Search results for "EXPRESSION"

showing 10 items of 5168 documents

Tumor protein 53-induced nuclear protein 1 expression is repressed by miR-155, and its restoration inhibits pancreatic tumor development.

2007

Pancreatic cancer is a disease with an extremely poor prognosis. Tumor protein 53-induced nuclear protein 1 ( TP53INP1 ) is a proapoptotic stress-induced p53 target gene. In this article, we show by immunohistochemical analysis that TP53INP1 expression is dramatically reduced in pancreatic ductal adenocarcinoma (PDAC) and this decrease occurs early during pancreatic cancer development. TP53INP1 reexpression in the pancreatic cancer-derived cell line MiaPaCa2 strongly reduced its capacity to form s.c., i.p., and intrapancreatic tumors in nude mice. This anti-tumoral capacity is, at least in part, due to the induction of caspase 3-mediated apoptosis. In addition, TP53INP1 −/− mouse embryonic…

Settore MED/06 - Oncologia MedicaTransplantation HeterologousGene ExpressionMice NudeMicePancreatic tumorPancreatic cancerCell Line TumormicroRNAGene expressionmedicineAnimalsHumansRNA NeoplasmNuclear proteinCaspaseHeat-Shock ProteinsMice KnockoutMultidisciplinarybiologyBase Sequenceapoptosis pancreatic cancer ponasterone A tumor suppressor micro RNANuclear ProteinsBiological Sciencesmedicine.diseaseTransplantationPancreatic NeoplasmsMicroRNAsCell Transformation NeoplasticApoptosisCancer researchbiology.proteinTumor Suppressor Protein p53Carrier ProteinsNeoplasm TransplantationCarcinoma Pancreatic DuctalProceedings of the National Academy of Sciences of the United States of America
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miRNA Signature and Dicer Requirement during Human Endometrial Stromal Decidualization In Vitro

2012

Decidualization is a morphological and biochemical transformation of endometrial stromal fibroblast into differentiated decidual cells, which is critical for embryo implantation and pregnancy establishment. The complex regulatory networks have been elucidated at both the transcriptome and the proteome levels, however very little is known about the post-transcriptional regulation of this process. miRNAs regulate multiple physiological pathways and their de-regulation is associated with human disorders including gynaecological conditions such as endometriosis and preeclampsia. In this study we profile the miRNAs expression throughout human endometrial stromal (hESCs) decidualization and analy…

Sexual ReproductionRibonuclease IIISmall interfering RNAAnatomy and PhysiologyCellular differentiationGene ExpressionBioinformaticsCell morphologyTranscriptomeEndocrinologyMolecular Cell BiologyMultidisciplinarybiologyStem CellsQDeciduaRObstetrics and GynecologyCell DifferentiationForkhead Transcription FactorsCell biologyFemale Genital Diseasesmedicine.anatomical_structureMedicineFemaleResearch ArticleAdultScienceMolecular GeneticsYoung AdultmicroRNAGeneticsDeciduamedicineReproductive EndocrinologyHumansGene RegulationBiologyEmbryonic Stem CellsHomeodomain ProteinsGene Expression ProfilingReproductive SystemComputational BiologyDecidualizationFibroblastsFemale SubfertilityInsulin-Like Growth Factor Binding Protein 1MicroRNAsHomeobox A10 ProteinsGene Expression Regulationbiology.proteinStromal CellsDevelopmental BiologyDicerPLoS ONE
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Oral and Vaginal Epithelial Cell Lines Bind and Transfer Cell-Free Infectious HIV-1 to Permissive Cells but Are Not Productively Infected

2014

The majority of HIV-1 infections worldwide are acquired via mucosal surfaces. However, unlike the vaginal mucosa, the issue of whether the oral mucosa can act as a portal of entry for HIV-1 infection remains controversial. To address potential differences with regard to the fate of HIV-1 after exposure to oral and vaginal epithelium, we utilized two epithelial cell lines representative of buccal (TR146) and pharyngeal (FaDu) sites of the oral cavity and compared them with a cell line derived from vaginal epithelium (A431) in order to determine (i) HIV-1 receptor gene and protein expression, (ii) whether HIV-1 genome integration into epithelial cells occurs, (iii) whether productive viral in…

Sexual transmissionTranscription GeneticVirus IntegrationScienceReceptors Cell SurfaceGenome ViralBiologyMicrobiologyCXCR4EpitheliumVirusCell LineFlow cytometryViral ProteinsImmunodeficiency VirusesmedicineHumansRNA MessengerOral mucosaMicrobial PathogensMultidisciplinarymedicine.diagnostic_testQMouth MucosaRBiology and Life SciencesHIVCorrectionEpithelial CellsVirologyMolecular biologyEpitheliumBiological Tissuemedicine.anatomical_structureGene Expression RegulationTranscytosisMedical MicrobiologyCell cultureViral PathogensDNA ViralVaginaHIV-1MedicineFemaleAnatomyResearch Article
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Construction of Metatranscriptomic Libraries for 5′ End Sequencing of rRNAs for Microbiome Research

2021

Metatranscriptomic sequencing enables studying community-wide gene expression profiles of microbial samples and getting functional insight on their up- or downregulated pathways. However, shotgun sequencing is not the most efficient way to study expression of ribosomal RNA genes or to compare lot of samples in experimental setups. Here we describe an efficient primer-independent method for processing and barcoding libraries for directional sequencing of the 5' end region of the RNA. When applying size selection of the original RNA, the method forms an optimal solution for the simultaneous analysis of bacterial, archaeal, and eukaryotic rRNA diversity.

Shotgun sequencingSSU rRNARibosomal rna geneGene expressionRNAComputational biologyMicrobiomeBiologyRibosomal RNA
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dfh is a Drosophila homolog of the Friedreich's ataxia disease gene

2000

Abstract A putative Drosophila homolog of the Friedreich's ataxia disease gene (FRDA) has been cloned and characterized; it has been named Drosophila frataxin homolog (dfh). It is located at 8C/D position on X chromosome and is spread over 1 kb, a much smaller genomic region than the human gene. Its genomic organization is simple, with a single intron dividing the coding region into two exons. The predicted encoded product has 190 amino acids, being considered a frataxin-like protein on the basis of the sequence and secondary structure conservation when compared with human frataxin and related proteins from other eukaryotes. The closest match between the Drosophila and the human proteins in…

Signal peptideDNA ComplementaryEmbryo NonmammalianMolecular Sequence DataMutantEmbryonic DevelopmentGenes InsectExonIron-Binding ProteinsGeneticsAnimalsDrosophila ProteinsCoding regionAmino Acid SequenceRNA MessengerCloning MolecularGeneIn Situ HybridizationGenomic organizationGeneticsSequence Homology Amino AcidbiologyIntronGene Expression Regulation DevelopmentalDNAExonsSequence Analysis DNAGeneral MedicineBlotting NorthernIntronsPhosphotransferases (Alcohol Group Acceptor)Drosophila melanogasterFriedreich AtaxiaFrataxinbiology.proteinDrosophilaSequence AlignmentGene
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Sequence of the M28 dsRNA: Preprotoxin Is Processed to an α/β Heterodimeric Protein Toxin

1995

The killer and immunity phenotypes of K28 killer strains of Saccharomyces cerevisiae are determined by the 1.75-kb M28 dsRNA virus. In the plus strand, M28p, the K28 preprotoxin gene, comprises bases 13-1047 and is followed, after an additional 85 bases, by a 63-bp poly(A) sequence and a 553-base 3'-sequence. This 3'-sequence contains two potential stem-loop structures predicted to bind the L-A encoded cap-pol protein, initiating encapsidation; high-level expression results in curing of M1 dsRNA. Expression of M28p confers the complete K28 killer and immunity phenotype on a cell lacking M28 dsRNA. K28 toxin is a disulfide-bonded heterodimer of alpha (10.5 kDa) and beta (11 kDa) components w…

Signal peptideDNA ComplementaryGlycosylationSaccharomyces cerevisiae ProteinsGlycosylationMolecular Sequence DataMutantCarboxypeptidasesSaccharomyces cerevisiaeBiologymedicine.disease_causeCleavage (embryo)Fungal Proteinschemistry.chemical_compoundGene Expression Regulation FungalVirologyEndopeptidasesmedicineSecretionAmino Acid SequenceSubtilisinsGeneDNA PrimersRNA Double-StrandedBase SequenceToxinSerine EndopeptidasesMembrane ProteinsRNA FungalMycotoxinsMolecular biologyKiller Factors YeastRNA silencingchemistryProprotein ConvertasesProtein Processing Post-TranslationalVirology
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Structure, organization and expression of two clustered cuticle protein genes during the metamorphosis of an insect, Tenebrio molitor.

1998

A 4-kb DNA segment of Tenebrio molitor (Insecta, Coleoptera) genomic DNA containing two larval-pupal cuticular genes has been cloned and sequenced. These genes, transcribed in opposite directions, are related in DNA sequence and the proteins encoded are very similar. Each of them contains a single intron located inside the sequence encoding the signal peptide, and a conserved sequence at -200 bp from the mRNA start position. These similarities in sequence suggest that these genes have evolved by duplication followed by diversification and that they are members of a family of genes with a common ancestry. They are the first example of clustered genes in Tenebrio molitor.

Signal peptideDNA ComplementaryMolecular Sequence DataGenes InsectBiologyBiochemistryDNA sequencingConserved sequenceEvolution MolecularGene duplicationAnimalsAmino Acid SequenceTenebrioPeptide sequenceGeneIn Situ HybridizationGeneticsBase SequenceSequence Homology Amino AcidfungiIntronMetamorphosis BiologicalGene Expression Regulation DevelopmentalIntronsgenomic DNAMultigene FamilyInsect ProteinsEuropean journal of biochemistry
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A novel cell wall protein specific to the mycelial form of Yarrowia lipolytica.

1996

A cDNA clone specifying a cell wall protein was isolated from a Yarrowia lipolytica cDNA library. The cDNA library was constructed in the expression vector lambda gt 11, with the RNA isolated from actively growing mycelial cells. The deduced amino acid sequence shows that the encoded protein contains an N-terminal hydrophobic signal peptide. We have designated this protein YWP1 for Yarrowia lipolytica cell Wall Protein. Northern hybridization identified YWP1 transcript only when Y. lipolytica was growing in the mycelial form. The encoded protein seems to be covalently bound to the glucan cell wall since it is not released from the cell walls by sodium dodecyl sulphate extraction, but it is …

Signal peptideDNA ComplementaryTranscription GeneticHydrolasesBlotting WesternGenetic VectorsMolecular Sequence DataRestriction MappingBioengineeringApplied Microbiology and BiotechnologyBiochemistryCell wallFungal ProteinsOpen Reading FramesTransformation GeneticCell WallComplementary DNAGene Expression Regulation FungalYeastsGeneticsEscherichia coliAmino Acid SequenceCloning MolecularFluorescent Antibody Technique IndirectPeptide sequenceAntibodies FungalGene LibraryExpression vectorbiologyBase SequencecDNA libraryRNASodium Dodecyl SulfateYarrowiaRNA Fungalbiology.organism_classificationBlotting NorthernBlotting SouthernBiochemistrySaccharomycetalesElectrophoresis Polyacrylamide GelBiotechnologyYeast (Chichester, England)
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AtPGAP1 functions as a GPI inositol-deacylase required for efficient transport of GPI-anchored proteins

2021

Abstract Glycosylphosphatidylinositol (GPI)-anchored proteins (GPI-APs) play an important role in a variety of plant biological processes including growth, stress response, morphogenesis, signaling, and cell wall biosynthesis. The GPI anchor contains a lipid-linked glycan backbone that is synthesized in the endoplasmic reticulum (ER) where it is subsequently transferred to the C-terminus of proteins containing a GPI signal peptide by a GPI transamidase. Once the GPI anchor is attached to the protein, the glycan and lipid moieties are remodeled. In mammals and yeast, this remodeling is required for GPI-APs to be included in Coat Protein II-coated vesicles for their ER export and subsequent t…

Signal peptideGlycanGenotypePhysiologyGlycosylphosphatidylinositolsPlant ScienceGenes Plantchemistry.chemical_compoundGene Expression Regulation PlantArabidopsisGeneticsArabidopsis thalianaInositolbiologyChemistryArabidopsis ProteinsEndoplasmic reticulumGenetic VariationMembrane Proteinsbiology.organism_classificationYeastPhosphoric Monoester HydrolasesCell biologyFocus Issue on Transport and Signalingcarbohydrates (lipids)Protein Transportbiology.proteinlipids (amino acids peptides and proteins)Function (biology)
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Characterization of a putative extracellular matrix protein from the beetle Tenebrio molitor: hormonal regulation during metamorphosis.

2004

0949-944X (Print) Journal Article Research Support, Non-U.S. Gov't; We used differential display to isolate epidermis cDNAs corresponding to juvenile-hormone analog-regulated mRNA from the beetle Tenebrio molitor. One of them encodes a putative extracellular matrix (ECM) protein, named Tenebrin. Indeed, the deduced protein sequence contains ECM typical features like the presence of a signal peptide, internal repeats, a RGD tripeptide sequence motif known to bind integrins and von Willebrand factor type c domains involved in protein-protein interactions. Northern blot analysis reveals a single transcript of about 11 kb with an expression pattern correlated to 20-hydroxyecdysone fluctuations …

Signal peptideIntegrinMolecular Sequence DataCycloheximideBiologyExtracellular matrixchemistry.chemical_compoundExtracellular Matrix Proteins/*genetics/metabolismGeneticsAnimalsDevelopmentalHormones/physiologyNorthern blotAmino Acid SequenceTenebrioTenebrio/*geneticsDifferential displayMessenger RNAExtracellular Matrix ProteinsMetamorphosisMetamorphosis BiologicalGene Expression Regulation DevelopmentalBiological/*physiologyHormoneschemistryBiochemistryGene Expression RegulationJuvenile hormonebiology.proteinDevelopmental BiologyDevelopment genes and evolution
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