Search results for "Sarcolemma"

showing 10 items of 26 documents

Muscle follistatin gene delivery increases muscle protein synthesis independent of periodical physical inactivity and fasting

2020

Blocking of myostatin and activins effectively counteracts muscle atrophy. However, the potential interaction with physical inactivity and fasting in the regulation of muscle protein synthesis is poorly understood. We used blockade of myostatin and activins by recombinant adeno-associated virus (rAAV)-mediated follistatin (FS288) overexpression in mouse tibialis anterior muscle. To investigate the effects on muscle protein synthesis, muscles were collected 7 days after rAAV-injection in the nighttime or in the daytime representing high and low levels of activity and feeding, respectively, or after overnight fasting, refeeding, or ad libitum feeding. Muscle protein synthesis was increased by…

Male0301 basic medicineFollistatinMuscle Proteinsphysical activitylihaksetMyostatinBiochemistryMice0302 clinical medicineTibialis anterior musclemedia_common2. Zero hungerbiologyChemistryactivinsFastingDependovirusMuscle atrophyCircadian RhythmMuscular Atrophymyostatinmedicine.symptomfyysinen aktiivisuusBiotechnologymedicine.medical_specialtyfastingmedia_common.quotation_subjectMechanistic Target of Rapamycin Complex 1Gene delivery03 medical and health sciencesPhysical Conditioning AnimalInternal medicineGeneticsmedicineAnimalsMolecular BiologypaastoPI3K/AKT/mTOR pathwaysolufysiologiaSarcolemmaJNK Mitogen-Activated Protein Kinasesmechanistic target of rapamycin proteinAppetiteGenetic TherapyMice Inbred C57BL030104 developmental biologyEndocrinologybiology.protein1182 Biochemistry cell and molecular biology3111 BiomedicineproteiinitEnergy Metabolismlihassurkastumasairaudet030217 neurology & neurosurgeryFollistatin
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RELATIONSHIP BETWEEN THEOPHYLLINE UPTAKE AND INOTROPIC EFFECT IN THE GUINEA-PIG HEART

1974

1 The time course of the positive inotropic effect of theophylline was compared with the time course of the uptake and release of [(3)H]-theophylline in guinea-pig isolated, electrically driven hearts perfused by the Langendorff method.2 Formation of theophylline metabolites could not be detected under the experimental conditions used.3 Theophylline entered myocardial tissue very rapidly in two different phases. The first process (half-time 21 s) amounted to 93% and the second (half-time 5 min 50 s) to 7% of the total uptake. The development of the positive inotropic effect of theophylline was about four times faster than even the rapid component of the uptake of the drug into the myocardiu…

MaleInotropemedicine.medical_specialtyGuinea PigsStimulationIn Vitro TechniquesCalcium in biologychemistry.chemical_compoundTheophyllineCaffeineInternal medicinemedicineExtracellularAnimalsTheophyllinePharmacologySarcolemmaChemistryMyocardiumHeartCoronary VesselsElectric StimulationStimulation ChemicalPerfusionKineticsEndocrinologyDrug MechanismsFemaleCaffeinePerfusionmedicine.drugBritish Journal of Pharmacology
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Subcellular Localization of GLUT4 in Nonstimulated and Insulin-Stimulated Soleus Muscle of Rat

1992

Soleus muscles of fed rats were fixed by vascular perfusion with paraformaldehyde; individual fibers were teased and immunostained with a polyclonal antibody against the COOH-terminal of GLUT4. The binding sites were visualized by a horseradish peroxidase–coupled secondary antibody and diaminobenzidine. The fibers were embedded in epoxy resin and studied by electron microscopy. Strong immunoreactivity was found in subsarcolemmal clusters of vesicles and cisternae, Golgilike structures, and triadic junctions. Clusters of vesicles between myofibrils were occasionally stained. The plasma membrane was unlabeled. However, the plasma membrane was labeled when the rats had been injected with insul…

MaleMonosaccharide Transport ProteinsEndocrinology Diabetes and MetabolismGlucose uptakeCoated vesicleImmunoenzyme TechniquesCell membraneSarcolemmaInternal MedicinemedicineAnimalsInsulinSarcolemmabiologyMusclesVesicleCell MembraneRats Inbred StrainsRatsmedicine.anatomical_structureBiochemistrybiology.proteinBiophysicsMyofibrilGLUT4IntracellularDiabetes
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Endocytosis in skeletal muscle fibers.

1999

Defining the organization of endocytic pathway in multinucleated skeletal myofibers is crucial to understand the routing of membrane proteins, such as receptors and glucose transporters, through this system. Here we analyzed the organization of the endocytic trafficking pathways in isolated rat myofibers. We found that sarcolemmal-coated pits and transferrin receptors were concentrated in the I band areas. Fluid phase markers were taken up into vesicles in the same areas along the whole length of the fibers and were then delivered into structures around and between the nuclei. These markers also accumulated beneath the neuromuscular and myotendinous junctions. The recycling compartment, lab…

Monosaccharide Transport ProteinsEndosomeEndocytic cycleMuscle Fibers SkeletalFluorescent Antibody TechniqueGene ExpressionMuscle ProteinsTransferrin receptorEndosomesBiologyEndocytosisMicrotubulesSarcolemmaMicrotubuleReceptors TransferrinMyocyteAnimalsMuscle SkeletalCells Culturedchemistry.chemical_classificationGlucose Transporter Type 4Cell MembraneCoated Pits Cell-MembraneCell BiologyEndocytosisCell biologyCell CompartmentationRatsMicroscopy ElectronMembrane proteinchemistryTransferrinLysosomesExperimental cell research
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Homozygous mutations incaveolin-3cause a severe form of rippling muscle disease

2003

Heterozygous missense mutations in the caveolin-3 gene (CAV3) cause different muscle disorders. Most patients with CAV3 alterations present with rippling muscle disease (RMD) characterized by signs of increased muscle irritability without muscle weakness. In some patients, CAV3 mutations underlie the progressive limb-girdle muscular dystrophy type 1C (LGMD1C). Here, we report two unrelated patients with novel homozygous mutations (L86P and A92T) in CAV3. Both presented with a more severe clinical phenotype than usually seen in RMD. Immunohistochemical and immunoblot analyses of muscle biopsies showed a strong reduction of caveolin-3 in both homozygous RMD patients similar to the findings in…

MutationPathologymedicine.medical_specialtySarcolemmabiologyMuscle weaknessMuscle disordermedicine.disease_causemedicine.diseaseDysferlinCaveolin 3Neurologymedicinebiology.proteinMissense mutationNeurology (clinical)Muscular dystrophymedicine.symptomAnnals of Neurology
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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
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Muscle degeneration in neuramindase 1 deficient mice results from infiltration of the muscle fibers by expanded connective tissue

2010

AbstractNeuraminidase 1 (NEU1) regulates the catabolism of sialoglycoconjugates in lysosomes. Congenital NEU1 deficiency in children is the basis of sialidosis, a severe neurosomatic disorder in which patients experience a broad spectrum of clinical manifestations varying in the age of onset and severity. Osteoskeletal deformities and muscle hypotonia have been described in patients with sialidosis. Here we present the first comprehensive analysis of the skeletal muscle pathology associated with loss of Neu1 function in mice. In this animal model, skeletal muscles showed an expansion of the epimysial and perimysial spaces, associated with proliferation of fibroblast-like cells and abnormal …

Pathologymedicine.medical_specialtyMuscle HypotoniaMuscle Fibers SkeletalNeuraminidaseConnective tissueApoptosisNEU1BiologyArticleMiceNecrosisNEU1SarcolemmaCell MovementSettore BIO/10 - BiochimicamedicineAnimalsSialidosisMuscular dystrophyMyopathyMolecular BiologySialidosiMetalloproteinaseCell ProliferationMice KnockoutMuscle biopsySialidosisECMmedicine.diagnostic_testSkeletal muscleFibroblastsMuscular Dystrophy Animalmedicine.diseaseLysosomeExtracellular MatrixMuscular Atrophymedicine.anatomical_structureConnective TissueImmunologyMolecular MedicineMuscle biopsymedicine.symptom
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Desmin pathology in neuromuscular diseases

1993

Desmin is an intermediate filament protein that in striated muscle is normally located at Z-bands, beneath the sarcolemma, and prominently at neuromuscular junctions. It is abundant during myogenesis and in regenerating fibers, but decreases in amount with maturation; in regenerating and denervated muscle fibers it is co-expressed with vimentin. Aggregates of desmin occur as nonspecific cytoplasmic bodies or cytoplasmic spheroid complexes, similar to the aggregates of keratin filaments in Mallory bodies or the neurofilament aggregates in Lewy bodies. In all three instances, alpha-B crystallin may be associated with desmin. There are now increasing numbers of neuromuscular disorders in which…

Pathologymedicine.medical_specialtyNeurofilamentmacromolecular substancesDesminmedicineAnimalsHumansRegenerationIntermediate Filament ProteinMallory bodyMyopathyCytoskeletonSarcolemmabiologyMyogenesisChemistryMusclesNeuromuscular Diseasesmedicine.diseaseMuscle Denervationbiology.proteinDesminmedicine.symptomCardiomyopathiesDystrophinVirchows Archiv B Cell Pathology Including Molecular Pathology
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Filamin C accumulation is a strong but nonspecific immunohistochemical marker of core formation in muscle.

2002

Filamin C is the muscle isoform of a group of large actin-crosslinking proteins. On the one hand, filamin C is associated with the Z-disk of the myofibrillar apparatus and binds to myotilin; on the other hand, it interacts with the sarcoglycan complex at the sarcolemma. Filamin C may be involved in reorganizing the cytoskeleton in response to signalling events and in muscle it may, in addition, fulfill structural functions at the Z-disk. An examination of biopsies from patients with multi-minicore myopathy, central core myopathy and neurogenic target fibers with core-like target formations (TF) revealed strong reactivity of all the cores and target formations with two different anti-filamin…

Pathologymedicine.medical_specialtyanimal structuresBiopsyFilaminsmacromolecular substancesBiologyFilamin03 medical and health sciences0302 clinical medicineContractile ProteinsMuscular DiseasesReference ValuesmedicineMyotilinHumansProtein IsoformsCytoskeletonMyopathyMicroscopy ImmunoelectronMuscle Skeletal030304 developmental biology0303 health sciencesSarcolemmaMicrofilament Proteinsmedicine.diseaseImmunohistochemistryCell biologybody regionsNeurologyDesminNeurology (clinical)medicine.symptomMyofibrilCarrier Proteins030217 neurology & neurosurgeryCentral core diseaseBiomarkersJournal of the neurological sciences
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Primary desminopathies.

2007

•  Introduction •  Desmin is an essential component of the extrasarcomeric cytoskeleton in striated muscle cells •  Distal myopathy,cardiac arrhythmias,cardiomyopathy:classical criteria of primary desminopathies •  Sub-sarcolemmal and cytoplasmic desmin-positive protein aggregates:the morphological hallmark of primary and secondary desminopathies •  The spectrum of pathogenic desmin gene mutations •  The molecular pathogenesis of primary desminopathies: some answers gained,but even more questions raised •  Diagnostic work-up to distinguish primary from secondary desminopathies •  Treatment and clinical management of primary desminopathy patients Abstract Mutations of the human desmin gene o…

Pathologymedicine.medical_specialtyintermediate filamentsCardiomyopathyReviewsgranulofilamentous materialdesmininclusion bodiesmacromolecular substancesBiologymyofibrillar myopathyprotein aggregationdesmin-related myopathySarcolemmaMuscular DiseasesmedicineMyocyteAnimalsHumansIntermediate filamentMyopathyMuscle SkeletalCytoskeletonGenetic heterogeneityCardiac muscleCell Biologymedicine.diseasemusculoskeletal systemmutationsmedicine.anatomical_structuredesminopathyMutationMolecular MedicineDesminmedicine.symptomMyofibrilJournal of cellular and molecular medicine
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