Search results for "Membrane glycoprotein"

showing 10 items of 312 documents

Identification of Two Mannoproteins Released from Cell Walls of a Saccharomyces cerevisiae mnn1 mnn9 Double Mutant by Reducing Agents

1999

The cell wall of Saccharomyces cerevisiae represents some 30% of the total weight of the cell and is made up of β-glucans, mannose-containing glycoproteins (mannoproteins), and small amounts of chitin (9, 15). The mannoproteins can be divided into three groups according to the linkages that bind them to the structure of the cell wall: (i) noncovalently bound, (ii) covalently bound to the structural glucan, and (iii) disulfide bound to other proteins that are themselves covalently bound to the structural glucan of the cell wall (8). Our work has focused on the disulfide-bound mannoproteins, probably the least well known of the three groups mentioned above. Previous work (25) showed that trea…

GlycosylationSaccharomyces cerevisiae ProteinsGlycosylationBlotting WesternMolecular Sequence DataSaccharomyces cerevisiaeSaccharomyces cerevisiaeMicrobiologyGene Expression Regulation EnzymologicFungal ProteinsCell wallOpen Reading FramesSurface-Active Agentschemistry.chemical_compoundCell WallGene Expression Regulation FungalEndopeptidasesAspartic Acid EndopeptidasesAmino Acid SequenceSubtilisinsFluorescent Antibody Technique IndirectMolecular BiologyMercaptoethanolGlucanGel electrophoresischemistry.chemical_classificationFungal proteinMembrane GlycoproteinsbiologySodium Dodecyl SulfateBiological Transportbiology.organism_classificationRecombinant ProteinsYeastMolecular Weightcarbohydrates (lipids)Cytoskeletal ProteinsEukaryotic CellsPhenotypechemistryBiochemistryMutagenesisReducing AgentsElectrophoresis Polyacrylamide GelProprotein ConvertasesProtein Tyrosine PhosphatasesGlycoproteinGene DeletionJournal of Bacteriology
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Cell wall mannoproteins during the population growth phases in Saccharomyces cerevisiae.

1987

Mannoproteins from cell walls of Saccharomyces cerevisiae synthesized at successive stages of the population growth cycle have been solubilized with Zymolyase and subsequently analyzed. The major change along the population cycle concerned a large size mannoprotein material; the size of the newly-synthesized molecules varied from 120,000–500,000 (mean of about 200,000) at early exponential phase to 250,000–350,000 (mean of about 300,000) at late exponential phase. These differences are due to modifications in the amount of N-glycosidically linked mannose residues, since the size of the peptide moiety was 90,000–100,000 at all growth stages and the level of O-glycosylation changed only sligh…

GlycosylationSaccharomyces cerevisiaeMannosePeptideSaccharomyces cerevisiaeBiologyBiochemistryMicrobiologylaw.inventionCell wallFungal Proteinschemistry.chemical_compoundlawCell WallGeneticsConcanavalin AMolecular BiologyIncubationGlucanGlycoproteinschemistry.chemical_classificationMembrane GlycoproteinsGlucan Endo-13-beta-D-GlucosidaseSodium Dodecyl SulfateGeneral Medicinebiology.organism_classificationcarbohydrates (lipids)Molecular WeightDithiothreitolMicroscopy ElectronchemistryBiochemistryConcanavalin AFerritinsbiology.proteinChromatography GelElectrophoresis Polyacrylamide GelElectron microscopeArchives of microbiology
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A role for the immunoglobulin-like domain of the human IL-6 receptor. Intracellular protein transport and shedding.

1999

Interleukin (IL)-6, IL-11 and cililary neurotrophic factor (CNTF) belong to the same family of hematopoietic and neurotrophic cytokines. Their receptor complexes contain a cytokine-binding alpha receptor and the common glycoprotein (gp)130 subunit for signal transduction. The extracellular parts of the alpha-receptor subunits consist of a membrane-proximal cytokine-binding domain and an N-terminal immunoglobulin (Ig)-like domain with unknown function. We examined the role of the Ig-like domain of IL-6R by constructing deletion mutants lacking the Ig domain (IL-6RDeltaIg and soluble IL-6RDeltaIg). IL-6RDeltaIg was shed as effectively as wild-type IL-6R from transfected COS-7 cells upon 4beta…

GlycosylationTime FactorsImmunoglobulin domainBiologyTransfectionBiochemistryModels BiologicalCell LineMiceAnimalsHumansSecretionSecretory pathwayMembrane GlycoproteinsDose-Response Relationship DrugInterleukin-6Lysosome-Associated Membrane GlycoproteinsTransfectionGlycoprotein 130Flow CytometryMolecular biologyReceptors Interleukin-6Transmembrane proteinRecombinant ProteinsCell biologyInterleukin-6 receptorCOS CellsTetradecanoylphorbol AcetateSignal transductionSignal TransductionEuropean journal of biochemistry
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A comparative study of the incorporation of a 1,6-beta-glucan and an O-glycosylated protein epitope into the cell wall of Candida albicans.

1996

The topological distribution of two epitopes in the cell wall of Candida albicans, the kinetics of their incorporation into the regenerating protoplast wall, and the effect of different antibiotics upon their incorporation and localization have been studied. To do so, two monoclonal antibodies that react against an O-glycosylated mannoprotein (1B12) and against a 1,6-beta-glucan epitope (JRR1) were used. The results show that the JRR1 epitope is localized in an internal layer of the cell wall, in contrast to the 1B12 epitope, which is superficial, and that the incorporation of the JRR1 epitope into walls of regenerating protoplasts precedes that of the 1B12 epitope. The JRR1 epitope is norm…

Glycosylationbeta-Glucansmedicine.drug_classEnzyme-Linked Immunosorbent AssayBiologyMonoclonal antibodyMicrobiologyEpitopeCell wallchemistry.chemical_compoundEpitopesCell WallCandida albicansmedicineSecretionCandida albicansFluorescent Antibody Technique IndirectGlucansMembrane GlycoproteinsLinear epitopeProtoplastsAntibodies MonoclonalTunicamycinbiology.organism_classificationMolecular biologycarbohydrates (lipids)KineticsBiochemistrychemistrybiology.proteinAntibodyMicrobiology (Reading, England)
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Protective role of the complement regulatory protein human CD-55 in cardiac xenograft: a descriptive study and a revision of the literature.

2002

The limited and inadequate availability of organs from human donors has resulted in the utilisation of xenografts as an alternative tool. Nevertheless, hyperacute rejection (HAR) following xenograft determines the loss of the transplanted organ. The “primum movens” is the activation of the complement pathway mediated by the binding of natural xenogenic antibodies to the endothelium of the graft, followed by the lysis of the endothelial cells with subsequent oedema, thrombosis and necrosis of the transplanted organ. In this work we describe morphological and biomolecular observations of isolated human-decay accelerating factor (h-DAF, CD55) transgenic pig hearts, after perfusion for four hou…

Graft RejectionHistologyCD55 AntigensSwineEndothelial cells2734Blotting WesternTransplantation HeterologousComplementCell BiologyOrgan SizeImmunohistochemistryMicroscopy ElectronEndothelial cellMembrane glycoproteinCoronary CirculationGenetic engineering:6 - Ciencias aplicadas::61 - Medicina::611 - Anatomía [CDU]AnimalsHeart TransplantationHumansXenotransplantationAnatomyComplement; Endothelial cells; Genetic engineering; Membrane glycoproteins; Xenotransplantation; Anatomy; 2734; Histology; Cell Biology
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Apoptosis induced by (E)-5-(2-bromovinyl)-2'-deoxyuridine in varicella zoster virus thymidine kinase-expressing cells is driven by activation of c-Ju…

2003

The molecular mode of cell killing by the antiviral drug (E)-5-(2-bromovinyl-2'-deoxyuridine (BVDU) was studied in Chinese hamster ovary (CHO) cells stably transfected with the thymidine kinase gene (tk) of varicella zoster virus (CHO-VZVtk). The colony-forming ability of the cells was reduced to <1% at a concentration of approximately 1 microM BVDU, whereas for nontransfected cells or cells transfected with tk gene of herpes simplex virus type 1 (CHO-HSVtk), a 1000-fold higher dose was required to achieve the same response. BVDU inhibited thymidylate synthase in CHO-VZVtk but not in CHO-HSVtk and control cells. On the other hand, the drug was incorporated into DNA of VZVtk- and HSVtk-expre…

Herpesvirus 3 HumanFas Ligand ProteinFas-Associated Death Domain ProteinApoptosisCHO CellsBiologyTransfectionAntiviral AgentsThymidine KinaseFas ligandchemistry.chemical_compoundNecrosisCricetinaeCytotoxic T cellAnimalsSimplexvirusAdaptor Proteins Signal TransducingPharmacologyCaspase 8GenomeMembrane GlycoproteinsChinese hamster ovary cellCell CycleJNK Mitogen-Activated Protein KinasesTransfectionDNAThymidylate SynthaseMolecular biologyCaspase 9Transcription Factor AP-1Cell killingchemistryBromodeoxyuridineApoptosisThymidine kinaseCaspasesMolecular MedicineMitogen-Activated Protein KinasesCarrier ProteinsBromodeoxyuridineMolecular pharmacology
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RCS1, a gene involved in controlling cell size inSaccharomyces cerevisiae

1991

Cloning and sequencing of RCS1, Saccharomyces cerevisiae gene whose product seems to be involved in timing the budding event of the cell cycle, is described. A haploid strain in which the 3'-terminal region of the chromosomal copy of the gene has been disrupted produces cells that are, on average, twice the size of cells of the parental strain. The critical size for budding in the mutant is similarly increased, and the disruption mutation is dominant in a diploid heterozygous for the RCS1 gene. Spores from this diploid have a reduced ability to germinate, the effect being more pronounced in the spores carrying the disrupted copy of RCS1. However, disrupted cells recover from alpha-factor tr…

HeterozygoteMolecular Sequence DataSaccharomyces cerevisiaeMutantBioengineeringSaccharomyces cerevisiaemedicine.disease_causeApplied Microbiology and BiotechnologyBiochemistryGeneticsSpore germinationmedicineAmino Acid SequenceCloning MolecularDNA FungalGeneGene LibraryGeneticsBuddingMutationMembrane GlycoproteinsBase SequencebiologyCell CyclefungiSpores Fungalbiology.organism_classificationYeastMutationPloidyPlasmidsBiotechnologyYeast
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Origin of metazoan adhesion molecules and adhesion receptors as deduced from cDNA analyses in the marine sponge Geodia cydonium: a review.

1997

The phylogenetic relationships of the kingdom Animalia (Metazoa) have long been questioned. Whether the lowest eukaryotic multicellular organisms, the metazoan phylum Porifera (sponges), independently evolved multicellularity from a separate protist lineage (polyphyly of animals) or whether they were derived from the same protist group as the other animal phyla (monophyly) remains unclear. Analyses of the genes that are typical for multicellularity, e.g. those coding for adhesion molecules (galectin) and adhesion receptors (receptor tyrosine kinase, integrin receptor, receptors featuring scavenger receptor cysteine-rich domains) or elements involved in signal transduction pathways (G-protei…

HistologyDNA ComplementaryMembrane GlycoproteinsbiologyCell adhesion moleculeProtistMembrane ProteinsCell Biologybiology.organism_classificationmedicine.disease_causeReceptor tyrosine kinasePathology and Forensic MedicineCell biologyPoriferaSuberites domunculaSpongeBiochemistryPlatelet Glycoprotein GPIb-IX Complexbiology.proteinmedicineAnimalsSignal transductionReceptorCell Adhesion MoleculesGalectinCell and tissue research
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Tropism of human cytomegalovirus for endothelial cells is determined by a post-entry step dependent on efficient translocation to the nucleus.

2000

Marked interstrain differences in the endothelial cell (EC) tropism of human cytomegalovirus (HCMV) isolates have been described. This study aimed to define the step during the replicative cycle of HCMV that determines this phenotype. The infection efficiency of various HCMV strains in EC versus fibroblasts was quantified by immunodetection of immediate early (IE), early and late viral antigens. Adsorption and penetration were analysed by radiolabelled virus binding assays and competitive HCMV-DNA-PCR. The translocation of penetrated viral DNA to the nucleus of infected cells was quantified by competitive HCMV-DNA-PCR in pure nuclear fractions. The intracytoplasmic translocation of capsids …

Human cytomegalovirusUmbilical VeinsvirusesBlotting WesternActive Transport Cell NucleusCytomegalovirusChromosomal translocationBiologyAntibodies ViralTransfectionVirus ReplicationVirusImmediate-Early ProteinsViral ProteinsViral Envelope ProteinsViral entryVirologyGene expressionmedicineHumansEndotheliumPromoter Regions GeneticAntigens ViralGenes Immediate-EarlyTropismCells CulturedCell NucleusMembrane GlycoproteinsAntibodies MonoclonalGenetic VariationFibroblastsmedicine.diseaseVirologyMolecular biologyCell nucleusMicroscopy Electronmedicine.anatomical_structureOrgan SpecificityDNA ViralTrans-ActivatorsAdsorptionImmunostainingThe Journal of general virology
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Non-redundant and redundant roles of cytomegalovirus gH/gL complexes in host organ entry and intra-tissue spread

2015

Herpesviruses form different gH/gL virion envelope glycoprotein complexes that serve as entry complexes for mediating viral cell-type tropism in vitro; their roles in vivo, however, remained speculative and can be addressed experimentally only in animal models. For murine cytomegalovirus two alternative gH/gL complexes, gH/gL/gO and gH/gL/MCK-2, have been identified. A limitation of studies on viral tropism in vivo has been the difficulty in distinguishing between infection initiation by viral entry into first-hit target cells and subsequent cell-to-cell spread within tissues. As a new strategy to dissect these two events, we used a gO-transcomplemented ΔgO mutant for providing the gH/gL/gO…

Human cytomegalovirusherpesvirusesvirusesgH/FL complexesCytomegalovirusMiceViral Envelope ProteinsMedizinische FakultätBiology (General)In Situ Hybridization0303 health sciencesMice Inbred BALB CMembrane GlycoproteinsImmunohistochemistrycytomegalovirus ; gH/FL complexes ; gO ; MCK-2 ; herpesvirusesCytomegalovirus InfectionsFemaleMCK-2BIOMEDICINA I ZDRAVSTVO. Temeljne medicinske znanosti.Research ArticleQH301-705.5Immunology-BiologyMicrobiologyVirus03 medical and health sciencesgOViral entryIn vivoVirologyGeneticsmedicineAnimalsddc:610Molecular BiologyTropism030304 developmental biology030306 microbiologyBIOMEDICINE AND HEALTHCARE. Basic Medical Sciences.RC581-607medicine.diseaseVirologyHerpesvirus glycoprotein BDisease Models AnimalViral TropismCell cultureTissue tropismParasitologyImmunologic diseases. Allergy
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