Search results for "Cell Nucleus"

showing 10 items of 379 documents

Enzymes of cancer nuclei*1

1963

chemistry.chemical_classificationCell nucleusmedicine.anatomical_structureEnzymechemistrymedicineCancer researchCancerCell BiologyBiologymedicine.diseaseExperimental Cell Research
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Two proteases from nuclei of rat testis cells. II. Inhibitors

1987

Abstract Proteases Rc and Kc of the nuclei of rat testis cells exhibit considerable differences in susceptibility to various protease inhibitors. Protease Rc is inhibited by D‐phenylalanyl‐L‐propyl‐L‐arginine chlormethylketone and p‐nitrophenyl‐p1‐guanidino ben‐zoate. Protease Kc is inhibited by Nα‐p‐tosyl‐L‐lysine chlormethylketone, N‐p‐tosyl‐phenylalanine chlormethylketone, N‐carbobenzoxy‐L‐phenylalanine chloromethylketone and p‐nitrophenyl‐p'‐guanidino‐benzoate. Neither protease is inhibited by 10 mM phenylmethanesulphonyl‐fluoride or p‐chloromercuri‐benzoate. p‐nitrophenyl‐p1‐guanidino‐benzoate is a substrate for protease Rc with release of p‐nitrophenol, however the protease activity i…

chemistry.chemical_classificationProteasesProteasemedicine.medical_treatmentSubstrate (chemistry)BiologyTesticleTrypsinMolecular biologyCell nucleusmedicine.anatomical_structureEnzymeBiochemistrychemistrymedicineAnimal Science and ZoologySpermatogenesismedicine.drugBollettino di zoologia
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ElaC Encodes a Novel Binuclear Zinc Phosphodiesterase

2002

ElaC is a widespread gene found in eubacteria, archaebacteria, and mammals with a highly conserved sequence. Two human ElaC variants were recently associated with cancer (Tavtigian, S. V., Simard, J., Teng, D. H., Abtin, V., Baumgard, M., Beck, A., Camp, N. J., Carillo, A. R., Chen, Y., Dayananth, P., Desrochers, M., Dumont, M., Farnham, J. M., Frank, D., Frye, C., Ghaffari, S., Gupte, J. S., Hu, R., Iliev, D., Janecki, T., Kort, E. N., Laity, K. E., Leavitt, A., Leblanc, G., McArthur-Morrison, J., Pederson, A., Penn, B., Peterson, K. T., Reid, J. E., Richards, S., Schroeder, M., Smith, R., Snyder, S. C., Swedlund, B., Swensen, J., Thomas, A., Tranchant, M., Woodland, A. M., Labrie, F., Sko…

chemistry.chemical_elementZincBiologymedicine.disease_causeBiochemistrybeta-LactamasesHomology (biology)Conserved sequenceGene productEscherichia colimedicineHistidineCloning MolecularBinding siteMolecular BiologyEscherichia coliHistidineCell NucleusIonsBinding SitesModels StatisticalPhosphoric Diester HydrolasesSpectrum AnalysisX-RaysPhosphodiesteraseCell BiologyProtein Structure TertiaryOxygenKineticsZincBiochemistrychemistryChromatography GelProtonsDimerizationProtein BindingJournal of Biological Chemistry
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All-trans to 11-cis retinol isomerization in nuclear membrane fraction from bovine retinal pigment epithelium

1991

Abstract Isomerization of all-trans to 11-cis retinol has been studied in a membrane preparation from the nuclear fraction of bovine retinal pigment epithelium. When the nuclear membrane preparation deprived of endogenous retinoids is incubated with 4·5 μ m all-trans-retinol, the mean value calculated for the isomerase activity is 1·32 nmol 11-cis retinol formed hr−1 mg protein−1. Simultaneous formation of all-trans and 11-cis retinyl esters is also observed in the nuclear preparation. When assayed under the same experimental condition, RPE 150 000 g post-nuclear sediment shows about 70% of the isomerase activity found in the nuclear membrane fraction. Treatment of the nuclear membrane frac…

cis-trans-IsomerasesIsomerase activityNuclear EnvelopeDetergentsIsomeraseCellular and Molecular Neurosciencechemistry.chemical_compoundIsomerismChapsmedicineAnimalsBovine serum albuminNuclear membraneIsomerasesPigment Epithelium of EyeVitamin AChromatography High Pressure LiquidCell NucleusChromatographybiologyRetinolCholic AcidsSensory SystemsEnzyme assayOphthalmologyMembranemedicine.anatomical_structureSolubilityBiochemistrychemistrybiology.proteinCattleExperimental Eye Research
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Epigenetic involvement in Hutchinson-Gilford progeria syndrome: a mini-review.

2013

Hutchinson-Gilford progeria syndrome (HGPS) is a rare human genetic disease that leads to a severe premature ageing phenotype, caused by mutations in the <i>LMNA</i> gene. The <i>LMNA</i> gene codes for lamin-A and lamin-C proteins, which are structural components of the nuclear lamina. HGPS is usually caused by a de novo <i>C1824T</i> mutation that leads to the accumulation of a dominant negative form of lamin-A called progerin. Progerin also accumulates physiologically in normal ageing cells as a rare splicing form of lamin-A transcripts. From this perspective, HGPS cells seem to be good candidates for the study of the physiological mechanisms of ageing…

congenital hereditary and neonatal diseases and abnormalitiesAgingEuchromatinSettore BIO/11 - Biologia MolecolarecernaBiologySettore MED/13 - EndocrinologiaEpigenesis GeneticLMNAHistonesAdenosine TriphosphateProgeriaHGPS Progeria; epigenetics; chromatin; cernamedicineHumansEpigeneticsProtein PrecursorsChildEpigenesisGeneticsCell NucleusProgeriaintegumentary systemnutritional and metabolic diseasesNuclear ProteinsDNA Methylationmedicine.diseaseProgerinChromatin Assembly and DisassemblyLamin Type AChromatinCell biologySettore BIO/18 - GeneticaMicroRNAsSettore MED/03 - Genetica MedicaMutationHGPS ProgeriachromatinNuclear laminaGeriatrics and GerontologyepigeneticMi-2 Nucleosome Remodeling and Deacetylase ComplexGerontology
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Phosphorylation of mismatch repair proteins MSH2 and MSH6 affecting MutSα mismatch-binding activity

2002

Mismatch repair (MMR) is involved in the removal of mispaired bases from DNA and thus plays an important role in the maintenance of genomic stability and the prevention of mutations and cancer. Moreover, MMR triggers genotoxicity and apoptosis upon processing of DNA lesions such as O6-methylguanine. Whereas the enzymology of MMR has been elucidated in great detail, only limited data are available concerning its regulation. Here we show that the major mismatch-binding proteins MSH2 and MSH6, forming the MutSalpha complex, are phosphorylated in vitro by protein kinase C and casein kinase II, but not by protein kinase A. Phosphorylation of MSH2 and MSH6 was also found within the cell, with MSH…

congenital hereditary and neonatal diseases and abnormalitiesDNA RepairDNA repairBase Pair MismatchMacromolecular SubstancesActive Transport Cell NucleusBiologyProtein Serine-Threonine KinasesArticleProto-Oncogene ProteinsGeneticsHumansProtein phosphorylationPhosphorylationProtein kinase ACasein Kinase IIneoplasmsProtein kinase CProtein Kinase CCell Nucleusnutritional and metabolic diseasesdigestive system diseasesDNA-Binding ProteinsMutS Homolog 2 ProteinBiochemistryMSH2PhosphorylationDNA mismatch repairCasein kinase 2HeLa Cells
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Nuclear calcium signaling by inositol trisphosphate in GH3 pituitary cells

2008

It has been proposed that nuclear and cytosolic Ca2+ ([Ca2+]N and [Ca2+]C) may be regulated independently. We address here the issue of whether inositol trisphosphate (IP3) can, bypassing changes of [Ca2+]C, produce direct release of Ca2+ into the nucleoplasm. We have used targeted aequorins to selectively measure and compare the changes in [Ca2+]C and [Ca2+]N induced by IP3 in GH3 pituitary cells. Heparin, an IP3 inhibitor that does not permeate the nuclear pores, abolished the [Ca2+]C peaks but inhibited only partly the [Ca2+]N peaks. The permeant inhibitor 2-aminoethoxy-diphenyl-borate (2-APB) blocked both responses. Removal of ATP also inhibited more strongly the [Ca2+]C than [Ca2+]N pe…

endocrine systemCytoplasm[SDV.OT]Life Sciences [q-bio]/Other [q-bio.OT]PhysiologyAequorinNucleoplasmic reticulumaequorinInositol 145-TrisphosphateCell Line03 medical and health scienceschemistry.chemical_compound0302 clinical medicinenuclear signal transductionmedicineAnimalsInositol 145-Trisphosphate Receptorsinositol trisphosphate receptorsCalcium SignalingReceptorMolecular Biology030304 developmental biologyCell Nucleus0303 health sciencesNucleoplasmbiologypituitary cellsInositol trisphosphateCell Biologyherpes simplex virusMolecular biologyRatsCytosolmedicine.anatomical_structurechemistryCytoplasmPituitary Glandbiology.proteinnucleoplasmic reticulumNucleus030217 neurology & neurosurgery
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Extensive nuclear gyration and pervasive non-genic transcription during primordial germ cell development in zebrafish.

2020

ABSTRACT Primordial germ cells (PGCs) are the precursors of germ cells, which migrate to the genital ridge during early development. Relatively little is known about PGCs after their migration. We studied this post-migratory stage using microscopy and sequencing techniques, and found that many PGC-specific genes, including genes known to induce PGC fate in the mouse, are only activated several days after migration. At this same time point, PGC nuclei become extremely gyrated, displaying general broad opening of chromatin and high levels of intergenic transcription. This is accompanied by changes in nuage morphology, expression of large loci (PGC-expressed non-coding RNA loci, PERLs) that ar…

endocrine systemRNA UntranslatedTranscription GeneticZygotePiwi-interacting RNApiRNABiology03 medical and health sciences0302 clinical medicineGyrationTranscription (biology)Primordial germ cellmedicineAnimalsRNA Small InterferingMolecular BiologyZebrafishGeneZebrafish030304 developmental biologyCell NucleusNuage0303 health sciencesGonadal ridgeurogenital systemNuclear morphologyGene Expression Regulation DevelopmentalDNA-Directed RNA PolymerasesZygotic activationZebrafish Proteinsbiology.organism_classificationChromatinCell biologyUp-Regulationmedicine.anatomical_structureGerm CellsGenetic Loci207FertilizationMutationIntergenic transcriptionDNA Transposable ElementsDNA Intergenic030217 neurology & neurosurgeryGerm cellBiogenesisDevelopmental BiologyResearch ArticleDevelopment (Cambridge, England)
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Nuclear entry and egress of parvoviruses.

2022

Parvoviruses are small non-enveloped single-stranded DNA viruses, which depend on host cell nuclear transcriptional and replication machinery. After endosomal exposure of nuclear localization sequence and a phospholipase A2 domain on the capsid surface, and escape into the cytosol, parvovirus capsids enter the nucleus. Due to the small capsid diameter of 18–26 nm, intact capsids can potentially pass into the nucleus through nuclear pore complexes (NPCs). This might be facilitated by active nuclear import, but capsids may also follow an alternative entry pathway that includes activation of mitotic factors and local transient disruption of the nuclear envelope. The nuclear entry is followed b…

import and exportCell NucleusisäntäsolutviruksetparvovirusesNuclear Envelopenuclear pore complexesnucleusActive Transport Cell NucleusDNA Single-Strandednuclear envelopeVirus ReplicationMicrobiologyinfektiotParvovirusPhospholipasestumaNuclear PoreCapsid ProteinsMolecular BiologyparvoviruksetkapsidiMolecular microbiologyREFERENCES
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The effect of nanoparticle size and NLS density on nuclear targeting in cancer and normal cells; impaired nuclear import and aberrant nanoparticle in…

2017

The cell nucleus is an interesting target in many diseases with particular interest in cancer. Previously, nuclear targeted small and large chitosan nanoparticles (S-NPs≈25nm, and L-NPs≈150nm respectively), modified with low, intermediate and high densities of NLS (L-NLS, I-NLS and H-NLS) were developed and assessed in L929 fibroblasts. However, to evade apoptosis and stimulate tumor growth cancer cells are capable of manipulating the nuclear-cytoplasmic transport on many levels, making NPs that are capable of nuclear targeting in normal cells incapable of doing so in cancer. For such reason, here, the nuclear delivery efficiency of S-NPs and L-NPs was assessed as a function of their NLS de…

inorganic chemicals0301 basic medicineNuclear Localization SignalsPharmaceutical Science02 engineering and technologyImportinBiologyenvironment and public healthCell Line03 medical and health sciencesCell Line TumormedicineHumansNLSParticle SizeCells Culturedhealth care economics and organizationsChitosanHEK 293 cellstechnology industry and agricultureBiological TransportGliomaFibroblastsrespiratory system021001 nanoscience & nanotechnologyVirologyCell biologyCell nucleus030104 developmental biologymedicine.anatomical_structureApoptosisCancer cellNanoparticlesNuclear transport0210 nano-technologyNuclear localization sequenceJournal of Controlled Release
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