Search results for "Cytoplasm"

showing 10 items of 659 documents

Neuroglobin and cytoglobin:two new entries in the hemoglobin superfamily.

2004

Abstract: Neuroglobin (Ngb) and cytoglobin (Cygb) are two newly discovered intracellular members of the vertebrate hemoglobin (Hb) family. Ngb, predominantly expressed in nerve cells, is of ancient evolutionary origin and is homologous to nerve-globins of invertebrates. Cygb, present in many different tissues, shares common ancestry with myoglobin (Mb) and can be traced to early vertebrate evolution. Ngb and Cygb display the classical three-on-three -helical globin fold and are endowed with a hexa-coordinate heme Fe atom, in both their ferrous and ferric forms, having the heme distal HisE7 residue as the endogenous sixth ligand. Reversible intramolecular hexa- to penta-coordination of the h…

CytoglobinOxidative phosphorylationBiologyLigand (biochemistry)BiochemistryGlobin foldchemistry.chemical_compoundchemistryBiochemistryCytoplasmNeuroglobinHepatic stellate cellHuman medicineMolecular BiologyHemeBiology
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Myc Promoter-Binding Protein-1 (MBP-1) Is a Novel Potential Prognostic Marker in Invasive Ductal Breast Carcinoma

2010

BackgroundAlpha-enolase is a glycolytic enzyme that catalyses the formation of phosphoenolpyruvate in the cell cytoplasm. α-Enolase and the predominantly nuclear Myc promoter-binding protein-1 (MBP-1) originate from a single gene through the alternative use of translational starting sites. MBP-1 binds to the P2 c-myc promoter and competes with TATA-box binding protein (TBP) to suppress gene transcription. Although several studies have shown an antiproliferative effect of MBP-1 overexpression on several human cancer cells, to date detailed observations of α-enolase and MBP-1 relative expression in primary tumors versus normal tissues and their correlation with clinicopathological features ha…

CytoplasmAlpha-enolasePROGRESSIONAged 80 and overRegulation of gene expressionMultidisciplinaryQRGenetics and Genomics/Gene ExpressionMiddle AgedPrognosisPathology/Molecular PathologyNUDE-MICETransport proteinCarcinoma DuctalDNA-Binding ProteinsGene Expression Regulation NeoplasticProtein Transportmedicine.anatomical_structureGLYCOLYTIC ENZYMEOncology/Breast CancerMedicineCELL LUNG-CANCER; ALPHA-ENOLASE; PROTEOMIC ANALYSIS; GLYCOLYTIC ENZYME; NUDE-MICE; GENE; IDENTIFICATION; PROGRESSION; EXPRESSION; METASTASESFemalePROTEOMIC ANALYSISEnolase MBP-1 Breast cancer ImmunohistochemistryResearch ArticleAdultEXPRESSIONScienceCELL LUNG-CANCERBreast NeoplasmsBiologyDNA-binding proteinBiomarkers TumormedicineHumansNeoplasm InvasivenessGeneAgedCell NucleusIDENTIFICATIONBinding proteinALPHA-ENOLASEGENEMolecular biologySettore BIO/18 - GeneticaCell nucleusMETASTASESCytoplasmPhosphopyruvate Hydratasebiology.proteinPLoS ONE
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Nuclear–Cytoplasmic Interactions in Early Development

1985

CytoplasmBiologyCell biology
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Subcellular localization of pentachlorophenol 4-monooxygenase in Sphingobium chlorophenolicum ATCC 39723.

2002

Abstract We have studied the subcellular localization of pentachlorophenol 4-monooxygenase (PCP4MO) in Sphingobium chlorophenolicum ATCC 39723 during induction by pentachlorophenol (PCP). Using a monoclonal antibody CL6 specific to the native and recombinant PCP4MO, the enzyme was primarily found soluble as determined by immunoblot and ELISA analyses of cellular fractions. However, the enzyme was observed both in the soluble and membrane-bound forms during induction for 2–4 h, suggesting its translocation out from the cytoplasm. Electron microscopy confirmed that PCP4MO was predominantly present in the cytoplasm at 1 h, whereas at 4 h significant amount was detected also in the membrane and…

CytoplasmBiophysicsBiologyProtein Sorting SignalsBiochemistryMixed Function Oxygenaseschemistry.chemical_compoundBiosynthesisAntibody SpecificityInner membraneMolecular BiologySphingobium chlorophenolicumAlphaproteobacteriachemistry.chemical_classificationAntibodies MonoclonalCell BiologyPeriplasmic spacebiology.organism_classificationSubcellular localizationMolecular biologyImmunohistochemistryPentachlorophenolKineticsEnzymechemistryBiochemistryCytoplasmPeriplasmBiochemical and biophysical research communications
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Nuclear and Cytoplasmic Survivin: Molecular Mechanism, Prognostic, and Therapeutic Potential.

2007

Abstract Survivin's proposed dual role as an apoptosis inhibitor and a mitotic effector positioned it in the front line of cancer research. Notably, survivin is detected as a cytoplasmic and nuclear protein in cancer patients, which stimulated numerous studies to investigate and to speculate on the functional and prognostic significance of its dynamic localization. Recent evidence shows that the direct interaction of survivin with the nuclear export receptor Crm1 is critically involved in its intracellular localization and cancer-relevant functions. Here, we review our current understanding of the Crm1/survivin interface and discuss its potential prognostic and therapeutic relevance. [Cance…

CytoplasmCancer ResearchPathologymedicine.medical_specialtyApoptosis InhibitorSurvivinActive Transport Cell NucleusMitosisReceptors Cytoplasmic and NuclearKaryopherinsBiologyModels BiologicalInhibitor of Apoptosis ProteinsNeoplasmsSurvivinmedicineHumansNuclear proteinNuclear export signalReceptorMitosisCell NucleusEffectorCancerPrognosismedicine.diseaseNeoplasm ProteinsGene Expression Regulation NeoplasticOncologyCancer researchMicrotubule-Associated ProteinsBiologie
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The differentiation antigen NY-BR-1 is a potential target for antibody-based therapies in breast cancer

2007

Antibody-based cancer immunotherapy relies on the identification and characterization of target antigens and the development of potent antibodies recognizing the target. Here we report the expression analysis and molecular characterization of the differentiation antigen NY-BR-1, which we previously identified by using the SEREX (serological analysis of recombinant cDNA expression libraries) method. Corroborating methodologies, including mRNA quantitation and immunoblotting show that NY-BR-1 is strongly expressed in >70% of 129 breast tumors. Application of a NY-BR-1 specific antibody demonstrated NY-BR-1 expression in primary and metastastic breast cancers. In contrast, most of the breast c…

CytoplasmCancer ResearchPathologymedicine.medical_specialtyRecombinant Fusion Proteinsmedicine.medical_treatmentCellular differentiationGreen Fluorescent ProteinsImmunoblottingBreast NeoplasmsBiologyTargeted therapyBreast cancerAntigenCancer immunotherapyAntigens NeoplasmCell Line TumormedicineHumansRNA MessengerBinding SitesMicroscopy ConfocalReverse Transcriptase Polymerase Chain ReactionCell MembraneAntibodies MonoclonalMembrane ProteinsFlow Cytometrymedicine.diseaseAntigens DifferentiationImmunohistochemistryTumor antigenGene Expression Regulation NeoplasticOncologyCancer researchbiology.proteinImmunohistochemistryFemaleAntibodyHydrophobic and Hydrophilic InteractionsInternational Journal of Cancer
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Glutathione is recruited into the nucleus in early phases of cell proliferation.

2007

We have studied the possible correlation between nuclear glutathione distribution and the progression of the cell cycle. The former was studied by confocal microscopy using 5-chloromethyl fluorescein diacetate and the latter by flow cytometry and protein expression of Id2 and p107. In proliferating cells, when 41% of them were in the S+G(2)/M phase of the cell cycle GSH was located mainly in the nucleus. When cells reached confluence (G(0)/G(1)) GSH was localized in the cytoplasm with a perinuclear distribution. The nucleus/cytoplasm fluorescence ratio for GSH reached a maximal mean value of 4.2 +/- 0.8 at 6 h after cell plating. A ratio higher than 2 was maintained during exponential cell …

CytoplasmCellActive Transport Cell NucleusRetinoblastoma-Like Protein p107BiologyBiochemistry3T3 cellsFlow cytometrychemistry.chemical_compoundMicemedicineAnimalsMolecular BiologyInhibitor of Differentiation Protein 2Cell NucleusMicroscopy Confocalmedicine.diagnostic_testCell growthCell CycleCell BiologyGlutathione3T3 CellsCell cycleFlow CytometryMolecular biologyGlutathioneCell biologymedicine.anatomical_structurechemistryGene Expression RegulationCytoplasmNucleusThe Journal of biological chemistry
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The role of cell interactions in the control of RNA synthesis.

1967

CytoplasmChemistryCellular differentiation5.8S ribosomal RNACellRNAPhosphorus IsotopesCell DifferentiationRNA integrity numberNon-coding RNABiochemistry Genetics and Molecular Biology (miscellaneous)RNA polymerase IIICell biologymedicine.anatomical_structureRNA editingmedicineCentrifugation Density GradientAnimalsRNAUltracentrifugationEchinodermataBiochimica et biophysica acta
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Study of the Evolutionary Relationships among Limonium Species (Plumbaginaceae) Using Nuclear and Cytoplasmic Molecular Markers

2000

The genus Limonium, due to the patchiness of the natural habitats of its species as well as the high frequency of hybridization and polyploidy and the possibility of reproduction by apomixis, provides an example of all the principal mechanisms of rapid speciation of plants. As an initial study of evolution in this genus, we have analyzed intra- and interspecific variability in 17 species from section Limonium, the largest in the genus, based on RFLPs of cpDNA and nuclear rDNA ITS sequences. In the cpDNA analysis, 21 restriction enzymes were used, resulting in 779 fragments, 490 of which were variable and 339 parsimony informative. L. furfuraceum exhibited two relatively divergent cpDNA hapl…

CytoplasmChloroplastsLimoniumMolecular Sequence DataBiologyDNA RibosomalPhylogeneticsSequence Homology Nucleic AcidApomixisPolyphylyBotanyGeneticsMolecular BiologyPhylogenyPlant Physiological PhenomenaEcology Evolution Behavior and SystematicsCell NucleusBase SequencePhylogenetic treeMediterranean RegionReproductionGenetic VariationPlantsbiology.organism_classificationBiological EvolutionReticulate evolutionChloroplast DNARestriction fragment length polymorphismPolymorphism Restriction Fragment LengthMolecular Phylogenetics and Evolution
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Nuclear Translocation of Mismatch Repair Proteins MSH2 and MSH6 as a Response of Cells to Alkylating Agents

2000

Mammalian mismatch repair has been implicated in mismatch correction, the prevention of mutagenesis and cancer, and the induction of genotoxicity and apoptosis. Here, we show that treatment of cells specifically with agents inducing O(6)-methylguanine in DNA, such as N-methyl-N'-nitro-N-nitrosoguanidine and N-methyl-N-nitrosourea, elevates the level of MSH2 and MSH6 and increases GT mismatch binding activity in the nucleus. This inducible response occurs immediately after alkylation, is long-lasting and dose-dependent, and results from translocation of the preformed MutSalpha complex (composed of MSH2 and MSH6) from the cytoplasm into the nucleus. It is not caused by an increase in MSH2 gen…

CytoplasmDNA RepairBase Pair MismatchRNA StabilityChromosomal translocationmedicine.disease_causeBiochemistrychemistry.chemical_compoundMismatch Repair Endonuclease PMS2Adenosine TriphosphatasesNuclear ProteinsMethylnitrosoureaNeoplasm ProteinsDNA-Binding ProteinsMutS Homolog 2 ProteinDNA mismatch repairMutL Protein Homolog 1Protein BindingAlkylating AgentsMethylnitronitrosoguanidinecongenital hereditary and neonatal diseases and abnormalitiesGuanineActive Transport Cell NucleusBiologyCell LineO(6)-Methylguanine-DNA MethyltransferaseProto-Oncogene ProteinsDNA Repair ProteinmedicineHumansRNA MessengerneoplasmsMolecular BiologyAdaptor Proteins Signal TransducingCell NucleusMutagenesisnutritional and metabolic diseasesDNACell BiologyDNA MethylationMolecular biologydigestive system diseasesMSH6DNA Repair EnzymesGene Expression RegulationchemistryMSH2Carrier ProteinsGenotoxicityDNADNA DamageHeLa CellsJournal of Biological Chemistry
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