Search results for "GREG"

showing 10 items of 1242 documents

Impaired Platelet Function in Sept8-Deficient Mice In Vitro.

2020

AbstractSeptins (Septs) are a widely expressed protein family of 13 mammalian members, recognized as a unique component of the cytoskeleton. In human platelets, we previously described that SEPT4 and SEPT8 are localized surrounding α-granules and move to the platelet surface after activation, indicating a possible role in platelet physiology. In this study, we investigated the impact of Sept8 on platelet function in vitro using Sept8-deficient mouse platelets. Deletion of Sept8 in mouse platelets caused a pronounced defect in activation of the fibrinogen receptor integrin αIIbβ3, α-granule exocytosis, and aggregation, especially in response to the glycoprotein VI agonist convulxin. In contr…

0301 basic medicineBlood PlateletsGenotypePlatelet AggregationFibrinogen receptorIntegrinPlatelet Glycoprotein GPIIb-IIIa Complex030204 cardiovascular system & hematologyFibrinogenCytoplasmic GranulesExocytosisExocytosis03 medical and health sciences0302 clinical medicineLysosomeCrotalid VenomsmedicineAnimalsPlateletLectins C-TypeLactadherinMice KnockoutbiologyChemistryThrombinFibrinogenConvulxinHematologyPlatelet ActivationCell biologyMice Inbred C57BL030104 developmental biologymedicine.anatomical_structurePhenotypebiology.proteinFemaleLysosomesSeptinsmedicine.drugThrombosis and haemostasis
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Temporal quantitative phosphoproteomics of ADP stimulation reveals novel central nodes in platelet activation and inhibition

2017

Adenosine diphosphate (ADP) enhances platelet activation by virtually any other stimulant to complete aggregation. It binds specifically to the G-protein-coupled membrane receptors P2Y1 and P2Y12, stimulating intracellular signaling cascades, leading to integrin aIIbb3 activation, a process antagonized by endothelial prostacyclin. P2Y12 inhibitors are among the most successful antiplatelet drugs, however, show remarkable variability in efficacy. We reasoned whether a more detailed molecular understanding of ADP-induced protein phosphorylation could identify (1) critical hubs in platelet signaling toward aggregation and (2) novel molecular targets for antiplatelet treatment strategies. We ap…

0301 basic medicineBlood PlateletsPHOSPHATASEImmunologyBlotting WesternUBIQUITINATIONBINDING PROTEIN STXBP5Biochemistry03 medical and health scienceschemistry.chemical_compoundGTP-binding protein regulatorsP2Y12HumansProtein phosphorylationPlatelet activationIloprostPHOSPHORYLATIONCOMBINATIONChemistryPhosphoproteomicsPATHWAYSCell BiologyHematologyPlatelet ActivationSIGNALING REVEALSCell biologyAdenosine DiphosphateAdenosine diphosphate030104 developmental biologyCLOPIDOGRELPhosphorylationPROTEOMICSSECRETIONSignal transductionPlatelet Aggregation InhibitorsSignal TransductionBlood
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Taking the stock of granule cargo: Platelet releasate proteomics.

2016

Human platelets are key players in a multitude of physiological and pathological processes. Upon activation they release cargo from different types of granules as well as microparticles in an apparently well-regulated and orchestrated manner. The resulting specific platelet releasates create microenvironments of biologically active compounds and proteins during platelet aggregation and thrombus formation, allowing efficient delivery of growth factors and immune modulators to their sites of effect and enhancing the coagulative response in a positive feedback loop. Thus, platelet releasates play a central role in the regulation of platelet homeostasis and heterotypic cell interaction. Additio…

0301 basic medicineBlood PlateletsProteomicsFuture perspectivePlatelet aggregationProteomeGranule (cell biology)HematologyGeneral MedicineComputational biologyBiologyProteomicsCytoplasmic Granules03 medical and health sciencesImmune Modulators030104 developmental biologyImmunologyProteomeAnimalsHumansPlateletPlatelets
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Gut microbiota regulate hepatic von Willebrand factor synthesis and arterial thrombus formation via Toll-like receptor-2.

2016

The symbiotic gut microbiota play pivotal roles in host physiology and the development of cardiovascular diseases, but the microbiota-triggered pattern recognition signaling mechanisms that impact thrombosis are poorly defined. In this article, we show that germ-free (GF) and Toll-like receptor-2 (Tlr2)-deficient mice have reduced thrombus growth after carotid artery injury relative to conventionally raised controls. GF Tlr2-/- and wild-type (WT) mice were indistinguishable, but colonization with microbiota restored a significant difference in thrombus growth between the genotypes. We identify reduced plasma levels of von Willebrand factor (VWF) and reduced VWF synthesis, specifically in he…

0301 basic medicineBlood Plateletsmedicine.medical_specialtyEndotheliumPlatelet AggregationImmunologyBiologyBiochemistry03 medical and health sciencesMiceVon Willebrand factorhemic and lymphatic diseasesInternal medicinevon Willebrand FactormedicineAnimalsGerm-Free LifePlateletThrombusIntegrin bindingMice KnockoutToll-like receptorThrombosisCell BiologyHematologymedicine.diseaseToll-Like Receptor 2Gastrointestinal MicrobiomeTLR2030104 developmental biologymedicine.anatomical_structureEndocrinologyLivercardiovascular systembiology.proteinSignal transductioncirculatory and respiratory physiologySignal TransductionBlood
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Standardization of Light Transmission Aggregometry for Diagnosis of Platelet Disorders: An Inter-Laboratory External Quality Assessment.

2019

AbstractSeveral in vitro platelet function tests are available for the diagnosis of inherited platelet function disorders. Currently, the light transmission aggregometry (LTA) is recommended as one of the first-step tests. LTA is available in most specialized hemostasis laboratories. Although the LTA is accepted as a ‘gold standard’ assay for the evaluation of platelet function, its standardization in the clinical practice is still challenging. The GTH-based THROMKID-Plus Study Group has performed an inter-laboratory trial in Germany and Austria. Five different agonists were selected according to the Scientific and Standardization Committee/International Society on Thrombosis and Haemostasi…

0301 basic medicineBlood Plateletsmedicine.medical_specialtyLight transmissionStandardizationPlatelet AggregationPlatelet Function TestsQuality Assurance Health CarePlatelet disorder030204 cardiovascular system & hematology03 medical and health sciences0302 clinical medicineReference ValuesInternal medicineGermanyExternal quality assessmentmedicineHumansPlateletInter-laboratoryHemostasisbusiness.industryPlatelet-Rich PlasmaHematologyGold standard (test)Reference StandardsHealthy Volunteers030104 developmental biologyHemostasisAustriaBlood Platelet DisordersbusinessThrombosis and haemostasis
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Toxic Tau Oligomers Modulated by Novel Curcumin Derivatives

2019

AbstractThe pathological aggregation and accumulation of tau, a microtubule-associated protein, is a common feature amongst more than 18 different neurodegenerative diseases that are collectively known as tauopathies. Recently, it has been demonstrated that the soluble and hydrophobic tau oligomers are highly toxic in vitro due to their capacity towards seeding tau misfolding, thereby propagating the tau pathology seen across different neurodegenerative diseases. Modulating the aggregation state of tau oligomers through the use of small molecules could be a useful therapeutic strategy to target their toxicity, regardless of other factors involved in their formation. In this study, we screen…

0301 basic medicineCell biologyCurcuminCell SurvivalNeurotoxinsChemical biologyBiophysicsDrug Evaluation Preclinicallcsh:Medicinetau ProteinsProtein aggregationOligomerBiochemistryArticleBiophysical Phenomena03 medical and health scienceschemistry.chemical_compoundMiceProtein Aggregates0302 clinical medicineCell Line Tumormental disordersAnimalsHumanslcsh:ScienceNeuronsMultidisciplinaryCell DeathDrug discoveryDrug discoverySettore BIO/16 - Anatomia Umanalcsh:RSettore CHIM/06 - Chimica OrganicaSmall moleculeChemical biologyIn vitro3. Good healthTau protein Curcumin030104 developmental biologychemistryCell cultureBiophysicsCurcuminAlzheimerlcsh:QProtein Multimerization030217 neurology & neurosurgeryNeuroscience
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CENP-A Is Dispensable for Mitotic Centromere Function after Initial Centromere/Kinetochore Assembly

2016

SummaryHuman centromeres are defined by chromatin containing the histone H3 variant CENP-A assembled onto repetitive alphoid DNA sequences. By inducing rapid, complete degradation of endogenous CENP-A, we now demonstrate that once the first steps of centromere assembly have been completed in G1/S, continued CENP-A binding is not required for maintaining kinetochore attachment to centromeres or for centromere function in the next mitosis. Degradation of CENP-A prior to kinetochore assembly is found to block deposition of CENP-C and CENP-N, but not CENP-T, thereby producing defective kinetochores and failure of chromosome segregation. Without the continuing presence of CENP-A, CENP-B binding …

0301 basic medicineChromosomal Proteins Non-HistoneMedical PhysiologyEpigenesis GeneticChromosome segregationModelsChromosome SegregationKinetochoresGeneticsTumormitosiKinetochorekinetochoreCell biologyChromatinChromosomal Proteinsprotein degradationCENP-ACENP-BepigeneticCENP-C1.1 Normal biological development and functioningKinetochore assemblyCentromerechromosome segregationMitosismacromolecular substancesBiologyProtein degradationModels BiologicalGeneral Biochemistry Genetics and Molecular BiologyArticleCell Line03 medical and health sciencesGeneticUnderpinning researchCentromere Protein ACell Line TumorCentromereGeneticsHumansMitosisNon-HistoneBiologicalSettore BIO/18 - Genetica030104 developmental biologyGeneric health relevanceBiochemistry and Cell BiologyauxinCentromere Protein AEpigenesisCell Reports
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Aza-macrocyclic triphenylamine ligands for G-quadruplex recognition

2018

A new series of triphenylamine-based ligands with one (TPA1PY), two (TPA2PY) or three pendant aza-macrocycle(s) (TPA3PY) has been synthesised and studied by means of pH-metric titrations, UV/Vis spectroscopy and fluorescence experiments. The affinity of these ligands for G-quadruplex (G4) DNA and the selectivity they show for G4s over duplex DNA were investigated by Forster resonance energy transfer (FRET) melting assays, fluorimetric titrations and circular dichroism spectroscopy. Interestingly, the interactions of the bi- and especially the tri-branched ligands with G4s lead to a very intense redshifted fluorescence emission band that may be associated with intermolecular aggregation betw…

0301 basic medicineCircular dichroismaggregation-induced emissionChemistry Multidisciplinaryamines010402 general chemistryG-quadruplexTriphenylamine01 natural sciencesCatalysisCIRCULAR-DICHROISM03 medical and health scienceschemistry.chemical_compoundGeneral chemistryfluorescent probestriphenylamine polyaminesMoleculeSpectroscopyFLUORESCENT-PROBESScience & TechnologyG-quadruplexChemistryINTRAMOLECULAR CHARGE-TRANSFERANTICANCER DRUG DESIGNOrganic ChemistryaggregationFORMING REGIONDNAGeneral ChemistryFluorescenceG-quadruplexes0104 chemical sciencesCrystallographyChemistry030104 developmental biologyFörster resonance energy transfer2-PHOTON ABSORPTIONPROMOTER REGIONPhysical SciencesEQUILIBRIUM-CONSTANTSGRAPHENE OXIDE03 Chemical Sciencesmacrocyclic ligands
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Dual proteotoxic stress accelerates liver injury via activation of p62‐Nrf2

2021

Protein accumulation is the hallmark of various neuronal, muscular, and other human disorders. It is also often seen in the liver as a major protein-secretory organ. For example, aggregation of mutated alpha1-antitrypsin (AAT), referred to as PiZ, is a characteristic feature of AAT deficiency, whereas retention of hepatitis B surface protein (HBs) is found in chronic hepatitis B (CHB) infection. We investigated the interaction of both proteotoxic stresses in humans and mice. Animals overexpressing both PiZ and HBs (HBs-PiZ mice) had greater liver injury, steatosis, and fibrosis. Later they exhibited higher hepatocellular carcinoma load and a more aggressive tumor subtype. Although PiZ and H…

0301 basic medicineCirrhosisNF-E2-Related Factor 2medicine.disease_causePathology and Forensic MedicineMice03 medical and health sciences0302 clinical medicineSDG 3 - Good Health and Well-beingStress PhysiologicalFibrosisSequestosome-1 ProteinmedicineAnimalsHumansLiver injuryHepatitis B Surface Antigensbusiness.industryLiver DiseasesAutophagyHepatitis Bmedicine.diseasedigestive system diseasesaggregate Hepatitis B Surface Antigens Humans Liver Diseases Mice NF-E2-Related Factor 2 Sequestosome-1 Protein Stress Physiological alpha 1-Antitrypsin cirrhosis inclusionlipophagy oxidative stress SERPINA1 Animals030104 developmental biologyalpha 1-Antitrypsin030220 oncology & carcinogenesisHepatocellular carcinomaCancer researchSteatosisbusinessOxidative stressThe Journal of Pathology
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Loss of ISWI Function in Drosophila Nuclear Bodies Drives Cytoplasmic Redistribution of Drosophila TDP-43

2018

Over the past decade, evidence has identified a link between protein aggregation, RNA biology, and a subset of degenerative diseases. An important feature of these disorders is the cytoplasmic or nuclear aggregation of RNA-binding proteins (RBPs). Redistribution of RBPs, such as the human TAR DNA-binding 43 protein (TDP-43) from the nucleus to cytoplasmic inclusions is a pathological feature of several diseases. Indeed, sporadic and familial forms of amyotrophic lateral sclerosis (ALS) and fronto-temporal lobar degeneration share as hallmarks ubiquitin-positive inclusions. Recently, the wide spectrum of neurodegenerative diseases characterized by RBPs functions’ alteration and loss was coll…

0301 basic medicineCytoplasmCytoplasmic inclusionFluorescent Antibody TechniqueProtein aggregationHeterogeneous ribonucleoprotein particleHeterogeneous-Nuclear Ribonucleoproteinslcsh:Chemistry0302 clinical medicineDrosophila Proteinsneurodegenerative diseasesnuclear bodylcsh:QH301-705.5SpectroscopyGeneral MedicinehnRNPsComputer Science ApplicationsCell biologyChromatinTransport proteinDNA-Binding ProteinsProtein Transportmedicine.anatomical_structureDrosophilaDrosophila ProteinProtein BindingImitation SWIBiologyCatalysisArticleInorganic Chemistryomega speckles03 medical and health sciencesmedicineAnimalsPhysical and Theoretical ChemistryMolecular BiologyGenetic Association StudiesCell NucleusOrganic Chemistryta1182Chromatin Assembly and DisassemblyCell nucleus030104 developmental biologylcsh:Biology (General)lcsh:QD1-999gene expression<i>Drosophila</i>; nuclear body; omega speckles; dTDP-43; hnRNPs; omega speckles; neurodegenerative diseases; gene expression; gene regulationdTDP-43gene regulation030217 neurology & neurosurgeryInternational Journal of Molecular Sciences
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