Search results for "huntingtin"

showing 10 items of 20 documents

The

2016

ABSTRACT Members of the Junctophilin (JPH) protein family have emerged as key actors in all excitable cells, with crucial implications for human pathophysiology. In mammals, this family consists of four members (JPH1-JPH4) that are differentially expressed throughout excitable cells. The analysis of knockout mice lacking JPH subtypes has demonstrated their essential contribution to physiological functions in skeletal and cardiac muscles and in neurons. Moreover, mutations in the human JPH2 gene are associated with hypertrophic and dilated cardiomyopathies; mutations in JPH3 are responsible for the neurodegenerative Huntington's disease-like-2 (HDL2), whereas JPH1 acts as a genetic modifier …

NotchGenotypeCardiomyopathyGenes InsectAnimals Genetically ModifiedAnimalsDrosophila ProteinsAllelesMammalsNeuronsHuntingtin ProteinReceptors NotchMusclesMyocardiumMembrane ProteinsReproducibility of ResultsDrosHuntington's diseaseDisease Models AnimalDrosophila melanogasterPhenotypeGene Knockdown TechniquesMutationNerve DegenerationPhotoreceptor Cells InvertebrateRNA InterferenceJunctophilinDrosophilaTrinucleotide Repeat ExpansionSignal TransductionResearch ArticleDisease modelsmechanisms
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Polymorphism of Amyloid Fibrils and their Complexes with Catalase

2014

Catalase binding to amyloid fibrils has been shown for the Alzheimer’s amyloid-β (Aβ), type 2 diabetes-associated islet amyloid polypeptide (IAPP) and Creutzfeldt-Jakob disease-associated prion protein (PrP). Catalase targets a specific domain with a GAII-like sequence and there are a number of other amyloid fibril-forming proteins that contain related sequences, such as the Parkinson’s associated α-synuclein protein and the Huntington disease protein Huntingtin. Using transmission electron microscopy (TEM) analysis, interactions show specific binding of catalase to some, but not all, fibrillar forms of Aβ, IAPP and PrP fragments, allowing determination of the fibrillar forms that contain a…

geographyHuntingtingeography.geographical_feature_categorybiologyP3 peptideIsletnervous system diseaseschemistry.chemical_compoundKisspeptinschemistryPolymorphism (materials science)BiochemistryCatalasemental disordersHuntingtin Proteinbiology.proteinEthylene glycol
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Expression of genes encoding the calcium signalosome in cellular and transgenic models of Huntington's disease

2013

Huntington's disease (HD) is a hereditary neurodegenerative disease caused by the expansion of a polyglutamine stretch in the huntingtin (HTT) protein and characterized by dysregulated calcium homeostasis. We investigated whether these disturbances are correlated with changes in the mRNA level of the genes that encode proteins involved in calcium homeostasis and signaling (i.e., the calciosome). Using custom-made TaqMan low-density arrays containing probes for 96 genes, we quantified mRNA in the striatum in YAC128 mice, a model of HD, and wildtype mice. HTT mutation caused the increased expression of some components of the calcium signalosome, including calretinin, presenilin 2, and calmyri…

Huntingtinhuntingtincalcium signalosomechemistry.chemical_elementtransgenic miceCalciumlcsh:RC321-571Cellular and Molecular Neurosciencehuntingtin-associated protein 1mental disordersGene expressionOriginal Research Articlelcsh:Neurosciences. Biological psychiatry. NeuropsychiatryMolecular BiologyCalcium metabolismTaqMan low-density arraysbiologyHuntingtin-associated protein 1Calcium channelTaqMan Low Density Arraysstore-operated calcium entrycalcyclin-binding proteinHuntington's diseaseMolecular biologyStore-operated calcium entrynervous systemchemistrybiology.proteinCalretininHuntington’s diseaseNeuroscienceFrontiers in Molecular Neuroscience
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Pharmacological disruption of the MID1/α4 interaction reduces mutant Huntingtin levels in primary neuronal cultures.

2017

Expression of mutant Huntingtin (HTT) protein is central to the pathophysiology of Huntington's Disease (HD). The E3 ubiquitin ligase MID1 appears to have a key role in facilitating translation of the mutant HTT mRNA suggesting that interference with the function of this complex could be an attractive therapeutic approach. Here we describe a peptide that is able to disrupt the interaction between MID1 and the α4 protein, a regulatory subunit of protein phosphatase 2A (PP2A). By fusing this peptide to a sequence from the HIV-TAT protein we demonstrate that the peptide can disrupt the interaction within cells and show that this results in a decrease in levels of ribosomal S6 phosphorylation a…

0301 basic medicinecongenital hereditary and neonatal diseases and abnormalitiesHuntingtinMid1 protein mouseProtein subunitUbiquitin-Protein LigasesMutantPrimary Cell CulturePeptide03 medical and health sciencesMiceHuntington's diseasemental disordersmedicineAnimalsHumansHtt protein mouseddc:610Protein Phosphatase 2Neuronschemistry.chemical_classificationMessenger RNAHuntingtin ProteinbiologyChemistryGeneral NeuroscienceProteinsgenetics [Huntingtin Protein]metabolism [Protein Phosphatase 2]metabolism [Proteins]Protein phosphatase 2medicine.diseaseUbiquitin ligaseCell biology030104 developmental biologyHEK293 Cellsmetabolism [Neurons]metabolism [Huntingtin Protein]Mutationbiology.proteinProtein Binding
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Huntingtin mediates dendritic transport of β-actin mRNA in rat neurons

2011

Transport of mRNAs to diverse neuronal locations via RNA granules serves an important function in regulating protein synthesis within restricted sub-cellular domains. We recently detected the Huntington's disease protein huntingtin (Htt) in dendritic RNA granules; however, the functional significance of this localization is not known. Here we report that Htt and the huntingtin-associated protein 1 (HAP1) are co-localized with the microtubule motor proteins, the KIF5A kinesin and dynein, during dendritic transport of β-actin mRNA. Live cell imaging demonstrated that β-actin mRNA is associated with Htt, HAP1, and dynein intermediate chain in cultured neurons. Reduction in the levels of Htt, H…

congenital hereditary and neonatal diseases and abnormalitiesHuntingtinDyneinModels NeurologicalBiological Transport ActiveKinesinsRNA-binding proteinNerve Tissue Proteinsmacromolecular substancesBiologyCytoplasmic GranulesMicrotubulesArticle03 medical and health sciences0302 clinical medicineMicrotubulemental disordersProtein biosynthesisMRNA transportAnimalsRNA MessengerRNA Small InterferingRats WistarCells Cultured030304 developmental biologyNeurons0303 health sciencesHuntingtin ProteinMultidisciplinaryMolecular Motor ProteinsBrainDyneinsNuclear ProteinsRNA-Binding ProteinsDendritesActinsCell biologynervous system diseasesRatsDendritic transportnervous systemGene Knockdown TechniquesKinesinFemale030217 neurology & neurosurgerySignal TransductionScientific Reports
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Flanking regions determine the structure of the poly-glutamine homo- repeat in huntingtin through mechanisms common among glutamine-rich human protei…

2020

International audience; The causative agent of Huntington's disease, the poly-Q homo-repeat in the N-terminal region of huntingtin (httex1), is flanked by a 17-residue-long fragment (N17) and a proline-rich region (PRR), which promote and inhibit the aggregation propensity of the protein, respectively, by poorly understood mechanisms. Based on experimental data obtained from site-specifically labeled NMR samples, we derived an ensemble model of httex1 that identified both flanking regions as opposing poly-Q secondary structure promoters. While N17 triggers helicity through a promiscuous hydrogen bond network involving the side chains of the first glutamines in the poly-Q tract, the PRR prom…

Repetitive Sequences Amino AcidHuntingtinAmino Acid Motifs[SDV.BBM.BP] Life Sciences [q-bio]/Biochemistry Molecular Biology/Biophysics03 medical and health sciencesHuntington's diseaseStructural BiologyHuman proteome projectmedicineHumans[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Molecular BiologyHuman proteinsProtein secondary structure[SDV.BBM.BC] Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]030304 developmental biology[INFO.INFO-BI] Computer Science [cs]/Bioinformatics [q-bio.QM]Huntingtin Protein0303 health sciencesChemistry030302 biochemistry & molecular biologyPromotermedicine.diseaseCell biologyIntrinsically Disordered ProteinsGlutamine[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsPolyglutamic Acid[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]Low Complexity Region
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AAV Vector–mediated RNAi of Mutant Huntingtin Expression Is Neuroprotective in a Novel Genetic Rat Model of Huntington's Disease

2008

We report the characterization of a new rapid-onset model of Huntington's disease (HD) generated by adeno-associated virus (AAV) vector–mediated gene transfer of N-terminal huntingtin (htt) constructs into the rat striatum. Expression of exon 1 of mutant htt containing 70 CAG repeats rapidly led to neuropathological features associated with HD. In addition, we report novel data relating to neuronal transduction of AAV vectors that modulated the phenotype observed in this model. Quantitative reverse transcriptase–polymerase chain reaction (RT–PCR) revealed that AAV vector–mediated expression in the striatum increased by >100-fold as compared to the endogenous htt level. Moreover, AAV vectors…

HuntingtinvirusesGenetic VectorsNerve Tissue ProteinsSubstantia nigraBiologyArticleViral vectorHuntington's diseaseRNA interferenceDrug DiscoverymedicineHuntingtin ProteinGeneticsAnimalsHumansMolecular BiologyNeuronsPharmacologyHuntingtin ProteinGene knockdownReverse Transcriptase Polymerase Chain ReactionNeurodegenerationNuclear ProteinsExonsGenetic TherapyDependovirusmedicine.diseaseMolecular biologyCorpus StriatumRatsHuntington DiseaseNeuroprotective AgentsPhenotypenervous systemMolecular MedicineRNA InterferenceMolecular Therapy
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A novel function of Huntingtin in the cilium and retinal ciliopathy in Huntington's disease mice

2015

Huntington's disease (HD) is a neurodegenerative disorder caused by the toxic expansion of polyglutamine in the Huntingtin (HTT) protein. The pathomechanism is complex and not fully understood. Increasing evidence indicates that the loss of normal protein function also contributes to the pathogenesis, pointing out the importance of understanding the physiological roles of HTT. We provide evidence for a novel function of HTT in the cilium. HTT localizes in diverse types of cilia — including 9 + 0 non-motile sensory cilia of neurons and 9 + 2 motile multicilia of trachea and ependymal cells — which exert various functions during tissue development and homeostasis. In the photoreceptor cilium,…

AxonemeMalecongenital hereditary and neonatal diseases and abnormalitiesHuntingtinCentrioleMice TransgenicNerve Tissue ProteinsBiologyMicrotubulesPhotoreceptor cellRetinalcsh:RC321-571MiceHuntington's diseaseIntraflagellar transportmental disordersmedicineAnimalsHumansPhotoreceptor CellsHuntingtinCilialcsh:Neurosciences. Biological psychiatry. NeuropsychiatryComputingMilieux_MISCELLANEOUSHuntingtin ProteinPhotoreceptorCiliumNuclear ProteinsHuntington's diseasemedicine.diseaseCell biologyCiliopathyDisease Models Animalmedicine.anatomical_structureHEK293 CellsHuntington DiseaseNeurologyFemale[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]sense organs
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The Role of Low Complexity Regions in Protein Interaction Modes: An Illustration in Huntingtin

2021

Low complexity regions (LCRs) are very frequent in protein sequences, generally having a lower propensity to form structured domains and tending to be much less evolutionarily conserved than globular domains. Their higher abundance in eukaryotes and in species with more cellular types agrees with a growing number of reports on their function in protein interactions regulated by post-translational modifications. LCRs facilitate the increase of regulatory and network complexity required with the emergence of organisms with more complex tissue distribution and development. Although the low conservation and structural flexibility of LCRs complicate their study, evolutionary studies of proteins …

Protein Conformation alpha-Helical0301 basic medicineNetwork complexityHuntingtinintrinsically disordered regionsAmino Acid MotifsComputational biologyBiologyprotein interactionsArticlecompositionally biased regionsCatalysisProtein–protein interactionlcsh:ChemistryEvolution MolecularInorganic ChemistryLow complexity03 medical and health sciencesProtein DomainsProtein Interaction MappingAnimalsHumansp300-CBP Transcription FactorsAmino Acid SequenceProtein Interaction MapsHuntingtinTissue distributionPhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologySpectroscopyHuntingtin Protein030102 biochemistry & molecular biologyOrganic ChemistryNuclear Proteinsp120 GTPase Activating ProteinGeneral MedicineMultiple modesSynapsinslow complexity regionsComputer Science ApplicationshomorepeatsMicroscopy Electron030104 developmental biologylcsh:Biology (General)lcsh:QD1-999Sequence AlignmentFunction (biology)Protein BindingInternational Journal of Molecular Sciences
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0204: Proteome-wide sex-related differences in response to mouse thoracic aortic constriction: molecular bio-signature of failing hearts

2014

Chronic pressure overload (PO) induces pathological left ventricular hypertrophy (LVH) leading to congestive heart failure (HF). Over-expression of FKBP12.6 (FK506 binding protein (K)) in mice should prevent Ca2+-leak during diastole and may improve overall cardiac function. In order to decipher molecular mechanisms involved in thoracic aortic constriction (TAC)-induced cardiac remodelling and the influence of gender and genotype, we performed a proteomic analysis using 2D-DIGE, mass spectrometry and bioinformatics techniques to identify alterations in characteristic biological networks. Wild type (W) and K mice of both genders underwent TAC. Thirty days post-TAC, the altered cardiac remode…

Pressure overloadCardiac function curvemedicine.medical_specialtyHuntingtinFatty acid metabolismbiologybusiness.industryDiastolemedicine.diseaseLeft ventricular hypertrophychemistry.chemical_compoundEndocrinologychemistryHeart failureInternal medicinebiology.proteinmedicineCardiology and Cardiovascular MedicinebusinessCalreticulinArchives of Cardiovascular Diseases Supplements
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