Search results for "RBPs"

showing 10 items of 12 documents

Extracellular Vesicles Shed by Melanoma Cells Contain a Modified Form of H1.0 Linker Histone and H1.0 mRNA-binding Proteins

2016

Extracellular vesicles (EVs) are shed in the extracellular environment by both prokaryotes and eukaryotes. Although produced from both normal and cancer cells, malignant cells release a much higher amount of EVs, which also contain tumor-specific proteins and RNAs. We previously found that G26/24 oligodendroglioma cells shed EVs that contain the pro-apoptotic factors FasL and TRAIL1-2. Interestingly, G26/24 release, via EVs, extracellular matrix remodelling proteases3, and H1° histone protein4, and mRNA. To shed further light on the role of EVs in discarding proteins and mRNAs otherwise able to counteract proliferative signals, we studied a melanoma cell line (A375). We found that also thes…

0301 basic medicineCancer ResearchCellular differentiationBlotting WesternFluorescent Antibody TechniqueMYEF2ApoptosisRNA-binding proteinexosomesmembrane vesiclesReal-Time Polymerase Chain ReactionChromatography AffinityHistones03 medical and health sciencesH1.0 linker histone; RNA-binding proteins (RBPs); extracellular vesicles (EVs) membrane vesicles (MVs); exosomes; MYEF2Settore BIO/10 - BiochimicaTumor Cells CulturedHumansexosomeSecretionRNA MessengerSettore BIO/06 - Anatomia Comparata E Citologiamelanoma cell line (A375) myelin expression factor-2 (MYEF2)MelanomaTranscription factorCell ProliferationH1.0 linker histonebiologyReverse Transcriptase Polymerase Chain ReactionEXTRACELLULAR VESICLESRNA-Binding ProteinsRNACell DifferentiationArticlesCell biologyBlotCell Transformation Neoplastic030104 developmental biologyHistoneOncologySpectrometry Mass Matrix-Assisted Laser Desorption-IonizationCancer cellbiology.proteinRNA-binding proteins (RBPs)extracellular vesicles (EVs) membrane vesicles (MVs)
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Extracellular Vesicle‐Associated RNA as a Carrier of Epigenetic Information

2017

Post-transcriptional regulation of messenger RNA (mRNA) metabolism and subcellular localization is of the utmost importance both during development and in cell differentiation. Besides carrying genetic information, mRNAs contain cis-acting signals (zip codes), usually present in their 5'- and 3'-untranslated regions (UTRs). By binding to these signals, trans-acting factors, such as RNA-binding proteins (RBPs), and/or non-coding RNAs (ncRNAs), control mRNA localization, translation and stability. RBPs can also form complexes with non-coding RNAs of different sizes. The release of extracellular vesicles (EVs) is a conserved process that allows both normal and cancer cells to horizontally tran…

0301 basic medicinelcsh:QH426-470mRNAnon‐coding RNA (ncRNA)RNA-binding proteinReviewBiology03 medical and health sciencesRNA‐binding proteins (RBPs)Settore BIO/10 - Biochimicanon-coding RNA (ncRNA)Gene expressionGeneticsSettore BIO/06 - Anatomia Comparata E CitologiaTranscription factorGenetics (clinical)GeneticsmRNA; non-coding RNA(ncRNA); RNA-binding proteins (RBPs); extracellular vesicles (EVs)Messenger RNARNATranslation (biology)Extracellular vesicleCell biologyChromatinlcsh:Genetics030104 developmental biologyRNA-binding proteins (RBPs)extracellular vesicles (EVs)non-coding RNA(ncRNA)Genes
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Retinol oxidation to retinoic acid in human thyroid glandular cells.

2014

Abstract Retinoic acid is regarded as the retinol metabolite that controls proliferation and differentiation of epithelial cells. In the present study, we investigated the potential role of xanthine dehydrogenase (XDH) in retinoic acid biosynthesis in human thyroid glandular cells (HTGC). In particular, we observed that cellular retinoids binding proteins (CRBPs) are also implicated in the biosynthetic pathway leading to retinoic acid formation in primary cultures of HTGC, as we have already reported for human mammary epithelial cells (HMEC). After partial protein purification, the enzyme responsible for retinoic acid biosynthesis was identified and quantified as XDH by immunoassay, by its …

AdultMaleXanthine DehydrogenasePrimary Cell CultureRetinoic acidThyroid GlandOxypurinolRetinoic acid receptor betaTretinoinBiologyXanthinechemistry.chemical_compoundBiosynthesisSettore BIO/10 - BiochimicaDrug DiscoveryHumansEnzyme InhibitorsVitamin AEnzyme AssaysPharmacologyImmunoassayRetinolEpithelial CellsRetinol-Binding Proteins CellularGeneral MedicineMiddle AgedXanthineUric AcidRetinoic acid receptorchemistryXanthine dehydrogenaseBiochemistryCRABPs CRBPs human glandular cells. retinoic acid biosynthesis. retinol oxidation xanthine dehydrogenaseUric acidFemaleOxidation-ReductionJournal of enzyme inhibition and medicinal chemistry
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Identification of nuclear proteins which interact with H1° mRNA.

2012

In developing rat brain the synthesis of H1° histone is mainly regulated at posttranscriptional level and probably depends on RNA-binding proteins (RBPs) (1). We previously identified RBPs apparently specific for this messenger (2) and cloned two novel proteins by screening an expression cDNA library by binding to radiolabeled RNA (3-10). Here we report the use of biotinylated H1° RNA as bait to isolate by chromatography nuclear proteins which interact with H1° mRNA. We identified by mass spectrometry abundant RBPs and molecular chaperones. By western blot we also evidenced, among the RNA-bound proteins, the cold shock domain-containing protein 2 (CSD-C2, also know as PIPPin), a brain-enric…

H1°RBPs ribonucleoproteinSettore BIO/10 - Biochimica
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ROLE OF RNA BINDING PROTEIN IN THE NERVE CELL DIFFERENTIATION

2014

Synthesis of H1˚ and H3.3 histone proteins, in the developing rat brain, seems to be regulated mainly at the post-transcriptional level. Since regulation of RNA metabolism depends on a series of RNA-binding proteins (RBPs), we have been searching for RBPs involved in the post-transcriptional regulation of the H1˚ and H3.3 genes. Previously, we reported isolation, from a cDNA expression library, of an insert encoding a novel protein, the C-terminal half of which is identical to that of PEP-19, a brain-specific protein involved in calcium metabolism. The novel protein was called long PEP-19 isoform (LPI). We showed that LPI, as well as PEP-19, can bind H1˚ RNA. Since PEP19 and LPI contain a c…

RBPs mRNA
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Developing rat brain as well as cultured astrocytes contain H1° mRNA-protein complexes

2015

RNA-binding proteins (RBPs) regulate intracellular transport, pre-localization, stability, and translation of mRNAs [1]. We previously identified a set of proteins which interact with mRNAs encoding H1° and H3.3 histones [2-5]. All these proteins are probably part of a ribonucleoprotein particle [6]. Here we report the results of a more detailed study on the expression and intracellular localization of some of these RBPs, such as hnRNP K and A1, and Hsc70, during rat brain development and in cultured rat astrocytes. We also investigated the presence in the complexes of PIPPin/CSD-C2 protein. Affinity chromatography was performed as already described [6]. Preparation of total lysates and cel…

RNA-binding proteins (RBPs) H1° and H3.3 histones PIPPin/CSD-C2 protein cultured astrocytesSettore BIO/10 - BiochimicaSettore BIO/06 - Anatomia Comparata E Citologia
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H1° mRNA-containing complexes in rat brain cells. In: Proceedings of the Abstracts

2015

Post-transcriptional regulation of gene expression depends on RNA-binding proteins (RBPs), which are able to regulate translation, stability and subcellular localization of mRNAs [1]. RNA-protein complexes start to be built up since transcription; some proteins remain then bound to the transcript, while others behave as only transient components. In the developing nervous system of mammals, the postnatal production of the histone variants H1° and H3.3 is mainly regulated at the post-transcriptional level. Synthesis and incorporation into chromatin of the two histone proteins has been suggested to be involved in the epigenetic regulation of gene expression, both in normal brain development a…

Settore BIO/10 - BiochimicaHistone H1.0 Histone H3.3 Post-transcriptional regulation RNA-binding proteins (RBPs) rat brain maturationSettore BIO/06 - Anatomia Comparata E Citologia
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Melanoma cells release extracellular vesicle which contain H1° linker histone as well as RNA-binding proteins which bind to the H1° mRNA

2015

We previously demonstrated that G26/24 oligodendroglioma cells release EVs that contain proteins, such as FasL and TRAIL, which induce apoptosis in rat cortical neurons [1] and astrocytes [2]. We also reported that cancer cells use EVs for transferring, into the environment [3], proteins such as extracellular matrix remodelling proteases [4], and H1°, a differentiation-specific histone [5]. In particular, by releasing H1°, cells could escape differentiation cues [5]. To verify the role of EVs in releasing specific proteins and mRNAs, in this study we used as a model A375 melanoma cells. METHODS EVs were purified from cell culture media as previously reported [1, 2]. T1 RNase-protection assa…

Settore BIO/10 - BiochimicaOligodendroglioma cells extracellular vesicles (EVS) histone H1.0 RNA-binding proteins (RBPs) myelin expression factor-2 (MYEF2)Settore BIO/06 - Anatomia Comparata E Citologia
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Expression and intracellular localization of H1° mRNA-containing complexes in developing rat brain and astrocytes

2015

INTRODUCTION: Post-transcriptional regulation of gene expression relies on RNA-binding proteins (RBPs), which regulate intracellular transport, stability, and translation of mRNAs [1]. We previously identified a set of proteins which interact with mRNAs encoding H1° and H3.3 histones [2-5]. All these proteins are probably part of a ribonucleoprotein particle [6]. Here we report more details on the expression and intracellular localization of some of these RBPs, during rat brain development and in isolated rat astrocytes. METHODS: Affinity chromatography was performed as already described [6]. Preparation of total lysates and cellular sub-fractions was done as reported in [3]. Possible co-lo…

Settore BIO/10 - BiochimicaPost-transcriptional regulation RNA-binding proteins (RBPs) H1° and H3.3 histones variants CSD-C2.Settore BIO/06 - Anatomia Comparata E Citologia
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Extracellular membrane vesicles can mediate intercellular transfer of molecules

2012

Many eukaryotic cell types, including neural cells, release into the extracellular environment vesicles of different sizes and composition. Neurons and astrocytes shed extracellular vesicles which contain FGF2 and VEGF and could be involved in interaction with endothelial cells, to form the blood-brain barrier. Also brain tumor cells, such as glioblastomas, release vesicles in the extracellular space. Microvesicles (MVs) shed from G26/24 oligodendro¬glioma cells were previously reported to contain FAS-L and to cause a reproducible, dose-dependent, inhibitory effect on neurite outgrowth, and neuronal apoptosis, when added to primary cultures of rat cortical neurons. More recently, they were …

apoptosis astrocyteRBPsSettore BIO/10 - BiochimicaSettore BIO/06 - Anatomia Comparata E Citologiaoligodendrogliomashedding vesicle
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