Search results for "FIBRILS"

showing 10 items of 48 documents

Phasor-FLIM analysis of Thioflavin T self-quenching in Concanavalin amyloid fibrils

2020

The formation of amyloid structures has traditionally been related to human neurodegenerative pathologies and, in recent years, the interest in these highly stable nanostructures was extended to biomaterial sciences. A common method to monitor amyloid growth is the analysis of Thioflavin T fluorescence. The use of this highly selective dye, diffused worldwide, allows mechanistic studies of supramolecular assemblies also giving back important insight on the structure of these aggregates. Here we present experimental evidence of self-quenching effect of Thioflavin T in presence of amyloid fibrils. A significant reduction of fluorescence lifetime of this dye which is not related to the propert…

Fluorescence-lifetime imaging microscopyAmyloidFLIMHistologyAmyloid02 engineering and technologyProtein aggregationprotein aggregation03 medical and health scienceschemistry.chemical_compound0302 clinical medicineself-quenchingmental disordersamyloid fibrilConcanavalin Afluorescence lifetimeHumansBenzothiazolesInstrumentationFluorescent DyesInclusion BodiesQuenching (fluorescence)biologyStaining and LabelingChemistryOptical ImagingPhasorNeurodegenerative Diseases030206 dentistry021001 nanoscience & nanotechnologyFluorescenceSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Medical Laboratory TechnologyMicroscopy FluorescenceConcanavalin APhasorbiology.proteinBiophysicsThioflavin TThioflavinamyloid fibrils Concanavalin A FLIM fluorescence lifetime Phasor protein aggregation self-quenching Thioflavin TAnatomy0210 nano-technology
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Morphology of experimentally denervated and reinnervated rat facial muscle I. Histochemical and histological findings

1994

The morphological changes in rat facial muscles were evaluated after permanent denervation and were compared with findings after immediate reinnervation. Thirty rats underwent transection of the left and right facial nerves immediately followed by hypoglossal-facial nerve anastomosis on the right side (muscular reinnervation) and removal of 8-10 mm of the facial plexus on the left side (permanent muscular denervation). Levator labii muscle samples of both sides were collected sequentially at 2, 6, 7, 10, 20, and 24 weeks after surgery and submitted to routine histological and enzyme histochemical staining procedures. In normal levator labii muscles a typical "chessboard" pattern was found, …

Hypoglossal NervePathologymedicine.medical_specialtyVitamin KFacial MusclesMyofibrilsPerimysialmedicineAnimalsRegenerationRats WistarNerve TransferAdenosine TriphosphatasesNADH Tetrazolium ReductaseDenervationMuscle DenervationHistocytochemistrybusiness.industryAnastomosis SurgicalGeneral MedicineAnatomyFibrosisFacial nerveMuscle DenervationRatsFacial NerveFacial musclesmedicine.anatomical_structureOtorhinolaryngologyConnective TissueGlycerophosphatesNerve TransferFemaleAtrophybusinessHypoglossal nerveReinnervationEuropean Archives of Oto-Rhino-Laryngology
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Nouvelles perspectives concernant la structure et la fonction du domaine carboxyl terminal de Hfq

2015

Accumulating evidence indicates that RNA metabolism components assemble into supramolecular cellular structures to mediate functional compartmentalization within the cytoplasmic membrane of the bacterial cell. This cellular compartmentalization could play important roles in the processes of RNA degradation and maturation. These components include Hfq, the RNA chaperone protein, which is involved in the post-transcriptional control of protein synthesis mainly by the virtue of its interactions with several small regulatory ncRNAs (sRNA). The Escherichia coli Hfq is structurally organized into two domains. An N-terminal domain that folds as strongly bent β-sheets within individual protomers to…

IDP intrinsically-disordered proteinslcsh:Lifelcsh:QR1-502sub-membrane macromolecular assemblyPlasma protein bindingsRNA small non-coding RNABiochemistrylcsh:Microbiologyamyloid fibrilsProtein biosynthesis0303 health sciences[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]Escherichia coli Proteins030302 biochemistry & molecular biologyHfqCTRp Hfq C-terminal peptideFTIR Fourier transform infrared spectroscopyNTR N-terminal regionCompartmentalization (psychology)Cell biology[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsRNA Bacterialsmall non-coding ribonucleic acid (RNA)BiochemistryFSD Fourier self-deconvolutionTransfer RNAAmyloid fibrilProtein BindingBiophysicsBiologyHost Factor 1 Protein03 medical and health sciencesEscherichia coliThT thioflavin T[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyProtein Structure QuaternaryncRNA regulatory non-coding RNAPost-transcriptional regulationMolecular Biology030304 developmental biologyOriginal PaperC-terminusRNA[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyCell Biologycellular compartmentalizationWT wild-typeProtein Structure Tertiarylcsh:QH501-531Host Factor 1 ProteinCTR Hfq C-terminal regionribonucleic acid (RNA) processing and degradationBiophysicpost-transcriptional regulationBioscience Reports
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Self-Organization Pathways and Spatial Heterogeneity in Insulin Amyloid Fibril Formation

2009

At high temperature and low pH, the protein hormone insulin is highly prone to form amyloid fibrils, and for this reason it is widely used as a model system to study fibril formation mechanisms. In this work, we focused on insulin aggregation mechanisms occurring in HCl solutions (pH 1.6) at 60 degrees C. By means of in situ Thioflavin T (ThT) staining, the kinetics profiles were characterized as a function of the protein concentration, and two concurrent aggregation pathways were pointed out, being concentration dependent. In correspondence to these pathways, different morphologies of self-assembled protein molecules were detected by atomic force microscopy images also evidencing the prese…

In situAmyloidHot Temperaturemedicine.medical_treatmentKineticsNucleationMicroscopy Atomic ForceFibrilchemistry.chemical_compoundMicroscopyMaterials ChemistrymedicineAnimalsInsulinBenzothiazolesPhysical and Theoretical ChemistryInsulin Amyloid Fibrils Secondary Nucleation Thioflavin T (ThT) Scanning Force Microscopy (SFM) Spatial HeterogeneityChemistryInsulinfluorescence spectroscopyFluorescenceSurfaces Coatings and FilmsThiazolesBiochemistryBiophysicsCattleThioflavinHydrochloric AcidProtein aggregation
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Kinetics of Insulin Aggregation: Disentanglement of Amyloid Fibrillation from Large-Size Cluster Formation

2006

Kinetics of human insulin aggregation has been studied at pH 1.6 and 60 degrees C, when amyloid fibrils are formed. We developed a novel approach based on the analysis of scattered light intensity distribution, which allows distinguishing between small and large size aggregates. By this method, we observed an exponential growth of fibrillar aggregates implying a heterogeneous aggregation mechanism. Also, the apparent lag time observed, correlated with the major increase of thioflavin T fluorescence, has been assigned to the onset of large size cluster formation.

MECHANISMModels MolecularAmyloidAmyloidmedicine.medical_treatmentKineticsBiophysicschemistry.chemical_compoundExponential growthFIBRILSmedicineCluster (physics)HumansInsulinComputer SimulationBenzothiazolesParticle SizeATOMIC-FORCE MICROSCOPYInsulinPATHWAYSProteinsFluorescenceLIGHT-SCATTERINGCrystallographyKineticsThiazoleschemistryModels ChemicalMultiprotein ComplexesBiophysicsThioflavinParticle sizeBETA-PROTEINNUCLEATIONBiophysical Journal
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Downregulation and Nuclear Relocation of MLP During the Progression of Right Ventricular Hypertrophy Induced by Chronic Pressure Overload

2000

Abstract The cardiac LIM domain protein MLP plays a crucial role in the architecture and mechanical function of cardiac myocytes. Mice lacking the MLP gene develop cardiac hypertrophy, dilated cardiopathy and heart failure. We investigated whether downregulation of MLP is induced by pressure overload and contributes to the physiopathology of cardiac hypertrophy and failure. We studied this mechanism in rat right ventricles submitted to pulmonary arterial hypertension, because it is known that this ventricle is very vulnerable to the deleterious effects of pressure overload. During the progression of cardiac hypertrophy to failure over a 31 days period there was a dramatic decrease by 50% of…

MaleCytoplasmmedicine.medical_specialtyTime FactorsTranscription GeneticHeart VentriclesDown-RegulationMuscle ProteinsCardiomegalyCytosolMyofibrilsDownregulation and upregulationRight ventricular hypertrophyInternal medicinePressureAnimalsVentricular FunctionMedicineMyocyteRNA MessengerRats WistarLungMolecular BiologyCell NucleusHomeodomain ProteinsPressure overloadReverse Transcriptase Polymerase Chain Reactionbusiness.industryMyocardiumLIM Domain Proteinsmedicine.diseaseImmunohistochemistryPulmonary hypertensionRatsMicroscopy Electronmedicine.anatomical_structureVentricleHeart failureCardiologyCardiology and Cardiovascular MedicinebusinessMyofibrilJournal of Molecular and Cellular Cardiology
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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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Novel slow-skeletal myosin (MYH7) mutation in the original myosin storage myopathy kindred

2006

Abstract Myosin storage myopathy (OMIM 608358), a congenital myopathy characterised by subsarcolemmal, hyaline-like accumulations of myosin in Type I muscle fibres, was first described by Cancilla and Colleagues in 1971 [Neurology 1971;21:579–585] in two siblings as ‘familial myopathy with probable lysis of myofibrils in type I muscle fibres'. Two mutations in the slow skeletal myosin heavy chain gene ( MYH7 ) have recently been associated with the disease in other families. We have identified a novel heterozygous Leu1793Pro mutation in MYH7 in DNA from paraffin sections of one of the original siblings. This historical molecular analysis confirms the original cases had myosin storage myopat…

MaleHeterozygotemacromolecular substancesMyosinsBiologymedicine.disease_causeMuscular DiseasesMyofibrilsMyosinmedicineHumansMyopathyGeneGenetics (clinical)GeneticsMutationMyosin Heavy ChainsMyosin storage myopathyDNAExonsmedicine.diseaseMolecular biologyCongenital myopathyMuscle Fibers Slow-TwitchNeurologyChild PreschoolMutationPediatrics Perinatology and Child HealthFemaleMYH7Neurology (clinical)medicine.symptomMyofibrilCardiac MyosinsNeuromuscular Disorders
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Evidence of Transient IgA Anti-Endomysial Antibody Positivity in a Patient with Graves’ Disease

1999

<i>Background:</i> Anti-endomysial antibodies (EmA) have been shown to have a high specificity and sensitivity in celiac disease (CD) diagnosis, and their use is considered effective in improving the diagnostic accuracy of CD screening. <i>Aims:</i> To report the clinical details of transient IgA EmA positivity in a patient with Graves’ disease. <i>Methods:</i> We screened 48 patients (7 males, age range 19–79, median 58.3 years) for CD. They were hospitalized for thyroid disorders (30 patients had autoimmune hypothyroidism and 18 had Graves’ disease with clinical hyperthyroidism associated with diffuse goitre). CD screening was carried out on all patient…

MaleImmunoglobulin ATime FactorsBiopsyGraves' diseasemedicine.disease_causeGliadinCoeliac diseaseAutoimmunityMyofibrilsImmunopathologyHumansMedicineAgedbiologybusiness.industryGastroenterologyMiddle AgedEndomysiummedicine.diseaseGraves DiseaseImmunoglobulin ACeliac Diseasemedicine.anatomical_structureImmunologyAnti-gliadin antibodiesbiology.proteinFemaleAntibodybusinessFollow-Up StudiesDigestion
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A new familial congenital myopathy in children with desmin and dystrophin reacting plaques.

1995

In 5 children with a progressive congenital myopathy representing 3 different families, unusual histological, immunohistochemical and ultrastructural changes in skeletal muscle have been found. Histologically, this myopathy was characterized by the presence of fine hyaline plaques devoid of oxidative as well as ATPase enzyme activities. At the ultrastructural level plaques were composed of helical filaments and amorphous dense material. Helical filament storage corresponded to strong desmin as well as ubiquitin immunoreactivity. In addition they were also dystrophin positive. The exclusive appearance of desmin, ubiquitin and dystrophin positive plaques in muscle specimens from 5 children em…

MalePathologymedicine.medical_specialtyAdolescentImmunocytochemistryBiologyDesminDystrophinMyofibrilsBiopsymedicineHumansMyopathyChildUbiquitinsHyalinemedicine.diagnostic_testMusclesSkeletal muscleNeuromuscular Diseasesmedicine.diseaseCongenital myopathyImmunohistochemistryMicroscopy Electronmedicine.anatomical_structureNeurologyChild Preschoolbiology.proteinDesminFemaleNeurology (clinical)medicine.symptomDystrophinJournal of the neurological sciences
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