Search results for "Myofilament"

showing 8 items of 8 documents

Myofilament function and body mass index.

2017

Body mass is reported to influence myocardial performance. Recent studies have emphasised the importance of negative inotropic adipocyte-derived factors and their impact on cardiac contractile function. However, the underlying mechanisms remain unclear. We aimed to determine whether body mass impacts cardiac force development on the level of the contractile apparatus. We examined the influence of body mass index (BMI) (3 groups: group I >25, group II 25–30, group III >30) on the myocardial performance of skinned muscle fibres. Right atrial tissue preparations of 70 patients undergoing aortocoronary bypass operation (CABG, 48 patients, group a) and aortic valve replacement (AVR, 22 patients,…

0301 basic medicineInotropeCardiac function curveMyofilamentmedicine.medical_specialtyobesitybody mass index030204 cardiovascular system & hematologyBiologyBioinformaticsGroup AcontractilityGeneral Biochemistry Genetics and Molecular BiologyContractility03 medical and health sciences0302 clinical medicineAortic valve replacementInternal medicinemedicineClinical significanceGeneral Pharmacology Toxicology and PharmaceuticsmyofilamentsGeneral Neuroscienceskinned fibersGeneral MedicineArticlesmedicine.disease030104 developmental biologyCardiologyBody mass indexBiomedical reports
researchProduct

Mutations in the skeletal muscle alpha-actin gene in patients with actin myopathy and nemaline myopathy

1999

Muscle contraction results from the force generated between the thin filament protein actin and the thick filament protein myosin, which causes the thick and thin muscle filaments to slide past each other. There are skeletal muscle, cardiac muscle, smooth muscle and non-muscle isoforms of both actin and myosin. Inherited diseases in humans have been associated with defects in cardiac actin (dilated cardiomyopathy and hypertrophic cardiomyopathy), cardiac myosin (hypertrophic cardiomyopathy) and non-muscle myosin (deafness). Here we report that mutations in the human skeletal muscle alpha-actin gene (ACTA1) are associated with two different muscle diseases, 'congenital myopathy with excess o…

AdultMalemedicine.medical_specialtyMyofilamentAdolescentDNA Mutational AnalysisMolecular Sequence Datamacromolecular substancesBiologyMyopathies NemalineTPM203 medical and health sciences0302 clinical medicineNemaline myopathyMuscular DiseasesInternal medicineMyosinGeneticsmedicineHumansPoint MutationAmino Acid SequenceChildMuscle SkeletalPolymorphism Single-Stranded ConformationalActin030304 developmental biologyFamily Health0303 health sciencesPolymorphism GeneticBase SequenceSequence Homology Amino AcidInfantSkeletal muscleDNASequence Analysis DNAmedicine.diseaseCongenital myopathyActins3. Good healthEndocrinologymedicine.anatomical_structureAmino Acid SubstitutionChild PreschoolMutationFemaleMYH7030217 neurology & neurosurgery
researchProduct

Actin-related myopathy without any missense mutation in the ACTA1 gene.

2004

Actinopathies are defined by missense mutations in the ACTA1 gene coding for sarcomeric actin, of which some 70 families have, so far, been identified. Often, but not always, muscle fibers carry large patches of actin filaments. Many such patients also have nemaline myopathy, qualifying actinopathies as a subgroup of nemaline myopathies. This article concerns a then newborn, now 21/2-year-old boy, the first and single child of nonconsanguineous parents, who was born floppy, requiring immediate postnatal assisted ventilation. A quadriceps muscle biopsy revealed large patches of thin myofilaments reacting at light and electron microscopic levels with antibodies against actin but only a few s…

MaleMyofilamentBiopsyDNA Mutational AnalysisMutation MissenseGene mutationBiologymedicine.disease_cause03 medical and health sciences0302 clinical medicineNemaline myopathyMuscular Diseases030225 pediatricsmedicineMissense mutationHumansPoint MutationMyopathyMuscle SkeletalActinMutationInfantmedicine.diseaseMolecular biologyCongenital myopathyActinsPediatrics Perinatology and Child HealthNeurology (clinical)medicine.symptom030217 neurology & neurosurgeryJournal of child neurology
researchProduct

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
researchProduct

Structure and closure mechanism of the human umbilical artery

1978

The structure of the fully-patent umbilical artery and rearrangement of its structural elements with postnatal closure were examined in 10 centimeter long umbilical cord segments which were double-clamped at different time intervals after delivery. The fully-patent umbilical artery consists of two main layers: an outer layer of circularly arranged smooth muscle cells and an inner layer which shows rather irregularly and loosely arranged cells embedded in abundant metachromatic ground substance. No predominantly longitudinal arrangements of cells and fibers reported by earlier investigators could be identified in the inner layer. Closure of the umbilical arteries is initiated by numerous loc…

MyofilamentGround substanceLumen (anatomy)Cell DifferentiationMuscle SmoothUmbilical arteryAnatomyBiologyUmbilical ArteriesLong umbilical cordlaw.inventionMicroscopy Electronmedicine.anatomical_structurelawmedicine.arteryPediatrics Perinatology and Child HealthmedicineHumansMyocyteElectron microscopeBlood vesselEuropean Journal of Pediatrics
researchProduct

Myogenesis and contraction in the early embryonic heart of the rainbow trout

1977

Myogenesis in the embryonic heart of the rainbow trout, Salmo galrdneri (Rich.), was investigated electron microscopically from the 29th to the 41st somite stage. Thick and thin myofilaments are formed simultaneously as well as precursors of Z-lines, to which the thin filaments are attached. The genesis of filaments takes place in the region around the intracellular yolk droplets. The first myofibrils appear by the 33rd somite stage, probably formed by a mechanism of self-assembly in which the binding sites of actin and myosin participate. A- and I-bands do not develop before the 38th somite stage. The contraction already begins during the 33rd somite stage in the middle of the tubular hear…

MyofilamentHistologyTubular heartEmbryonic heartmacromolecular substancesCell BiologyAnatomyBiologyPathology and Forensic MedicineCell biologySomitemedicine.anatomical_structureMyosinmedicineMyocyteMyofibrilActinCell and Tissue Research
researchProduct

DNA-fragmentation and expression of apoptosis-related proteins in muscular dystrophies

1997

Although numerous sarcolemmal protein defects in muscular dystrophies have been identified, the mechanisms linking these defects and muscle fibre degeneration are not fully characterized. As there is evidence that apoptosis is part of muscle fibre loss in dystrophin-deficient mdx-mice, apoptotic muscle fibre death may also play a role in humans with muscular dystrophies. We investigated in-situ DNA-fragmentation by the TUNEL-method and expression of apoptosis-related proteins immunohistochemically in 14 children suffering from deficiencies of dystrophin, adhalin, and merosin, and found TUNEL-positive chromatin-cleavage of muscle fibre nuclei in about 10% of non-necrotic muscle fibres. DNA-f…

MyofilamentPathologymedicine.medical_specialtyHistologySarcolemmabiologyMyogenesismedicine.diseasePathology and Forensic MedicineCell biologyNeurologyApoptosisPhysiology (medical)Gene expressionmedicinebiology.proteinNeurology (clinical)Muscular dystrophyITGA7DystrophinNeuropathology and Applied Neurobiology
researchProduct

M-cadherin and its sisters in development of striated muscle

1999

Cadherins are calcium-dependent, transmembrane intercellular adhesion proteins with morphoregulatory functions in the development and maintenance of tissues. In the development of striated muscle, the expression and function of mainly M-, N-, and R-cadherin has been studied so far. While these three cadherins are expressed in skeletal muscle cells, of these only N-cadherin is expressed in cardiac muscle. In this review, M-, N-, and R-cadherin are discussed as important players in the terminal differentiation and possibly also in the commitment of skeletal muscle cells. Furthermore, reports are described which evaluate the essential role of N-cadherin in the formation of heart tissue.

medicine.medical_specialtyMyofilamentHistologyBiologyMuscle DevelopmentSarcomerePathology and Forensic MedicineEmbryonic and Fetal DevelopmentMiceInternal medicineMyosinmedicineAnimalsHumansMyocyteMuscle SkeletalCardiac muscleGene Expression Regulation DevelopmentalSkeletal muscleCell DifferentiationHeartCell BiologyCadherinsCell biologyEndocrinologymedicine.anatomical_structureITGA7MyofibrilCell and Tissue Research
researchProduct