Search results for "AMyloid"

showing 10 items of 494 documents

Lead(II) ions adsorption onto amyloid particulates: An in depth study

2022

The production of new cost-effective biocompatible sorbent sustainable materials, with natural origins, able to remove heavy metals from water resources is nowadays highly desirable in order to reduce pollution and increase clean water availability. In this context, self-assembled protein materials with amyloid structures seem to have a great potential as natural platform for a broader development of highly-tunable structures. In this work we show how protein particulates, a generic form of protein aggregates, with spherical micro sized shape can be used as adsorbents of Pb2+ ions from aqueous solution. The effect of pH, ionic medium, ionic strength and temperature of the metal ion solution…

IonsMetal pollutionTemperatureRemediationWaterHydrogen-Ion ConcentrationEnvironmental pollutionHydration waterSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Surfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsWater PurificationBiomaterialsKineticsColloid and Surface ChemistryBovine serum albuminLeadMetals HeavySettore CHIM/01 - Chimica AnaliticaAdsorptionAmyloid superstructuresWater Pollutants Chemical
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Amiloīda-beta 42 peptīda agregācijas pētījumi ar 19F KMR spektroskopiju

2020

Maģistra darba literatūras apskatā apkopota vispārīga informācija par amiloīda-beta peptīdiem, to agregāciju un tās pētīšanas metodēm. Maģistra darbā eksperimentālajā daļā izstrādātas metodes fluorēto aminoskābju inkorporēšanai amiloīda-beta 42 peptīdā, un veikti fluorēto peptīdu KMR eksperimenti.

KMR SPEKTROSKOPIJAAGREGĀCIJAAMILOĪDA-BETAFLUORSAMYLOID-BETAĶīmija
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Melittin Modulates Keratinocyte Function through P2 Receptor-dependent ADAM Activation

2012

Melittin, the major component of the bee venom, is an amphipathic, cationic peptide with a wide spectrum of biological properties that is being considered as an anti-inflammatory and anti-cancer agent. It modulates multiple cellular functions but the underlying mechanisms are not clearly understood. Here, we report that melittin activates disintegrin-like metalloproteases (ADAMs) and that downstream events likely contribute to the biological effects evoked by the peptide. Melittin stimulated the proteolysis of ADAM10 and ADAM17 substrates in human neutrophil granulocytes, endothelial cells and murine fibroblasts. In human HaCaT keratinocytes, melittin induced shedding of the adhesion molecu…

KeratinocytesCell SurvivalBlotting WesternADAM17 ProteinP2 receptorBiologyModels Biologicalcomplex mixturesBiochemistryMelittinCell LineADAM10 ProteinMicechemistry.chemical_compoundTransactivationAdenosine TriphosphateAnimalsHumansPhosphorylationExtracellular Signal-Regulated MAP KinasesReceptorMolecular BiologyCells CulturedMice KnockoutDose-Response Relationship DrugReverse Transcriptase Polymerase Chain ReactionPurinergic receptorHEK 293 cellstechnology industry and agricultureMembrane ProteinsCell BiologyFibroblastsCadherinsEmbryo MammalianMelittenCell biologyErbB ReceptorsADAM ProteinsHaCaTHEK293 CellschemistryPhosphorylationlipids (amino acids peptides and proteins)Receptors Purinergic P2X7Amyloid Precursor Protein SecretasesJournal of Biological Chemistry
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Unsaturated Fatty Acids Drive Disintegrin and Metalloproteinase (ADAM)-dependent Cell Adhesion, Proliferation, and Migration by Modulating Membrane F…

2011

The disintegrin-metalloproteinases ADAM10 and ADAM17 mediate the release of several cell signaling molecules and cell adhesion molecules such as vascular endothelial cadherin or L-selectin affecting endothelial permeability and leukocyte transmigration. Dysregulation of ADAM activity may contribute to the pathogenesis of vascular diseases, but the mechanisms underlying the control of ADAM functions are still incompletely understood. Atherosclerosis is characterized by lipid plaque formation and local accumulation of unsaturated free fatty acids (FFA). Here, we show that unsaturated FFA increase ADAM-mediated substrate cleavage. We demonstrate that these alterations are not due to genuine ch…

KeratinocytesMembrane FluidityADAM10Lipid BilayersVascular permeabilityBiologyADAM17 ProteinBiochemistryCapillary PermeabilityADAM10 ProteinCell MovementMembrane fluidityCell AdhesionAnimalsHumansCell adhesionMolecular BiologyCell ProliferationCell adhesion moleculeCell growthFluorescence recovery after photobleachingEndothelial CellsMembrane ProteinsCell BiologyAtherosclerosisADAM ProteinsCell biologyLipoproteins LDLADAM ProteinsHEK293 CellsFatty Acids UnsaturatedCholesterol EstersRabbitsAmyloid Precursor Protein SecretasesGranulocytes
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Amyloid P component--a special type of collagen?

1978

The localization of amyloid P-components is demonstrated by immunofluorescence microscopy in normal human tissue (kidney, spleen, liver). The relation to collagen and to amyloidosis is discussed.

KidneyPathologymedicine.medical_specialtyAmyloidAmyloidChemistryAmyloidosisGoatsImmune SeraFluorescent Antibody TechniqueSpleenImmunofluorescence MicroscopyMiddle Agedmedicine.diseaseKidneyPathology and Forensic MedicineAmyloid P ComponentCollagen type I alpha 1medicine.anatomical_structureLivermedicineAnimalsHumansCollagenSpleenVirchows Archiv. B, Cell pathology
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Conformational Transitions upon Maturation Rule Surface and pH-Responsiveness of α-Lactalbumin Microparticulates

2021

De novo designed protein supramolecular structures are nowadays attracting much interest as highly performing biomaterials. While a clear advantage is provided by the intrinsic biocompatibility and...

LactalbuminAmyloidFluorescence-lifetime imaging microscopyAmyloidBiocompatibilitySurface PropertiesChemistryBiochemistry (medical)Biomedical EngineeringSupramolecular chemistryBiocompatible MaterialspH-responsivenessGeneral ChemistryMicroparticlesHydrogen-Ion ConcentrationFluorescence Lifetime ImagingBiomaterialsMaturationMaterials TestingThioflavin TLactalbuminBiophysicsProtein CondensatesParticle SizeLiquid-Liquid Phase SeparationACS Applied Bio Materials
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CO(2)-laser treatment of laryngeal amyloidosis.

2003

Four consecutive female patients (age: 14–47 years) with laryngeal amyloidosis, treated with endoscopic CO2-laser surgery, entered the study. All patients underwent periodic microlaryngoscopies following surgery to confirm the adequacy of the surgical resection. Recurrences or suspected lesions were resected and fibrin deposits were removed to prevent the formation of synechiae or healing adhesions. After two negative microlaryngoscopies, performed two months apart, the patients were followed-up approximately every six months over a period from six months to 18 years, with no evidence of recurrences. The endoscopic CO2-laser technique is highly effective in the treatment of localized laryng…

Laser surgeryLarynxSurgical resectionAdultmedicine.medical_specialtyEvery Six MonthsAdolescentmedicine.medical_treatmentFibrinLaryngeal DiseasesCo 2 laserLaryngeal amyloidosisFemale patientmedicineHumansbiologyLaryngoscopybusiness.industryGeneral MedicineAmyloidosisCarbon DioxideMiddle AgedSurgerymedicine.anatomical_structureTreatment OutcomeOtorhinolaryngologybiology.proteinFemaleLaser TherapyLarynxbusinessThe Journal of laryngology and otology
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The neuropeptide PACAP promotes ?‐secretase pathway for processing Alzheimer amyloid precursor protein

2006

SPECIFIC AIMSProteolytic cleavage of the amyloid precursor protein (APP) by α-secretase within the Aβ sequence precludes formation of amyloidogenic peptides and leads to a release of soluble APPsα,...

MAP kinase kinase kinasebiologyNeuropeptideMitogen-activated protein kinase kinaseCleavage (embryo)BiochemistryAlpha secretaseBiochemistrymental disordersGeneticsAmyloid precursor proteinbiology.proteinASK1Molecular BiologyBiotechnologyG protein-coupled receptorThe FASEB Journal
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Oestradiol or genistein rescues neurons from amyloid beta-induced cell death by inhibiting activation of p38.

2007

Oestrogenic compounds have been postulated as neuroprotective agents. This prompted us to investigate their mechanism action in neurons in primary culture. Cells were pretreated with physiological concentrations of 17-beta estradiol (0.2 nm) or with nutritionally relevant concentrations of genistein (0.5 microm), and 48 h later treated with 5 microm of amyloid beta (Abeta) for 24 h. We found that Abeta increased oxidative stress, measured as peroxide levels or oxidized glutathione/reduced glutathione ratio, which in turn, caused phosphorylation of p38 MAP kinase. Amyloid beta subsequently induced neuronal death. Inhibiting the MAP kinase pathway prevented cell death, confirming the role of …

MAPK/ERK pathwayAgingProgrammed cell deathmedicine.medical_specialtyAmyloid betaCell Survivalp38 mitogen-activated protein kinasesGenisteinPhytoestrogensIn Vitro Techniquesmedicine.disease_causeNeuroprotectionp38 Mitogen-Activated Protein Kinaseschemistry.chemical_compoundInternal medicinemedicineAnimalsCells CulturedCerebral CortexNeuronsAmyloid beta-PeptidesbiologyCell DeathEstradiolEstrogensCell BiologyGlutathioneGenisteinMitochondriaRatsOxidative StressEndocrinologychemistrybiology.proteinOxidation-ReductionOxidative stressAging cell
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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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