Search results for " Immunoelectron"

showing 10 items of 64 documents

Pollen-stigma adhesion in Brassica spp involves SLG and SLR1 glycoproteins.

1999

The adhesion of pollen grains to the stigma is the first step of pollination in flowering plants. During this step, stigmas discriminate between pollen grains that can and cannot be permitted to effect fertilization. This selection is operated by various constituents of the cell walls of both partners. Several genes structurally related to the self-incompatibility system that prevents self-pollination in Brassica spp are known to target their products into the stigma cell wall. We proposed previously that one of these genes, the one encoding the S locus glycoprotein (SLG)-like receptor 1 (SLR1), which is coexpressed with that encoding SLG, may participate in pollen-stigma adhesion. Here, we…

PollinationPlant ScienceBrassicaBiologymedicine.disease_causeAntibodiesCell wallPollenmedicineCell AdhesionPollen adhesionCell adhesionMicroscopy ImmunoelectronGeneGlycoproteinsPlant Proteinschemistry.chemical_classificationGeneticsfood and beveragesCell BiologyOligonucleotides AntisensePlants Genetically ModifiedPollen hydrationCell biologychemistryMicroscopy Electron ScanningPollenIsoelectric FocusingGlycoproteinResearch ArticleThe Plant cell
researchProduct

Calpain 1 and 2 Are Required for RNA Replication of Echovirus 1▿

2007

ABSTRACT Calpains are calcium-dependent cysteine proteases that degrade cytoskeletal and cytoplasmic proteins. We have studied the role of calpains in the life cycle of human echovirus 1 (EV1). The calpain inhibitors, including calpeptin, calpain inhibitor 1, and calpain inhibitor 2 as well as calpain 1 and calpain 2 short interfering RNAs, completely blocked EV1 infection in the host cells. The effect of the inhibitors was not specific for EV1, because they also inhibited infection by other picornaviruses, namely, human parechovirus 1 and coxsackievirus B3. The importance of the calpains in EV1 infection also was supported by the fact that EV1 increased calpain activity 3 h postinfection. …

ProteasesImmunoelectron microscopyImmunologyParechovirusVirus ReplicationMicrobiologyCell LineViral entryVirologyHumansGene SilencingEnzyme InhibitorsMicroscopy ImmunoelectronMicroscopy ConfocalbiologyCalpainCytoplasmic VesiclesRNACalpainMolecular biologyCell biologyVirus-Cell InteractionsEnterovirus B HumanViral replicationCell cultureInsect ScienceCalpain-2biology.proteinRNA Viral
researchProduct

Clustering induces a lateral redistribution of α2β1 integrin from membrane rafts to caveolae and subsequent protein kinase C-dependent internalization

2004

Integrin alpha 2 beta 1 mediates the binding of several epithelial and mesenchymal cell types to collagen. The composition of the surrounding plasma membrane, especially caveolin-1- and cholesterol-containing membrane structures called caveolae, may be important to integrin signaling. On cell surface alpha 2 beta 1 integrin was located in the raft like membrane domain, rich in GPI-anchored proteins, rather than in caveolae. However, when antibodies were used to generate clusters of alpha 2 beta 1 integrin, they started to move laterally on cell surface along actin filaments. During the lateral movement small clusters fused together. Finally alpha 2 beta 1 integrin was found inside caveolae …

Protein Kinase C-alphaEndosomeintegrinkinasemedia_common.quotation_subjectCaveolin 1IntegrinCoated VesiclesEndosomesCaveolaeCaveolinsCell Membrane StructuresCD49cCollagen receptorCell membraneCaveolaemedicineHumansantibodiesMicroscopy ImmunoelectronInternalizationMolecular BiologyCells CulturedProtein Kinase Cmedia_commonbiologyCell MembraneArticlesCell BiologyIntegrin alphaVproteinsEnterovirus B HumanCell biologyActin Cytoskeletonmedicine.anatomical_structureIntegrin alphaVcaveolaebiology.proteinIntegrin alpha2beta1
researchProduct

Immuno-electron microscopic localization of the alpha(1) and beta(1)-subunits of soluble guanylyl cyclase in the guinea pig organ of corti.

2000

Guanylyl cyclases (GC) catalyze the formation of the intracellular signal molecule cyclic GMP from GTP. For some years it has been known that the heme-containing soluble guanylyl cyclase (sGC) is stimulated by NO and NO-containing compounds. The sGC enzyme consists of two subunits (alpha(1) and beta(1)). In the present study, the alpha(1) and beta(1)-subunits were identified in the guinea pig cochlea at the electron microscopic level using a post-embedding immuno-labeling procedure. Ultrathin sections of LR White embedded specimens were incubated with various concentrations of two rabbit polyclonal antibodies to the alpha(1)- and beta(1)-subunit, respectively. The immunoreactivity was visua…

Protein subunitImmunocytochemistryGuinea PigsAntibodiesmedicineAnimalsMicroscopy ImmunoelectronMolecular BiologyHair Cells Auditory InnerbiologyTissue EmbeddingGeneral NeuroscienceMolecular biologyPrimary and secondary antibodiesHair Cells Auditory Outermedicine.anatomical_structureBiochemistrySolubilityOrgan of CortiCytoplasmGuanylate Cyclasebiology.proteinDeiters cellssense organsNeurology (clinical)Hair cellNitric Oxide SynthaseSoluble guanylyl cyclaseDevelopmental BiologySignal TransductionBrain research
researchProduct

Rhodopsin transport in the membrane of the connecting cilium of mammalian photoreceptor cells

2000

The transport of the photopigment rhodopsin from the inner segment to the photosensitive outer segment of vertebrate photoreceptor cells has been one of the main remaining mysteries in photoreceptor cell biology. Because of the lack of any direct evidence for the pathway through the photoreceptor cilium, alternative extracellular pathways have been proposed. Our primary aim in the present study was to resolve rhodopsin trafficking from the inner to the outer segment. We demonstrate, predominantly by high-sensitive immunoelectron microscopy, that rhodopsin is also densely packed in the membrane of the photoreceptor connecting cilium. Present prominent labeling of rhodopsin in the ciliary mem…

RhodopsinOpsingenetic structuresPhotoreceptor Connecting CiliumImmunoblottingMolecular Sequence Datamacromolecular substancesMyosinsBiologyPhotoreceptor cellRats Sprague-DawleyMiceRetinal Rod Photoreceptor CellsStructural BiologymedicineAnimalsHumansPhotopigmentAmino Acid SequenceCiliaMicroscopy ImmunoelectronCiliary membraneCiliumRod OpsinsAntibodies MonoclonalDyneinsBiological TransportCell BiologyMiddle AgedRod Cell Outer SegmentActin cytoskeletonImmunohistochemistryActinseye diseasesRatsCell biologyMice Inbred C57BLmedicine.anatomical_structureRhodopsinMyosin VIIabiology.proteinCattleFemalesense organsRetinitis PigmentosaCell Motility and the Cytoskeleton
researchProduct

Differential expression and interaction with the visual G-protein transducin of centrin isoforms in mammalian photoreceptor cells.

2004

Photoisomerization of rhodopsin activates a heterotrimeric G-protein cascade leading to closure of cGMP-gated channels and hyperpolarization of photoreceptor cells. Massive translocation of the visual G-protein transducin, Gt, between subcellular compartments contributes to long term adaptation of photoreceptor cells. Ca(2+)-triggered assembly of a centrin-transducin complex in the connecting cilium of photoreceptor cells may regulate these transducin translocations. Here we demonstrate expression of all four known, closely related centrin isoforms in the mammalian retina. Interaction assays revealed binding potential of the four centrin isoforms to Gtbetagamma heterodimers. High affinity b…

Rhodopsingenetic structuresLightBlotting WesternBiologyBiochemistryRetinaRats Sprague-DawleyMiceCalcium-binding proteinHeterotrimeric G proteinmedicineAnimalsProtein IsoformsScattering RadiationCiliaTransducinMicroscopy ImmunoelectronMolecular BiologyCyclic GMPGlutathione TransferaseCentrosomeRetinaChromatographyDose-Response Relationship DrugReverse Transcriptase Polymerase Chain ReactionCiliumCalcium-Binding ProteinsCell BiologySequence Analysis DNARod Cell Outer SegmentRecombinant ProteinsCell biologyRatsMice Inbred C57BLKineticsProtein Transportmedicine.anatomical_structureMicroscopy FluorescenceRhodopsinCentrosomeCentrinbiology.proteinCalciumCattleElectrophoresis Polyacrylamide Gelsense organsTransducinProtein BindingThe Journal of biological chemistry
researchProduct

A novel Usher protein network at the periciliary reloading point between molecular transport machineries in vertebrate photoreceptor cells.

2008

Contains fulltext : 69178.pdf (Publisher’s version ) (Closed access) The human Usher syndrome (USH) is the most frequent cause of combined deaf-blindness. USH is genetically heterogeneous with at least 12 chromosomal loci assigned to three clinical types, USH1-3. Although these USH types exhibit similar phenotypes in human, the corresponding gene products belong to very different protein classes and families. The scaffold protein harmonin (USH1C) was shown to integrate all identified USH1 and USH2 molecules into protein networks. Here, we analyzed a protein network organized in the absence of harmonin by the scaffold proteins SANS (USH1G) and whirlin (USH2D). Immunoelectron microscopic anal…

Scaffold proteinGenetics and epigenetic pathways of disease [NCMLS 6]XenopusCell Cycle ProteinsNerve Tissue ProteinsBiologyIn Vitro TechniquesNeuroinformatics [DCN 3]TransfectionModels BiologicalReceptors G-Protein-CoupledMiceChlorocebus aethiopsProtein Interaction MappingGeneticsPerception and Action [DCN 1]otorhinolaryngologic diseasesAnimalsHumansNeurosensory disorders [UMCN 3.3]Cell Cycle ProteinMicroscopy ImmunoelectronMolecular BiologyIntegral membrane proteinGenetics (clinical)Adaptor Proteins Signal TransducingRenal disorder [IGMD 9]GeneticsMice KnockoutExtracellular Matrix ProteinsCiliumSignal transducing adaptor proteinMembrane ProteinsGeneral MedicineTransmembrane proteinCell biologyMice Inbred C57BLCytoskeletal ProteinsEctodomainGenetic defects of metabolism [UMCN 5.1]COS CellsNIH 3T3 CellsCervical collarUsher SyndromesFunctional Neurogenomics [DCN 2]Photoreceptor Cells VertebrateSubcellular FractionsImmunity infection and tissue repair [NCMLS 1]
researchProduct

Contactus adherens, a special type of plaque-bearing adhering junction containing M-cadherin, in the granule cell layer of the cerebellar glomerulus.

1995

In the glomeruli of the granule cell layer of mammalian cerebellum, neuronal extensions are interconnected by numerous small, nearly isodiametric (diameters up to 0.1 micron), junctions previously classified as puncta adherentia related to the vinculin-containing, actin microfilament-anchoring junctions of the zonula adherens of epithelial and certain other cells. Using immunofluorescence and immunoelectron microscopy, we have found, however, that these junctions are negative for E- and VE-cadherin, for desmosomal cadherins, and also for vinculin, alpha-actinin, and desmoplakin, but they do contain, in addition to the protein plakoglobin common to all forms of adhering junctions, the plaque…

SwineImmunoelectron microscopyPlakoglobinFluorescent Antibody TechniqueSeptate junctionsMice Inbred StrainsAntibodiesAdherens junctionMiceCerebellummedicineAnimalsHumansDesmosomal CadherinsMicroscopy ImmunoelectronActinNeuronsMultidisciplinarybiologyVinculinGranule cellCadherinsEmbryo MammalianCell biologymedicine.anatomical_structureIntercellular Junctionsbiology.proteinCattleRabbitsResearch ArticleProceedings of the National Academy of Sciences of the United States of America
researchProduct

Keyhole Limpet Hemocyanin Type 2 (KLH2): Detection and Immunolocalization of a Labile Functional Unit h

2000

Keyhole limpet hemocyanin (KLH) is a mixture of two hemocyanin isoforms, termed KLH1 and KLH2. Within KLH1 eight oxygen-binding functional units (FUs), 1-a to 1-h, have been identified, in contrast to KLH2, which was previously thought to be organized in seven FUs (2-a to 2-g). By limited proteolysis of KLH2 subunits, isolation of the polypeptide fragments, and N-terminal sequencing, we have now identified an eighth FU of type h, with a molecular mass of 43 kDa. This is unusually small for a FU h from a gastropodan hemocyanin. It is also shown that KLH2 didecamers can be split into a stable and homogeneous population of decamers by dialysis against 50 mM Tris/HCl, pH 7.5, in the absence of …

Trismedicine.medical_treatmentProteolysisMolecular Sequence DataPopulationMegathura crenulataDivalentStructure-Activity Relationshipchemistry.chemical_compoundStructural BiologyEndopeptidasesmedicineAnimalsProtein IsoformsAmino Acid SequenceMicroscopy ImmunoelectronProtein Structure Quaternaryeducationchemistry.chemical_classificationeducation.field_of_studybiologymedicine.diagnostic_testMolecular massAntibodies MonoclonalHemocyaninbiology.organism_classificationMolecular biologyMolecular WeightchemistryMolluscaHemocyaninsbiology.proteinKeyhole limpet hemocyaninJournal of Structural Biology
researchProduct

B and T lymphocytes are affected in lysosomal disorders--an immunoelectron microscopic study.

1991

Circulating lymphocytes of four patients with mucopolysaccharidoses II and IIIA, four patients with juvenile neuronal ceroid-lipofuscinosis, one patient each with glycogenosis type II, infantile neuronal ceroid-lipofuscinosis, and Gaucher disease were classified by immunoelectron microscopy as B or T lymphocytes. Disease-specific lysosomal inclusions as well as non-specific lysosomal organelles, especially Gall bodies were identified in B and T lymphocytes. These non-quantitative studies indicate that both B and T lymphocytes participate in the lysosomal storage process.

congenital hereditary and neonatal diseases and abnormalitiesPathologymedicine.medical_specialtyHistologyImmunoelectron microscopyMucopolysaccharidosisT-LymphocytesCentral nervous systemVacuoleBiologyPathology and Forensic MedicinePhysiology (medical)OrganellemedicineLysosomal storage diseaseHumansMicroscopy ImmunoelectronB-Lymphocytesnutritional and metabolic diseasesT lymphocytemedicine.diseasemedicine.anatomical_structureNeurologyNeuronal ceroid lipofuscinosisNeurology (clinical)Metabolism Inborn ErrorsNeuropathology and applied neurobiology
researchProduct