Search results for "Muscle proteins"

showing 10 items of 76 documents

Genotype-phenotype correlations in nemaline myopathy caused by mutations in the genes for nebulin and skeletal muscle alpha-actin.

2003

We present comparisons of the clinical pictures in a series of 60 patients with nemaline myopathy in whom mutations had been identified in the genes for nebulin or skeletal muscle alpha-actin. In the patients with nebulin mutations, the typical form of nemaline myopathy predominated, while severe, mild or intermediate forms were less frequent. Autosomal recessive inheritance had been verified or appeared likely in all nebulin cases. In the patients with actin mutations, the severe form of nemaline myopathy was the most common, but some had the mild or typical form, and a few showed other associated features such as intranuclear rods or actin accumulation. Most cases were sporadic, but in ad…

AdultMalePathologymedicine.medical_specialtyAdolescentGenotypeNonsense mutationDNA Mutational AnalysisMuscle ProteinsBiologymedicine.disease_causeMyopathies Nemaline03 medical and health sciencesNebulin0302 clinical medicineNemaline myopathyGenotypemedicineHumansChildMuscle SkeletalGenetics (clinical)Actin030304 developmental biologyGenetics0303 health sciencesMutationInfantmedicine.diseaseCongenital myopathyPhenotypeActinsPhenotypeNeurologyChild PreschoolPediatrics Perinatology and Child HealthMutationbiology.proteinFemaleNeurology (clinical)030217 neurology & neurosurgeryNeuromuscular disorders : NMD
researchProduct

Direct interaction of the Usher syndrome 1G protein SANS and myomegalin in the retina

2011

Contains fulltext : 96822.pdf (Publisher’s version ) (Closed access) The human Usher syndrome (USH) is the most frequent cause of combined hereditary deaf-blindness. USH is genetically heterogeneous with at least 11 chromosomal loci assigned to 3 clinical types, USH1-3. We have previously demonstrated that all USH1 and 2 proteins in the eye and the inner ear are organized into protein networks by scaffold proteins. This has contributed essentially to our current understanding of the function of USH proteins and explains why defects in proteins of different families cause very similar phenotypes. We have previously shown that the USH1G protein SANS (scaffold protein containing ankyrin repeat…

Scaffold proteinUsher syndromePhosphodiesterase 4D interacting protein (PDE4DIP)Muscle ProteinsPlasma protein bindingMice0302 clinical medicineYeastsChlorocebus aethiopsNuclear proteinCells CulturedGenetics0303 health scienceseducation.field_of_studyNuclear ProteinsCell biologyCOS CellssymbolsPhotoreceptor Cells VertebrateProtein BindingMicrotubule based transportNerve Tissue ProteinsBiologyModels BiologicalRetina03 medical and health sciencessymbols.namesakemedicineAnimalsHumanseducationMolecular BiologyAdaptor Proteins Signal Transducing030304 developmental biologyCell BiologyGlycostation disorders [IGMD 4]Golgi apparatusmedicine.diseaseMacaca mulattaMice Inbred C57BLCytoskeletal ProteinsPhotoreceptor cell functionMyomegalinGenetics and epigenetic pathways of disease Functional Neurogenomics [NCMLS 6]CattleAnkyrin repeatCiliary baseIntracellular transport030217 neurology & neurosurgerySensorineuronal degeneration
researchProduct

Diagnostic immunohistochemistry in neuromuscular disorders.

2005

Most neuromuscular disorders display only non-specific myopathological features in routine histological preparations. However, a number of proteins, including sarcolemmal, sarcomeric, and nuclear proteins as well as enzymes with defects responsible for neuromuscular disorders, have been identified during the past two decades, allowing a more specific and firm diagnosis of muscle diseases. Identification of protein defects relies predominantly on immunohistochemical preparations and on Western blot analysis. While immunohistochemistry is very useful in identifying abnormal expression of primary protein abnormalities in recessive conditions, it is less helpful in detecting primary defects in …

Denervationmedicine.medical_specialtyPathologyHistologymedicine.diagnostic_testCell adhesion moleculeBlotting WesternMuscle Fibers SkeletalMuscle ProteinsAnatomical pathologyGeneral MedicineNeuromuscular DiseasesBiologyImmunohistochemistryPathology and Forensic MedicineBlotWestern blotmedicineImmunohistochemistryAnimalsHumansMuscle fibreNuclear proteinForecastingHistopathology
researchProduct

Neuromuscular electrical stimulation training induces atypical adaptations of the human skeletal muscle phenotype: a functional and proteomic analysis

2011

Import JabRef | WosArea Physiology; Sport Sciences; International audience; The aim of the present study was to define the chronic effects of neuromuscular electrical stimulation (NMES) on the neuromuscular properties of human skeletal muscle. Eight young healthy male subjects were subjected to 25 sessions of isometric NMES of the quadriceps muscle over an 8-wk period. Needle biopsies were taken from the vastus lateralis muscle before and after training. The training status, myosin heavy chain (MHC) isoform distribution, and global protein pattern, as assessed by proteomic analysis, widely varied among subjects at baseline and prompted the identification of two subgroups: an "active" (ACT) …

AdultMalemedicine.medical_specialtyPathologyProteomePhysiologyVastus lateralis muscleCHAIN ISOFORMMuscle ProteinsElectric Stimulation TherapyStimulationIsometric exerciseBiologyOBSTRUCTIVE PULMONARY-DISEASEMuscle hypertrophy03 medical and health sciences0302 clinical medicineSTRIATED-MUSCLEIsometric ContractionPhysiology (medical)Internal medicineMyosinmedicineHumansHEAT-SHOCK PROTEINSOXIDATIVE STRESSMuscle SkeletalRESISTANCE EXERCISE030304 developmental biologyCLUSTER-ANALYSISALPHA-ACTIN0303 health sciences[SCCO.NEUR]Cognitive science/Neuroscience[SCCO.NEUR] Cognitive science/NeuroscienceSkeletal muscleMYOFIBER HYPERTROPHYAdaptation PhysiologicalPhenotypeEndocrinologymedicine.anatomical_structureMotor unit recruitment[ SCCO.NEUR ] Cognitive science/NeuroscienceFIBER CONTRACTILE PROPERTIESMyofibril030217 neurology & neurosurgery
researchProduct

Desmin-related neuromuscular disorders

1995

Desmin, the intermediate filament protein of skeletal muscle fibers, cardiac myocytes, and certain smooth muscle cells, is a member of the cytoskeleton linking Z-bands with the plasmalemma and the nucleus. The pathology of desmin in human neuromuscular disorders is always marked by increased amounts, diffusely or focally. Desmin is highly expressed in immature muscle fibers, both during fetal life and regeneration as well as in certain congenital myopathies, together with vimentin. Desmin is also enriched in neonatal myotonic dystrophy and small fibers in infantile spinal muscular atrophy. Focal accretion of desmin may be twofold, in conjunction with certain inclusion bodies, cytoplasmic an…

Pathologymedicine.medical_specialtyPhysiologyIntermediate FilamentsMuscle ProteinsVimentinmacromolecular substancesDesminCellular and Molecular NeuroscienceMuscular DiseasesPhysiology (medical)medicineHumansMyocyteIntermediate Filament ProteinMuscle SkeletalMyopathyIntermediate filamentActinInclusion BodiesbiologyNeuromuscular Diseasesbiology.proteinDesminNeurology (clinical)medicine.symptomDystrophinMuscle & Nerve
researchProduct

Heterozygous nonsense SCN5A mutation W822X explains a simultaneous sudden infant death syndrome.

2008

The sudden, unexpected, and unexplained death of both members of a set of healthy twins (simultaneous sudden infant death syndrome (SSIDS)) is defined as a case in which both infants meet the definition of sudden infant death syndrome individually. A search of the world medical literature resulted in only 42 reported cases of SSIDS. We report the case of a pair of identical, male, monozygotic twins, 138 days old, who suddenly died, meeting the full criteria of SSIDS and where a genetic screen was performed, resulting in a heterozygous nonsense SCN5A mutation (W822X) in both twins. Immunohistochemistry was performed on cardiac tissue samples utilizing polyclonal antibodies anti-Na+ CP type V…

MalePathologymedicine.medical_specialtyNav1.5 protein functionv1.5 protein functionmedia_common.quotation_subject2734Nonsense mutationNonsenseNa+ channel functionMuscle ProteinsSocio-culturaleBiology+Nav1.5 protein function; Na+ channel function; SCN5A gene mutation; Simultaneous sudden infant death syndrome; W822X mutation; Codon Nonsense; Diseases in Twins; Humans; Infant; Male; Muscle Proteins; NAV1.5 Voltage-Gated Sodium Channel; Sodium Channels; Sudden Infant Death; 2734Sudden deathSodium ChannelsNAV1.5 Voltage-Gated Sodium ChannelPathology and Forensic MedicinePathogenesisSCN5A gene mutationDiseases in TwinsmedicineHumansSimultaneous sudden infant death syndromeSCN5A gene mutationW822X mutationNa+ channel functionNav1.5 protein functionNaSimultaneous sudden infant death syndrome SCN5A gene mutation W822X mutation Na+ channel function Nav1.5 protein function CodonMolecular BiologyCellular localizationmedia_commonSimultaneous sudden infant death syndromeSettore BIO/16 - Anatomia UmanaSimultaneous sudden infant death syndrome SCN5A gene mutation W822X mutation Na+ channel function Nav1.5 protein functionW822X mutationInfantCell BiologyGeneral MedicineSudden infant death syndromeNonsenseTerminal deoxynucleotidyl transferaseCodon NonsenseImmunohistochemistryNa; v; 1.5 protein function; Na; +; channel function; SCN5A gene mutation; Simultaneous sudden infant death syndrome; W822X mutationchannel functionSudden Infant Death
researchProduct

Reduction of mdx mouse muscle degeneration by low-intensity endurance exercise: a proteomic analysis in quadriceps muscle of exercised versus sedenta…

2015

By proteomic analysis we found an up-regulation of four carbonic anhydrase-3 (CA3) isoforms and a down-regulation of superoxide dismutase [Cu-Zn] (SODC) in quadriceps of sedentary X-linked muscular dystrophy (mdx) mice as compared with wild–type (WT) mice and the levels were significantly restored to WT values following low-intensity endurance exercise.

MaleProteomicsmuscular dystrophymdx mousemedicine.medical_specialtycarbonic anhydrase exercise mdx muscle oxidative stress muscle proteomic muscular dystrophyBlotting Westerncarbonic anhydraseBiophysicsMuscle Proteinsmedicine.disease_causeBiochemistryQuadriceps Musclemuscle proteomicSuperoxide dismutaseWestern blotEndurance trainingInternal medicinemedicineAnimalsoxidative stressElectrophoresis Gel Two-DimensionalMuscular dystrophyMolecular BiologyOriginal Paperexercisebiologymedicine.diagnostic_testSuperoxide Dismutasebusiness.industryReproducibility of ResultsSkeletal muscleCell Biologymedicine.diseaseOriginal PapersCarbonic Anhydrase IIIMice Inbred C57BLMuscular Dystrophy Duchennemedicine.anatomical_structureEndocrinologyX-linked muscular dystrophy (mdx)carbonic anhydrase; oxidative stress; muscle proteomicMice Inbred mdxPhysical Endurancebiology.proteinCarbonic anhydrase 3businessmuscle oxidative stressOxidative stress
researchProduct

Characterization of a Ryanodine Receptor inPeriplaneta Americana

1997

Specific binding sites for the alkaloid ryanodine were characterized in membrane preparations from sarcoplasmatic reticulum of Periplaneta americana skeletal muscle. Binding of [3H]ryanodine was optimal at pH 8 and at CaCl2 concentration of about 300 mumol l-1. The Ca-chelating agents EGTA (100 mumol l-1) and EDTA (100 mumol l-1) abolished 95% and 90% of the [3H]ryanodine binding respectively. Preincubation with Ca2+ (100 mumol l-1) restored the ryanodine binding in presence of up to 300 mumol l-1 EGTA. Radioligand binding experiments showed one class of high affinity binding sites for ryanodine. Determination of rate constants revealed 7.05 x 10(6) l mol-1 min-1 for associating and 3.77 x …

Maleanimal structuresMuscle ProteinsBiochemistrymedicineAnimalsPeriplanetaheterocyclic compoundsBinding siteEgtazic AcidMolecular BiologyEdetic AcidbiologyRyanodineRyanodine receptorChemistryMusclesAlkaloidSodiumfungiSkeletal muscleRyanodine Receptor Calcium Release ChannelCell BiologyHydrogen-Ion Concentrationbiology.organism_classificationmedicine.anatomical_structureBiochemistryPotassiumCalciumCalmodulin-Binding ProteinsFemaleCalcium ChannelsReticulumPeriplanetaJournal of Receptors and Signal Transduction
researchProduct

Label-free profiling of skeletal muscle using high-definition mass spectrometry

2014

We report automated and time efficient (2 h per sample) profiling of muscle using ultra-performance liquid chromatography (LC) coupled directly with high-definition mass spectrometry (HDMSE). Soluble proteins extracted from rat gastrocnemius (n=10) were digested with trypsin and analysed in duplicate using a 90 min RPLC gradient. Protein identification and label-free quantitation were performed from HDMSE spectra analysed using TransOmics Informatics for Proteomics software. In total 1,514 proteins were identified. Of these, 811 had at least 3 unique peptides and were subsequently used to assess the dynamic range and precision of LC-HDMSE label-free profiling. Proteins analysed by LC-HDMSE …

ProteomicsMuscle Proteinsta3111ProteomicsMass spectrometryBiochemistryArticleMass Spectrometryion mobilityLiquid chromatography–mass spectrometryanimal proteomicsdata-independent acquisitionmedicineAnimalsData-independent acquisitionMuscle Skeletalta315Molecular Biologychemistry.chemical_classificationChromatographyta1184Skeletal muscleTricarboxylic acidTrypsinRatsLC-MSEnzymemedicine.anatomical_structurechemistryBiochemistryChromatography Liquidmedicine.drugPROTEOMICS
researchProduct

Proteomic identification of FHL1 as the protein mutated in human reducing body myopathy

2007

Reducing body myopathy (RBM) is a rare disorder causing progressive muscular weakness characterized by aggresome-like inclusions in the myofibrils. Identification of genes responsible for RBM by traditional genetic approaches has been impossible due to the frequently sporadic occurrence in affected patients and small family sizes. As an alternative approach to gene identification, we used laser microdissection of intracytoplasmic inclusions identified in patient muscle biopsies, followed by nanoflow liquid chromatography-tandem mass spectrometry and proteomic analysis. The most prominent component of the inclusions was the Xq26.3-encoded four and a half LIM domain 1 (FHL1) protein, expresse…

Models MolecularProteomicsMolecular Sequence DataMuscle ProteinsBiologyTransfectionProteomicsInclusion bodiesMuscular DiseasesmedicineAmino Acid SequenceLaser capture microdissectionInclusion BodiesIntracellular Signaling Peptides and ProteinsCardiac muscleSkeletal muscleGenetic Diseases X-LinkedGeneral MedicineLIM Domain Proteinsmedicine.diseaseCongenital myopathyMolecular biologyFHL1medicine.anatomical_structureMutationMyofibrilResearch Article
researchProduct