Search results for "Myosins"

showing 6 items of 36 documents

Resveratrol initiates differentiation of mouse skeletal muscle-derived C2C12 myoblasts.

2012

Resveratrol is one of the most widely studied bio-active plant polyphenols. While its effect on endothelial blood vessel cells, cancer cells, inflammatory processes and neurodegenerative events is well documented, little is known about the implication of this phytophenol in differentiating processes, particularly in skeletal muscle cells. Here, we report the effects of resveratrol on mouse skeletal muscle-derived cells (C2C12) in either a nondifferentiated (myoblasts) or differentiated state (myotubes) by evaluating resveratrol uptake, cell proliferation, changes in cell shape, and the expression of genes encoding muscle-specific transcription factors or contractile proteins. Resveratrol: (…

Transcription GeneticCellular differentiationMyoblasts SkeletalMuscle Fibers SkeletalBiologyResveratrolMyosinsBiochemistryCell Linechemistry.chemical_compoundMiceStilbenesmedicineMyocyteAnimalsCell ShapeMyogeninCell ProliferationPharmacologyMyogenesisfood and beveragesSkeletal muscleCell DifferentiationMolecular biologyMicroRNAsmedicine.anatomical_structurechemistryResveratrolCancer cellC2C12Transcription FactorsBiochemical pharmacology
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Study of USH1 Splicing Variants through Minigenes and Transcript Analysis from Nasal Epithelial Cells

2012

Usher syndrome type I (USH1) is an autosomal recessive disorder characterized by congenital profound deafness, vestibular areflexia and prepubertal retinitis pigmentosa. The first purpose of this study was to determine the pathologic nature of eighteen USH1 putative splicing variants found in our series and their effect in the splicing process by minigene assays. These variants were selected according to bioinformatic analysis. The second aim was to analyze the USH1 transcripts, obtained from nasal epithelial cells samples of our patients, in order to corroborate the observed effect of mutations by minigenes in patient’s tissues. The last objective was to evaluate the nasal ciliary beat fre…

Usher syndromelcsh:Medicinemedicine.disease_causeGene SplicingMolecular cell biologyAutosomal Recessivelcsh:ScienceGeneticsMutationMultidisciplinaryCadherinsMyosin VIIaRNA splicingSensory PerceptionUsher SyndromesResearch ArticleRNA SplicingCadherin Related ProteinsBiologyMyosinsNoseGenetic MutationRetinitis pigmentosamedicineGeneticsotorhinolaryngologic diseasesHumansCiliaBiologyMessenger RNAlcsh:RIntronMutation TypesComputational BiologyGenetic VariationEpithelial CellsHuman Geneticsmedicine.diseaseMolecular biologyRNA processingMutagenesisCase-Control StudiesMutationGenetics of Diseaselcsh:QGene expressionSensory DeprivationPCDH15MinigeneCloningNeuroscience
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Creatine kinase is the main target of reactive oxygen species in cardiac myofibrils.

1996

Abstract Reactive oxygen species (ROS) have been reported to alter cardiac myofibrillar function as well as myofibrillar enzymes such as myosin ATPase and creatine kinase (CK). To understand their precise mode and site of action in myofibrils, the effects of the xanthine/xanthine oxidase (X/XO) system or of hydrogen peroxide (H 2 O 2 ) have been studied in the presence and in the absence of phosphocreatine (PCr) in Triton X-100–treated cardiac fibers. We found that xanthine oxidase (XO), with or without xanthine, induced a decrease in maximal Ca 2+ -activated tension. We attributed this effect to the high contaminating proteolytic activity in commercial XO preparations, since it could be p…

Xanthine OxidasebiologyFree RadicalsPhysiologyMyosin ATPaseSuperoxideHydrogen PeroxideMyosinsXanthineMyocardial ContractionPhosphocreatineRatschemistry.chemical_compoundchemistryBiochemistryMyofibrilsbiology.proteinAnimalsCreatine kinasePMSFCardiology and Cardiovascular MedicineMyofibrilXanthine oxidaseReactive Oxygen SpeciesCreatine KinaseCirculation research
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Interactions in the network of Usher syndrome type 1 proteins

2004

International audience; Defects in myosin VIIa, harmonin (a PDZ domain protein), cadherin 23, protocadherin 15 and sans (a putative scaffolding protein), underlie five forms of Usher syndrome type I (USH1). Mouse mutants for all these proteins exhibit disorganization of their hair bundle, which is the mechanotransduction receptive structure of the inner ear sensory cells, the cochlear and vestibular hair cells. We have previously demonstrated that harmonin interacts with cadherin 23 and myosin VIIa. Here we address the extent of interactions between the five known USH1 proteins. We establish the previously suggested sans-harmonin interaction and find that sans also binds to myosin VIIa. We …

[SDV]Life Sciences [q-bio]Hearing Loss SensorineuralStereocilia (inner ear)PDZ domainCadherin Related ProteinsProtocadherinCell Cycle ProteinsNerve Tissue ProteinsCuticular plateMyosinsBiologyMiceTwo-Hybrid System TechniquesHair Cells AuditoryBone plateMyosinotorhinolaryngologic diseasesGeneticsAnimalsHumansProtein PrecursorsMolecular BiologyGenetics (clinical)GeneticsStereociliumDyneinsSyndromeGeneral MedicineCadherinsCell biologyCytoskeletal ProteinsMyosin VIIaMutationsense organsCarrier ProteinsRetinitis PigmentosaPCDH15HeLa CellsProtein BindingHuman Molecular Genetics
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Microarray-based mutation analysis of 183 Spanish families with Usher syndrome.

2010

PURPOSE. The purpose of this study was to test the ability of the genotyping microarray for Usher syndrome (USH) to identify the mutations responsible for the disease in a cohort of 183 patients with USH. METHODS. DNA from 183 patients with Usher syndrome from the Spanish population was analyzed using a genotyping microarray containing 429 previously identified disease-associated variants in eight USH genes. Mutations detected by the array were confirmed by direct sequencing. Haplotype analysis was also performed in families carrying common Spanish mutations. RESULTS. The genotyping microarray identified 43 different variants, divided into 32 disease causative and 11 probably non-pathologic…

medicine.medical_specialtyGenotypeMicroarrayUsher syndromeDNA Mutational AnalysisCadherin Related ProteinsCell Cycle ProteinsNerve Tissue ProteinsMyosinsBiologymedicine.disease_causePolymerase Chain ReactionReceptors G-Protein-CoupledMolecular geneticsGenotypemedicineotorhinolaryngologic diseasesHumansGenotypingAllelesAdaptor Proteins Signal TransducingOligonucleotide Array Sequence AnalysisGeneticsExtracellular Matrix ProteinsMutationGene Expression ProfilingHaplotypeMembrane ProteinsCadherinsmedicine.diseaseGene expression profilingCytoskeletal ProteinsSpainMyosin VIIaMutationUsher Syndromes
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Regulation of motility of cells from marine sponges by calcium ions

1996

Sponges are known not to contain muscle and nerve cells. Since sponge cells are characterized by high motility we determined the effect of intracellular calcium ion concentration ([Ca2+]i) on their motility. Addition of the Ca2+ ionophore ionomycin to dissociated cells from the marine sponge Suberites domuncula caused in Ca(2+)-containing artificial seawater (ASW) an increase in motility from 0.2 micron/min (absence of the ionophore) to 3.7 microns/min (presence of ionomycin). When the experiments were performed in Ca(2+)-free medium, no effect of ionomycin could be observed. In parallel experiments the changes of [Ca2+]i using the dye Fura-2 were measured. The experiments revealed that ion…

xThapsigarginFura-2Molecular Sequence DataMotilitychemistry.chemical_elementArtificial seawaterCalciumBiologyMyosinschemistry.chemical_compoundCell MovementMyosinAnimalsHumansSeawaterAmino Acid SequenceFluorescent DyesIonsIonophoresSequence Homology Amino AcidIonomycinCell BiologyPoriferachemistryBiochemistryIonomycinBiophysicsCalciumCyclopiazonic acidFura-2
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