Search results for "Cellular localization"

showing 10 items of 93 documents

HSP90 and eNOS partially co-localize and change cellular localization in relation to different ECM components in 2D and 3D cultures of adult rat card…

2007

Background information. Cultivation techniques promoting three-dimensional organization of mammalian cells are of increasing interest, since they confer key functionalities of the native ECM (extracellular matrix) with a power for regenerative medicine applications. Since ECM compliance influences a number of cell functions, Matrigel-based gels have become attractive tools, because of the ease with which their mechanical properties can be controlled. In the present study, we took advantage of the chemical and mechanical tunability of commonly used cell culture substrates, and co-cultures to evaluate, on both two- and three-dimensional cultivated adult rat cardiomyocytes, the impact of ECM c…

Nitric Oxide Synthase Type IIICell Culture TechniquesFluorescent Antibody TechniqueBiocompatible Materialslaw.inventionExtracellular matrixMicroscopy Electron TransmissionLamininConfocal microscopylawEnosAnimalsMyocytes CardiacHSP90 Heat-Shock ProteinsCellular localizationCells CulturedMatrigelMicroscopy ConfocalbiologyCell BiologyGeneral MedicineFibroblastsbiology.organism_classificationCoculture TechniquesCell biologyExtracellular MatrixFibronectinsRatsFibronectinDrug CombinationsProtein TransportCell culturebiology.proteinhsp90 ENOSProteoglycansCollagenLamininBiology of the cell
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Cellular complexity in MAPK signaling in plants: Questions and emerging tools to answer them

2018

International audience; Mitogen activated protein kinase (MAPK) cascades play an important role in many aspects of plant growth, development, and environmental response. Because of their central role in many important processes, MAPKs have been extensively studied using biochemical and genetic approaches. This work has allowed for the identification of the MAPK genes and proteins involved in a number of different signaling pathways. Less well developed, however, is our understanding of how MAPK cascades and their corresponding signaling pathways are organized at subcellular levels. In this review, we will provide an overview of plant MAPK signaling, including a discussion of what is known a…

0301 basic medicineMAPK/ERK pathwayactivity sensorsPlant growth[SDV]Life Sciences [q-bio]plantComputational biologyPlant ScienceReviewlcsh:Plant culture03 medical and health sciences[SDV.BV]Life Sciences [q-bio]/Vegetal Biologylcsh:SB1-1110biologyphosphorylationsignaling cascade;MAPK;phosphorylation;plant;microscopy;activity sensorsSubcellular localizationMAPKMapk signaling030104 developmental biologyMitogen-activated protein kinasebiology.proteinmicroscopyPhosphorylationSignal transductionExperimental methodssignaling cascade
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Signal sequences modulate the immunogenic performance of human hepatitis C virus E2 gene

2005

Abstract Envelope protein E2 of human hepatitis C virus (HCV) is an attractive component of a prototype HCV vaccine. Delivered by DNA immunogens, E2 evokes specific immune response of Th1-type, failing to induce either considerable antibody production, or T-helper cell proliferation. We aimed at modulating the immunogenic performance of E2 gene by changing the mode of protein expression in eukaryotic cells. Plasmids were constructed encoding full-length E2 and nonstructural protein 1 (p7) fused to either 13 or 38 C-terminal amino acids (aa) of HCV E1 that contain second hydrophobic segment of E1 stop-transfer signal, or a complete E1 stop-transfer signal with duplicated second hydrophobic s…

Viral Hepatitis VaccinesSignal peptideGenes ViralMolecular Sequence DataImmunologyHeterologousHepacivirusProtein Sorting SignalsBiologyInjections IntramuscularEpitopeMiceViral ProteinsPlasmidViral Envelope ProteinsChlorocebus aethiopsEscherichia coliAnimalsHumansAmino Acid SequenceMolecular BiologyGeneCellular localizationCell Line TransformedMice Inbred BALB CImmunogenicityGenetic VariationCell Transformation ViralMolecular biologyCOS Cellsbiology.proteinAntibodyHeLa CellsPlasmidsMolecular Immunology
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Heterozygous nonsense SCN5A mutation W822X explains a simultaneous sudden infant death syndrome.

2008

The sudden, unexpected, and unexplained death of both members of a set of healthy twins (simultaneous sudden infant death syndrome (SSIDS)) is defined as a case in which both infants meet the definition of sudden infant death syndrome individually. A search of the world medical literature resulted in only 42 reported cases of SSIDS. We report the case of a pair of identical, male, monozygotic twins, 138 days old, who suddenly died, meeting the full criteria of SSIDS and where a genetic screen was performed, resulting in a heterozygous nonsense SCN5A mutation (W822X) in both twins. Immunohistochemistry was performed on cardiac tissue samples utilizing polyclonal antibodies anti-Na+ CP type V…

MalePathologymedicine.medical_specialtyNav1.5 protein functionv1.5 protein functionmedia_common.quotation_subject2734Nonsense mutationNonsenseNa+ channel functionMuscle ProteinsSocio-culturaleBiology+Nav1.5 protein function; Na+ channel function; SCN5A gene mutation; Simultaneous sudden infant death syndrome; W822X mutation; Codon Nonsense; Diseases in Twins; Humans; Infant; Male; Muscle Proteins; NAV1.5 Voltage-Gated Sodium Channel; Sodium Channels; Sudden Infant Death; 2734Sudden deathSodium ChannelsNAV1.5 Voltage-Gated Sodium ChannelPathology and Forensic MedicinePathogenesisSCN5A gene mutationDiseases in TwinsmedicineHumansSimultaneous sudden infant death syndromeSCN5A gene mutationW822X mutationNa+ channel functionNav1.5 protein functionNaSimultaneous sudden infant death syndrome SCN5A gene mutation W822X mutation Na+ channel function Nav1.5 protein function CodonMolecular BiologyCellular localizationmedia_commonSimultaneous sudden infant death syndromeSettore BIO/16 - Anatomia UmanaSimultaneous sudden infant death syndrome SCN5A gene mutation W822X mutation Na+ channel function Nav1.5 protein functionW822X mutationInfantCell BiologyGeneral MedicineSudden infant death syndromeNonsenseTerminal deoxynucleotidyl transferaseCodon NonsenseImmunohistochemistryNa; v; 1.5 protein function; Na; +; channel function; SCN5A gene mutation; Simultaneous sudden infant death syndrome; W822X mutationchannel functionSudden Infant Death
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P-cadherin expression and survival rate in oral squamous cell carcinoma: an immunohistochemical study

2005

Abstract Background P-cadherin (P-cad) is a transmembrane molecule involved in the cell-cell adhesion and similar to E-cadherin (E-cad), but less investigated in oncology, especially in in vivo studies. Aims of the present study were to assess the prevalence of P-cad expression in oral squamous cell carcinoma (OSCC) and to verify whether P-cad can be considered a marker of prognosis in patients with OSCC. Methods In a retrospective study, a cohort of 67 OSCC patients was investigated for P-cad expression and its cellular localization by immunohistochemistry; some respective healthy margins of resection were similarly investigated as standard controls. After grouping for P-cad expression, OS…

OncologyMalePathologyCancer ResearchCytoplasmTime FactorsCohort StudiesSurgical oncologyCellular localizationMouth neoplasmAged 80 and overMiddle Agedlcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogensCadherinsPrognosisImmunohistochemistryTreatment OutcomeOncologycell-cell adhesionCarcinoma Squamous CellImmunohistochemistryRegression AnalysisFemaleMouth NeoplasmsResearch ArticleAdultmedicine.medical_specialtyAdolescentlcsh:RC254-282Internal medicinemedicineGeneticsBiomarkers TumorHumanscardiovascular diseasesGrading (tumors)Survival rateAgedProportional Hazards ModelsRetrospective StudiesModels StatisticalProportional hazards modelCadherinbusiness.industryCell MembraneCateninstomatognathic diseasesMultivariate AnalysisCadherinbusinessCell Adhesion Molecules
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Nuclear signaling of plant MAPKs

2018

This article is part of the research topic: Post-Translational Modifications in Plant Nuclear Signaling: Novel Insights into Responses to Environmental Changes; International audience; Mitogen-activated protein kinases (MAPKs) are conserved protein kinases in eukaryotes that establish signaling modules where MAPK kinase kinases (MAPKKKs) activate MAPK kinases (MAPKKs) which in turn activate MAPKs. In plants, they are involved in the signaling of multiple environmental stresses and developmental programs. MAPKs phosphorylate their substrates and this post-translational modification (PTM) contributes to the regulation of proteins. PTMs may indeed modify the activity, subcellular localization,…

0301 basic medicineMAPK/ERK pathwayabiotic stressmitogen-activated protein kinaseReviewPlant Sciencelcsh:Plant culture03 medical and health sciencesbiotic stress[SDV.BV]Life Sciences [q-bio]/Vegetal Biologylcsh:SB1-1110nucleus;mitogen-activated protein kinase;phosphorylation;signaling;biotic stress;abiotic stress;developmentdevelopmentVegetal BiologybiologyKinasephosphorylationnucleusfood and beveragesBiotic stressSubcellular localizationCell biologyCytosol030104 developmental biologyMitogen-activated protein kinasebiology.proteinPhosphorylationSignal transductionsignalingBiologie végétale
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Differential subcellular localization of endogenous and transfected soluble epoxide hydrolase in mammalian cells: evidence for isozyme variants

1999

AbstractEndogenous, constitutive soluble epoxide hydrolase in mice 3T3 cells was localized via immunofluorescence microscopy exclusively in peroxisomes, whereas transiently expressed mouse soluble epoxide hydrolase (from clofibrate-treated liver) accumulated only in the cytosol of 3T3 and HeLa cells. When the C-terminal Ile of mouse soluble epoxide hydrolase was mutated to generate a prototypic putative type 1 PTS (-SKI to -SKL), the enzyme targeted to peroxisomes. The possibility that soluble epoxide hydrolase-SKI was sorted slowly to peroxiosmes from the cytosol was examined by stably expressing rat soluble epoxide hydrolase-SKI appended to the green fluorescent protein. Green fluorescent…

Epoxide hydrolase 2animal structuresRecombinant Fusion ProteinsBiophysicsBiologyEpoxide hydrolasePeroxisomeTransfectionBiochemistryIsozymeMicrobodies3T3 cellsGreen fluorescent protein03 medical and health sciencesMiceStructural BiologyGeneticsmedicineAnimalsHumansClofibrateEpoxide hydrolaseMolecular Biology030304 developmental biologyEpoxide HydrolasesMammals0303 health sciences030302 biochemistry & molecular biologyPeroxisome targeting signalCell Biology3T3 CellsPeroxisomeSubcellular localizationMolecular biologyRatsIsoenzymesCytosolmedicine.anatomical_structureBiochemistrySolubilityhuman activitiesHeLa CellsSubcellular FractionsFEBS Letters
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Cloning, structure, cellular localization, and possible function of the tumor suppressor gene lethal(3)malignant blood neoplasm-1 of Drosophila melan…

1994

The tumor suppressor gene, lethal(3)malignant blood neoplasm-1+, of Drosophila melanogaster is required for the differentiation of the phagocytic blood-cell type, the plasmatocyte. In the homozygously mutated state it causes the malignant transformation of these blood cells. We present here the cloning, sequencing, structure, and expression of the l(3)mbn-1+ gene during development. The cloned gene was identified by germ-line transformation, generation of revertants, and the detection of the corresponding mRNA in blood cells and other tissues. Homologies of the G-S-rich C-terminus of the putative MBN83 protein to human cytokeratins K1, K10, and mouse loricrin were found. The structure and p…

DNA ComplementaryTumor suppressor geneMolecular Sequence DataMalignant transformationGene expressionAnimalsGenes Tumor SuppressorAmino Acid SequenceRNA MessengerCloning MolecularMolecular BiologyGeneCellular localizationAllelesCloningBlood CellsbiologyBase SequenceChromosome MappingCell Biologybiology.organism_classificationMolecular biologyCell Transformation NeoplasticDrosophila melanogasterLoricrinDrosophila melanogasterDevelopmental BiologyDevelopmental biology
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2013

Clusterin, also known as apolipoprotein J, is expressed from a variety of tissues and implicated in pathological disorders such as neurodegenerative diseases, ischemia and cancer. In contrast to secretory clusterin (sCLU), which acts as an extracellular chaperone, the synthesis, subcellular localization and function(s) of intracellular CLU isoforms is currently a matter of intense discussion. By investigating human CLU mRNAs we here unravel mechanisms leading to the synthesis of distinct CLU protein isoforms and analyze their subcellular localization and their impact on apoptosis and on NF-κB-activity. Quantitative PCR-analyses revealed the expression of four different stress-inducible CLU …

Gene isoformMessenger RNAMultidisciplinaryBcl-2-associated X proteinClusterinbiologyIntrinsic apoptosisHEK 293 cellsbiology.proteinSignal transductionSubcellular localizationMolecular biologyPLOS ONE
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Localization of the two constitutively expressed nitric oxide synthase isoforms (nNOS and eNOS) in the same cell types in the saccule maculae of the …

2003

There is growing evidence for a nitric oxide/cyclic GMP pathway of signal transduction in the vestibular system. Recently, two isoforms of nitric oxide (NO) synthase (nNOS and eNOS) and NO itself have been identified at the light microscopic level in the vestibulocochlear system of mice using specific antibodies and a new fluorescence indicator. In order to acquire more information about signal transduction and tissue modulation in this neuroepithelium at the cellular and subcellular levels, ultrathin sections of London Resin White-embedded saccule maculae of the frog Rana pipiens were incubated with various concentrations of commercially available antibodies to nNOS and eNOS. The immunorea…

Gene isoformCell typemedicine.medical_specialtyNitric Oxide Synthase Type IIIImmunoelectron microscopyImmunocytochemistryNitric Oxide Synthase Type IBiologyInternal medicineAcoustic MaculaeHair Cells AuditorymedicineAnimalsMicroscopy ImmunoelectronOrgan of CortiInstrumentationRana pipiensSubcellular localizationImmunohistochemistryCell biologyIsoenzymesNitric oxide synthaseNeuroepithelial cellEndocrinologyCytoplasmbiology.proteinNitric Oxide SynthaseJournal of Electron Microscopy
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