Search results for "fibrils"

showing 10 items of 48 documents

Trifluoroethanol modulates α-synuclein amyloid-like aggregate formation, stability and dissolution

2016

The conversion of proteins into amyloid fibrils and other amyloid-like aggregates is closely connected to the onset of a series of age-related pathologies. Upon changes in environmental conditions, amyloid-like aggregates may also undergo disassembly into oligomeric aggregates, the latter being recognized as key effectors in toxicity. This indicates new possible routes for in vivo accumulation of toxic species. In the light of the recognized implication of α-Synuclein (αSN) in Parkinson's disease, we present an experimental study on supramolecular assembly of αSN with a focus on stability and disassembly paths of such supramolecular aggregate species. Using spectroscopic techniques, two-pho…

0301 basic medicineAmyloidAmyloidBiophysicsSupramolecular chemistryProtein aggregationBiochemistrySupramolecular assembly03 medical and health scienceschemistry.chemical_compoundProtein AggregatesHumansDissolutionAlpha-synucleinProtein Stabilityproteins amyloid fibrils amyloid-like aggregates oligomeric aggregatesSpectrum AnalysisOrganic ChemistryAggregate (data warehouse)TemperatureTrifluoroethanolAmyloid fibrilCrystallography030104 developmental biologychemistryBiophysicsalpha-Synuclein
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Extracellular Assembly of the Elastin Cable Line Element in the Developing Lung

2017

In the normal lung, a dominant structural element is an elastic "line element" that originates in the central bronchi and inserts into the distal airspaces. Despite its structural importance, the process that leads to development of the cable line element is unknown. To investigate the morphologic events contributing to its development, we used optical clearing methods to examine the postnatal rat lung. An unexpected finding was numerous spheres, with a median diameter of 1-2 µm, within the primary septa of the rat lung. The spheres demonstrated green autofluorescence, selective fluorescent eosin staining, reactivity with carboxyfluorescein succinimidyl ester, and specific labeling with ant…

0301 basic medicineScaffold proteinHistologyTropoelastinbiologyEosinCarboxyfluorescein succinimidyl esterAnatomy03 medical and health sciencesAutofluorescencechemistry.chemical_compound030104 developmental biology0302 clinical medicinechemistryFibrillin Microfibrilsbiology.proteinExtracellularBiophysicsAnatomyElastin030217 neurology & neurosurgeryEcology Evolution Behavior and SystematicsBiotechnologyThe Anatomical Record
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Celiac disease and selective immunoglobulin A deficiency

1997

Selective IgA deficiency was observed in 12 of 688 (1.7%) patients with celiac disease who were clinically undistinguishable from patients with celiac disease with normal IgA levels. This high prevalence of IgA deficiency in patients with celiac disease makes serum IgA assay advisable when screening for celiac disease is performed by measurement of antigliadin antibodies or anti-IgA endomysium antibodies. Similarly, subjects with IgA deficiency should be considered at risk of celiac disease.

AdolescentGlutensCross-sectional studyMuscle Fibers SkeletalDiseaseSelective IgA deficiencyImmunoglobulin EGliadinCoeliac diseaseMyofibrilsRisk FactorsImmunopathologyConfidence IntervalsDiet Protein-RestrictedPrevalencemedicineHumansChildChi-Square Distributionbiologybusiness.industryAge FactorsIgA DeficiencyInfantnutritional and metabolic diseasesmedicine.diseaseEndomysiumdigestive system diseasesImmunoglobulin ACeliac DiseaseIntestinal DiseasesCross-Sectional Studiesmedicine.anatomical_structureImmunoglobulin MChild PreschoolImmunoglobulin GPediatrics Perinatology and Child HealthImmunologybiology.proteinAntibodybusinessFollow-Up StudiesThe Journal of Pediatrics
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Endogenous 3-methylhistidine excretion in healthy women and men with reference to muscle protein metabolism.

1984

Presently 3-methylhistidine excretion is widely used for monitoring the metabolic status of patients during different kinds of clinical conditions. Aim of the study was to reconsider its predicative value on the basis of a larger collective of healthy persons and to find a standardization independent from sex. Therefore endogenous 3-methylhistidine release of 40 healthy adults (24 women and 16 men) was measured and related to body weight, body surface area, arm muscle circumference, and nitrogen and creatinine excretion. A positive correlation could be observed only for 3-methylhistidine and creatinine excretion and that to the same extent both for females and males. Assuming that the excre…

AdultMalemedicine.medical_specialtyMedicine (miscellaneous)Renal functionMuscle ProteinsEndogenyBiologyBiochemistryExcretionchemistry.chemical_compoundSex FactorsMyofibrilsInternal medicinemedicineHumansHistidineBody surface areaCreatinineAnthropometryMusclesBody WeightAge FactorsMetabolismMiddle AgedMethylhistidinesProtein catabolismSkinfold ThicknessEndocrinologychemistryCreatinineFemaleMyofibrilFood ScienceZeitschrift fur Ernahrungswissenschaft
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Nucleation mechanisms and morphologies in insulin amyloid fibril formation

2011

Aggregation amyloid fibrils insulinSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)
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Age-related accumulation of congophilic fibrillar inclusions in endocrine cells

1991

Intracellular fibrillar congophilic inclusions are well known as neurofibrillary tangles in neurons and as Biondi bodies in choroid plexus epithelial cells. Recently similar amyloid-like inclusions in adrenal cortical cells were described (Eriksson and Westermark 1990). This study on 150 adrenal glands confirms these observations. In our material the age-related accumulation of congophilic inclusions starts earlier (in the sixth decade) and reaches a higher incidence (42.7%). We found similar intracellular inclusions in other endocrine organs, for example in the anterior lobe of the pituitary, in the cells of parathyroid glands and in Sertoli cells. The age-related incidence of these fibril…

AgingAmyloidPituitary glandmedicine.medical_specialtyPathologyEnteroendocrine cellBiologyTesticlePathology and Forensic MedicineEndocrine GlandsInternal medicineAdrenal GlandsmedicineHumansEndocrine systemMolecular BiologyBrain ChemistryAdrenal glandCongo RedCell BiologyGeneral MedicineSertoli cellmedicine.anatomical_structureEndocrinologyPituitary GlandChoroid PlexusNeurofibrilsChoroid plexusExtracellular SpaceEndocrine glandVirchows Archiv A Pathological Anatomy and Histopathology
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Amyloid Fibrils Formation of Concanavalin A at Basic pH

2011

Mechanisms of partial unfolding and aggregation of proteins are of extreme interest in view of the fact that several human pathologies are characterized by the formation and deposition of protein-insoluble material, mainly composed of amyloid fibrils. Here we report on an experimental study on the heat-induced aggregation mechanisms, at basic pH, of concanavalin A (ConA), used as a model system. Thioflavin T (ThT) fluorescence and multiangle light scattering allowed us to detect different intertwined steps in the formation of ConA aggregates. In particular, the ThT fluorescence increase, observed in the first phase of aggregation, reveals the formation of intermolecular β-sheet structure wh…

Amyloid Fibrils Concanavalin A Light scatteringAmyloidLightMultiangle light scatteringFibrilProtein Structure SecondaryLight scatteringchemistry.chemical_compoundPhase (matter)Scattering Small AngleConcanavalin AMaterials ChemistryBenzothiazolesPhysical and Theoretical ChemistrybiologyIntermolecular forceTemperatureHydrogen-Ion ConcentrationFluorescenceSurfaces Coatings and FilmsThiazolesCrystallographySpectrometry FluorescencechemistryConcanavalin ABiophysicsbiology.proteinThioflavinProtein MultimerizationThe Journal of Physical Chemistry B
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Decoding vibrational states of Concanavalin A amyloid fibrils.

2015

International audience; Amyloid and amyloid-like fibrils are a general class of protein aggregates and represent a central topic in life sciences for their involvement in several neurodegenerative disorders and their unique mechanical and supramolecular morphological properties. Both their biological role and their physical properties, including their high mechanical stability and thermodynamic inertia, are related to the structural arrangement of proteins in the aggregates at molecular level. Significant variations may exist in the supramolecular organization of the commonly termed cross-β structure that constitutes the amyloid core. In this context, a fine knowledge of the structural deta…

AmyloidAbsorption spectroscopy[SDV]Life Sciences [q-bio]BiophysicsSupramolecular chemistry02 engineering and technologymacromolecular substancesProtein aggregationAntiparallel (biochemistry)FibrilSpectrum Analysis RamanBiochemistryVibrationProtein Structure Secondary03 medical and health sciencessymbols.namesakeSpectroscopy Fourier Transform InfraredConcanavalin AHumansFourier transform infrared spectroscopyRaman030304 developmental biology0303 health sciencesChemistryOrganic ChemistryIntermolecular force021001 nanoscience & nanotechnologyAmyloid FTIR RAMAN hydration water THz spectroscopy[SDV] Life Sciences [q-bio]CrystallographyFTIRTerahertz spectroscopysymbolsBiophysicsFibrils0210 nano-technologyRaman spectroscopy
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Detection of Type VII collagen in odontogenic keratocyst: An immunohistochemical study

2019

Background Separation of the epithelial lining from the underlying connective tissue wall has been a frequently observed and unique feature in odontogenic keratocysts (OKC), but not in other odontogenic cysts nor neoplasms. No study on OKC has been reported evaluating the role of type VII Collagen, the anchoring fibrils, which function in stabilising the epithelial structure. The purpose of this study was to assess the role of type VII collagen in the fragility of the epithelium leading to a high recurrence rate in OKCs. Material and Methods Immunohistochemical staining with Abcam® Monoclonal Mouse Anti-Collagen VII Antibody [LH7.2] (used at a dilution of 1:200) on 30 tissues of OKC. The ch…

Basement membranePathologymedicine.medical_specialtyOral Medicine and PathologyChemistryResearchConnective tissue030206 dentistry:CIENCIAS MÉDICAS [UNESCO]EpitheliumStaining03 medical and health sciences0302 clinical medicinemedicine.anatomical_structure030220 oncology & carcinogenesisUNESCO::CIENCIAS MÉDICASAnchoring fibrilsmedicineImmunohistochemistryBasal laminaKeratocystmedicine.symptomGeneral DentistryJournal of Clinical and Experimental Dentistry
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THERMALLY INDUCED FIBRILLAR AGGREGATION OF BOVINE SERUM ALBUMIN

2008

Bovine Serum Albumin Fibrils
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