that the requireme…

QH301-705.5ScienceStructural Biology and Molecular Biophysicspermeabilized cellsimport kineticsNuclear Localization SignalsBiophysicslarge cargoActive Transport Cell NucleusNLSnuclear transportGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciences0302 clinical medicinemedicinecapsidNLSHumansNuclear poreBiology (General)030304 developmental biologyCell Nucleus0303 health sciencesGeneral Immunology and MicrobiologyChemistryGeneral NeuroscienceMolecular biophysicsQRE. coliGeneral MedicineCell Biologymedicine.anatomical_structureStructural biologyNucleocytoplasmic TransportBiophysicsNuclear PoreMedicineNuclear transportCarrier ProteinsFlux (metabolism)Nucleus030217 neurology & neurosurgeryResearch ArticleHumaneLife
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Genome-wide significant association of ANKRD55 rs6859219 and multiple sclerosis risk.

2013

Multiple sclerosis (MS) is a genetically complex disease that shares a substantial proportion of risk loci with other autoimmune diseases.1 Along these lines, ANKRD55 , originally implicated in rheumatoid arthritis, was recently reported as a potential novel MS risk gene (rs6859219, p=1.9×10−7).2 Here, we comprehensively validated this effect in independent datasets comprising 8846 newly genotyped subjects from Germany and France as well as 5003 subjects from two genome-wide association studies (GWAS). Upon meta-analysis of all available data (19 686 subjects), ANKRD55 rs6859219 now shows compelling evidence for association with MS at genome-wide significance (OR=1.19, p=3.1×10−11). Our stu…

RFXANKAdultMalemedicine.medical_specialtyMultiple SclerosisLocus (genetics)Genome-wide association studySingle-nucleotide polymorphismBiologyPolymorphism Single NucleotideWhite PeopleMolecular geneticsDatabases GeneticGeneticsmedicineHumansGenetic Predisposition to DiseaseGenetics (clinical)Genetic associationGeneticsMultiple sclerosisMiddle Agedmedicine.diseaseAnkyrin RepeatCase-Control StudiesAnkyrin repeatFemaleCarrier ProteinsGenome-Wide Association StudyJournal of medical genetics
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Expression of the fibrinogen binding mannoprotein and the laminin receptor of Candida albicans in vitro and in infected tissues.

1996

We have previously reported a 37 kDa laminin-binding protein (p37) and a 58 kDa fibrinogen-binding mannoprotein (mp58) on the surface of Candida albicans. A few yeast cells expressed both functional receptors at the surface while germ tubes expressed a functional mp58 fibrinogen but not a functional p37 laminin receptor. These receptors were heterogeneously dispersed at the surface as shown by binding of rabbit antiserum to mp58 (PAb anti-mp58) and antiserum to the human high affinity laminin receptor. In this report we have used a dual fluorescence technique to determine if the two receptors colocalize, perhaps as part of a receptor complex. Fibrinogen was used as a probe for mp58 and poly…

Receptor complexBiologyImmunofluorescenceMicrobiologyReceptors LamininBacterial ProteinsLamininCandida albicansGeneticsmedicineAnimalsHumansReceptorCandida albicansFluorescent Antibody Technique IndirectMolecular BiologyAntibodies FungalAntiserumMembrane Glycoproteinsmedicine.diagnostic_testBinding proteinCandidiasisFibrinogen bindingFibrinogenbiology.organism_classificationMolecular biologyImmunohistochemistryBiochemistrybiology.proteinRabbitsCarrier ProteinsFEMS microbiology letters
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The function of the soluble interleukin 6 (IL-6) receptor in vivo: sensitization of human soluble IL-6 receptor transgenic mice towards IL-6 and prol…

1996

Interleukin 6 (IL-6) is considered an important mediator of acute inflammatory responses. Moreover, IL-6 functions as a differentiation and growth factor of hematopoietic precursor cells, B cells, T cells, keratinocytes, neuronal cells, osteoclasts, and endothelial cells. IL-6 exhibits its action via a receptor complex consisting of a specific IL-6 receptor (IL-6R) and a signal transducing subunit (gp130). Soluble forms of both receptor components are generated by shedding and are found in patients with various diseases such as acquired immune deficiency syndrome, rheumatoid arthritis, and others. The function of the soluble (s)IL-6R in vivo is unknown. Since human (h)IL-6 acts on human and…

Receptor complexImmunologyMice TransgenicInterleukin 1 receptor type IIBiologyMiceSpecies SpecificityAntigens CDInterleukin-4 receptorImmunology and AllergyAnimalsHumansAcute-Phase ReactionInterleukin 12 receptor beta 1 subunitInterleukin 3HaptoglobinsInterleukin-6Receptors InterleukinArticlesMolecular biologyReceptors Interleukin-6Interleukin 10LiverSolubilityInterleukin-6 receptorPhosphoenolpyruvate Carboxykinase (GTP)Interleukin 1 receptor type ICarrier ProteinsHalf-LifeThe Journal of experimental medicine
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In vivo Trafficking and Localization of p24 Proteins in Plant Cells

2008

p24 proteins constitute a family of putative cargo receptors that traffic in the early secretory pathway. p24 proteins can be divided into four subfamilies (p23, p24, p25 and p26) by sequence homology. In contrast to mammals and yeast, most plant p24 proteins contain in their cytosolic C-terminus both a dilysine motif in the -3, -4 position and a diaromatic motif in the -7, -8 position. We have previously shown that the cytosolic tail of Arabidopsis p24 proteins has the ability to interact with ARF1 and coatomer (through the dilysine motif) and with COPII subunits (through the diaromatic motif). Here, we establish the localization and trafficking properties of an Arabidopsis thaliana p24 pr…

Recombinant Fusion ProteinsMolecular Sequence DataArabidopsisGolgi ApparatusVacuoleProtein Sorting SignalsBiologyEndoplasmic ReticulumBiochemistrysymbols.namesakeStructural BiologyArabidopsisGeneticsAnimalsHumansProtein IsoformsAmino Acid SequenceMolecular BiologyCOPIISecretory pathwayArabidopsis ProteinsLysineEndoplasmic reticulumMembrane ProteinsCell BiologyCOPIGolgi apparatusbiology.organism_classificationActinsCell biologyDNA-Binding ProteinsProtein TransportBiochemistryCoatomerVacuolessymbolsCOP-Coated VesiclesCarrier ProteinsTranscription FactorsTraffic
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