Search results for "Myosins"

showing 10 items of 36 documents

Vezatin, a novel transmembrane protein, bridges myosin VIIA to the cadherin-catenins complex

2000

International audience; Defects in myosin VIIA are responsible for deafness in the human and mouse. The role of this unconventional myosin in the sensory hair cells of the inner ear is not yet understood. Here we show that the C-terminal FERM domain of myosin VIIA binds to a novel transmembrane protein, vezatin, which we identi®ed by a yeast two-hybrid screen. Vezatin is a ubiquitous protein of adherens cell±cell junctions, where it interacts with both myosin VIIA and the cadherin±catenins complex. Its recruitment to adherens junctions implicates the C-terminal region of a-catenin. Taken together, these data suggest that myosin VIIA, anchored by vezatin to the cadherin±catenins complex, cre…

MESH: Cytoskeletal ProteinsMESH: alpha CateninStereocilia (inner ear)[SDV]Life Sciences [q-bio]MESH: Amino Acid SequenceDeafnessMESH: CadherinsMiceMESH: Protein Structure Tertiary0302 clinical medicine[SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseasesMyosinMESH: Hair Cells AuditoryMESH: AnimalsCytoskeleton0303 health sciencesFERM domainGeneral NeuroscienceMESH: Alternative SplicingArticlesCadherinsCell biologymedicine.anatomical_structureIntercellular Junctions[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyMyosin VIIaHair cellMESH: Membrane ProteinsMESH: DyneinsProtein BindingMESH: MutationMacromolecular SubstancesMolecular Sequence DataMESH: Deafnessmacromolecular substancesBiologyIn Vitro TechniquesMyosinsGeneral Biochemistry Genetics and Molecular BiologyCell LineAdherens junction03 medical and health sciencesHair Cells Auditorymedicineotorhinolaryngologic diseasesAnimalsHumansMESH: Myosin VIIaMESH: Protein BindingAmino Acid SequenceMolecular BiologyMESH: Mice030304 developmental biologyMESH: In Vitro TechniquesMESH: Molecular Sequence DataMESH: HumansGeneral Immunology and MicrobiologyCadherinDyneinsMembrane ProteinsMESH: Macromolecular SubstancesMESH: MyosinsActin cytoskeleton[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/BacteriologyProtein Structure TertiaryMESH: Cell LineAlternative SplicingCytoskeletal ProteinsMutationsense organs030217 neurology & neurosurgeryalpha Catenin[SDV.MHEP]Life Sciences [q-bio]/Human health and pathologyMESH: Intercellular Junctions
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Mutation profile of the MYO7A gene in Spanish patients with Usher syndrome type I.

2006

Usher syndrome type I is the most severe form of Usher syndrome. It is an autosomal recessive disorder characterized by profound congenital sensorineural deafness, retinitis pigmentosa, and vestibular abnormalities. Mutations in the myosin VIIA gene (MYO7A) are responsible for Usher syndrome type 1B (USH1B). This gene is thought to bear greatest responsibility for USH1 and, depending on the study, has been reported to account for between 24% and 59% of USH1 cases. In this report a mutation screening of the MYO7A gene was carried out in a series of 48 unrelated USH1 families using single strand conformation polymorphism analysis (SSCP) and direct sequencing of those fragments showed an abnor…

MYO7AUsher syndromeDNA Mutational AnalysisBiologyMyosinsFrameshift mutationRetinitis pigmentosaotorhinolaryngologic diseasesGeneticsmedicineMissense mutationHumansGenetic Predisposition to DiseaseGeneGenetics (clinical)Polymorphism Single-Stranded ConformationalGeneticsPolymorphism GeneticModels GeneticDyneinsSingle-strand conformation polymorphismmedicine.diseaseeye diseasesStop codonGene Expression RegulationSpainMyosin VIIaMutationUsher SyndromesHuman mutation
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Functional analysis of splicing mutations in MYO7A and USH2A genes.

2010

Usher syndrome is defined by the association of sensorineural hearing loss, retinitis pigmentosa and variable vestibular dysfunction. Many disease-causative mutations have been identified in MYO7A and USH2A genes, which play a major role in Usher syndrome type I and type II, respectively. The pathogenic nature of mutations that lead to premature stop codons is not questioned; nevertheless, additional studies are needed to verify the pathogenicity of some changes such as those putatively involved in the splice process. Five putative splice-site variants were detected in our cohort of patients: c.2283-1G>T and c.5856G>A in MYO7A and c.1841-2A>G, c.2167+5G>A and c.5298+1G>C in the USH2A gene. …

MaleGenotypeUsher syndromeRNA SplicingBiologyMyosinsmedicine.disease_causeExonChlorocebus aethiopsGene OrderGeneticsmedicineotorhinolaryngologic diseasesAnimalsHumansspliceGeneGenetics (clinical)GeneticsMutationExtracellular Matrix Proteinsmedicine.diseaseStop codonMyosin VIIaRNA splicingCOS CellsMutationFemaleRNA Splice SitesUsher SyndromesMinigeneClinical genetics
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Novel slow-skeletal myosin (MYH7) mutation in the original myosin storage myopathy kindred

2006

Abstract Myosin storage myopathy (OMIM 608358), a congenital myopathy characterised by subsarcolemmal, hyaline-like accumulations of myosin in Type I muscle fibres, was first described by Cancilla and Colleagues in 1971 [Neurology 1971;21:579–585] in two siblings as ‘familial myopathy with probable lysis of myofibrils in type I muscle fibres'. Two mutations in the slow skeletal myosin heavy chain gene ( MYH7 ) have recently been associated with the disease in other families. We have identified a novel heterozygous Leu1793Pro mutation in MYH7 in DNA from paraffin sections of one of the original siblings. This historical molecular analysis confirms the original cases had myosin storage myopat…

MaleHeterozygotemacromolecular substancesMyosinsBiologymedicine.disease_causeMuscular DiseasesMyofibrilsMyosinmedicineHumansMyopathyGeneGenetics (clinical)GeneticsMutationMyosin Heavy ChainsMyosin storage myopathyDNAExonsmedicine.diseaseMolecular biologyCongenital myopathyMuscle Fibers Slow-TwitchNeurologyChild PreschoolMutationPediatrics Perinatology and Child HealthFemaleMYH7Neurology (clinical)medicine.symptomMyofibrilCardiac MyosinsNeuromuscular Disorders
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Identification of three novel mutations in the MYO7A gene

1999

Three new mutations in the myosin VIIA gene involved in the pathogenesis of Usher syndrome type Ib are reported. These mutations are K1080X in exon 25, E1170K in exon 28, and Y1719C in exon 37. It is presumed that these mutations are involved in the Usher syndrome Ib phenotype. Hum Mutat 14:181, 1999. Copyright 1999 Wiley-Liss, Inc.

MaleMYO7AHearing Loss SensorineuralUsher syndromeMyosinsBiologymedicine.disease_causeExonRetinitis pigmentosaMyosinotorhinolaryngologic diseasesGeneticsmedicineHumansGenePolymorphism Single-Stranded ConformationalGenetics (clinical)GeneticsMutationBase SequenceChromosomes Human Pair 11fungiDyneinsSyndromemedicine.diseasePhenotypeeye diseasesPedigreePhenotypeMyosin VIIaMutationFemaleRetinitis PigmentosaHuman Mutation
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Cytoskeletal features in longitudinal and circular smooth muscles during development of the rat portal vein.

1995

Immunohistochemistry of alpha-smooth muscle actin and desmin, two markers of smooth muscle cell differentiation, and electron-microscopic observation of thick filaments of myosin were performed on the media of the developing rat hepatic portal vein to gain insights into the chronology of differentiation of its longitudinal and circular smooth muscles. In accordance with the ultrastructural distribution of thin filaments, staining of alpha-smooth muscle actin is lightly positive in the myoblasts at postnatal day 1 and then extends in probably all muscle cells of the developing vessel. Desmin, which appears later than alpha-smooth muscle actin in the two muscles, is distributed throughout the…

MaleMyofilamentHistologySmooth muscle cell differentiationmacromolecular substancesActininBiologyMyosinsMuscle DevelopmentSarcomereMuscle Smooth VascularPathology and Forensic MedicineDesminMyosinMyocyteAnimalsRats WistarCytoskeletonPortal VeinGene Expression Regulation DevelopmentalCell BiologyAnatomyActinsRatsMicroscopy ElectronDesminFemaleMyofibrilCell and tissue research
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Detection of a novel Cys628STOP mutation of the myosin VIIA gene in Usher syndrome type Ib.

1998

A Spanish family with three Usher I syndrome-affected members was linked to markers located on chromosome 11q. A search for mutations on the myosin VIIA gene revealed a novel mutation (Cys628STOP) on exon 16 segregating with the disorder in a homozygous state. This nonsense mutation could be responsible for the disease since it leads to a truncated protein that presumably has no function.

MaleUsher syndromeNonsense mutationDNA Mutational AnalysisGenes RecessiveBiologyDeafnessMyosinsPolymerase Chain ReactionExonotorhinolaryngologic diseasesmedicineHumansCysteineMolecular BiologyGenePolymorphism Single-Stranded ConformationalGeneticsMyosin VIIaChromosomeDyneinsCell BiologyDNAExonsSyndromeMiddle Agedmedicine.diseasePedigreeMyosin VIIaMutation (genetic algorithm)MutationCodon TerminatorFemaleNovel mutationRetinitis PigmentosaMolecular and cellular probes
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Cytogenetic study of a spindle-cell rhabdomyosarcoma of the parotid gland.

1999

The cytogenetic analysis of a spindle-cell rhabdomyosarcoma of the parotid gland in a 6-year-old boy is reported. The tumor cells showed an abnormal karyotype with a hypotriploid modal chromosome number and clonal structural rearrangements affecting chromosomes 1, 8, 12, 21, and 22. The tumor karyotype was: 59, XY, -1, -3, -4, -5, -6, +8, +8, +del(8)(q22q24), -9, -10, del(12)(q13), -15, -16, -17, -18, der(21)t(12;21)(p11;p11), -22, der(22)t(1;22)(q12;p11).

Malecongenital hereditary and neonatal diseases and abnormalitiesCancer Researchmedicine.medical_specialtyPathologyTransplantation HeterologousMice NudeBiologyMyosinsDesminMiceRhabdomyosarcomaGeneticsmedicineAnimalsChromosomes HumanHumansVimentinRhabdomyosarcomaSpindle cell rhabdomyosarcomaChildMolecular BiologyChromosome AberrationsMyoglobinCytogeneticsKaryotypeModal Chromosome NumberAnatomymedicine.diseaseImmunohistochemistryActinsParotid glandParotid Neoplasmsmedicine.anatomical_structureKaryotypingImmunohistochemistrySarcomaNeoplasm TransplantationCancer genetics and cytogenetics
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Transmural distribution of biochemical markers of total protein and collagen synthesis, myocardial contraction speed and capillary density in the rat…

1988

The effect of angiotensin II-induced hypertension on selected biochemical parameters was studied in Sprague-Dawley rats. Angiotensin II infusion at rates of 41.7 micrograms h-1 kg-1 and 12.5 micrograms h-1 kg-1 for 2, 5, 10 and 15 days elevated the systolic blood pressure from 143 +/- 7 mmHg to 215-230 mmHg (P less than 0.001) and 185-195 mmHg (P less than 0.001), respectively. The left ventricular weight/body weight ratio increased 10-14% (P less than 0.05) and 23-32% (P less than 0.001) after 2-15 days in rats treated at the lower and higher infusion rates, respectively. Prolyl 4-hydroxylase (PH) activity, a marker of collagen synthesis, was evenly distributed in the left ventricle. PH ac…

Malemedicine.medical_specialtyContraction (grammar)PhysiologyHeart VentriclesPhenylalanineMyosinsContractilityHydroxyprolinechemistry.chemical_compoundInternal medicineRenin–angiotensin systemmedicineAnimalsAngiotensin IIRats Inbred StrainsAlkaline PhosphataseAngiotensin IIMyocardial ContractionCapillariesRatsHydroxyprolineBlood pressuremedicine.anatomical_structureEndocrinologychemistryVentricleProtein BiosynthesisHypertensionAlkaline phosphataseCollagenBiomarkersActa physiologica Scandinavica
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Paradoxically, iron overload does not potentiate doxorubicin-induced cardiotoxicity in vitro in cardiomyocytes and in vivo in mice

2015

Doxorubicin (DOX) is known to induce serious cardiotoxicity, which is believed to be mediated by oxidative stress and complex interactions with iron. However, the relationship between iron and DOX-induced cardiotoxicity remains controversial and the role of iron chelation therapy to prevent cardiotoxicity is called into question. Firstly, we evaluated in vitro the effects of DOX in combination with dextran-iron on cell viability in cultured H9c2 cardiomyocytes and EMT-6 cancer cells. Secondly, we used an in vivo murine model of iron overloading (IO) in which male C57BL/6 mice received a daily intra-peritoneal injection of dextran-iron (15mg/kg) for 3weeks (D0-D20) and then (D21) a single su…

Malemedicine.medical_specialtyIron OverloadCell SurvivalHeart VentriclesIronCardiomegaly030204 cardiovascular system & hematologyToxicologymedicine.disease_causeCell LineVentricular MyosinsMice03 medical and health sciences0302 clinical medicine[SDV.MHEP.CSC]Life Sciences [q-bio]/Human health and pathology/Cardiology and cardiovascular systemAtrial natriuretic peptideIn vivoCell Line TumorInternal medicineNatriuretic Peptide Brainpolycyclic compoundsmedicineAnimalsMyocytes CardiacDoxorubicinViability assay030304 developmental biologyPharmacology0303 health sciencesCardiotoxicityCell growthChemistryDextransBrain natriuretic peptideCardiotoxicity[SDV.MHEP.CSC] Life Sciences [q-bio]/Human health and pathology/Cardiology and cardiovascular systemUp-Regulation3. Good healthMice Inbred C57BLOxidative Stresscell proliferationEndocrinologyDoxorubicincardiovascular systemOxidative stressmedicine.drugToxicology and Applied Pharmacology
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