Search results for "glycoproteins"

showing 10 items of 496 documents

IRSp53 controls plasma membrane shape and polarized transport at the nascent lumen in epithelial tubules.

2020

It is unclear whether the establishment of apical–basal cell polarity during the generation of epithelial lumens requires molecules acting at the plasma membrane/actin interface. Here, we show that the I-BAR-containing IRSp53 protein controls lumen formation and the positioning of the polarity determinants aPKC and podocalyxin. Molecularly, IRSp53 acts by regulating the localization and activity of the small GTPase RAB35, and by interacting with the actin capping protein EPS8. Using correlative light and electron microscopy, we further show that IRSp53 ensures the shape and continuity of the opposing plasma membrane of two daughter cells, leading to the formation of a single apical lumen. G…

ScienceSialoglycoproteinsQCell MembraneCell PolarityEpithelial CellsNerve Tissue ProteinsApicobasal polaritySettore MED/08 - Anatomia PatologicaActins Cell Membrane Cell Polarity Epithelial Cells Female Morphogenesis Nerve Tissue Proteins Protein Transport Sialoglycoproteins rab GTP-Binding ProteinsActinsArticleProtein Transportrab GTP-Binding ProteinsMorphogenesisHumanslcsh:QFemalelcsh:ScienceNature communications
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Characterization of aging-associated up-regulation of constitutive nuclear factor-kappa B binding activity.

2001

Changes occur in gene expression during aging in vivo and in replicative senescence in vitro, suggesting that aging can affect gene regulation. We have recently observed age-related changes in ubiquitously expressed, oxidative stress-responsive nuclear factor-kappa B (NF-kappa B) pathway during aging. Here we report a significant age-related increase in nuclear NF-kappa B binding activity together with increased protein levels of p52 and p65 components in rat liver. An additional, higher molecular weight protein band seen in their western blots suggests that their post-translational modification (but not phosphorylation) occurs in liver, which might affect their nuclear localization and bin…

SenescenceAgingPhysiologyClinical BiochemistryBlotting WesternCell Cycle ProteinsNerve Tissue ProteinsIκB kinaseBiologyTransfectionBiochemistrySynaptotagminsCalcium-binding proteinGene expressionAnimalsRats WistarPromoter Regions GeneticMolecular BiologyCells CulturedGeneral Environmental ScienceRegulation of gene expressionMembrane GlycoproteinsCalcium-Binding ProteinsNF-kappa BCell BiologyBlotting NorthernMolecular biologyRatsUp-RegulationIκBαGene Expression RegulationLiverSynaptotagmin IGeneral Earth and Planetary SciencesPhosphorylationNuclear localization sequenceAntioxidantsredox signaling
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Overexpression of apolipoprotein J in human fibroblasts protects against cytotoxicity and premature senescence induced by ethanol and tert-butylhydro…

2008

Human diploid fibroblasts (HDFs) exposed to subcytotoxic stresses under H2O2, tert-butylhydroperoxide (t-BHP), and ethanol (EtOH) undergo stress-induced premature senescence (SIPS) characterized by many biomarkers of HDFs replicative senescence. Among these biomarkers are a growth arrest, an increase in the senescence-associated β-galactosidase activity, a senescent morphology, an overexpression of p21waf-1 and the subsequent inability to phosphorylate pRb, the presence of the common 4977-bp mitochondrial deletion, and an increase in the steady-state level of several senescence-associated genes such as apolipoprotein J (apo J). Apo J has been described as a survival gene against cytotoxic s…

SenescenceCell SurvivalGene ExpressionSimian virus 40Biologymedicine.disease_causeTritiumBiochemistrytert-ButylhydroperoxideGene expressionmedicineHumansOsteonectinRNA MessengerCytotoxicityCells CulturedCellular SenescenceCell Line TransformedGlycoproteinsClusterinEthanolCentral Nervous System DepressantsCell BiologyTransfectionOriginal ArticlesFibroblastsbeta-GalactosidaseMolecular biologyRecombinant ProteinsFibronectinsOxidative StressClusterinbiology.proteinPhosphorylationMitogensCell agingOxidative stressMolecular ChaperonesThymidineCell Stress and Chaperones
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Antigenic cell wall mannoproteins in Candida albicans isolates and in other Candida species.

1991

Polyclonal antibodies (pAbs) and monoclonal antibodies (mAbs), raised against mannoprotein components from Candida albicans ATCC 26555 (serotype A) blastoconidia and mycelial cell walls, were used to investigate antigenic similarities among wall mannoproteins from other C. albicans serotype A and B strains, and from C. tropicalis and C. guilliermondii. Radioactively labelled walls isolated from cells grown at either 28 degrees C or 37 degrees C were digested with a beta-glucanase complex (Zymolyase 20T) to release cell-wall-bound mannoproteins. Numerous molecular species with different electrophoretic mobilities were released from the various isolates. Differences appeared to be related to …

SerotypeAntigenicityAntigens FungalHydrolasesMicrobiologyBlastoconidiumMicrobiologyCell wallFungal ProteinsEpitopesSpecies SpecificityCell WallCandida albicansCandida albicansCandidaMembrane GlycoproteinsMolecular massbiologyImmunochemistryAntibodies MonoclonalMembrane Proteinsbiology.organism_classificationCorpus albicanscarbohydrates (lipids)BiochemistrySolubilityPolyclonal antibodiesbiology.proteinJournal of general microbiology
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Host glycoprotein Gp96 and scavenger receptor SREC interact with PorB of disseminating Neisseria gonorrhoeae in an epithelial invasion pathway.

2007

Neisseria gonorrhoeae expresses numerous surface proteins that mediate bacterial adherence and invasion during infection. Gonococci expressing serotype A of the major outer membrane porin PorB (PorB(IA)) are frequently isolated from patients with severe disseminating infections. PorB(IA) triggers efficient adherence and invasion under low phosphate conditions mimicking systemic bloodstream infections. Here, we identify the human heat shock glycoprotein Gp96 and the scavenger receptor SREC as PorB(IA)-specific receptors. Gonococci expressing PorB(IA), but not those expressing PorB serotype B instead, bind to purified native or recombinant Gp96. Depletion of Gp96 from host cells prevented adh…

SerotypeCancer ResearchMICROBIO2405 ParasitologyPorinsBiologymedicine.disease_causeEndoplasmic ReticulumMicrobiologyBacterial Adhesionlaw.inventionMicrobiologyGonorrhealawVirologyImmunology and Microbiology(all)medicineAnimalsHumansScavenger receptorReceptorMolecular BiologyCells Culturedchemistry.chemical_classificationMembrane Glycoproteins10061 Institute of Molecular Cancer Research2404 MicrobiologyEpithelial CellsNeisseria gonorrhoeaeScavenger Receptors Class FchemistryPorin2406 VirologyRecombinant DNANeisseria gonorrhoeae570 Life sciences; biologyParasitologyGlycoproteinBacterial outer membraneProtein BindingCell hostmicrobe
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Hp, Gc, Cp, Tf, Bg and Pi phenotypes in leprosy patients and healthy controls from West Bengal (India)

1972

On a sample of n=601 leprous individuals and n=386 healthy controls from West Bengal (India) the question is discussed, if there are existing any associations between leprosy and several serum protein groups like haptoglobin, Gc, ceruloplasmin, transferrin, β2 I and Pi. No associations were found concerning the haptoglobins and transferrins. Certain associations came out respecting ceruloplasmin, β2 I and Pi phenotypes. However, these associations, which were found in connection with the different types and clinical courses of leprosy, should be reexamined by further research. The most striking results were obtained concerning the Gc proteins. In accordance with previously performed investi…

Serum proteinIndiaGene FrequencyLeprosyGeneticsmedicineHumansMetabolic diseaseGenetics (clinical)Glycoproteinschemistry.chemical_classificationPolymorphism GeneticHaptoglobinsbiologyHaptoglobinTransferrinCeruloplasminPi phenotypesmedicine.diseasePhenotypechemistryTransferrinImmunologybiology.proteinSerum GlobulinsWest bengalLeprosyFactor Analysis StatisticalCeruloplasminHuman Genetics
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The colocalizations of pulp neural stem cells markers with dentin matrix protein-1, dentin sialoprotein and dentin phosphoprotein in human denticle (…

2021

Abstract Background The primary dentin, secondary dentin, and reactive tertiary dentin are formed by terminal differentiated odontoblasts, whereas atubular reparative tertiary dentin is formed by odontoblast-like cells. Odontoblast-like cells differentiate from pulpal stem cells, which express the neural stem cell markers nestin, S100β, Sox10, and P0. The denticle (pulp stone) is an unique mineralized extracellular matrix that frequently occurs in association with the neurovascular structures in the dental pulp. However, to date, the cellular origin of denticles in human dental pulp is unclear. In addition, the non-collagenous extracellular dentin matrix proteins dentin matrix protein 1 (DM…

SialoglycoproteinsMatrix (biology)Neural Stem Cellsstomatognathic systemDentinmedicineHumansDental PulpExtracellular Matrix ProteinsOdontoblastsChemistryCell DifferentiationGeneral MedicinePhosphoproteinsDentin phosphoproteinDMP1Cell biologystomatognathic diseasesmedicine.anatomical_structureDentinal TubuleOdontoblastDentinDental Pulp CalcificationPulp (tooth)AnatomyDentin sialoproteinDevelopmental BiologyAnnals of Anatomy - Anatomischer Anzeiger
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Apical transport of osteopontin is independent of N-glycosylation and sialylation.

2002

Studies of how epithelial surface polarity into apical and basolateral domains is generated and maintained have proposed that carbohydrate modifications serve as apical targeting signals for proteins by interacting with lectin sorters. However, the experimental evidence in support of N-glycans, O-glycans and sialic acids mediating apical transport is still very controversial. This could be partly due to the fact that in most studies exogenously expressed proteins were analysed. One has, therefore, examined the role of carbohydrate moieties in apical targeting of the endogenous secretory protein osteopontin in MDCK cells. It was found, however, that sorting of osteopontin does not require N-…

Signal peptideAcetylgalactosamineGlycosylationProtein ConformationSialoglycoproteinsOligosaccharidesBiologyProtein Sorting SignalsKidneyCell Linechemistry.chemical_compoundDogsN-linked glycosylationLectinsCell polarityBenzyl CompoundsAnimalsOsteopontinMolecular BiologyCell PolarityEpithelial CellsCell BiologySialic acidTransport proteincarbohydrates (lipids)Molecular WeightProtein TransportProtein Sorting SignalsSecretory proteinchemistryBiochemistrybiology.proteinSialic AcidsOsteopontinMolecular membrane biology
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Molecular cloning and primary structure of a Rhesus (Rh)-like protein from the marine sponge Geodia cydonium

1997

In humans, the 30,000 M(r) Rhesus (Rh) polypeptide D (RhD) is a dominant antigen (Ag) of the Rh blood group system. To date, an Rh-like protein has been found in chimpanzees, gorillas, gibbons, and rhesus monkeys. Related to the 30,000 M(r) Rh Ag protein are two polypeptides of 50,000 M(r), the human 50,000 M(r) Rh Ag and the RhD-like protein from Caenorhabditis elegans. The function of all these proteins is not sufficiently known. Here we characterize a cDNA clone (GCRH) encoding a putative 57,000 M(r) polypeptide from the marine sponge Geodia cydonium, which shares sequence similarity both to the RhD Ag and the Rh50 glycoprotein. The sponge Rh-like protein comprises 523 aa residues; hydro…

Signal peptideDNA ComplementaryMolecular Sequence DataImmunologyMolecular cloningGeneticsAnimalsHumansAmino Acid SequenceCloning MolecularCaenorhabditis elegansGlycoproteinschemistry.chemical_classificationRh-Hr Blood-Group SystemBase SequenceSequence Homology Amino AcidbiologyProtein primary structurebiology.organism_classificationMolecular biologyPoriferaSpongeTransmembrane domainchemistryGlycoproteinRh blood group systemImmunogenetics
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Characterization of a glycosylphosphatidylinositol-bound cell-wall protein (GPI-CWP) in Yarrowia lipolytica.

2004

The structure and composition of the cell wall of yeast has so far been studied mainly in Saccharomyces cerevisiae. It is basically made up of three components: beta-glucans, chitin and mannose-containing glycoproteins, also called mannoproteins. Most covalently bound cell-wall mannoproteins belong to the so-called glycosylphosphatidylinositol cell-wall protein (GPI-CWP) family, cell-wall proteins that are bound through the remnant of a GPI residue to 1,6-beta-glucan. The non-conventional yeast Yarrowia lipolytica shares Generally Regarded As Safe (GRAS) status with S. cerevisiae, has some industrial applications and is increasingly being proposed as a host for the production of recombinant…

Signal peptideSaccharomyces cerevisiae ProteinsGlycosylphosphatidylinositolsSaccharomyces cerevisiaeGenes FungalMolecular Sequence DataYarrowiaSaccharomyces cerevisiaeBiologyMicrobiologyGene productFungal ProteinsSpecies SpecificityCell WallAmino Acid SequenceDNA FungalPeptide sequencechemistry.chemical_classificationMembrane GlycoproteinsBase SequenceSequence Homology Amino AcidFungal geneticsMembrane ProteinsYarrowiabiology.organism_classificationYeastcarbohydrates (lipids)BiochemistrychemistryGlycoproteinMicrobiology (Reading, England)
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