Search results for "contractile"

showing 10 items of 41 documents

In-frame deletion in the seventh immunoglobulin-like repeat of filamin C in a family with myofibrillar myopathy.

2009

Myofibrillar myopathies (MFMs) are an expanding and increasingly recognized group of neuromuscular disorders caused by mutations in DES, CRYAB, MYOT, and ZASP. The latest gene to be associated with MFM was FLNC; a p.W2710X mutation in the 24th immunoglobulin-like repeat of filamin C was shown to be the cause of a distinct type of MFM in several German families. We studied an International cohort of 46 patients from 39 families with clinically and myopathologically confirmed MFM, in which DES, CRYAB, MYOT, and ZASP mutations have been excluded. In patients from an unrelated family a 12-nucleotide deletion (c.2997_3008del) in FLNC resulting in a predicted in-frame four-residue deletion (p.Val…

MaleFilaminsDNA Mutational AnalysisImmunoblottingMolecular Sequence DataImmunoglobulinsmacromolecular substancesBiologymedicine.disease_causeFilaminArticle03 medical and health sciences0302 clinical medicineContractile ProteinsMuscular DiseasesMyofibrilsGeneticsmedicineHumansFLNCAmino Acid SequenceMyopathyRepeated sequenceMuscle SkeletalGenePeptide sequenceGenetics (clinical)030304 developmental biologyRepetitive Sequences Nucleic AcidSequence DeletionGeneticsFamily Health0303 health sciencesMutationSequence Homology Amino AcidMicrofilament Proteinsmedicine.diseaseMolecular biologyImmunohistochemistry3. Good healthMicroscopy ElectronMutationFemalemedicine.symptom030217 neurology & neurosurgeryLimb-girdle muscular dystrophyEuropean journal of human genetics : EJHG
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Effect of xanthine oxidase-generated extracellular superoxide on skeletal muscle force generation

2009

Skeletal muscle contractions increase superoxide anion in skeletal muscle extracellular space. We tested the hypotheses that 1) after an isometric contraction protocol, xanthine oxidase (XO) activity is a source of superoxide anion in the extracellular space of skeletal muscle and 2) the increase in XO-derived extracellular superoxide anion during contractions affects skeletal muscle contractile function. Superoxide anion was monitored in the extracellular space of mouse gastrocnemius muscles by following the reduction of cytochrome c in muscle microdialysates. A 15-min protocol of nondamaging isometric contractions increased the reduction of cytochrome c in microdialysates, indicating an …

MaleXanthine Oxidasemedicine.medical_specialtyPhysiologyOxypurinolfree radicalsSuperoxide dismutaseExtensor digitorum longus muscleMice03 medical and health sciencesGastrocnemius musclechemistry.chemical_compound0302 clinical medicineSuperoxidescontractile functionIsometric ContractionPhysiology (medical)Internal medicinemedicineAnimalsMuscle Skeletal030304 developmental biologySoleus muscle0303 health sciencesexercisebiologyMuscle fatigueSuperoxide DismutaseChemistrySuperoxideCytochromes cSkeletal muscleArticlesmusculoskeletal systemElectric StimulationMice Inbred C57BLmedicine.anatomical_structureEndocrinologyBiochemistryModels AnimalMuscle Fatiguebiology.proteinmedicine.symptomExtracellular Space030217 neurology & neurosurgeryMuscle ContractionMuscle contractionAmerican Journal of Physiology-Regulatory, Integrative and Comparative Physiology
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Effect of Divalent Cations on the Contractile Response of Rat Aorta to Depolarization before and after Nifedipine Treatment

1996

The influence of the divalent cations, Ca2+, Mg2+ and Ba2+, on the contractile response of the rat aorta to KCl and on the recovery of this response after nifedipine treatment was analyzed. KCl (80 mmol/l) promoted a two-phase (phasic and tonic) contractile response in Krebs solution but, as expected, no contractile response in Ca(2+)-free medium. In Mg(2+)-free medium, the phasic response to KCl was unaffected but the tonic one decreased slowly, suggesting that a long incubation time in the absence of Mg2+ (65 min) promotes a loss of or a change in the intracellular distribution of this ion that modifies Ca2+ entry through L channels or Ca2+ handling. Ba2+ (1.8 mmol/l) contracted the rat a…

Malemedicine.medical_specialtyNifedipineCations DivalentAorta ThoracicMuscle Smooth VascularPotassium ChlorideDivalentTonic (physiology)NifedipineInternal medicinemedicine.arterymedicineAnimalsRats WistarPharmacologychemistry.chemical_classificationAnalysis of VarianceAortaChemistryContractile responseDepolarizationGeneral MedicineCalcium Channel BlockersRatsEndocrinologyKrebs solutionIntracellularMuscle Contractionmedicine.drugPharmacology
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Effect of different treatments in calcium-free medium on basal tone and contractile responses of guinea pig tracheae.

1995

Acetylcholine (ACh; 0.1 mmol/l) and KCl (80 mmol/l) induce a biphasic contractile response in isolated guinea pig tracheae maintained at 37 degrees C either in the presence or absence of extracellular Ca2+. Exposure of the tissue to Ca(2+)-free solution evokes a significant decrease in basal tone and the sources of Ca2+ appear to be decreased by prolonged agonist stimulation, and even more by successive agonist stimulation. After an incubation period of 20 min in Ca(2+)-containing solution, the response is restored. Mg(2+)-depletion in Ca(2+)-free medium increased the contractile response to ACh, but not to KCl, and delayed the tonic component of the next contraction elicited in Ca(2+)-cont…

Malemedicine.medical_specialtyTime FactorsGuinea Pigschemistry.chemical_elementCalciumPotassium ChlorideGuinea pigBasal (phylogenetics)Tone (musical instrument)Organ Culture TechniquesInternal medicinemedicineExtracellularAnimalsMagnesiumPharmacologyIon TransportContractile responseMuscle SmoothGeneral MedicineFree mediumAcetylcholineTracheaCalcium Channel AgonistsEndocrinologychemistryCalciumAcetylcholinemedicine.drugMuscle ContractionPharmacology
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Assembly of a Filamin Four-domain Fragment and the Influence of Splicing Variant-1 on the Structure

2011

Filamins are scaffold proteins that bind to various proteins, including the actin cytoskeleton, integrin adhesion receptors, and adaptor proteins such as migfilin. Alternative splicing of filamin, largely constructed from 24 Ig-like domains, is thought to have a role in regulating its interactions with other proteins. The filamin A splice variant-1 (FLNa var-1) lacks 41 amino acids, including the last β-strand of domain 19, FLNa(19), and the first β-strand of FLNa(20) that was previously shown to mask a key binding site on FLNa(21). Here, we present a structural characterization of domains 18-21, FLNa(18-21), in the FLNa var-1 as well as its nonspliced counterpart. A model of nonspliced FLN…

Models MolecularFilaminsProtein domainBiologyFilaminBiochemistryProtein Structure SecondaryStructure-Activity RelationshipContractile ProteinsProtein structureHumansFLNANuclear Magnetic Resonance BiomolecularMolecular BiologyMicrofilament ProteinsAlternative splicingta1182Signal transducing adaptor proteinCell BiologyActin cytoskeletonMolecular biologyProtein Structure TertiaryCell biologyAlternative SplicingProtein Structure and FoldingRNA splicingJournal of Biological Chemistry
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Structural basis of the migfilin-filamin interaction and competition with integrin beta tails.

2008

A link between sites of cell adhesion and the cytoskeleton is essential for regulation of cell shape, motility, and signaling. Migfilin is a recently identified adaptor protein that localizes at cell-cell and cell-extracellular matrix adhesion sites, where it is thought to provide a link to the cytoskeleton by interacting with the actin cross-linking protein filamin. Here we have used x-ray crystallography, NMR spectroscopy, and protein-protein interaction studies to investigate the molecular basis of migfilin binding to filamin. We report that the N-terminal portion of migfilin can bind all three human filamins (FLNa, -b, or -c) and that there are multiple migfilin-binding sites in FLNa. H…

Models MolecularIntegrin beta ChainsMagnetic Resonance SpectroscopyFilaminsIntegrinMolecular ConformationPlasma protein bindingmacromolecular substancesBiologyFilaminLigandsBiochemistryMiceContractile ProteinsFLNAAnimalsHumansCytoskeletonCell adhesionMolecular BiologyActinCytoskeletonDose-Response Relationship DrugMicrofilament ProteinsMechanisms of Signal TransductionSignal transducing adaptor proteinCell BiologyCell biologyCytoskeletal Proteinsbiology.proteinNIH 3T3 CellsCell Adhesion MoleculesProtein BindingThe Journal of biological chemistry
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Structure of three tandem filamin domains reveals auto-inhibition of ligand binding

2007

Human filamins are large actin-crosslinking proteins composed of an N-terminal actin-binding domain followed by 24 Ig-like domains (IgFLNs), which interact with numerous transmembrane receptors and cytosolic signaling proteins. Here we report the 2.5 A resolution structure of a three-domain fragment of human filamin A (IgFLNa19-21). The structure reveals an unexpected domain arrangement, with IgFLNa20 partially unfolded bringing IgFLNa21 into close proximity to IgFLNa19. Notably the N-terminus of IgFLNa20 forms a beta-strand that associates with the CD face of IgFLNa21 and occupies the binding site for integrin adhesion receptors. Disruption of this IgFLNa20-IgFLNa21 interaction enhances fi…

Models MolecularIntegrinsanimal structuresintegrinFilaminsIntegrinmacromolecular substancesPlasma protein bindingLigandsFilaminBiochemistryArticleGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciencesFilamin bindingContractile ProteinsHumansBinding siteCell adhesionCytoskeletonMolecular BiologyX-ray crystallography030304 developmental biologyIntegrin binding0303 health sciencesGeneral Immunology and MicrobiologybiologyGeneral NeuroscienceMicrofilament Proteins030302 biochemistry & molecular biologycell adhesioncytoskeletonfilaminProtein Structure TertiaryCell biologybiology.proteinProtein BindingThe EMBO Journal
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Crystal Structure of Human Filamin C Domain 23 and Small Angle Scattering Model for Filamin C 23–24 Dimer

2007

Filamin C is a dimeric, actin-binding protein involved in organization of cortical cytoskeleton and of the sarcomere. We performed crystallographic, small-angle X-ray scattering and analytical ultracentrifugation experiments on the constructs containing carboxy-terminal domains of the protein (domains 23-24 and 19-21). The crystal structure of domain 23 of filamin C showed that the protein adopts the expected immunoglobulin (Ig)-like fold. Small-angle X-ray scattering experiments performed on filamin C tandem Ig-like domains 23 and 24 reveal a dimer that is formed by domain 24 and that domain 23 has little interactions with itself or with domain 24, while the analytical ultracentrifugation …

Models MolecularProtein FoldingFilaminsDimermacromolecular substancesCrystal structureCrystallography X-RayFilaminSarcomereAnalytical Ultracentrifugationchemistry.chemical_compoundContractile ProteinsNickelStructural BiologyScattering Small AngleHumansMolecular BiologyBinding SitesSmall-angle X-ray scatteringScatteringMicrofilament ProteinsProtein Structure TertiaryCrystallographychemistrySmall-angle scatteringDimerizationUltracentrifugationJournal of Molecular Biology
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The regulation mechanism for the auto-inhibition of binding of human filamin A to integrin.

2009

The ability of adhesion receptors to transmit biochemical signals and mechanical force across cell membranes depends on interactions with the actin cytoskeleton. Human filamins are large actin cross-linking proteins that connect integrins to the cytoskeleton. Filamin binding to the cytoplasmic tail of beta integrins has been shown to prevent integrin activation in cells, which is important for controlling cell adhesion and migration. The molecular-level mechanism for filamin binding to integrin has been unclear, however, as it was recently demonstrated that filamin undergoes intramolecular auto-inhibition of integrin binding. In this study, using steered molecular dynamics simulations, we f…

Models MolecularProtein Foldinganimal structuresIntegrin beta ChainsFilaminsmacromolecular substancesBiologyFilaminCD49cCollagen receptorFilamin bindingPhosphoserineContractile ProteinsStructural BiologyHumansPhosphorylationMolecular BiologyIntegrin bindingBinding SitesMicrofilament ProteinsActin cytoskeletonCell biologybody regionsIntegrin alpha Mbiology.proteinIntegrin beta 6Stress MechanicalPeptidesProtein BindingJournal of molecular biology
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β2 integrin phosphorylation on Thr758 acts as a molecular switch to regulate 14-3-3 and filamin binding

2008

AbstractLeukocyte integrins of the β2 family are essential for immune cell-cell adhesion. In activated cells, β2 integrins are phosphorylated on the cytoplasmic Thr758, leading to 14-3-3 protein recruitment to the β2 integrin. The mutation of this phosphorylation site impairs cell adhesion, actin reorganization, and cell spreading. Thr758 is contained in a Thr triplet of β2 that also mediates binding to filamin. Here, we investigated the binding of filamin, talin, and 14-3-3 proteins to phosphorylated and unphosphorylated β2 integrins by biochemical methods and x-ray crystallography. 14-3-3 proteins bound only to the phosphorylated integrin cytoplasmic peptide, with a high affinity (Kd, 261…

Models MolecularTalinThreonineanimal structuresFilaminsT-LymphocytesStatic ElectricityImmunologyIntegrinCD18macromolecular substancesPlasma protein bindingIn Vitro TechniquesFilaminBiochemistryJurkat Cells03 medical and health sciencesFilamin bindingContractile Proteins0302 clinical medicineCell AdhesionHumansProtein Interaction Domains and MotifsPhosphorylationCell adhesion030304 developmental biology0303 health sciencesBinding SitesbiologyChemistryMicrofilament ProteinsCell BiologyHematologyIntercellular Adhesion Molecule-1Talin bindingRecombinant ProteinsCell biology14-3-3 ProteinsAmino Acid SubstitutionCD18 AntigensMultiprotein Complexes030220 oncology & carcinogenesisbiology.proteinPhosphorylationProtein BindingBlood
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