Search results for "nucleoplasm"

showing 7 items of 17 documents

Cytoplasmic parvovirus capsids recruit importin beta for nuclear delivery

2020

Parvoviruses are an important platform for gene and cancer therapy. Their cell entry and the following steps including nuclear import are inefficient limiting their use in therapeutic applications. Two models exist on parvoviral nuclear entry: classical import of the viral capsid using nuclear transport receptors of the importin (karyopherin) family, or direct attachment of the capsid to the nuclear pore complex leading to local disintegration of the nuclear envelope. Here, by laser scanning confocal microscopy and in situ proximity ligation analysis combined with co-immunoprecipitation we showed that infection requires importin β-mediated access into the nuclear pore complex and nucleopori…

nucleoplasmkaryoferiinitsolulimatumaimportin βcytoplasminteractionparvoviruksetParvovirus capsidkapsidi
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Localization of antigens PwA33 and La on lampbrush chromosomes and on nucleoplasmic structures in the oocyte of the urodele Pleurodeles waltl: Light …

1994

Monoclonal antibodies A33/22 and La11G7 have been used to study the distribution of the corre-sponding antigens, PwA33 and La, on the lampbrush chromosome loops and nucleoplasmic structures of P. waltl oocytes, using immunofluorescence, confocal laser scanning microscopy and immunogold labeling. The results obtained with these antibodies have been compared with those obtained with the Sm-antigen-specific monoclonal antibody Y12. All these monoclonal antibodies (mAbs) labeled the matrices of the majority of normal loops along their whole length. Nucleoplasmic RNP granules showed a strong staining with the mAbs La11G7 and Y12 throughout their mass, but with the mAb A33/22, they showed only a …

PleurodelesTranscription Geneticmedicine.drug_classFluorescent Antibody TechniqueMonoclonal antibodyImmunofluorescenceAutoantigensChromosomeslaw.inventionPleurodeleslawGeneticsmedicineAnimalsMicroscopy ImmunoelectronGenetics (clinical)OrganellesNucleoplasmbiologymedicine.diagnostic_testAntibodies MonoclonalNuclear ProteinsImmunogold labellingbiology.organism_classificationImmunohistochemistryMolecular biologyCell biologyStainingLampbrush chromosomeRibonucleoproteinsOocytesFemaleElectron microscopeChromosoma
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Freeze-fracture features of epithelioid cells, multinucleated giant cells, and phagocytic macrophages

1987

The freeze-fracture morphology of epithelioid cells, multinucleated giant cells (Langhans' type), and phagocytic macrophages was investigated. The intensely folded and interdigitating surface membranes of epithelioid cells and multinucleated giant cells displayed no specialized areas of cell contact. The size of the intramembranous particles (IMP) and the fact that the area density of IMPs was higher in the cytoplasmic (P) faces than in the external (E) faces of the cell membranes agreed with observations in other eukaryotic cells. The area densities of the IMPs suggest lower transport rates of molecules across the cell membranes of granuloma cells than of certain epithelial cells. Small pi…

Nuclear EnvelopeLanghans giant cellBiologyEpitheliumCell membranemedicineAnimalsFreeze FracturingCell NucleusPhagocytesGranulomaNucleoplasmMacrophagesCell MembraneGranule (cell biology)Membrane ProteinsIntracellular MembranesRatsCell biologyCell nucleusmedicine.anatomical_structureGiant cellCytoplasmNephritis InterstitialLysosomesEpithelioid cellVirchows Archiv B Cell Pathology Including Molecular Pathology
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Viral highway to nucleus exposed by image correlation analyses.

2018

AbstractParvoviral genome translocation from the plasma membrane into the nucleus is a coordinated multistep process mediated by capsid proteins. We used fast confocal microscopy line scan imaging combined with image correlation methods including auto-, pair- and cross-correlation, and number and brightness analysis, to study the parvovirus entry pathway at the single-particle level in living cells. Our results show that the endosome-associated movement of virus particles fluctuates from fast to slow. Fast transit of single cytoplasmic capsids to the nuclear envelope is followed by slow movement of capsids and fast diffusion of capsid fragments in the nucleoplasm. The unique combination of …

0301 basic medicineparvovirusesviruseslcsh:MedicineGene ExpressionmikroskopiaMicroscopy Atomic Forcelaw.inventionXenopus laevisCytosollawImage Processing Computer-AssistedOrganic Chemicalslcsh:ScienceMultidisciplinaryMicroscopy ConfocalbiologyChemistryimagingbeta Karyopherinsmedicine.anatomical_structurekuvantaminenCapsidmicroscopyParvovirus CanineGreen Fluorescent ProteinsActive Transport Cell NucleusImportinVirusArticleCell Line03 medical and health sciencesCapsidConfocal microscopymedicineAnimalsparvoviruksetFluorescent DyesCell NucleusNucleoplasmParvoviruslcsh:RVirionEpithelial Cellsbiology.organism_classification030104 developmental biologySpectrometry FluorescenceCytoplasmBiophysicsCatsOocyteslcsh:QCapsid ProteinsNucleusScientific reports
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Midregion PTHrP regulates Rip1 and caspase expression in MDA-MB231 breast cancer cells.

2007

It was previously reported that the midregion PTHrP domain (38-94)-amide restrains growth and invasion "in vitro", causes striking toxicity and accelerates death of some breast cancer cell lines, the most responsive being MDA-MB231 whose tumorigenesis was also attenuated "in vivo". In addition, we have demonstrated that midregion PTHrP is imported in the nucleoplasm of cultured MDA-MB231 cells, and that "in vitro" it can bind chromatin of metaphase spread preparations and also an isolated 20-mer oligonucleotide, thereby appearing endowed with a putative transcription factor-like DNA-binding ability. Here, we examined whether PTHrP (38-94)-amide was able to modulate the expression of genes e…

Cancer ResearchProgrammed cell deathbcl-X ProteinApoptosisBreast NeoplasmsPTHrP Rip1 caspase breast cancer cellsmedicine.disease_causeTransfectionCell MovementCell Line TumorGene expressionmedicineTranscriptional regulationHumansNeoplasm InvasivenessSettore BIO/06 - Anatomia Comparata E Citologiaskin and connective tissue diseasesCaspaseCell ProliferationNucleoplasmbiologyJNK Mitogen-Activated Protein KinasesParathyroid Hormone-Related ProteinRNA-Binding ProteinsOligonucleotides AntisenseMolecular biologyPeptide FragmentsChromatinCell biologyNuclear Pore Complex ProteinsSettore BIO/12 - Biochimica Clinica E Biologia Molecolare ClinicaOncologyApoptosisCaspasesbiology.proteinFemalebcl-Associated Death ProteinCarcinogenesisSignal TransductionBreast cancer research and treatment
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Midregion PTHrP and Human Breast Cancer Cells

2010

PTHrP is a polyhormone undergoing proteolytic processing into smaller bioactive forms, comprising an N-terminal peptide, which is the mediator of the “classical” PTH-like effect, as well as midregion and C-terminal peptides. The midregion PTHrP domain (38-94)-amide was found to restrain growth and invasionin vitroof some breast cancer cell lines, causing striking toxicity and accelerating death; the most responsive being MDA-MB231, whose tumorigenesis was also attenuatedin vivo. In addition, midregion PTHrP appears to be imported in the nucleoplasm of cultured MDA-MB231 cells andin vitro, it can bind chromatin of metaphase spread preparations and also an isolated 20-mer oligonucleotide, the…

Gene Expressionlcsh:MedicineBreast NeoplasmsDNA FragmentationBiologymedicine.disease_causelcsh:TechnologyGeneral Biochemistry Genetics and Molecular BiologyTranscription (biology)Cell Line TumorPTHrP breast cancer cancer cell gene expression cytotoxicityGene expressionmedicineHumansSettore BIO/06 - Anatomia Comparata E CitologiaMDA-MB231lcsh:ScienceDNA statusGeneral Environmental ScienceMini-Review ArticleNucleoplasmlcsh:Tmidregion PTHrPlcsh:RParathyroid Hormone-Related ProteinapoptosisGeneral MedicineMolecular biologynuclear importIn vitroCell biologyChromatinPTHrP (38-94)Cancer cellprotein degradationFemalelcsh:QCarcinogenesisReprogrammingbreast cancer cellsThe Scientific World Journal
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Itraconazole inhibits nuclear delivery of extracellular vesicle cargo by disrupting the entry of late endosomes into the nucleoplasmic reticulum

2021

ABSTRACT Extracellular vesicles (EVs) are mediators of intercellular communication under both healthy and pathological conditions, including the induction of pro‐metastatic traits, but it is not yet known how and where functional cargoes of EVs are delivered to their targets in host cell compartments. We have described that after endocytosis, EVs reach Rab7+ late endosomes and a fraction of these enter the nucleoplasmic reticulum and transport EV biomaterials to the host cell nucleoplasm. Their entry therein and docking to outer nuclear membrane occur through a tripartite complex formed by the proteins VAP‐A, ORP3 and Rab7 (VOR complex). Here, we report that the antifungal compound itracona…

Models MolecularHistologyAntifungal AgentsEndosomeNuclear EnvelopeNucleoplasmic reticulumActive Transport Cell NucleusVesicular Transport ProteinsHost cell nucleoplasmEndosomesEndocytosisFatty Acid-Binding ProteinsExosomeCell LineExtracellular VesiclesCell MovementSettore BIO/13 - Biologia ApplicataHumanscancerexosomemetastasisendosomeResearch ArticlesCholestenonesmicro‐vesicleQH573-671Chemistryrab7 GTP-Binding ProteinsCell BiologyExtracellular vesicleSaponinsEndocytosisCell biologyKetoconazoleCancer cellintercellular communicationnucleoplasmic reticulumcancer endosome exosome intercellular communication metastasis micro-vesicle nucleoplasmicreticulumItraconazoleCytologyIntracellularResearch ArticleJournal of Extracellular Vesicles
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