Search results for "G proteins"

showing 10 items of 992 documents

Inactivation of the KSRP gene modifies collagen antibody induced arthritis.

2017

Abstract The KH type splicing regulatory protein (KSRP) is a nucleic acid binding protein, which negatively regulates the stability and/or translatability of many mRNA species encoding immune-relevant proteins. As KSRP is expressed in immune cells including T and B cells, neutrophils, macrophages and dendritic cells, we wanted to analyze its importance for the development of autoimmune diseases. We chose collagen antibody-induced arthritis (CAIA) as an appropriate autoimmune disease mouse model in which neutrophils and macrophages constitute the main effector cell populations. We compared arthritis induction in wild type (WT) and KSRP−/− mice and paws were taken for histological sections an…

0301 basic medicinemedicine.drug_classmedicine.medical_treatmentInflammatory arthritisChemokine CXCL1ImmunologyArthritisAntigens Differentiation MyelomonocyticNitric Oxide Synthase Type IISpleenBiologyMonoclonal antibodyPeripheral blood mononuclear cellAntibodiesFlow cytometry03 medical and health sciencesInterferon-gammaMiceImmune systemAntigens CDmedicineAnimalsAntigens LyCalgranulin ARNA MessengerMolecular BiologyInflammationmedicine.diagnostic_testTumor Necrosis Factor-alphaMacrophagesRNA-Binding Proteinsmedicine.diseaseMolecular biologyArthritis ExperimentalLymphocyte Function-Associated Antigen-1Mice Inbred C57BL030104 developmental biologyCytokinemedicine.anatomical_structureImmunologyTrans-ActivatorsCytokinesCollagenMolecular immunology
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Altered synaptic phospholipid signaling in PRG-1 deficient mice induces exploratory behavior and motor hyperactivity resembling psychiatric disorders.

2017

Abstract Plasticity related gene 1 (PRG-1) is a neuron specific membrane protein located at the postsynaptic density of glutamatergic synapses. PRG-1 modulates signaling pathways of phosphorylated lipid substrates such as lysophosphatidic acid (LPA). Deletion of PRG-1 increases presynaptic glutamate release probability leading to neuronal over-excitation. However, due to its cortical expression, PRG-1 deficiency leading to increased glutamatergic transmission is supposed to also affect motor pathways. We therefore analyzed the effects of PRG-1 function on exploratory and motor behavior using homozygous PRG-1 knockout (PRG-1−/−) mice and PRG-1/LPA2–receptor double knockout (PRG-1−/−/LPA2−/−)…

0301 basic medicinemedicine.medical_specialtyGlutamic AcidNerve Tissue ProteinsBiologyHyperkinesisHippocampusOpen field03 medical and health sciencesBehavioral NeuroscienceGlutamatergicchemistry.chemical_compoundMice0302 clinical medicineLysophosphatidic acidmedicineAnimalsReceptors Lysophosphatidic AcidPsychiatryMice KnockoutNeuronsMental DisordersGlutamate receptorSomatosensory CortexMice Inbred C57BL030104 developmental biologymedicine.anatomical_structurechemistrySynapsesExploratory BehaviorGABAergicCalmodulin-Binding ProteinsFemaleNeuronSignal transductionLysophospholipidsPostsynaptic density030217 neurology & neurosurgerySignal TransductionBehavioural brain research
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Increased Muscleblind levels by chloroquine treatment improve myotonic dystrophy type 1 phenotypes in in vitro and in vivo models

2019

Myotonic dystrophy type 1 (DM1) is a life-threatening and chronically debilitating neuromuscular disease caused by the expansion of a CTG trinucleotide repeat in the 3′ UTR of the DMPK gene. The mutant RNA forms insoluble structures capable of sequestering RNA binding proteins of the Muscleblind-like (MBNL) family, which ultimately leads to phenotypes. In this work, we demonstrate that treatment with the antiautophagic drug chloroquine was sufficient to up-regulate MBNL1 and 2 proteins in Drosophila and mouse (HSA LR ) models and patient-derived myoblasts. Extra Muscleblind was functional at the molecular level and improved splicing events regulated by MBNLs in all disease models. In vivo,…

0301 basic medicinemusculoskeletal diseasesMaleRNA SplicingRNA-binding proteinBiologyMyotonic dystrophychloroquinemuscleblindMyoblasts03 medical and health scienceschemistry.chemical_compoundMice0302 clinical medicineIn vivomedicineAutophagyMBNL1AnimalsDrosophila ProteinsHumansMyotonic DystrophytherapyMultidisciplinarymyotonic dystrophyMusclesRNANuclear ProteinsRNA-Binding ProteinsChloroquinemedicine.diseaseMyotoniaCell biologyDNA-Binding ProteinsDisease Models Animal030104 developmental biologyPhenotypechemistryPNAS PlusRNA splicingDrosophilaFemaleTrinucleotide repeat expansion030217 neurology & neurosurgery
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miR-23b and miR-218 silencing increase Muscleblind-like expression and alleviate myotonic dystrophy phenotypes in mammalian models

2018

Functional depletion of the alternative splicing factors Muscleblind-like (MBNL 1 and 2) is at the basis of the neuromuscular disease myotonic dystrophy type 1 (DM1). We previously showed the efficacy of miRNA downregulation in Drosophila DM1 model. Here, we screen for miRNAs that regulate MBNL1 and MBNL2 in HeLa cells. We thus identify miR-23b and miR-218, and confirm that they downregulate MBNL proteins in this cell line. Antagonists of miR-23b and miR-218 miRNAs enhance MBNL protein levels and rescue pathogenic missplicing events in DM1 myoblasts. Systemic delivery of these “antagomiRs” similarly boost MBNL expression and improve DM1-like phenotypes, including splicing alterations, histo…

0301 basic medicinemusculoskeletal diseasesMalecongenital hereditary and neonatal diseases and abnormalitiesScienceMyoblasts SkeletalGeneral Physics and AstronomyMice TransgenicBiologyMyotonic dystrophyGeneral Biochemistry Genetics and Molecular BiologyArticleCell Line03 medical and health scienceschemistry.chemical_compoundMice0302 clinical medicineRNA interferencemicroRNAmedicineMBNL1Gene silencingAnimalsHumansMyotonic DystrophyGene SilencingRNA Messengerlcsh:ScienceMuscle Skeletal3' Untranslated RegionsMultidisciplinaryThree prime untranslated regionAlternative splicingQRNA-Binding ProteinsGeneral Chemistrymedicine.diseaseMyotoniaCell biologyUp-RegulationAlternative SplicingDisease Models AnimalMicroRNAs030104 developmental biologyPhenotypechemistrylcsh:Q030217 neurology & neurosurgeryHeLa CellsNature Communications
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Paternal uniparental disomy chromosome 14-like syndrome due a maternal de novo 160 kb deletion at the 14q32.2 region not encompassing the IG- and the…

2015

The human chromosome 14q32 carries a cluster of imprinted genes which include the paternally expressed genes (PEGs) DLK1 and RTL1, as well as the maternally expressed genes (MEGs) MEG3, RTL1as, and MEG8. PEGs and MEGs expression at the 14q32.2-imprinted region are regulated by two differentially methylated regions (DMRs): the IG-DMR and the MEG3-DMR, which are respectively methylated on the paternal and unmethylated on the maternal chromosome 14 in most cells. Genetic and epigenetic abnormalities affecting these imprinted gene clusters result in two different phenotypes currently known as maternal upd(14) syndrome and paternal upd(14) syndrome. However, only few patients carrying a maternal…

14q32.2 imprinted regionGenotypeBiologyPregnancy ProteinsMEG3-DMRGenomic ImprintingPaternal uniparental disomy chromosome 14 [upd(14)pat]GeneticsmedicineHumans14q32.2 maternal deletionEpigenetics"coat-hanger" rib signGeneGenetics (clinical)Sequence DeletionGeneticsMEG3Chromosomes Human Pair 14Comparative Genomic HybridizationIG-DMRMEG3 geneCalcium-Binding ProteinsInfant NewbornChromosomeMembrane ProteinsSyndromeDNA MethylationUniparental Disomymedicine.diseasePrognosisPhenotypeMolecular biologyUniparental disomyDifferentially methylated regionsPhenotypeSkeletal dysplasiaIntercellular Signaling Peptides and ProteinsFemaleRNA Long NoncodingRTL1as geneGenomic imprintingAmerican journal of medical genetics. Part A
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PEG 400/Cerium Ammonium Nitrate Combined with Microwave-Assisted Synthesis for Rapid Access to Beta-Amino Ketones. An Easy-to-Use Protocol for Discov…

2018

Compound libraries are important requirement in target-based drug discovery. In the present work, a small focused compound library based on β-aminoketone scaffold has been prepared combining microwave-assisted organic synthesis (MAOS) with polymer-assisted solution phase synthesis (PASPS) and replacing reaction workup standard purification procedures with solid phase extraction (SPE). Specifically, the effects of solvent, such as dioxane, dimethylformamide (DMF), polyethylene glycol 400 (PEG 400), temperature, irradiation time, stoichiometric ratio of reagents, and catalysts (HCl, acetic acid, cerium ammonium nitrate (CAN)) were investigated to maximize both conversion and yield. The optimi…

3003Transcription FactorPharmaceutical ScienceNitratePolyethylene Glycol01 natural sciencesPolyethylene GlycolsPolymer-assisted solution phase synthesiAnalytical Chemistrychemistry.chemical_compoundDrug DiscoveryMannich reactionSolid phase extractionMicrowavesβ-aminoketonesCeriumKetonesKetoneDNA-Binding ProteinsSolventCeriumChemistry (miscellaneous)Molecular MedicineDimethylformamideMicrowave-assisted organic synthesiMannich reaction; β-aminoketones; microwave-assisted organic synthesis; polymer-assisted solution phase synthesis; solid phase extraction; drug discoveryDNA-Binding ProteinBacterial Proteinchemistry.chemical_elementPolyethylene glycol010402 general chemistryArticlelcsh:QD241-441Bacterial Proteinslcsh:Organic chemistryΒ-aminoketonePhysical and Theoretical ChemistrySolid phase extractionpolymer-assisted solution phase synthesisPEG 400Nitrates010405 organic chemistryDrug Discovery3003 Pharmaceutical ScienceOrganic ChemistrySettore CHIM/08 - Chimica FarmaceuticaCombinatorial chemistry0104 chemical scienceschemistryYield (chemistry)microwave-assisted organic synthesisOrganic synthesisMicrowaveTranscription FactorsMolecules
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Exploration of the Activation Mechanism of the Epigenetic Regulator MLL3: A QM/MM Study

2021

The mixed lineage leukemia 3 or MLL3 is the enzyme in charge of the writing of an epigenetic mark through the methylation of lysine 4 from the N-terminal domain of histone 3 and its deregulation has been related to several cancer lines. An interesting feature of this enzyme comes from its regulation mechanism, which involves its binding to an activating dimer before it can be catalytically functional. Once the trimer is formed, the reaction mechanism proceeds through the deprotonation of the lysine followed by the methyl-transfer reaction. Here we present a detailed exploration of the activation mechanism through a QM/MM approach focusing on both steps of the reaction, aiming to provide new…

570StereochemistryLysineTrimerMolecular Dynamics Simulation01 natural sciencesBiochemistryMicrobiologyenzyme catalysisDFTArticleEpigenesis GeneticEnzyme catalysisQM/MM03 medical and health sciencesResidue (chemistry)Deprotonation0103 physical sciencesprotein regulationHumanscancerCàncerMolecular Biology030304 developmental biology0303 health sciencesBinding Sites010304 chemical physicsbiologyChemistryLysineNuclear ProteinsMethylation540QR1-502DNA-Binding ProteinsHistonebiology.proteinTyrosinemethyltransferaseProtein MultimerizationProtonsProteïnesTranscription Factors
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Post-Transcriptional Regulation of Iron Homeostasis in Saccharomyces cerevisiae

2013

Iron is an essential micronutrient for all eukaryotic organisms because it participates as a redox cofactor in a wide variety of biological processes. Recent studies in Saccharomyces cerevisiae have shown that in response to iron deficiency, an RNA-binding protein denoted Cth2 coordinates a global metabolic rearrangement that aims to optimize iron utilization. The Cth2 protein contains two Cx8Cx5Cx3H tandem zinc fingers (TZFs) that specifically bind to adenosine/uridine-rich elements within the 3' untranslated region of many mRNAs to promote their degradation. The Cth2 protein shuttles between the nucleus and the cytoplasm. Once inside the nucleus, Cth2 binds target mRNAs and stimulate…

572 Biochemistryalternative 3' end processingSaccharomyces cerevisiae ProteinsIronTristetraprolinSaccharomyces cerevisiaeSaccharomyces cerevisiaeReviewyeastCatalysisInorganic Chemistrylcsh:ChemistryCth1TristetraprolinmRNA decayGene Expression Regulation FungalCth2medicineRNA MessengerRnt1Physical and Theoretical Chemistry3' Untranslated RegionsMolecular BiologyTranscription factorlcsh:QH301-705.5SpectroscopyMessenger RNAalternative 3′ end processingbiologyThree prime untranslated regionOrganic ChemistryQR MicrobiologyGeneral MedicineIron deficiencymedicine.diseasebiology.organism_classificationComputer Science ApplicationsDNA-Binding ProteinsRibonucleotide reductaseBiochemistrylcsh:Biology (General)lcsh:QD1-999Cytoplasmalternative 3' end processingTranscription Factorspost-transcriptional regulationInternational Journal of Molecular Sciences
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9-cis-Retinoic acid enhances fatty acid-induced expression of the liver fatty acid-binding protein gene

1997

The role of retinoic acids (RA) on liver fatty acid- binding protein (L-FABP) expression was investigated in the well differentiated FAO rat hepatoma cell line. 9-cis-Retinoic acid (9-ci's-RA) specifically enhanced L-FABP mRNA levels in a time- and dose-dependent manner. The higher induction was found 6 h after addition of 10 -6 M 9-CK-RA in the medium. RA also enhanced further both L-FABP mRNA levels and cytosolic L-FABP protein content induced by oleic acid. The retinoid X receptor (RXR) and the peroxisome proliferator-activated receptor (PPAR), which are known to be activated, respectively, by 9-c/s-RA and long chain fatty acid (LCFA), co-operated to bind specifically the peroxisome prol…

9-cw-Retinoic acidReceptors Retinoic Acid[SDV]Life Sciences [q-bio]Receptors Cytoplasmic and NuclearPeroxisome proliferator-activated receptorMyelin P2 ProteinMicrobodiesBiochemistry0302 clinical medicineStructural BiologyTumor Cells CulturedAlitretinoinchemistry.chemical_classification0303 health sciencesChemistryFatty AcidsDrug SynergismPeroxisomeNeoplasm Proteins9-cis-Retinoic acidLiverBiochemistryFree fatty acid receptorlipids (amino acids peptides and proteins)Peroxisome proliferator-activated receptor alphaLong chain fatty acidFatty Acid-Binding Protein 7DimerizationPeroxisome proliferator-activated receptor gammaCarcinoma HepatocellularBiophysicsNerve Tissue ProteinsTretinoinRetinoid X receptorFatty Acid-Binding ProteinsLiver fatty acid-binding protein03 medical and health sciencesGeneticsAnimalsRNA MessengerMolecular Biology030304 developmental biologyFAO hepatoma cellFatty acidCell BiologyFatty acidRatsRetinoid X ReceptorsGene Expression RegulationNuclear receptorGene expressionCarrier Proteins[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition030217 neurology & neurosurgeryTranscription FactorsFEBS Letters
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CitA/CitB Two-Component System Regulating Citrate Fermentation in Escherichia coli and Its Relation to the DcuS/DcuR System In Vivo

2011

ABSTRACT Citrate fermentation by Escherichia coli requires the function of the citrate/succinate antiporter CitT ( citT gene) and of citrate lyase ( citCDEFXG genes). Earlier experiments suggested that the two-component system CitA/CitB, consisting of the membrane-bound sensor kinase CitA and the response regulator CitB, stimulates the expression of the genes in the presence of citrate, similarly to CitA/CitB of Klebsiella pneumoniae . In this study, the expression of a chromosomal citC-lacZ gene fusion was shown to depend on CitA/CitB and citrate. CitA/CitB is related to the DcuS/DcuR two-component system which induces the expression of genes for fumarate respiration in response to C 4 -di…

ATP citrate lyaseOperonBiologymedicine.disease_causeMicrobiologyCitric AcidFusion geneGene clusterEscherichia colimedicinePromoter Regions GeneticMolecular BiologyEscherichia coliEscherichia coli ProteinsPromoterGene Expression Regulation BacterialArticlesMolecular biologyTwo-component regulatory systemDNA-Binding ProteinsResponse regulatorBiochemistryFermentationProtein KinasesProtein BindingTranscription FactorsJournal of Bacteriology
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