Search results for "Sarcomeres"

showing 8 items of 8 documents

Acute change of titin at mid-sarcomere remains despite 8 wk of plyometric training

2014

Purpose: The purpose of this study was to investigate skeletal muscle changes induced by an acute bout of plyometric exercise (PlyEx) both before and after PlyEx training, to understand if titin is affected differently after PlyEx training. Methods: Healthy untrained individuals (N=11) completed the 1stPlyEx (10x10 squat-jumps, 1min rest). Thereafter, 6 subjects completed 8 weeks of PlyEx, while 5 controls abstained from any jumping activity. Seven days after the last training session all subjects completed the 2ndPlyEx. Blood samples were collected before, 6 hours and 1, 2, 3 and 4 days after each acute bout of PlyEx, and muscle biopsies 4 days before and 3 days after each acute bout of Pl…

AdultMaleSarcomeresmedicine.medical_specialtyPhysiologyZ-disk streaming acute bouts calpain eccentric exerciseMuscle ProteinsPlyometric ExerciseSarcomerePhysiology (medical)HumansMedicinePlyometricsConnectinTissue DistributionMuscle SkeletalExercisebiologySettore BIO/16 - Anatomia UmanaCalpainbusiness.industrySkeletal musclemusculoskeletal systemAdaptation Physiologicalmedicine.anatomical_structurebiology.proteinPhysical therapyFemaleTitinPlyometric trainingAutolysisbusinessMuscle ContractionJournal of Applied Physiology
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Ultrastructural pathology in emetine-induced myopathy

1988

Progressive myopathy developed in two women who consumed ipecac syrup containing emetine hydrochloride to induce vomiting as part of their anorexia nervosa. Muscle biopsy specimens were characterized by severe disruption of the sarcomeres. The ultrastructural spectrum extended from "Z-band streaming" to the formation of cytoplasmic bodies and also comprised abnormalities of the sarcotubular system, thus suggesting that muscle weakness may be related to both sarcomeric and sarcotubular lesions in this self-inflicted myopathy. It is tempting to suggest that muscle weakness may be correlated with or based on the pathology in sarcomeres and the sarcotubular system. As the myopathy is clinically…

AdultSarcomeresPathologymedicine.medical_specialtyAnorexia NervosaSubstance-Related DisordersEmetineEmetine HydrochlorideEmetineBiologySarcomereUltrastructural PathologyPathology and Forensic MedicineCellular and Molecular NeuroscienceMuscular DiseasesmedicineHumansMyopathyMuscle biopsymedicine.diagnostic_testMusclesMuscle weaknessMitochondriaSarcoplasmic ReticulumAnorexia nervosa (differential diagnoses)FemaleNeurology (clinical)medicine.symptommedicine.drugActa Neuropathologica
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Fetal akinesia caused by a novel actin filament aggregate myopathy skeletal muscle actin gene (ACTA1) mutation.

2010

We report a female newborn, diagnosed with fetal akinesia in utero, who died one hour after birth. Post-mortem muscle biopsy demonstrated actin-filament myopathy based on immunolabelling for sarcomeric actin, and large areas of filaments, without rod formation, ultrastructurally. Analysis of DNA extracted from the muscle disclosed a novel de novo heterozygous c.44G>A, GGC>GAC, 'p.Gly15Asp' mutation in the ACTA1 gene. Analysis of the location of the mutated amino-acid in the actin molecule suggests the mutation most likely causes abnormal nucleotide binding, and consequent pathological actin polymerization. This case emphasizes the association of fetal akinesia with actin-filament myopathy.

AdultSarcomeresmacromolecular substancesBiologymedicine.disease_causeSarcomereNemaline myopathyPregnancymedicineHumansMyopathyMuscle SkeletalGenetics (clinical)ActinMutationMuscle biopsymedicine.diagnostic_testMicrofilament ProteinsInfant NewbornSkeletal muscleDNANeuromuscular DiseasesActin cytoskeletonmedicine.diseaseMolecular biologyActin CytoskeletonFetal Diseasesmedicine.anatomical_structureNeurologyBiochemistryPediatrics Perinatology and Child HealthMutationFemaleNeurology (clinical)medicine.symptomNeuromuscular disorders : NMD
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Deleting Full Length Titin Versus the Titin M-Band Region Leads to Differential Mechanosignaling and Cardiac Phenotypes

2019

Background: Titin is a giant elastic protein that spans the half-sarcomere from Z-disk to M-band. It acts as a molecular spring and mechanosensor and has been linked to striated muscle disease. The pathways that govern titin-dependent cardiac growth and contribute to disease are diverse and difficult to dissect. Methods: To study titin deficiency versus dysfunction, the authors generated and compared striated muscle specific knockouts (KOs) with progressive postnatal loss of the complete titin protein by removing exon 2 (E2-KO) or an M-band truncation that eliminates proper sarcomeric integration, but retains all other functional domains (M-band exon 1/2 [M1/2]-KO). The authors evaluated c…

Cardiomyopathy DilatedMaleSarcomeresanimal structuresVentricular Dysfunction Rightmacromolecular substances030204 cardiovascular system & hematologyMechanotransduction CellularVentricular Function LeftArticleMuscle hypertrophyVentricular Dysfunction Left03 medical and health sciences0302 clinical medicinePhysiology (medical)AnimalsMedicineMyocytes CardiacMuscle Skeletal030304 developmental biologyMice Knockout0303 health sciencesbiologybusiness.industryMolecular springmusculoskeletal systemPhenotypeCell biologyMuscular AtrophyPhenotypeMuscle diseasecardiovascular systemVentricular Function Rightbiology.proteinTitinCardiology and Cardiovascular MedicinebusinessProtein KinasesGene DeletionDifferential (mathematics)Circulation
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Arsenic trioxide alters the differentiation of mouse embryonic stem cell into cardiomyocytes

2015

AbstractChronic arsenic exposure is associated with increased morbidity and mortality for cardiovascular diseases. Arsenic increases myocardial infarction mortality in young adulthood, suggesting that exposure during foetal life correlates with cardiac alterations emerging later. Here, we investigated the mechanisms of arsenic trioxide (ATO) cardiomyocytes disruption during their differentiation from mouse embryonic stem cells. Throughout 15 days of differentiation in the presence of ATO (0.1, 0.5, 1.0 μM) we analysed: the expression of i) marker genes of mesoderm (day 4), myofibrillogenic commitment (day 7) and post-natal-like cardiomyocytes (day 15); ii) sarcomeric proteins and their orga…

Fetal ProteinsSarcomeresMesodermTime FactorsCellular differentiationBlotting WesternConnexinFluorescent Antibody TechniqueGene ExpressionAntineoplastic AgentsActininBiologyArticleArsenicalsCell Linechemistry.chemical_compoundMiceArsenic TrioxideTroponin TSpheroids CellularGene expressionmedicineAnimalsActininMyocytes CardiacArsenic trioxideHomeodomain ProteinsSyncytiumMultidisciplinaryReverse Transcriptase Polymerase Chain ReactionCell DifferentiationMouse Embryonic Stem CellsOxidesEmbryonic stem cellCell biologyBiomechanical PhenomenaGATA4 Transcription Factormedicine.anatomical_structurechemistryConnexin 43ImmunologyHomeobox Protein Nkx-2.5T-Box Domain ProteinsTroponin CTranscription FactorsScientific Reports
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Zasp/Cypher internal ZM-motif containing fragments are sufficient to co-localize with α-actinin—Analysis of patient mutations

2005

Z-band alternatively spliced PDZ-containing protein (ZASP/Cypher) has an important role in maintaining Z-disc stability in striated and cardiac muscle. ZASP/Cypher interacts through its PDZ domain with the major Z-disc actin cross-linker, alpha-actinin. ZASP/Cypher also has a conserved sequence called the ZM-motif, and it is found in two alternatively spliced exons 4 and 6. We have shown earlier that the ZM-motif containing internal regions of two related proteins ALP and CLP36 interact with alpha-actinin rod region, and that the ZM-motif is important in targeting ALP to the alpha-actinin containing structures in cell. Here, we show that the ZASP/Cypher internal fragments containing either …

SarcomeresAmino Acid MotifsPDZ domainCHO Cellsmacromolecular substancesBiologyConserved sequenceStress fiber assemblyMyoblastsMiceExonCricetinaeStress FibersmedicineAnimalsHumansMyocyteActininMuscle SkeletalActinAdaptor Proteins Signal TransducingOrganellesGeneticsMyocardiumPoint mutationCardiac muscleExonsIntracellular MembranesCell BiologyLIM Domain Proteinsmusculoskeletal systemPeptide FragmentsCell biologymedicine.anatomical_structureMutationCardiomyopathiesProtein BindingExperimental Cell Research
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Silk fibroin scaffolds enhance cell commitment of adult rat cardiac progenitor cells.

2015

The use of three-dimensional (3D) cultures may induce cardiac progenitor cells to synthesize their own extracellular matrix (ECM) and sarcomeric proteins to initiate cardiac differentiation. 3D cultures grown on synthetic scaffolds may favour the implantation and survival of stem cells for cell therapy when pharmacological therapies are not efficient in curing cardiovascular diseases and when organ transplantation remains the only treatment able to rescue the patient’s life. Silk fibroin-based scaffolds may be used to increase cell affinity to biomaterials and may be chemically modified to improve cell adhesion. In the present study, porous, partially orientated and electrospun nanometric n…

Sarcomeresprogenitor cellCell SurvivalCell Culture TechniquesBiocompatible MaterialsReal-Time Polymerase Chain ReactionZ-bodieMicroscopy Electron TransmissionCell AdhesionElectrochemistryAnimalsConnectinnatural polymermyocardial tissue; progenitor cells; Z-bodies; tissue engineering; natural polymers; silk fibroinTissue EngineeringTissue ScaffoldsMyocardiumStem CellsWaterCell Differentiationmyocardial tissueBombyxFlow CytometryExtracellular MatrixRatssilk fibroinMicroscopy Electron ScanningCollagenFibroinsPorosityJournal of tissue engineering and regenerative medicine
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Muscleblind, BSF and TBPH are mislocalized in the muscle sarcomere of a Drosophila myotonic dystrophy model

2012

SummaryMyotonic dystrophy type 1 (DM1) is a genetic disease caused by the pathological expansion of a CTG trinucleotide repeat in the 3' UTR of the DMPK gene. In the DMPK transcripts, the CUG expansions sequester RNA-binding proteins into nuclear foci, including transcription factors and alternative splicing regulators such as MBNL1. MBNL1 sequestration has been associated with key features of DM1. However, the basis behind a number of molecular and histological alterations in DM1 remain unclear. To help identify new pathogenic components of the disease, we carried out a genetic screen using a Drosophila model of DM1 that expresses 480 interrupted CTG repeats, i(CTG)480, and a collection of…

musculoskeletal diseasesSarcomerescongenital hereditary and neonatal diseases and abnormalitiesNeuroscience (miscellaneous)lcsh:MedicineMedicine (miscellaneous)RNA-binding proteinGenes InsectBiologyMyotonic dystrophyGeneral Biochemistry Genetics and Molecular BiologyAnimals Genetically Modifiedchemistry.chemical_compoundImmunology and Microbiology (miscellaneous)RNA interferencelcsh:PathologymedicineMBNL1AnimalsDrosophila ProteinsHumansMyotonic DystrophyGeneticsMuscleslcsh:RAlternative splicingNuclear ProteinsRNA-Binding ProteinsEpistasis Geneticmedicine.diseaseDisease Models AnimalchemistryGene Knockdown TechniquesDrosophilaFemaleRNA InterferenceTrinucleotide repeat expansionTrinucleotide Repeat ExpansionDrosophila Proteinlcsh:RB1-214Genetic screenResearch ArticleDisease Models & Mechanisms
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