Search results for "contractile"

showing 10 items of 41 documents

Atomic Structures of Two Novel Immunoglobulin-like Domain Pairs in the Actin Cross-linking Protein Filamin

2009

Filamins are actin filament cross-linking proteins composed of an N-terminal actin-binding domain and 24 immunoglobulin-like domains (IgFLNs). Filamins interact with numerous proteins, including the cytoplasmic domains of plasma membrane signaling and cell adhesion receptors. Thereby filamins mechanically and functionally link the cell membrane to the cytoskeleton. Most of the interactions have been mapped to the C-terminal IgFLNs 16–24. Similarly, as with the previously known compact domain pair of IgFLNa20–21, the two-domain fragments IgFLNa16–17 and IgFLNa18–19 were more compact in small angle x-ray scattering analysis than would be expected for two independent domains. Solution state NM…

EGF-like domainFilaminsMolecular Sequence DataMolecular ConformationImmunoglobulinsmacromolecular substancesPlasma protein bindingBiologyFilaminModels BiologicalBiochemistryCell membraneHAMP domain03 medical and health sciencesContractile Proteins0302 clinical medicineddc:570Cell AdhesionmedicineHumansScattering RadiationAmino Acid SequenceCytoskeletonCell adhesionMolecular BiologyCytoskeletonActin030304 developmental biology0303 health sciencesMicrofilament ProteinsCell BiologyActinsRecombinant ProteinsProtein Structure Tertiary3. Good healthCell biologyCross-Linking Reagentsmedicine.anatomical_structureProtein Structure and Folding030217 neurology & neurosurgeryProtein BindingJournal of Biological Chemistry
researchProduct

Dynamic force sensing of filamin revealed in single-molecule experiments

2012

Mechanical forces are important signals for cell response and development, but detailed molecular mechanisms of force sensing are largely unexplored. The cytoskeletal protein filamin is a key connecting element between the cytoskeleton and transmembrane complexes such as integrins or the von Willebrand receptor glycoprotein Ib. Here, we show using single-molecule mechanical measurements that the recently reported Ig domain pair 20–21 of human filamin A acts as an autoinhibited force-activatable mechanosensor. We developed a mechanical single-molecule competition assay that allows online observation of binding events of target peptides in solution to the strained domain pair. We find that fi…

Filaminsta221IntegrinPlasma protein bindingImmunoglobulin domainactin-binding proteinta3111LigandsFilaminoptical tweezerContractile ProteinsHumansCytoskeletonMultidisciplinarybiologyChemistryMicrofilament Proteinsta1182Microfilament ProteinBiological SciencesfilaminTransmembrane proteinCell biologyOptical tweezersbiology.proteinmechanosensingProtein Binding
researchProduct

Model of a six immunoglobulin-like domain fragment of filamin A (16-21) built using residual dipolar couplings.

2012

Filamins are actin-binding proteins that participate in a wide range of cell functions, including cell morphology, locomotion, membrane protein localization, and intracellular signaling. The three filamin isoforms found in humans, filamins A, B, and C, are highly homologous, and their roles are partly complementary. In addition to actin, filamins interact with dozens of other proteins that have roles as membrane receptors and channels, enzymes, signaling intermediates, and transcription factors. Filamins are composed of an N-terminal actin-binding domain and 24 filamin-type immunoglobulin-like domains (FLN) that form tail-to-tail dimers with their C-terminal FLN domain. Many of the filamin …

Gene isoformModels Molecularanimal structuresMagnetic Resonance SpectroscopyProtein ConformationFilaminsIntegrinBiomolecular structuremacromolecular substances010402 general chemistryFilaminCell morphologyCrystallography X-Ray01 natural sciencesBiochemistryCatalysis03 medical and health sciencesColloid and Surface ChemistryContractile ProteinsHumansTranscription factorImmunoglobulin FragmentsActin030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyChemistryMicrofilament ProteinsGeneral Chemistry0104 chemical sciencesCell biologybody regionsbiology.proteinGlycoproteinJournal of the American Chemical Society
researchProduct

Role of cyclic nucleotide phosphodiesterase isoenzymes in contractile responses of denuded rat aorta related to various Ca 2+ sources

2001

We have examined the cyclic nucleotide phosphodiesterase isoforms (PDE) involved in the contractile response of rat aorta to different agonists and different experimental procedures for use in functional studies. The inhibitory effect of AAL 05 on the different PDEs isolated from bovine aortic smooth muscle was examined. Compound AAL 05 appeared to be a selective PDE3 inhibitor. We analyzed the ability of the non-selective inhibitor IBMX (3-isobutyl-1-methylxanthine) and the isoenzyme selective inhibitors nimodipine (type 1), AAL 05 (6-(N-methyl-N-cyclohexyl butyl carboxamide) quinolin-2-one) and SKF 94120 (5-(4-acetamidophenyl) pyrazin-2(1H)-one; type3), rolipram (type4) and zaprinast (typ…

Gene isoformPurinonesPhosphodiesterase InhibitorsPhosphodiesterase 3BiologyIsozymeMuscle Smooth Vascular1-Methyl-3-isobutylxanthinemedicine.arterymedicineAnimalsFunctional studiesRats WistarInhibitory effectAortaPharmacologyAortaCyclic nucleotide phosphodiesteraseContractile responseGeneral MedicineRatsIsoenzymesBiochemistryVasoconstrictionCalcium2'3'-Cyclic-Nucleotide PhosphodiesterasesRolipramNaunyn-Schmiedeberg's Archives of Pharmacology
researchProduct

Centrins in retinal photoreceptor cells: regulators in the connecting cilium.

2008

Changes in the intracellular Ca2+ concentration regulate the visual signal transduction cascade directly or more often indirectly through Ca2+-binding proteins. Here we focus on centrins, which are members of a highly conserved subgroup of the EF-hand superfamily of Ca2+-binding proteins in photoreceptor cells of the vertebrate retina. Centrins are commonly associated with centrosome-related structures. In mammalian retinal photoreceptor cells, four centrin isoforms are expressed as prominent components in the connecting cilium linking the light-sensitive outer segment compartment with the metabolically active inner segment compartment. Our data indicate that Ca2+-activated centrin isoforms…

Gene isoformgenetic structuresChromosomal Proteins Non-HistoneBiologyContractile ProteinsHeterotrimeric G proteinmedicineCompartment (development)AnimalsHumansCiliaEye ProteinsVision OcularRetinaCalcium-Binding ProteinsSensory SystemsCell biologyOphthalmologymedicine.anatomical_structureCentrinCalciumsense organsTransducinSignal transductionIntracellularPhotoreceptor Cells VertebrateProgress in retinal and eye research
researchProduct

Molecular basis of filamin a-filGAP interaction and its impairment in congenital disorders associated with filamin a mutations

2008

Background Mutations in filamin A (FLNa), an essential cytoskeletal protein with multiple binding partners, cause developmental anomalies in humans. Methodology/Principal Findings We determined the structure of the 23rd Ig repeat of FLNa (IgFLNa23) that interacts with FilGAP, a Rac-specific GTPase-activating protein and regulator of cell polarity and movement, and the effect of the three disease-related mutations on this interaction. A combination of NMR structural analysis and in silico modeling revealed the structural interface details between the C and D β-strands of the IgFLNa23 and the C-terminal 32 residues of FilGAP. Mutagenesis of the predicted key interface residues confirmed the b…

ImmunoprecipitationFilaminsMolecular Sequence Dataeducationlcsh:MedicineComputational Biology/Protein Structure PredictionBiologyFilaminCell Biology/Cell SignalingCongenital AbnormalitiesBiochemistry/Protein Folding03 medical and health sciences0302 clinical medicineProtein structureContractile ProteinsCell Biology/CytoskeletonFLNAHumansFLNBFLNCAmino Acid Sequencelcsh:Science030304 developmental biologyGenetics0303 health sciencesMultidisciplinaryBinding SitesMolecular StructureSequence Homology Amino AcidPoint mutationlcsh:RGTPase-Activating ProteinsMicrofilament Proteins3. Good healthBiochemistry/BioinformaticsMutationProtein foldinglcsh:Q118 Biological sciences030217 neurology & neurosurgeryResearch Article
researchProduct

Pro-prion Binds Filamin A, Facilitating Its Interaction with Integrin β1, and Contributes to Melanomagenesis

2010

Filamin A (FLNA) is an integrator of cell mechanics and signaling. The spreading and migration observed in FLNA sufficient A7 melanoma cells but not in the parental FLNA deficient M2 cells have been attributed to FLNA. In A7 and M2 cells, the normal prion (PrP) exists as pro-PrP, retaining its glycosylphosphatidyl-inositol (GPI) anchor peptide signal sequence (GPI-PSS). The GPI-PSS of PrP has a FLNA binding motif and binds FLNA. Reducing PrP expression in A7 cells alters the spatial distribution of FLNA and organization of actin and diminishes cell spreading and migration. Integrin β1 also binds FLNA. In A7 cells, FLNA, PrP, and integrin β1 exist as two independent, yet functionally linked,…

Integrin beta ChainsGlycosylphosphatidylinositolsPrionsFilaminsanimal diseasesAmino Acid MotifsIntegrinPlasma protein bindingBiologyFilaminBiochemistryCell membraneContractile ProteinsCell MovementCell Line TumormedicineHumansFLNACytoskeletonMelanomaMolecular BiologyActinMicrofilament ProteinsCell Biologynervous system diseasesCell biologyGene Expression Regulation Neoplasticmedicine.anatomical_structurebiology.proteinCancer researchSignal transductionProtein BindingJournal of Biological Chemistry
researchProduct

Increased gene expression of a cytokine-related molecule and profilin after activation of Suberites domuncula cells with xenogeneic sponge molecule(s)

2000

Porifera (sponges) constitute the lowest metazoan phylum, Experiments examined whether sponges can recognize self/nonself molecules. Cells from the marine sponge Suberites domuncula were incubated with membranes from either S. domuncula or another marine sponge, Geodia cydonium, as well as with recombinant alpha-integrin from G. cydonium. The cells responded immediately with a rise of intracellular Ca2+ ([Ca-i(2+)]) if they were treated with membranes from G. cydonium but not after treatment by those from S. domuncula. This change of [Ca-i(2+)] was also recorded with G. cydonium alpha-integrin. In parallel, the expression of two genes was strongly upregulated; one codes for a cytokine-relat…

Integrinsmedicine.medical_treatmentMolecular Sequence DataGene ExpressionPolymerase Chain ReactionMicrobiologylaw.inventionProfilinsContractile ProteinsAntigenlawAntigens HeterophileGene expressionGeneticsmedicineAnimalsAmino Acid SequenceCloning MolecularMolecular Biologygeodia-cydonium; marine sponge; allogeneic recognition; immune recognition; adhesionMembranesbiologyMicrofilament ProteinsCell BiologyGeneral Medicinebiology.organism_classificationCell biologyPoriferaSuberites domunculaSpongeCytokineEchinodermProfilinbiology.proteinRecombinant DNACytokinesCalciumSequence Alignment
researchProduct

eNOS S-nitrosylates β-actin on Cys374 and regulates PKC-θ at the immune synapse by impairing actin binding to profilin-1.

2017

The actin cytoskeleton coordinates the organization of signaling microclusters at the immune synapse (IS); however, the mechanisms involved remain poorly understood. We show here that nitric oxide (NO) generated by endothelial nitric oxide synthase (eNOS) controls the coalescence of protein kinase C-¿ (PKC-¿) at the central supramolecular activation cluster (c-SMAC) of the IS. eNOS translocated with the Golgi to the IS and partially colocalized with F-actin around the c-SMAC. This resulted in reduced actin polymerization and centripetal retrograde flow of ß-actin and PKC-¿ from the lamellipodium-like distal (d)-SMAC, promoting PKC-¿ activation. Furthermore, eNOS-derived NO S-nitrosylated ß-…

Life Sciences & Biomedicine - Other Topics0301 basic medicinePOLARIZATIONIMMUNOLOGICAL SYNAPSEImmunological SynapsesT-LymphocytesPROTEINGolgi ApparatusCYTOSKELETONRetrograde FlowBiochemistryARP2/3 COMPLEXT-CELL-ACTIVATIONProfilinsWhite Blood CellsContractile ProteinsFluorescence MicroscopyAnimal CellsMedicine and Health SciencesPseudopodiaBiology (General)Post-Translational ModificationCells CulturedProtein Kinase CMicroscopyT CellsGeneral NeuroscienceLight MicroscopyNeurochemistryRecombinant Proteins3. Good healthIsoenzymesPOLYMERIZATIONProtein TransportCell ProcessesRNA InterferenceCellular TypesNeurochemicalsGeneral Agricultural and Biological SciencesLife Sciences & BiomedicineResearch ArticleBiochemistry & Molecular BiologyNitric Oxide Synthase Type IIIQH301-705.5Imaging TechniquesRecombinant Fusion ProteinsImmune CellsImmunologyLibrary scienceAntigen-Presenting Cellsmacromolecular substancesBiologyNitric OxideResearch and Analysis MethodsGeneral Biochemistry Genetics and Molecular BiologyCell Line03 medical and health sciencesFluorescence ImagingHumansCysteineNITRIC-OXIDE SYNTHASEBiologyScience & TechnologyBlood CellsRECEPTORGeneral Immunology and MicrobiologyBiology and Life SciencesProteinsCell BiologyActinsS-NitrosylationEnzyme ActivationLuminescent ProteinsCytoskeletal Proteins030104 developmental biologyAmino Acid SubstitutionRETROGRADE FLOWProtein Kinase C-thetaMutationProtein Processing Post-TranslationalNeuroscienceActin PolymerizationPLoS biology
researchProduct

Rats bred for low aerobic capacity become promptly fatigued and have slow metabolic recovery after stimulated, maximal muscle contractions.

2012

AIM. Muscular fatigue is a complex phenomenon affected by muscle fiber type and several metabolic and ionic changes within myocytes. Mitochondria are the main determinants of muscle oxidative capacity which is also one determinant of muscle fatigability. By measuring the concentrations of intracellular stores of high-energy phosphates it is possible to estimate the energy production efficiency and metabolic recovery of the muscle. Low intrinsic aerobic capacity is known to be associated with reduced mitochondrial function. Whether low intrinsic aerobic capacity also results in slower metabolic recovery of skeletal muscle is not known. Here we studied the influence of intrinsic aerobic capac…

Magnetic Resonance SpectroscopyAnatomy and PhysiologyPhosphocreatineEvolutionary Selectionlcsh:MedicineIsometric exerciseBreedingmetaboliset sairaudetBiochemistrychemistry.chemical_compound0302 clinical medicineTriceps surae muscleMyocyteta315lcsh:ScienceMusculoskeletal System0303 health sciencesMultidisciplinarycomplex diseaseMuscle BiochemistryAnatomyAnimal ModelsHydrogen-Ion Concentrationmedicine.anatomical_structureaerobinen kapasiteettiMuscle FatigueMuscleaerobinen suorituskykymedicine.symptomMuscle contractionMuscle ContractionResearch Articlemedicine.medical_specialtyEvolutionary ProcessessupistusominaisuudetBioenergeticsPhosphocreatinePhosphates03 medical and health sciencesModel OrganismsInternal medicinePhysical Conditioning AnimalmedicineGeneticsAnimalsskeletal muscleAdaptationBiologyAerobic capacity030304 developmental biologyEvolutionary BiologyMuscle fatiguelcsh:RSkeletal muscleElectric StimulationRatsraajalihasEndocrinologyMetabolismcontractile propertieschemistryRatlcsh:QEnergy MetabolismPhysiological ProcessesAnimal Genetics030217 neurology & neurosurgeryPLoS ONE
researchProduct