Search results for "Cytoplasm"

showing 9 items of 659 documents

INHIBITION OF CELLULAR GROWTH AND STEROID 11β-HYDROXYLATION INRAS-TRANSFORMED ADRENOCORTICAL CELLS BY THE FUNGAL TOXINS BETICOLINS

1996

Abstract The proliferation of GM16 and 4CDTras-transformed newborn rat adrenocortical (RTAC) cells and Y1 mouse adrenal tumor cells was inhibited by beticolins, the fungal toxins extracted fromCercospora beticola, at submicromolar concentrations in a dose-dependent manner. Inhibitory concentrations for half the maximum inhibition were 150, 75 and 25 n M for beticolin-1 and 230, 150 and 50 n M for beticolin-2 in GM16, 4CDT and Y1 cells respectively. Beticolins strongly inhibited the production of 11β-hydroxysteroids on the second and third days of treatment in a dose-dependent manner between 0.1 and 1 μ M . Beticolins were shown by confocal microscopy to be localized in cytoplasmic organelle…

medicine.medical_treatmentAdrenal Gland NeoplasmsBiologyTransfectionHeterocyclic Compounds 4 or More RingsSteroidlaw.inventionHydroxylationMiceStructure-Activity Relationshipchemistry.chemical_compoundConfocal microscopylawOrganelleTumor Cells CulturedmedicineAnimalsCells CulturedHydroxysteroidsMicroscopy ConfocalDose-Response Relationship DrugCell growthCell BiologyGeneral MedicineMycotoxinsGrowth InhibitorsNeoplasm ProteinsRatsCell Transformation NeoplasticGenes rasAnimals NewbornchemistryBiochemistryCytoplasmAdrenal CortexSteroid 11-beta-HydroxylaseSignal transductionGrowth inhibitionCell DivisionCell Biology International
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DNA fragmentation index, pAKT and pERK1/2 in cumulus cells are related to oocyte competence in patients undergoing in vitro fertilization programme

2019

SummaryActivated pERK1/2 and pAKT are key players in supporting cell survival and proliferation pathways. Translocation of pERK1/2 into the nucleus, where it interacts with transcription factors and DNA itself, is instrumental in exerting an anti-apoptotic effect. In this study, pAKT levels, pERK1/2 nuclear localization and DNA fragmentation index (DFI) in cumulus cells of single cumulus–oocyte complexes of patients undergoing in vitro fertilization programmes were evaluated and correlated with the clinical outcome of the related embryos. For a positive clinical outcome of blastocyst development, pERK1/2 nuclear localization and DFI value had a significant inverse relationship, whereas the …

medicine.medical_treatmentMolecular markerBiologyCell survivalIntracytoplasmic sperm injectionSettore MED/01 - Statistica MedicaAndrology03 medical and health sciences0302 clinical medicineOocyte qualitymedicineBlastocystViability assaySettore BIO/06 - Anatomia Comparata E Citologia030304 developmental biology0303 health sciences030219 obstetrics & reproductive medicineIn vitro fertilisationApoptosiCell BiologyOocytemedicine.anatomical_structureApoptosisDNA fragmentationDFIIntracellularDevelopmental BiologyZygote
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Osteoprotegerin (OPG) and RANKL expression and distribution in developing human craniomandibular joint.

2005

Abstract During embryogenesis the bone tissue of craniomandibular joint (CMJ) is formed through two pathways: intramembranous ossification and endochondral ossification. The development process is under the control of regulatory factors.The osteoprotegerin (OPG) and the receptor activator of nuclear factor (NF)-κB ligand are key regulators of osteoclastogenesis. The aim of this study is the localization of OPG and RANKL mRNA and protein in the foetal CMJ by immunohistochemistry (IHC) and in situ hybridization (ISH). The main results were: OPG and RANKL mRNA and protein were co-localized in the same cell types; OPG and RANKL were specially immunolocated in osteogenic cells; immunolabeling wa…

musculoskeletal diseasesCartilage Articularmedicine.medical_specialtyReceptors Cytoplasmic and NuclearIn situ hybridizationBiologyBone tissueReceptors Tumor Necrosis FactorBone remodelingOsteoprotegerinOsteogenesisInternal medicineBone cellmedicineHumansRNA MessengerEndochondral ossificationIn Situ HybridizationGlycoproteinsMembrane GlycoproteinsReceptor Activator of Nuclear Factor-kappa BTemporomandibular JointRANK LigandOsteoprotegerinCell BiologyGeneral MedicineImmunohistochemistryCell biologyEndocrinologymedicine.anatomical_structureRANKLIntramembranous ossificationbiology.proteinCarrier ProteinsDevelopmental BiologyTissuecell
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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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ALS-RELATED FUS PROTEIN IS MISLOCALIZED TO CYTOPLASM AND RECRUITED INTO STRESS GRANULES IN FIBROBLASTS OF ASYMPTOMATIC FUS P525L MUTATION CARRIERS

Symptoms onset in Amyotrophic Lateral Sclerosis (ALS) occur when over 70% of motor neurons is already lost, suggesting a relatively long pre-symptomatic phase. The description of several genes linked to ALS (e.g., SOD1, FUS, TARDP, C9orf72) has now allowed identification of pre-symptomatic carriers. These pre-symptomatic (or even preclinical) carriers can be followed up with the aim to identify the very early clinical disease-related changes or a valuable biomarker. These efforts seem at present the best approach for the implementation of an early symptomatic therapy or for the disease prevention. In this work, we studied the expression of FUS protein in cultured skin fibroblasts from pre-s…

stress granuleshuman fibroblastsFUS P525L carriersSettore MED/26 - NeurologiaALScytoplasmic FUS expressionSettore BIO/09 - Fisiologia
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Apoptosis in human unfertilized oocytes after intracytoplasmic sperm injection

2005

Objective To investigate the presence of programmed cell death in unfertilized oocytes after intracytoplasmic sperm injection (ICSI), assuming that previous apoptotic events could be correlated with the fertilization failure. Design Comparison of the rate of DNA fragmentation in human oocytes at different stages of maturation soon after pick-up (control) and in unfertilized oocytes after ICSI treatment. Setting In vitro fertilization (IVF) laboratory with extensive ICSI experience. Patient(s) Sixty-three patients undergoing assisted fertilization by ICSI. Intervention(s) Terminal deoxynucleotidyl transferase-mediated digoxigenin-dUTP nick-end labeling (TUNEL) assay and anticaspase-3 cleaved…

virgin oocytesmedicine.medical_treatmentintracytoplasmic sperm injectionApoptosisDNA FragmentationBiologyICSIIntracytoplasmic sperm injectionAndrologyHuman fertilizationhuman oocyteConfidence IntervalsmedicineHumansSperm Injections Intracytoplasmicreproductive and urinary physiologyFertilisationApoptosis; fertilization failure; intracytoplasmic sperm injection; ICSI; human oocytes; virgin oocytesChi-Square DistributionIn vitro fertilisationTUNEL assayurogenital systemfertilization failureApoptosiObstetrics and GynecologyOocyteSpermmedicine.anatomical_structureReproductive MedicineOocytesDNA fragmentationFemaleFertility and Sterility
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Assembly and Translocation of Papillomavirus Capsid Proteins

2002

ABSTRACT The major and minor capsid proteins of polyomavirus are preassembled in the cytoplasm and translocated to the nucleus only as a VP1-VP2/VP3 complex. In this study, we describe independent nuclear translocation of the L1 major protein and the L2 minor capsid protein of human papillomavirus type 33 by several approaches. First, we observed that expression and nuclear translocation of L2 in natural lesions precede expression of L1. Second, using a cell culture system for coexpression, we found that accumulation of L2 in nuclear domain 10 (ND10) subnuclear structures precedes L1 by several hours. In contrast, complexes of L2 and mutants of L1 forced to assemble in the cytoplasm are tra…

virusesImmunologyActive Transport Cell NucleusChromosomal translocationBiologyMicrobiologychemistry.chemical_compoundCapsidVirologyMG132medicineAnimalsHumansPapillomaviridaeCOS cellsStructure and AssemblyVirus AssemblyOncogene Proteins Viralbiochemical phenomena metabolism and nutritionMolecular biologymedicine.anatomical_structureCapsidchemistryCytoplasmCell cultureInsect ScienceCOS CellsProteasome inhibitorCapsid ProteinsFemaleNucleusmedicine.drug
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The human autoantigen La/SS-B accelerates herpes simplex virus type 1 replication in transfected mouse 3T3 cells.

1998

SUMMARY Permanently transfected mouse cell lines which expressed different levels of the human autoantigen La/SS-B were infected with different strains of herpes simplex virus type 1, including the strains ANG, HSZP, 17syn+ and HFEM. During infection the localization of the human La protein was followed using an anti-La MoAb, which recognized only the human La protein but did not cross-react with either the endogenous mouse La protein or any viral encoded protein. After infection La protein was transported from the nucleus to the cytoplasm. The time course of translocation was dependent on the amount of human La protein expressed in the respective cell line. Moreover, acceleration of viral …

virusesImmunologyHerpesvirus 1 Humanmedicine.disease_causeTransfectionVirus ReplicationAutoantigensVirus3T3 cellsSingle-stranded binding proteinMicemedicineImmunology and AllergyAnimalsHumansbiologyTransfection3T3 CellsOriginal ArticlesHerpes simplex virusmedicine.anatomical_structureViral replicationGene Expression RegulationRibonucleoproteinsCytoplasmCell cultureImmunologybiology.proteinClinical and experimental immunology
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SARS-CoV-2 envelope protein topology in eukaryotic membranes

2020

Coronavirus E protein is a small membrane protein found in the virus envelope. Different coronavirus E proteins share striking biochemical and functional similarities, but sequence conservation is limited. In this report, we studied the E protein topology from the new SARS-CoV-2 virus both in microsomal membranes and in mammalian cells. Experimental data reveal that E protein is a single-spanning membrane protein with the N-terminus being translocated across the membrane, while the C-terminus is exposed to the cytoplasmic side (Nt lum /Ct cyt ). The defined membrane protein topology of SARS-CoV-2 E protein may provide a useful framework to understand its interaction with other viral and ho…

virusescoronavirusmedicine.disease_causeViral Envelope Proteinsmembrane insertionPeptide sequencelcsh:QH301-705.5Topology (chemistry)PhylogenyCoronavirusMutationChemistryGeneral NeuroscienceProteïnes de membranaEukaryotavirus diseases129Recombinant ProteinsCell biologysars-cov-2MembraneProtein topologyCoronavirus InfectionsResearch Article1001topologyPneumonia ViralImmunologySequence alignmentBiologyTopologiaVirusGeneral Biochemistry Genetics and Molecular BiologyBetacoronavirusCoronavirus Envelope ProteinsViral envelopeMicrosomesmedicineHumansAmino Acid SequencePandemicsResearchCell MembraneCOVID-1915envelope proteinMembrane proteinlcsh:Biology (General)CytoplasmMutationSequence AlignmentOpen Biology
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