Search results for "H3.3"

showing 8 items of 8 documents

TOXICITY OF B-N-OXALYLAMINO-L-ALANINE ANDB-N-METHYLAMINO-L-ALANINE IN NIH3T3 CELLS IS MEDIATED BY INHIBITIONOF THE XC¯ ANTIPORTER

2012

Beta-N-oxalylamino-L-alanine (BOAA) and beta-N-methylamino-L-alanine (BMAA) are two non-protein amino acids reported to induce neuronal degeneration. They have been involved in the pathogenesis of rare motor neuron diseases, as neurolathyrism or the ALS-Parkinson-Dementia complex of Guam. The mechanisms by which BOAA and BMAA toxicity is explicated is still unknown, but there is evidence that it might involve the inhibition of Xc¯ antiporter, that is the rate-limiting transporter of the synthesis of intracellular glutathione. In the present study, we investigated the mechanisms of BOAA and BMAA toxicity in the non-neuronal NIH3T3 cells. First, we treated NIH3T3 cells with BOAA or BMAA at di…

BOAA BMAA ALS NIH3T3 Oxidative Stress
researchProduct

Kinetics of rat CSD-C2 binding to H3.3 RNA

2017

Cold-shock domain containing protein C2 (CSD-C2; also known as PIPPin) is an RNA-binding protein conserved in the evolution that interacts with the 3’-untranslated region (3’-UTR) of rat H1.0 and H3.3 histone messengers. Biolayer interferometry (BLI) is a technique that measures changes in an interference pattern generated from visible light, reflected from an optical layer, and a biolayer which contains molecules of interest. In this study, we used the BLI methodology in order to analyze and describe the binding properties of CSD-C2 and the mRNA encoding the rat brain histone protein H3.3. Recombinant CSD-C2 was incubated with in vitro transcribed, and biotinylated H3.3 RNA fragments bound…

Chemistry0206 medical engineeringKineticsRNA02 engineering and technology021001 nanoscience & nanotechnology020601 biomedical engineeringSettore BIO/10 - BiochimicaAutomotive EngineeringBiophysicsRNA-protein interactions CSD-C2 Histone H3.3 RNA Biolayer interferometry.Settore BIO/06 - Anatomia Comparata E Citologia0210 nano-technology
researchProduct

H3 and H3.3 histone mRNA amounts and ratio in oral squamous cell carcinoma and leukoplakia.

2006

Histone variants (e.g. H3) play an important role in chromatin structure and gene expression regulation of normal cells. Aims of this study were to: (1) estimate H3 and H3.3 histone mRNA expressions and their ratio in oral squamous cell carcinoma (OSCC) and oral leukoplakia (OL); (2) investigate whether H3 and H3.3 variants could play a role in the pathogenesis of OSCC and OL, also conditionally to HPV infection, age, gender, and main habits (tobacco smoking and alcohol drinking) in human beings studied. Twenty-three cases of OSCC and 20 cases of OL were examined in lesion site (LS) and juxtaposed clinically undamaged site (JUS) by RT-PCR for H3 and H3.3 histone mRNA; 13 healthy oral mucosa…

MaleHPVH3.3 histone mRNAAlcohol Drinking"carcinoma"BiologyH3 histone mRNAoral leukoplakiaPathogenesisHistonesleucoplakia"Sex FactorsRisk FactorsmedicineCarcinomaHumansRNA MessengerOral mucosaGeneral DentistryPapillomaviridaeLeukoplakiaAgedRegulation of gene expressionMessenger RNAPapillomavirus InfectionsSmoking"H3 histones"HPV infectionAge FactorsMouth MucosaMiddle Agedmedicine.diseaseMolecular biologyoral squamous cell carcinomastomatognathic diseasesmedicine.anatomical_structureHistoneOtorhinolaryngologyDNA Viralbiology.proteinCarcinoma Squamous CellFemaleMouth NeoplasmsLeukoplakia OralOral diseases
researchProduct

RNA-binding proteins expressed in differentiating rat astrocytes

2012

RBPSettore BIO/10 - BiochimicaH1°H3.3Settore BIO/06 - Anatomia Comparata E Citologiaatsrocytes
researchProduct

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
researchProduct

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
researchProduct

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
researchProduct

Europe between Mobility and Security: the challenges of illicit trades in the Mediterranean Area

Europe between Mobility and Security: the challenges of illicit trades in the Mediterranean Area

SH2_4 SH3_3
researchGroup